Purified Antigens
Discover precise autoimmune research with our purified antigens – trusted quality and reliable results.
DNA (Double Stranded) from Plasmid
The dsDNA antigen is a 2690 bp plasmid purified by alkaline lysis and chromatography. The purification process includes operations to minimize reactivity to antibodies against single-stranded DNA. Use of plasmid DNA in ELISA is an effective method for the detection of anti-double-stranded (ds) DNA antibodies (1). The presence of antibodies to dsDNA is included in the 1982 revised criteria for classification of Systemic Lupus Erythematosus (SLE) (2). Approximately 60-70% of SLE patients have antibodies to dsDNA, and there is considerable evidence to implicate immune complexes containing anti-dsDNA and DNA in the pathogenesis of SLE (3,4). In addition, levels of anti-dsDNA antibodies have been demonstrated to correlate with disease activity in many patients (5,6). Low levels of anti-dsDNA antibodies may occur in other rheumatic diseases (7) and may occur at a very low frequency (<2%) in individuals without any symptoms of rheumatic disease (8). Anti-dsDNA antibodies may appear in rheumatic patients prior to the development of disease manifestations (9).
| Code | Amount | Price | Inquiry |
|---|---|---|---|
| DNA-3000 | 1 mg | $1650.00 | |
| DNA-3250 | 250 microgram | $600.00 |
- Emlen W, et al. J.Immunol. Methods Vol 132:pg 91-101 (1990).
- Tan EM, et al. Arthrits Rheum Vol 25:pg 1271-1277 (1982).
- Nakamura RM, Peebles CL, Molden DP, Tan, EM. Lab. Medicine Vol 15: pg 190-198 (1984).
- Condemi JJ. JAMA Vol 258: pg 2920-2929 (1987).
- Tan EM, Schuer PH, Carr RI, Kunkel HG. J Clin Invest Vol 45: pg 1732-1740 (1966).
- Miniter MF, Stollar BD, Agnello V. Arthritis Rheum Vol 22: pg 959-968 (1979).
- Shoenfeld Y, Andre-Schwartz A, Stollar BD, Schwartz S. in Systemic Lupus Erythematosus, John Wiley & Sons, pg 213-255 (1987).
- Stollar BD. Clin. Immun. Allergy Vol 1: pg 243-260 (1981).
- Swaak AJG, et al. Annals of Rheum Dis Vol 41: pg 388-395 (1982).
| Product number: | DNA-3000 |
| Description: | Plasmid DNA |
| Amount: | 1mg in 1ml |
| Physical state: | Frozen liquid solution, buffered with 0.01M Tris, 0.001M EDTA pH 8.00 |
| Manufacturing method: | Plasmid DNA was isolated from E. coli by alkaline lysis and chromatographic methodologies. |
| Storage conditions: | Product unstable above 0° C, aliquot and store frozen at -70±10° C. Avoid repeated freeze-thaw. |
| Definitions: | A260nm equals 1.0 at 50µg/ml. |
| Instructions for use: | Recommended for use in standard solid phase immunoassays. |
| Warnings: | For research or further manufacturing use only. |
| Product number: | DNA-3250 |
| Description: | Plasmid DNA |
| Amount: | 0.25 mg in 0.25 ml |
| Physical state: | Frozen liquid solution, buffered with 0.01M Tris, 0.001M EDTA pH 8.00 |
| Manufacturing method: | Plasmid DNA was isolated from E. coli by alkaline lysis and chromatographic methodologies. |
| Storage conditions: | Product unstable above 0° C, aliquot and store frozen at -70±10° C. Avoid repeated freeze-thaw. |
| Definitions: | A260nm equals 1.0 at 50µg/ml. |
| Instructions for use: | Recommended for use in standard solid phase immunoassays. |
| Warnings: | For research or further manufacturing use only. |
Histones, Whole
Histones are a group of similar, small, highly conserved nuclear proteins that bind to DNA by their many basic residues. The histones are divided into fractions, with each fraction having a distinct amino acid composition and sequence. Histones are also classified by relatively high levels of lysine and arginine. The presence of autoantibodies to histones are frequently found in several rheumatic disorders (1). In one study, the predominant responses to histones in SLE sera were to H1, H2b, and H3. Marked elevations of binding occurred to H1 and H2b in 33% of patients, while 25% showed higher binding to H3 (2). The same study showed the highest anti-histone reactivity to be in patients with rheumatoid arthritis with vasculitis, while the highest reactivity in SLE sera was in those patients with a history of photosensitivity (3).
| Code | Amount | Price | Inquiry |
|---|---|---|---|
| HIS-1000 | 250 mg | $ 45.00 | |
| HIS-1010 | 1 gm | $ 90.00 |
- Bradbury EM. “Histone Nomenclature in the Structure and Function of Chromatin.” (Fitzsimmins, D. W, and Walstenholme, G.E. W., eds.) CIBA Foundation symposium 28, American Elsevier, New York, 1975, pg 4.
- Elgin SCR, and Weinbrauh H. “Chromosomal Proteins and Chromatin Structure” in Annual Review of Biochemistry, (Smell, E. E., Boyer, P.D., Meister, A., and Richardson, C.C. eds. Annual Reviews,, Palo Alto, 1975, pg 725.
- Johns EW, and Butler JAV. “Further Fractionations of Histones from Calf Thymus.” Biochem. J ,Vol 82: 1962 , pg 15.
| Product number: | HIS-1000, HIS-1010 |
| Description: | Whole Histones |
| Amount: | 250 mg, 1 gram |
| Physical state: | White powder |
| Manufacturing method: | |
| Purified from chicken red blood cells | |
| Storage conditions: | Histones should be stored in a cool, dry place. Storage over a desiccate or under vacuum is preferable. |
| Instructions for use: | Histones are most soluble in an acidic buffer but can be dissolved in deionized water, depending on the needs of your assay system. Allow sufficient time for complete dissolution. The histone solution is best made immediately before use, but if storage of the solution is necessary, aliquot into single use amounts and freeze. Avoid repeated freeze/thaws. |
| Warnings: | For research or further manufacturing use only. |
Histones subclass H1 (F1)
Histones are a group of similar, small, highly conserved nuclear proteins that bind to DNA by their many basic residues. The histones are divided into fractions, with each fraction having a distinct amino acid composition and sequence. Histones are also classified by relatively high levels of lysine and arginine. The presence of autoantibodies to histones are frequently found in several rheumatic disorders (1). In one study, the predominant responses to histones in SLE sera were to H1, H2b, and H3. Marked elevations of binding occurred to H1 and H2b in 33% of patients, while 25% showed higher binding to H3 (2). The same study showed the highest anti-histone reactivity to be in patients with rheumatoid arthritis with vasculitis, while the highest reactivity in SLE sera was in those patients with a history of photosensitivity (3).
| Code | Fractions | Class | MW | Amount | Price |
|---|---|---|---|---|---|
| HIS-1001 | H1(F1) | Lysine rich | 21,500 | 10mg | $45.00 |
| HIS-1011 | H1(F1) | Lysine rich | 21,500 | 25mg | $90.00 |
- Bradbury EM. “Histone Nomenclature in the Structure and Function of Chromatin.” (Fitzsimmins, D. W, and Walstenholme, G.E. W., eds.) CIBA Foundation symposium 28, American Elsevier, New York, 1975, pg 4.
