Good pasture antigen

For Research Use Only. Not for use in diagnostic procedures.

E Coli or Yeast or Baculovirus or Mammalian Cell

Greater than 90% as determined by SDS-PAGE. (lot specific)

Liquid containing glycerol

This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.

Sterile filter available upon request.

Low endotoxin available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.

Small volumes of COL4A3 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Type IV collagen is the major structural component of glomerular basent membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Tumstatin, a cleavage fragment corresponding to the collagen alpha 3(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity; these two anti-tumor properties may be regulated via RGD-independent ITGB3-mediated mechanisms.

Cell Adhesion

(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)

30.6kD

collagen type IV alpha 3

collagen alpha-3(IV) chain

Collagen alpha-3(IV) chain

CO4A3_HUMAN

Type IV collagen, the major structural component of basement membranes, is a multimeric protein composed of 3 alpha subunits. These subunits are encoded by 6 different genes, alpha 1 through alpha 6, each of which can form a triple helix structure with 2 other subunits to form type IV collagen. This gene encodes alpha 3. In the Goodpasture syndrome, autoantibodies bind to the collagen molecules in the basement membranes of alveoli and glomeruli. The epitopes that elicit these autoantibodies are localized largely to the non-collagenous C-terminal domain of the protein. A specific kinase phosphorylates amino acids in this same C-terminal region and the expression of this kinase is upregulated during pathogenesis. This gene is also linked to an autosomal recessive form of Alport syndrome. The mutations contributing to this syndrome are also located within the exons that encode this C-terminal region. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. [provided by RefSeq, Jun 2010]

COL4A3: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Autoantibodies against the NC1 domain of alpha 3(IV) are found in Goodpasture syndrome, an autoimmune disease of lung and kidney. Defects in COL4A3 are a cause of Alport syndrome autosomal recessive (APSAR). APSAR is characterized by progressive glomerulonephritis, glomerular basement membrane defects, renal failure, sensorineural deafness and specific eye abnormalities (lenticonous and macular flecks). The disorder shows considerable heterogeneity in that families differ in the age of end-stage renal disease and the occurrence of deafness. Defects in COL4A3 are a cause of benign familial hematuria (BFH); also known as thin basement membrane nephropathy. BFH is characterized by persistent hematuria, an electron microscopically detectable thin glomerular basement membrane (GBM) and an autosomal dominant mode of inheritance. Renal function remains normal. In children, differentiation between BFH and AS can be difficult, because both disorders are manifested by persistent hematuria and thin GBM at that age. Defects in COL4A3 are a cause of Alport syndrome autosomal dominant (APSAD). Alport syndrome is characterized by progressive glomerulonephritis, glomerular basement membrane defects, renal failure, sensorineural deafness and specific eye abnormalities (lenticonous and macular flecks). The disorder shows considerable heterogeneity in that families differ in the age of end-stage renal disease and the occurrence of deafness. Belongs to the type IV collagen family. 5 isoforms of the human protein are produced by alternative splicing.

Protein type: Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 2q36-q37

Cellular Component: basement membrane; collagen type IV; endoplasmic reticulum; endoplasmic reticulum lumen; extracellular region; intracellular membrane-bound organelle

Molecular Function: extracellular matrix structural constituent; integrin binding; metalloendopeptidase inhibitor activity; protein binding; structural molecule activity

Biological Process: axon guidance; blood circulation; caspase activation; cell adhesion; cell proliferation; cell surface receptor linked signal transduction; collagen catabolic process; extracellular matrix disassembly; extracellular matrix organization and biogenesis; glomerular basement membrane development; negative regulation of angiogenesis; negative regulation of cell proliferation; sensory perception of sound

Disease: Alport Syndrome, Autosomal Dominant; Alport Syndrome, Autosomal Recessive; Hematuria, Benign Familial

