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Collagen Alpha-3(iv) Chain (COL4A3) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS1265507

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… More details

$315 / 0.02 mg (E-Coli) +1 FREE 8GB USB
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Product Overview

Online Datasheet in PDF
Product Name
Collagen alpha-3(IV) chain (COL4A3), Recombinant Protein
Full Product Name
Recombinant Human Collagen alpha-3(IV) chain
Product Synonym Names
Good pasture antigen
Sequence
GLKGKRGDSG SPATWTTRGF VFTRHSQTTA IPSCPEGTVP LYSGFSFLFV QGNQRAHGQD LGTLGSCLQR FTTMPFLFCN VNDVCNFASR NDYSYWLSTP ALMPMNMAPI TGRALEPYIS RCTVCEGPAI AIAVHSQTTD IPPCPHGWIS LWKGFSFIMF TSAGSEGTGQ ALASPGSCLE EFRASPFLEC HGRGTCNYYS NSYSFWLASL NPERMFRKPI PSTVKAGELE KIISRCQVCM KK
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
30.6 kDa
Sequence Positions
1427-1668aa; Partial
Tag Information
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.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
104200
3D Structure
ModBase 3D Structure for Q01955

Product Categories/Family for COL4A3 recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for COL4A3 recombinant protein

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 binding sites 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)

Other Notes

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.

Searchable Terms for COL4A3 purchase

MBS1265507 is a recombinant protein targeting COL4A3. Also known as Recombinant Human Collagen alpha-3(IV) chain. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for COL4A3. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
collagen alpha-3(IV) chain
NCBI Official Synonym Full Names
collagen type IV alpha 3
NCBI Official Symbol
COL4A3
UniProt Protein Name
Collagen alpha-3(IV) chain
UniProt Synonym Protein Names
Goodpasture antigen
Protein Family
UniProt Gene Name
COL4A3
UniProt Entry Name
CO4A3_HUMAN
NCBI Protein Information
collagen alpha-3(IV) chain

NCBI Summary for COL4A3

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]
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UniProt Comments for COL4A3

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
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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