- Elgin SCR, and Weinbrauh H. “Chromosomal Proteins and Chromatin Structure” in Annual Review of Biochemistry, (Smell, E. E., Boyer, P.D., Meister, A., and Richardson, C.C. eds. Annual Reviews,, Palo Alto, 1975, pg 725.
- Johns EW, and Butler JAV. “Further Fractionations of Histones from Calf Thymus.” Biochem. J ,Vol 82: 1962 , pg 15.
| Product number: | HIS-1001 |
| Description: | Histone subclass F1 |
| Amount: | 10mg |
| Physical state: | Dry, white powder |
| Manufacturing method: | Purified from bovine tissue. |
| Storage conditions: | Histones should be stored in a cool, dry place. Storage over a desiccant, or under vacuum is preferable. |
| Instructions for use: | Histones are most soluble in an acidic buffer but can be dissolved in deionized water, depending on the needs of your assay system. Allow sufficient time for complete dissolution. The histone solution is best made immediately before use, but if storage of the solution is necessary, aliquot into single use amounts and freeze. Avoid repeated freeze/thaws. |
| Specificity: | Bands at 21.5 kD by 20% SDS-PAGE. |
| Product number: | HIS-1011 |
| Description: | Histone subclass F1 |
| Amount: | 25mg |
| Physical state: | Dry, white powder |
| Manufacturing method: | Purified from bovine tissue. |
| Storage conditions: | Histones should be stored in a cool, dry place. Storage over a desiccant, or under vacuum is preferable. |
| Instructions for use: | Histones are most soluble in an acidic buffer but can be dissolved in deionized water, depending on the needs of your assay system. Allow sufficient time for complete dissolution. The histone solution is best made immediately before use, but if storage of the solution is necessary, aliquot into single use amounts and freeze. Avoid repeated freeze/thaws. |
| Specificity: | Bands at 21.5 kD by 20% SDS-PAGE. |
| Warnings: | For research or further manufacturing use only. |
Histones H2a (F2A2)and H4(F2A1)
Histones are a group of similar, small, highly conserved nuclear proteins that bind to DNA by their many basic residues. The histones are divided into fractions, with each fraction having a distinct amino acid composition and sequence. Histones are also classified by relatively high levels of lysine and arginine. The presence of autoantibodies to histones are frequently found in several rheumatic disorders (1). In one study, the predominant responses to histones in SLE sera were to H1, H2b, and H3. Marked elevations of binding occurred to H1 and H2b in 33% of patients, while 25% showed higher binding to H3 (2). The same study showed the highest anti-histone reactivity to be in patients with rheumatoid arthritis with vasculitis, while the highest reactivity in SLE sera was in those patients with a history of photosensitivity (3).
| Code | Fractions | Class | MW | Amount | Price |
|---|---|---|---|---|---|
| HIS-1002 | H2a(F2a2) and H4(F2a1) | Slightly lysine rich | 14,004 and 11,300 | 25 mg | $ 90.00 |
| HIS-1012 | H2a(F2a2) and H4(F2a1) | Slightly lysine rich | 14,004 and 11,300 | 100 mg | $275.00 |
- Bradbury EM. “Histone Nomenclature in the Structure and Function of Chromatin.” (Fitzsimmins, D. W, and Walstenholme, G.E. W., eds.) CIBA Foundation symposium 28, American Elsevier, New York, 1975, pg 4.
- Elgin SCR, and Weinbrauh H. “Chromosomal Proteins and Chromatin Structure” in Annual Review of Biochemistry, (Smell, E. E., Boyer, P.D., Meister, A., and Richardson, C.C. eds. Annual Reviews,, Palo Alto, 1975, pg 725.
- Johns EW, and Butler JAV. “Further Fractionations of Histones from Calf Thymus.” Biochem. J ,Vol 82: 1962 , pg 15.
| Product number: | HIS-1002 |
| Description: | Histone subclasses H4(F2a1) and H2a(F2a2) |
| Amount: | 25 mg |
| Physical state: | Dry, white powder |
| Manufacturing method: | Purified from bovine thymus tissue. |
| Storage conditions: | Histones should be stored in a cool, dry place. Storage over a desiccant, or under vacuum is preferable. |
| Instructions for use: | Histones are most soluble in an acidic buffer but can be dissolved in deionized water, depending on the needs of your assay system. Allow sufficient time for complete dissolution. The histone solution is best made immediately before use, but if storage of the solution is necessary, aliquot into single use amounts and freeze. Avoid repeated freeze/thaws. |
| Specificity: | Bands at 14.0 kD and 11.3kD by 20% SDS-PAGE. |
| Warnings: | For research or further manufacturing use only. |
| Product number: | HIS-1012 |
| Description: | Histone subclass H4(F2a1) and H2a(F2a2) |
| Amount: | 100 mg |
| Physical state: | Dry, white powder |
| Manufacturing method: | Purified from bovine thymus tissue. |
| Storage conditions: | Histones should be stored in a cool, dry place. Storage over a desiccant, or under vacuum is preferable. |
| Instructions for use: | Histones are most soluble in an acidic buffer but can be dissolved in deionized water, depending on the needs of your assay system. Allow sufficient time for complete dissolution. The histone solution is best made immediately before use, but if storage of the solution is necessary, aliquot into single use amounts and freeze. Avoid repeated freeze/thaws. |
| Specificity: | Bands at 14.0 kD and 11.3kD by 20% SDS-PAGE. |
Histones H2b(F2b)
Histones are a group of similar, small, highly conserved nuclear proteins that bind to DNA by their many basic residues. The histones are divided into fractions, with each fraction having a distinct amino acid composition and sequence. Histones are also classified by relatively high levels of lysine and arginine. The presence of autoantibodies to histones are frequently found in several rheumatic disorders (1). In one study, the predominant responses to histones in SLE sera were to H1, H2b, and H3. Marked elevations of binding occurred to H1 and H2b in 33% of patients, while 25% showed higher binding to H3 (2). The same study showed the highest anti-histone reactivity to be in patients with rheumatoid arthritis with vasculitis, while the highest reactivity in SLE sera was in those patients with a history of photosensitivity (3).