Complete primary structure of the human alpha 3(IV) collagen chain. Coexpression of the alpha 3(IV) and alpha 4(IV) collagen chains in human tissues.Mariyama M., Leinonen A., Mochizuki T., Tryggvason K., Reeders S.T.J. Biol. Chem. 269:23013-23017(1994) Leinonen A.Structure of the human type IV collagen gene COL4A3 and mutations in autosomal Alport syndrome.Heidet L., Arrondel C., Forestier L., Cohen-Solal L., Mollet G., Gutierrez B., Stavrou C., Gubler M.-C., Antignac C.J. Am. Soc. Nephrol. 12:97-106(2001) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Two genes, COL4A3 and COL4A4 coding for the human alpha3(IV) and alpha4(IV) collagen chains are arranged head-to-head on chromosome 2q36.Momota R., Sugimoto M., Oohashi T., Kigasawa K., Yoshioka H., Ninomiya Y.FEBS Lett. 424:11-16(1998) Molecular cloning of the human Goodpasture antigen demonstrates it to be the alpha 3 chain of type IV collagen.Turner N., Mason P.J., Brown R., Fox M., Povey S., Rees A., Pusey C.D.J. Clin. Invest. 89:592-601(1992) Exon/intron structure of the human alpha 3(IV) gene encompassing the Goodpasture antigen (alpha 3(IV) NC1) . Identification of a potentially antigenic region at the triple helix/NC1 domain junction.Quinones S., Bernal D., Garcia-Sogo M., Elena S.F., Saus J.J. Biol. Chem. 267:19780-19784(1992) ErratumQuinones S., Bernal D., Garcia-Sogo M., Elena S.F., Saus J.J. Biol. Chem. 269:17358-17358(1994) Characterization and expression of multiple alternatively spliced transcripts of the Goodpasture antigen gene region. Goodpasture antibodies recognize recombinant proteins representing the autoantigen and one of its alternative forms.Penades J.R., Bernal D., Revert F., Johansson C., Fresquet V.J., Cervera J., Wieslander J., Quinones S., Saus J.Eur. J. Biochem. 229:754-760(1995) Distinct antitumor properties of a type IV collagen domain derived from basement membrane.Maeshima Y., Colorado P.C., Torre A., Holthaus K.A., Grunkemeyer J.A., Ericksen M.B., Hopfer H., Xiao Y., Stillman I.E., Kalluri R.J. Biol. Chem. 275:21340-21348(2000) Alternative splicing of the NC1 domain of the human alpha 3(IV) collagen gene. Differential expression of mRNA transcripts that predict three protein variants with distinct carboxyl regions.Feng L., Xia Y., Wilson C.B.J. Biol. Chem. 269:2342-2348(1994) Sequence and localization of a partial cDNA encoding the human alpha 3 chain of type IV collagen.Morrison K.E., Mariyama M., Yang-Feng T.L., Reeders S.T.Am. J. Hum. Genet. 49:545-554(1991) Ding J. The human mRNA encoding the Goodpasture antigen is alternatively spliced.Bernal D., Quinones S., Saus J.J. Biol. Chem. 268:12090-12094(1993) Complete primary structure of the human type IV collagen alpha 4(IV) chain. Comparison with structure and expression of the other alpha (IV) chains.Leinonen A., Mariyama M., Mochizuki T., Tryggvason K., Reeders S.T.J. Biol. Chem. 269:26172-26177(1994) Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen.Raya A., Revert F., Navarro S., Saus J.J. Biol. Chem. 274:12642-12649(1999) Two RGD-independent alpha vbeta 3 integrin s on tumstatin regulate distinct anti-tumor properties.Maeshima Y., Colorado P.C., Kalluri R.J. Biol. Chem. 275:23745-23750(2000) Autosomal dominant Alport syndrome caused by a COL4A3 splice site mutation.van der Loop F.T.L., Heidet L., Timmer E.D.J., van den Bosch B.J.C., Leinonen A., Antignac C., Jefferson J.A., Maxwell A.P., Monnens L.A.H., Schroder C.H., Smeets H.J.M.Kidney Int. 58:1870-1875(2000) Quaternary organization of the goodpasture autoantigen, the alpha 3(IV) collagen chain. Sequestration of two cryptic autoepitopes by intrapromoter interactions with the alpha4 and alpha5 NC1 domains.Borza D.B., Bondar O., Todd P., Sundaramoorthy M., Sado Y., Ninomiya Y., Hudson B.G.J. Biol. Chem. 277:40075-40083(2002) Human tumstatin and human endostatin exhibit distinct antiangiogenic activities mediated by alpha v beta 3 and alpha 5 beta 1 integrins.Sudhakar A., Sugimoto H., Yang C., Lively J., Zeisberg M., Kalluri R.Proc. Natl. Acad. Sci. U.S.A. 100:4766-4771(2003) Implication of tumstatin in tumor progression of human bronchopulmonary carcinomas.Caudroy S., Cucherousset J., Lorenzato M., Zahm J.-M., Martinella-Catusse C., Polette M., Birembaut P.Hum. Pathol. 35:1218-1222(2004) Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.Proteomics 7:868-874(2007) Mutations in the type IV collagen alpha 3 (COL4A3) gene in autosomal recessive Alport syndrome.Lemmink H.H., Mochizuki T., van den Heuvel L.P.W.J., Schroeder C.H., Barrientos A., Monnens L.A.H., van Oost B.A., Brunner H.G., Reeders S.T., Smeets H.J.M.Hum. Mol. Genet. 3:1269-1273(1994) Mutations in the COL4A4 and COL4A3 genes cause familial benign hematuria.Badenas C., Praga M., Tazon B., Heidet L., Arrondel C., Armengol A., Andres A., Morales E., Camacho J.A., Lens X., Davila S., Mila M., Antignac C., Darnell A., Torra R.J. Am. Soc. Nephrol. 13:1248-1254(2002) Novel COL4A5, COL4A4, and COL4A3 mutations in Alport syndrome.Nagel M., Nagorka S., Gross O.Hum. Mutat. 26:60-60(2005)

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