| Code | Fractions | Class | MW | Amount | Price |
|---|---|---|---|---|---|
| HIS-1003 | H2b(F2b) | Slightly lysine rich | 13,774 | 10 mg | $38.00 |
| HIS-1013 | H2b(F2b) | Slightly lysine rich | 13,774 | 25 mg | $72.00 |
- Bradbury EM. “Histone Nomenclature in the Structure and Function of Chromatin.” (Fitzsimmins, D. W, and Walstenholme, G.E. W., eds.) CIBA Foundation symposium 28, American Elsevier, New York, 1975, pg 4.
- Elgin SCR, and Weinbrauh H. “Chromosomal Proteins and Chromatin Structure” in Annual Review of Biochemistry, (Smell, E. E., Boyer, P.D., Meister, A., and Richardson, C.C. eds. Annual Reviews,, Palo Alto, 1975, pg 725.
- Johns EW, and Butler JAV. “Further Fractionations of Histones from Calf Thymus.” Biochem. J ,Vol 82: 1962 , pg 15.
| Product number: | HIS-1003 |
| Description: | Histone subclass F2b |
| Amount: | 10mg |
| Physical state: | Dry, white powder |
| Manufacturing method: | Purified from bovine tissue. |
| Storage conditions: | Histones should be stored in a cool, dry place. Storage over a desiccant, or under vacuum is preferable. |
| Instructions for use: | Histones are most soluble in an acidic buffer but can be dissolved in deionized water, depending on the needs of your assay system. Allow sufficient time for complete dissolution. The histone solution is best made immediately before use, but if storage of the solution is necessary, aliquot into single use amounts and freeze. Avoid repeated freeze/thaws. |
| Specificity: | Bands at 13.7 kD by 20% SDS-PAGE. |
| Warnings: | For research or further manufacturing use only. |
| Product number: | HIS-1013 |
| Description: | Histone subclass F2b |
| Amount: | 25mg |
| Physical state: | Dry, white powder |
| Manufacturing method: | Purified from bovine tissue. |
| Storage conditions: | Histones should be stored in a cool, dry place. Storage over a desiccant, or under vacuum is preferable. |
| Instructions for use: | Histones are most soluble in an acidic buffer but can be dissolved in deionized water, depending on the needs of your assay system. Allow sufficient time for complete dissolution. The histone solution is best made immediately before use, but if storage of the solution is necessary, aliquot into single use amounts and freeze. Avoid repeated freeze/thaws. |
| Specificity: | Bands at 13.7 kD by 20% SDS-PAGE. |
| Warnings: | For research or further manufacturing use only. |
Histones H3(F3), may also contain H2b(F2B) and H2a(F2A2)
Histones are a group of similar, small, highly conserved nuclear proteins that bind to DNA by their many basic residues. The histones are divided into fractions, with each fraction having a distinct amino acid composition and sequence. Histones are also classified by relatively high levels of lysine and arginine. The presence of autoantibodies to histones are frequently found in several rheumatic disorders (1). In one study, the predominant responses to histones in SLE sera were to H1, H2b, and H3. Marked elevations of binding occurred to H1 and H2b in 33% of patients, while 25% showed higher binding to H3 (2). The same study showed the highest anti-histone reactivity to be in patients with rheumatoid arthritis with vasculitis, while the highest reactivity in SLE sera was in those patients with a history of photosensitivity (3).
| Code | Fractions | Class | MW | Amount | Price |
|---|---|---|---|---|---|
| HIS-1004 | H3(F3) | Arginine rich | 15,324 | 10 mg | $45.00 |
| HIS-1014 | H3(F3) | Arginine rich | 15,324 | 25 mg | $90.00 |
- Bradbury EM. “Histone Nomenclature in the Structure and Function of Chromatin.” (Fitzsimmins, D. W, and Walstenholme, G.E. W., eds.) CIBA Foundation symposium 28, American Elsevier, New York, 1975, pg 4.
- Elgin SCR, and Weinbrauh H. “Chromosomal Proteins and Chromatin Structure” in Annual Review of Biochemistry, (Smell, E. E., Boyer, P.D., Meister, A., and Richardson, C.C. eds. Annual Reviews,, Palo Alto, 1975, pg 725.
- Johns EW, and Butler JAV. “Further Fractionations of Histones from Calf Thymus.” Biochem. J ,Vol 82: 1962 , pg 15.
| Product number: | HIS-1004 |
| Description: | Histone subclass H3(F3) may also contain H2b(F2b) and H2a(F2a2) |
| Amount: | 10mg |
| Physical state: | Dry, white powder |
| Manufacturing method: | Purified from bovine tissue. |
| Storage conditions: | Histones should be stored in a cool, dry place. Storage over a desiccant, or under vacuum is preferable. |
| Instructions for use: | Histones are most soluble in an acidic buffer but can be dissolved in deionized water, depending on the needs of your assay system. Allow sufficient time for complete dissolution. The histone solution is best made immediately before use, but if storage of the solution is necessary, aliquot into single use amounts and freeze. Avoid repeated freeze/thaws. |
| Specificity: | Bands at 15.3 and 14 kD by 20% SDS-PAGE. |
| Product number: | HIS-1014 |
| Description: | Histone subclass H3(F3) may also contain H2b(F2b) and H2a(F2a2) |
| Amount: | 25mg |
| Physical state: | Dry, white powder |
| Manufacturing method: | Purified from bovine tissue. |
| Storage conditions: | Histones should be stored in a cool, dry place. Storage over a desiccant or under vacuum is preferable. |
| Instructions for use: | Histones are most soluble in an acidic buffer but can be dissolved in deionized water, depending on the needs of your assay system. Allow sufficient time for complete dissolution. The histone solution is best made immediately before use, but if storage of the solution is necessary, aliquot into single use amounts and freeze. Avoid repeated freeze/thaws. |
| Specificity: | Bands at 15.3 and 14 kD by 20% SDS-PAGE. |
Jo-1 Antigen
The Jo-1 antigen is histidyl-transfer ribonucleic acid (t-RNA) synthetase. This enzyme is partially responsible for attaching t-RNA to their cognate rRNA (2). The Jo-1 antigen migrates as a 53 kD protein on SDS-PAGE. Anti-Jo-1 autoantibodies were originally described as precipitating autoantibodies in sera of patients with polymyositis. It was later realized that the anti-Jo-1 antibodies were specific for patients with polymyositis. The target for the anti-Jo-1 antibodies was one of a family of distinct cellular enzymes, the aminoacyl t-RNA synthetases (1). The presence of autoantibodies against the Jo-1 antigen has been reported in up to 23% of polymyositis patients by immunodiffusion (3). Anti-Jo-1 antibodies are almost completely specific for myositis, being more common in polymyositis than dermato-myositis(4), and rare in children (5). The presence of anti-Jo-1 antibodies defines a distinct group of polymyositis patients with interstitial disease, arthritis, and fevers (6). The anti-Jo-1 response appears to be self-antigen driven, having a broad spectrotype over time undergoing isotype switching. Anti-Jo-1 antibodies also inhibit the function of human histidyl tRNA synthetase more than they do from other species (6).
| Code | Amount | Price | NOTE |
|---|---|---|---|
| JO1-3000 | 1000 units | $ 600.00 | Temporarily unavailable |
- Targoff IN, Reichlin M. “Measurement of Antibody to Jo-1 by ELISA and Comparison to Enzyme Inhibitory.” A of Immun: Vol: 138, 1987, pg 2874-2882.
- Hershey JWB. “The Translational Machinery: Components and Mechanism.”, Cell Biology, Vol: 4, 1980, pg 1-68.
- Nishikai M and Reichlin M. “Heterogeneity of Precipitating Antibodies in Polymyositis and Dermatomyositis, Terization of the Jo-1 Antibody System.” Arthritis Rheum,1980, pg 881.
- Reichlin M, Maddison PJ, Targoff IN, Bunch T, Arnett FC, Sharp GC, Treadwell E, and Tan EM. “Antibodies Nuclear/Nucleolar Antigen in Patients with Polymyositis Overlap Syndrome.” J Clin Immunol, 1984.
- Pachman LM, Hardin JA, Cobb MA, and Arroyave CM. “The Antinuclear Antibody (ANA) in Juvenile Dermatomyositis (JDMS) is not Jo-1, Suggesting that JDMS and Polymyositis (PM) are Different Diseases.” Arthritis Rheum. , 1984.
- Takeuchi K, Tan EM, Pollard KM. “Similarity of Epitopes of an Autoantigen Fibrillarin-Recognized by Human Immmune Sera and Murine Autoimmune Models.” American College of Rheum, 56th Annual Scientific 0ct 11-15, 1992, Atlanta. Poster Presentations.
| JO1-3000 |
| Jo-1 Antigen, affinity purified, 1000 units |
| 1000 UNITS in 1 ml |
| Frozen liquid solution, buffered with 0.01M Tris, 0.53M NaCl, 0.02% NaN3, and 50% glycerol. |
| This material has been purified from calf and/or rabbit thymus through the use of immobilized human anti-Jo-1 immune globulins. Other antigens (Sm, RNP, SSA, Scl-70, and SSB) are not detected with ELISA assays. Homogeneity is verified by SDS PAGE. |
| Product unstable above 0° C, aliquot and store frozen at -70°±10° C. Avoid repeated freeze-thaw. |
| One unit of activity is defined as the amount of antigen that will generate an absorbance of 1.2 when assayed using ImmunoVision’s standard procedure for enzyme immunoassay. Activity will vary with assay conditions. |
| Recommended for use in standard solid phase immunoassays. |
Mitochondrial Antigen
Description: The mitochondrial antigen M2 is a cluster of four major mitochondrial innermembrane proteins of approximately 74, 52, 45, and 39 kD, which are found widely in nature. (2) These antigens have been identified as the E2 subunit of branched chain 2-oxo acid dehydrogenase, the E2 subunit of the 2-oxo dehydrogenase complex, protein X, and the E1a and E1b subunits of the pyruvate dehydrogenase complex (3). Autoantibodies to mitochondrial antigens were originally described in patients with Primary Biliary Cirrhosis. It was later realized that Primary Biliary Cirrhosis is an autoimmune liver disease characterized by autoantibodies to the mitochondrial antigen M2 in serum (1). The presence of autoantibodies against the mitochondrial antigens has been reported to have prognostic value in the diagnosis Primary Biliary Cirrhosis, as the disease rarely occurs without anti-M2. (2) Autoantibodies to M2 in Primary Biliary Cirrhosis usually occur in a very high titer and have an IgG3 subclass restriction (2).
| Code | Amount | Price | |
|---|---|---|---|
| MIT-3000 | 1000 units | $600.00 |
- Baum H, and Palmer C. Mol. Aspects Med. 8, 1985, pg 201-234.
- “Molecular basis of mitochondrial autoreactivity in primary biliary cirrhosis.” Immunology Today, Vol. 10, 1989.
- American College of Rheumatology, 55th Annual Scientific Meeting, Boston Mass, Poster Presentation, 1991.
| Product number: | MIT-3000 |
| Description: | Mitochondrial Antigen, affinity purified, 1000 units |
| Amount: | 1000 UNITS in 1ml |
| Physical state: | Frozen liquid solution, buffered with 0.01M Tris, 0.53M NaCl, 0.02% NaN3 |
| Manufacturing method: | This material has been purified from bovine spleen and/or thymus through the use of immobilized human anti-Mitochondrial immune globulins. Other antigens (Sm, RNP, Scl-70, SS-A(Ro), SS-B(La), Jo-1) are not detected with ELISA assays. |
| Storage conditions: | Product unstable above 0° C, aliquot and store frozen at -70°±10° C. Avoid repeated freeze-thaw. |
| Definitions: | One unit of activity is defined as the amount of antigen that will generate an absorbance of 1.2 when assayed using ImmunoVision’s standard procedure for enzyme immunoassay. Activity will vary with assay conditions. |
| Instructions for use: | Recommended for use in standard solid phase immunoassays. |
Myeloperoxidase (MPO) Antigen
The myeloperoxidase (MPO) antigen is a heme-containing protein found in the primary granules of neutrophils and monocytes. It’s primary function is to destroy phagocytosed microorganisms by generating highly reactive oxidative species within the phagosome (1). MPO is a heterodimer consisting of two 59 kD heavy chains and two 14 kD light chains. ImmunoVision’s MPO is purified from a human promyelocytic cell line using detergent extraction, salt fractionation, and chromatographic techniques. Anti-neutrophil cytoplasmic antibodies (ANCA) are autoantibodies against cytoplasmic constituents of neutrophils and monocytes (2). Staining by indirect immunofluorescence (IFA) shows two main staining patterns: cytoplasmic (c-ANCA) and perinuclear (p-ANCA) (3,4). Anti-MPO antibodies usually generate a p-ANCA pattern but not all p-ANCA patterns are caused by anti-MPO antibodies. Anti-MPO autoantibodies are strongly associated with idiopathic microscopic polyangiitis, crescentic glomeronephritis, polyarteritis nodosa, and Churg-Strauss syndrome (5,6). In addition, MPO antibody titer may correlate with disease activity (3).
| Code | Amount | Price | |
|---|---|---|---|
| MPO-3000 | 1mg | $825 | |
| MPO-3200 | 200 micrograms | $200 |
- Hope HR, Remsen EE, Lewis, Jr. C, Heuvelman DM, Walker MC, Jennings M, Connolly DT. Protein Expression and Purification Vol 18:pg 269-276 (2000).
- Savige J et al. Immunopathology Vol 111: pg 507-513 (1999).
- Peter JB. Use and Interpretation of Tests in Clinical Immunology, Eight Edition. Specialty Laboratories, Inc. Santa Monica, CA. pg 174-177.
- Hagen EC, et al. J.Immunol. Methods. Vol 196:pg 1-15 (1996).
- Cohen-Tervaert JW, et al. Arthritis Rheum. Vol 33(8):pg 1264-1272 (1990).
- Falk RJ, Jenette JC. N Engl J Med. Vol 318:pg 1651-1657 (1988).
| Product number: | MPO-3000, MPO-3200 |
| Description: | Myeloperoxidase |
| Amount: | 1 mg, 0.2 mg |
| Enzymatic Activity: | 1600 – 2400 units / mg. One unit will produce an increase in absorbance (A470nm) of 1.0 per minute at pH 7.0, 25C, using guaiacol as substrate. |
| Physical state: | Lyophilized solid from 0.025M sodium acetate, 0.1M NaCl, pH 6.0 |
| Manufacturing method: | This material has been purified from a human promyelocytic cell line using detergent extraction, salt fractionation, and chromatographic techniques. |
| Storage conditions: | Store lyophilized at -20C or lower. After reconstitution, store at 4C. Freezing of myeloperoxidase in solution may result in loss of activity. |
| Expiration: | After reconstitution, store at 4C for up to 12 months. |
Ribosomal P antigen
The Ribosomal P antigen consists of three proteins of the 60S ribosomal subunit (3). These three proteins are designated PO(38 kD), P1(19 kD), and P2(17 kD). Studies have suggested that one P1 homodimer and one P2 homodimer are attached to PO by the NH2-termini (4). P1 and P2 are believed to be the eukaryotic equivalent of the E. coli ribosomal protein L12 and have been shown to contain sequences that are highly conserved among eukaryotes (5). The major immunoreactive epitope of these ribosomal antigens has been mapped and is localized to the carboxy terminus. PO, P1, and P2 have an identical 17 amino acid carboxy terminus. The Ribosomal P antigens have GTPase activity (6) and have been shown to be phosphorylated by casein kinase II (7). Autoantibodies to Ribosomal antigens were originally described inpatients with Systemic Lupus Erythematosus (SLE), and have been associated with psychotic episodes in SLE (1). Anti-P antibodies are detected in the sera of 10-20% of SLE patients and are found in 80% of patients with Lupus Psychosis as opposed to SLE patients with other neurological manifestations (2). The results of one study have indicated that Anti-P antibodies show moderate restriction in spectrotype, isotype, subclass, and light chain type. (8) It has also been shown that Anti-Ribosomal P antisera may contain antibodies to a small fragment of 28SrRNA (6). Another study has shown a high frequency of Anti-Ro/SS-A in patients with Anti-P, while Anti-La/SS-B is present only in a low frequency (1). Other studies have presented evidence that Anti-P antibodies (IgG) may bind to the ribosome in vivo and inhibit protein synthesis (9). The original method for determining antibodies to ribosomal proteins was immunofluorescence.
| Code | Amount | Price | Inquiry |
|---|---|---|---|
| PAG-3000 | 1000 units | $600.00 |
- Bonfa E., Golombek SJ, Kaufman LD, Skelly S, et al. “Association Between Lupus Psychosis and Anti-Ribosomal P Protein Antibodies.” New England J of Med, 1987, pg 265-271.
- Elkon K, Weissbach H, Brot N. “Central Nervous System Function in Systemic Lupus Erythematosus.” Neurochemical Research, 1990, pg 401-406.
- Elkon KB, Pamassa AP, Foster C.L. J Exp Med, 1985, pg 459-471.
- Uchiumi T Wahba AJ, Traut RR. Proc Natl Acad Sci, 1987, pg 5580-5584.
- Towbin H, Ramjoue H-P, Kuster H, Liverani D, Gordon J. J Bio Chem, Vol 257: 1982, pg 12709-12715.
- Jia-Li Chu, Brot N, Weissbach H, Elkon K. “Lupus Anti-ribosomal P Anitsera Contain Antibodies to a Small Fragment of 28S rRNA Located in the Proposed Ribosomal GTPase Center.” J Exp Med, 1991, pg 507-514.
- Hasler P, Brot N, Weissbach H, et al. “Ribosomal Proteins PO, P1, and P2 Are Phosphorylated by Casein Kinase II at Their Conserved Carboxyl Termini.” J of Bio Chem, Vol: 266, 1991, pg 13815-13820.
- Bonfa E, Jia-Li-Chu, Brot N, and Elkon KB. “Lupus Anti-Ribosomal P Peptide Antibodies Show Limited Heterogeneity and Are Predominantly of the IgG, and IgG2 Subclasses.” Clinical Immunology and Immunopathology , Vol: 45, 1987, pg 129-138.
- Stacey DW, Skelly S, Watson T, Elkon K, et al. “The Inhibition of Protein Synthesis by IgG Containing Anti-ribosome P Autoantibodies from Systemic Lupus Erythematosus Patients.” Archives of Biochemistry and Biophysics, Vol: 267, 1988, pg 398-403.
Product Specifications
| Product number: | PAG-3000 |
| Description: | Ribosomal P Antigen, affinity purified, 1000 units |
| Amount: | 1000 UNITS in 1ml |
| Physical state: | Frozen liquid solution, buffered with 0.01M Tris, 0.53M NaCl, 0.02% NaN3 |
| Manufacturing method: | This material has been purified from bovine thymus and/or rabbit thymus through the use of immobilized human anti-Ribosomal P immune globulins. Other antigens (Sm, RNP, Scl-70, SSA(Ro), SSB(La), Jo-1) are not detected with ELISA assays. |
| Storage conditions: | Product unstable above 0° C, aliquot and store frozen at -70°±10° C. Avoid repeated freeze-thaw. |
| Definitions: | One unit of activity is defined as the amount of antigen that will generate an absorbance of 1.2 when assayed using ImmunoVision’s standard procedure for enzyme immunoassay. Activity will vary with assay conditions. |
| Instructions for use: | Recommended for use in standard solid phase immunoassays. |
| Warnings: | For research or further manufacturing use only. |
QC0164
PAG-3000.DOC
Ver 1.3
Effective Date 9-4-2003
Proteinase-3 (PR-3) Antigen
The Proteinase-3 (PR-3) antigen is 29 kD protein found in the primary granules of neutrophils and monocytes. It is a serine protease with broad proteolytic activity against a variety of extracellular matrix proteins (1). ImmunoVision’s PR-3 is purified fom a human promyelocytic cell line using detergent extraction, salt fractionation, and chromaographic techniques. Anti-neutrophil cytoplasmic antibodies (ANCA) are autoantibodies against various lysosomal enzymes (2). Staining by indirect immunofluorescence (IFA) shows two main staining patterns: cytoplasmic (c-ANCA) and perinuclear (p-ANCA) (2,3). The c-ANCA pattern is caused by autoantibodies to PR-3 (4,5). Anti-PR3 autoantibodies are found in 84-100% of patients with Wegener’s granulomatosis (3,6). In addition, PR-3 antibody titer may correlate with disease activity (2).
| Code | Amount | Price | Inquiry |
|---|---|---|---|
| PR3-3100 | 0.1 mg | $385.00 | |
| PR3-3000 | 1 mg | $3300.00 |
- Bonfa E., Golombek SJ, Kaufman LD, Skelly S, et al. “Association Between Lupus Psychosis and Anti-Ribosomal P Protein Antibodies.” New England J of Med, 1987, pg 265-271.
- Elkon K, Weissbach H, Brot N. “Central Nervous System Function in Systemic Lupus Erythematosus.” Neurochemical Research, 1990, pg 401-406.
- Elkon KB, Pamassa AP, Foster C.L. J Exp Med, 1985, pg 459-471.
- Uchiumi T Wahba AJ, Traut RR. Proc Natl Acad Sci, 1987, pg 5580-5584.
- Towbin H, Ramjoue H-P, Kuster H, Liverani D, Gordon J. J Bio Chem, Vol 257: 1982, pg 12709-12715.
- Jia-Li Chu, Brot N, Weissbach H, Elkon K. “Lupus Anti-ribosomal P Anitsera Contain Antibodies to a Small Fragment of 28S rRNA Located in the Proposed Ribosomal GTPase Center.” J Exp Med, 1991, pg 507-514.
- Hasler P, Brot N, Weissbach H, et al. “Ribosomal Proteins PO, P1, and P2 Are Phosphorylated by Casein Kinase II at Their Conserved Carboxyl Termini.” J of Bio Chem, Vol: 266, 1991, pg 13815-13820.
- Bonfa E, Jia-Li-Chu, Brot N, and Elkon KB. “Lupus Anti-Ribosomal P Peptide Antibodies Show Limited Heterogeneity and Are Predominantly of the IgG, and IgG2 Subclasses.” Clinical Immunology and Immunopathology , Vol: 45, 1987, pg 129-138.
- Stacey DW, Skelly S, Watson T, Elkon K, et al. “The Inhibition of Protein Synthesis by IgG Containing Anti-ribosome P Autoantibodies from Systemic Lupus Erythematosus Patients.” Archives of Biochemistry and Biophysics, Vol: 267, 1988, pg 398-403.
Product Specifications
| Product number: | PR3-3000, PR3-3100 |
| Description: | Proteinase-3 |
| Amount: | 1 mg, 0.1 mg |
| Physical state: | Frozen liquid in buffer containing 0.02M tris, 0.02% NaN3, 0.1M- 0.5M NaCl, pH 7.0 |
| Manufacturing method: | This material has been purified from a human promyelocytic cell line using detergent extraction and chromatographic techniques. |
| Storage conditions: | Store frozen at -70C or lower. |
| Instructions for use: | Recommended for use in standard solid phase immunoassays. |
| Warnings: | For research or further manufacturing use only. |
QC0763
PR3-3000.doc
Ver 1.1
Ver date 12-10-2004
Product Name: Scl-70 Antigen
The Scl-70 antigen is an abundant nuclear protein susceptible to proteolysis (2). It has been shown that the Scl-70 antigen can be obtained as an extractable immunoreactive fragment (70 kD) of a larger protein (100-105kD), which has been shown to be Topoisomerase I (3). Anti-Scl-70 antibodies were originally described as precipitating autoantibodies in sera of patients with a connective tissue disease. It was later realized that some patients with diffuse scleroderma characteristically have a high incidence of this autoantibody (1). The presence of autoantibodies against the Scl-70 antigen has been reported to have prognostic value in the diagnosis of diffuse scleroderma, also termed Progressive Systemic Sclerosis (1). It has also been reported that autoantibodies to Scl-70 are a specific serologic marker for Systemic Sclerosis (3), and present in high proportions of Acrosclerosis (4). Anti-Scl-70 is not usually present in other autoimmune rheumatic diseases unless some cutaneous symptoms of scleroderma are present (4).
| Code | Amount | Price | |
|---|---|---|---|
| SCL-3000 | 1000 units | $600.00 |
- Maul GG, French BT, van Venrooij WJ, Jimenez SA. “Topoisomerase 1 Identified by Scleroderma 70 Antisera. Enrichment of Topoisomerase I at the Centromere in Mouse Mitotic Cells Before Anaphase.” Proc Natl Acad Sci Vol 83: 1986, pg 5145-5149.
- Douvas AS, Achten M & Tan EM. J Biol Chem 1989, pg 10514-10522.
- Shero JH, Bordwell B, Rothfiel NF, Earnshaw WC. “High Titers of Autoantibodies to Topoisomerase I (Scl-70) in Sera from Scleroderma Patients” Science Vol 231: 1986, pg 737-740.
- Jarzabek-Chorzelska M, Blaszczyk M, Jablonska S, et al. “Scl 70 antibody – a specific marker of systemic sclerosis.” British J of Dermatology 1986, pg 393-401.
Product Name: Smith (Sm) Antigen
Sm antigen is a non-histone nuclear protein composed of several polypeptides of differing molecular weights. They include B (26 kD), B'(27 k D), and D (13 kD). The principle reactivity has been shown to reside in the B, B’, and D polypeptides (3). Anti-Sm autoantibodies were described originally as precipitating autoantibodies in sera of patients with Systemic Lupus Erythematosus (1). Anti-Sm antibodies are also usually accompanied by antinuclear ribonucleoprotein (nRNP) antibodies (2). The U1 RNP particle has both Sm and RNP binding specificities. The difference is that the RNP particles bound by U2, U4/6 and U5 are bound by anti-Sm autoantibodies, but not by anti-nRNP autoantibodies. Autoantibodies against the Sm antigen precipitate the U1, U2, U4/6, and U5, small nuclear RNAs (4). The Sm antigen is involved in normal post-transcriptional, premessenger RNA processing to excise introns (5). It has been demonstrated that the Sm antigenicity is both RNase and DNase resistant and partially resistant to tryptic digestion (6). Autoantibodies to Sm antigen have been observed in 15 to 30% of SLE sera as a diagnostic marker. (7) It is thought that IgG anti-Sm correlates with Lupus disease activity and is a useful variable in predicting exacerbation and prognosis of SLE. (8) It has been reported that IgG anti-Sm is specifically detected in patients with SLE. IgM anti-Sm has rarely been detected in SLE and was recognized in other diseases (2). It has also been reported in a study of clinical significance, that the frequency of lung fibrosis and pericarditis was significantly higher in patients with IgG, IgA, and/or IgM anti-Sm (2).
| Code | Amount | Price | |
|---|---|---|---|
| SMA-3000 | 1000 units | $600.00 |
- Tan EM, Kunkel HG. “Characteristics of a Soluble Nuclear Antigen Precipitating with Sera of Patients with Systemic Lupus Erythematosus.” J Immunol Vol 96: 1966, pg 464-471.
- Yasuma M, Takasaki Y, Matsumoto K, et al. “Clinical Significance of IgG Anti-Sm Antibodies in Patients with Systemic Lupus Erythematosus.” The J of Rheumatology Vol 17: 1990, pg 469-475.
- James JA, Harley JB. “Sequential Epitopes of an Sm B/B’ Protein” American College of Rheumatology 55th Annual Scientific Meeting, Boston, MA 1991.
- Lerner MR, & Steitz JA “Antibodies to Small Nuclear RNAs Complexed with Proteins are Produced by Patients with Systemic Lupus Erythematosus” Proc Natl Acad Sci Vol 76: 1979, pg 5495-5499.
- Yang VW, Lerner MR, Steitz JA & Flint SJ. “A Small Nuclear Ribonucleoprotein is Required for Splicing of Adenoviral Early RNA Sequences.” Proc Natl Acad Sci USA, Vol 78: 1981, pg 1371-1375.
- Schrier WH, Reddy R and Busch H. “Identification of An Antigenic Protein Recognized by Anti-Sm Autoantibody.” Cell Biology International Reports Vol 6: 1982.
- Tan EM. “Special Antibodies for the Study of Systemic Lupus Erythematosus.” Arthritis Rheum Vol 25: 1982, pg 753-756.
- Pollard KM, Tan EM. “Purification of the Sm Nuclear Autoantigen, Detection and Clinical Significance of IgM Antibody.” Clin Exp Immunol Vol 60: 1985, pg 586-596
Product Name: nRNP Complex
nRNP Complex antigen is a non-histone nuclear protein composed of several polypeptides of differing molecular weights. It has been shown that RNP and Sm are distinct antigenic sites on the same nuclear molecular matrix consisting of RNA and eight polypeptides, including 70 kD, A(33 kD), C(22 kD) and the Sm peptides B (26 kD), B'(27 kD), D(13 kD), E/F (11 kD doublet), and G (9 kD). Autoantibodies against the nRNP antigen precipitate the U1a and U1b small nuclear RNAs (2). The nRNP antigen is involved in normal post transcriptional, premessenger RNA processing to excise introns. (3) It has been demonstrated that the nRNP antigen is both RNase and tryptic digestion sensitive (4). Autoantibodies to the nRNP antigen, in high titers, have been strongly associated with patients who have Mixed Connective Tissue Disease (MCTD) (5). Other studies have shown that antibodies against the 70 kD polypeptide are found more frequently in sera of MCTD than in anti-nRNP positive SLE patients (6). It has been suggested that patients showing anti-nRNP antibodies tend to have some of the clinical features of MCTD, regardless of their overall disease diagnosis (7). Anti-nRNP antibodies only bind the U1 RNP while the anti-Sm binds with the U1 RNP, U2RNP, U4/6RNP, AND U5RNP. Anti-RNP antibodies are often accompanied by anti-Sm antibodies (1). Double immunodiffusion was the original method for detecting anti-nRNP. Passive hemagglutination was popularized later (8).
| Code | Amount | Price | |
|---|---|---|---|
| SRC-3000 | 1000 units | $275 |
- Yasuma M, Takasaki Y Matsumoto K, et al: Clinical Significance of IgG Anti-Sm Antibodies in Patients with Systemic Lupus Erythematosus, The J of Rheumatology, 1990, pg 469-475.
- Lerner MR & Steitz JA: Antibodies to small nuclear RNAs complexed with proteins are produced by patients with systemic lupus erythematosus: Proc natn Acad Sci, Vol 76, 1979, pg 5495-5499.
- Yang VW, Lerner MR, Steitz JA & Flint SJ: A small nuclear nbonucleoprotein is required for splicing of adenoviral early RNA sequences, Proc Natn Acad Sci, Vol 78, 1981, pg 1371-1375.
- Schrier WH, Reddy R and Busch H. Identification of an antigenic protein recognized by Anti-Sm autoantibody, Cell Biology International Reports, Vol 6, 1982, pg 925-932.
- Takeda Y Wang GS, Wang RJ, et al. Enzyme-Linked Immunosorbent Assay Using Isolated (U) Small Nuclear Ribonucleoprotein Polypeptides as Antigens to Investigate the Clinical Significance of Autoantibodies to these Polypeptides, Clinical Immunology and Immunopathology, Vol 50, 1989, pg 212-230.
- Habets WJ, de Rooij, DJ, Hoet MH, van de Putte LB, and van Venrooij WJ. Purification of anti-RNP and anti-Sm antibodies in MCTD and SLE patients by immunoblotting. Clin Exp Immunol, Vol 59, 1985, pg 457-466.
- Rader MD, O’Brien C, Liu Y, Harley JB, and Reichlin M. Heterogeneity of the Ro/SSA Antigen. J Clin Invest, Vol 83, 1989, pg 1293-1298.
- Holman HR. Partial purification and characterization of an extractable nuclear antigen which reacts with SLE sera. Ann NY Acad Sci, Vol 124, 1965, pg 800-806.
Product Name: (Ro) SSA Antigen
The (Ro) SS-A antigen is comprised or an acidic 60 kD protein that may also be associated with a RNA ranging in size from 80 to 112 bases (1). The antigenic activity of the (Ro) SS-A antigen appears to be independent of the RNA since the precipitin activity remains after treatment with RNase or separation from the RNA (1). Anti-(Ro) SS-A autoantibodies were described originally as precipitating autoantibodies in sera of Sjogren’s Syndrome and Systemic Lupus Erythematosus patients. The presence of autoantibodies against the (Ro)SS-A antigen may be used as a diagnostic aid. Elevated levels of Anti-(Ro) SS-A have been detected in as high as 96% of Sjogren’s Syndrome patients (2), 49% of patients with Systemic Lupus Erythematosus (2), 83% of mothers of infants with isolated complete congenital heartblock or Neonatal Lupus Dermatitis, and over 75% of patients with Subacute Cutaneous Lupus. Recently, a strong correlation between low positive levels of Anti-(Ro) SS-A and subdinical dry eyes or mouth was found in a substantial portion of an elderly population (3). In addition, it has been shown that 70% of patients with (Ro) SS-A precipitating antibodies also have rheumatoid factor (4). The titer of rheumatoid factor and the concentration of Anti-(Ro) SSA have been closely correlated in Primary Sjogren’s Syndrome (4).
| Code | Amount | Price | |
|---|---|---|---|
| SSA-3000 | 1000 units | $ 600.00 |
- Mamula MJ, Fox OF, Yamagata H, and Harley JB. “The (Ro) SS-A Autoantigen as an Immunogen Some Anti-(Ro) SSA Antibody Binds IgG.” J of Exp Med Vol 86: pg 1889-1901.
- Rader MD, O’Brien C, Liu Y, Harley JB, and Reichlin M. “Heterogeneity of the (Ro) SSA Antigen, Different Molecular Forms in Lymphocytes and Red Blood Cells.” J. Clin. Invest Vol 83: 1989, pg 1293-1298.
- Harley JB, Kaine JL, Fox OF, Reichlin M, Gruber B. “Ro SSA Antibody and Antigen in Cogenital Complete Heart Block ((Ro) SSA and Heart Block).” University of Oklahoma, Health Science Center, Arthritis and Immunology Program, Oklahoma Medical Research Foundation, pg 1-16.
- Harley JB, Alexander EL, Bias WB, Fox OF, et al. “Anti-(Ro) SSA and Anti-(La) SSB in Sjogren’s Syndrome.” Dept of Med, University of Oklahoma, Health Science Center, Arthritis and Immunology Program, Oklahoma Medical Research Foundation, pg 1-35.
Product Name: La/SS-B Antigen
The La/SS-B antigen is a 47 kD ribonucleic protein that is associated with a spectrum of small RNAs (2). La/SS-B appears to be readily susceptible to proteolysis, resulting in many smaller (42kD, 320, and 270) but still immunoreactive polypeptides (3). It has been shown that the La/SS-B antigen primarily resides in the nucleus (2), and it appears to be associated with RNA polymerase III transcripts (4). It has also been shown that the La/SS-B antigen shows strong conservation across species (5). Anti-La/SS-B autoantibodies were described originally as precipitating autoantibodies in sera of Sjogren’s Syndrome patients and referred to as SjT.(1) A precipitin with the same properties was rediscovered later and termed La and then SS-B. Anti-La/SS-B precipitins are most commonly found in Sjogren’s Syndrome and Systemic Lupus Erythematosus (SLE). The presence of autoantibodies against the La/SS-B antigen has been advocated as a diagnostic aid in Sjogren’s Syndrome patients (6). Autoantibodies against La/SS-B are also commonly found in Systemic Lupus Erythematosus and Subacute Cutaneous Lupus (4). In addition, there appears to be a correlation between anti-La/SS-B and the absence of nephritis in SLE patients. Studies have demonstrated that SLE patients with precipitating Anti-Ro/SS-A antibodies have a high incidence of serious nephritis (53%), while those with both Anti-Ro/SS-A and Anti-La/SS-B have a low (9%) frequency of nephritis (7).
| Code | Amount | Price | |
|---|---|---|---|
| SSB-3000 | 1000 units | $600.00 |
- Harley JB, Yamagata H, Reichlin M: Anti-La/SS-B antibody is present in some normal sera and is coincident with anti-Ro/SSA precipitins in systemic lupus erythematosus, J Rheum 11, 1984 pg 309-314.
- Bachman M, Mayet WJ, Shroder HC, et al: Association of La and Ro antigens with intracellular structures in HEp-2 carcinoma Cells. Cell Biology, Vol 83, 1986, pg 7770-7774.
- Habets WJ, den Brok JH, AM Th. Boerbooms, van de Putte LBA, and van Venrooij WJ: Characterization of SS-B (La) antigen in adenovirus-infected and uninfected HeLa cells. EMBO J. 1983, pg 1625.
- Harley JB, Rosario MO, Yamagata H, et al: Immunologic and Structural Studies of the Lupus/Sjogren’s Syndrome Autoantigen, La/SSB, with a Monoclonal Antibody: Vol 76, 1985, pg 801-806.
- Hoch SO, and Billings PB, Agouron Institute: Characterization of the La (SS-B) Antigen From Several Mammalian Sources: J of Immun, Vol 133, 1984, pg 1397-1403.
- Harley JB, Alexander EL, Bias WB, Fox OF, et al: Anti-Ro/SSA and Anti-La/SSB in Sjogren’s syndrome, Dept of Med, Okla Med Research Foundation. pg 1-35.
- Reichlin M: Clinical and Immunological Significance of Antibodies to Ro and La in Systemic Lupus Erythematosus. Arthritis and Rheumatism: Vol 25,1982, pg 767-772.
- Harley JB, Yamagata H, and Reichlin M. Anti-La/SSB Antibody is Present in Some Normal Sera and is Coincident with Anti-Ro/SSA Precipitins in Systemic Lupus Erythematosus: J of Rheumatology, 1984, pg 309-314.