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Collagen Alpha-1(iv) Chain (COL4A1) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS954904

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. Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and… More details

$395 / 0.02 mg (Mammalian-Cell) +1 FREE 8GB USB
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Product Overview

Online Datasheet in PDF
Product Name
Collagen alpha-1(IV) chain (COL4A1), Recombinant Protein
Full Product Name
Recombinant Human Collagen alpha-1(IV) chain (COL4A1), partial
Sequence
GFLVTRHSQT IDDPQCPSGT KILYHGYSLL YVQGNERAHG QDLGTAGSCL RKFSTMPFLF CNINNVCNFA SRNDYSYWLS TPEPMPMSMA PITGENIRPF ISRCAVCEAP AMVMAVHSQT IQIPPCPSGW SSLWIGYSFV MHTSAGAEGS GQALASPGSC LEEFRSAPFI ECHGRGTCNY YANAYSFWLA TIERSEMFKK PTPSTLKAGE LRTHVSRCQV CMRRT
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
40.9 kDa
Sequence Positions
1445-1669. Partial-length
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
120130
3D Structure
ModBase 3D Structure for P02462

Product Categories/Family for COL4A1 recombinant protein

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

Product References and Citations for COL4A1 recombinant protein

Structural organization of the gene for the alpha 1 chain of human type IV collagen.Soininen R., Huotari M., Ganguly A., Prockop D.J., Tryggvason K.J. Biol. Chem. 264:13565-13571(1989) The DNA sequence and analysis of human chromosome 13.Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.Nature 428:522-528(2004) Completion of the amino acid sequence of the alpha 1 chain of human basement membrane collagen (type IV) reveals 21 non-triplet interruptions located within the collagenous domain.Brazel D., Oberbaeumer I., Dieringer H., Babel W., Glanville R.W., Deutzmann R., Kuehn K.Eur. J. Biochem. 168:529-536(1987) The structural genes for alpha 1 and alpha 2 chains of human type IV collagen are divergently encoded on opposite DNA strands and have an overlapping promoter region.Soininen R., Huotari M., Hostikka S.L., Prockop D.J., Tryggvason K.J. Biol. Chem. 263:17217-17220(1988) Amino acid sequence of the N-terminal aggregation and cross-linking region (7S domain) of the alpha 1 (IV) chain of human basement membrane collagen.Glanville R.W., Qian R.Q., Siebold B., Risteli J., Kuehn K.Eur. J. Biochem. 152:213-219(1985) Complete primary structure of the alpha 1-chain of human basement membrane (type IV) collagen.Soininen R., Haka-Risku T., Prockop D.J., Tryggvason K.FEBS Lett. 225:188-194(1987) Structure of human-basement-membrane (type IV) collagen. Complete amino-acid sequence of a 914-residue-long pepsin fragment from the alpha 1(IV) chain.Babel W., Glanville R.W.Eur. J. Biochem. 143:545-556(1984) cDNA clones coding for the pro-alpha1(IV) chain of human type IV procollagen reveal an unusual homology of amino acid sequences in two halves of the carboxyl-terminal domain.Pihlajaniemi T., Tryggvason K., Myers J.C., Kurkinen M., Lebo R., Cheung M.-C., Prockop D.J., Boyd C.D.J. Biol. Chem. 260:7681-7687(1985) Restricted homology between human alpha 1 type IV and other procollagen chains.Brinker J.M., Gudas L.J., Loidl H.R., Wang S.-Y., Rosenbloom J., Kefalides N.A., Myers J.C.Proc. Natl. Acad. Sci. U.S.A. 82:3649-3653(1985) The arrangement of intra- and intermolecular disulfide bonds in the carboxyterminal, non-collagenous aggregation and cross-linking domain of basement-membrane type IV collagen.Siebold B., Deutzmann R., Kuehn K.Eur. J. Biochem. 176:617-624(1988) Anti-angiogenic cues from vascular basement membrane collagen.Colorado P.C., Torre A., Kamphaus G., Maeshima Y., Hopfer H., Takahashi K., Volk R., Zamborsky E.D., Herman S., Sarkar P.K., Ericksen M.B., Dhanabal M., Simons M., Post M., Kufe D.W., Weichselbaum R.R., Sukhatme V.P., Kalluri R.Cancer Res. 60:2520-2526(2000) Arresten, a collagen-derived inhibitor of angiogenesis.Fu J., Bai X., Wang W., Ruan C.Peng X., Yin B., Yuan J., Qiang B.Molecular cloning and sequencing of human arresten gene.Zheng Q.C., Song Z.F., Zheng Y.W., Li Y.Q., Shu X.Zhonghua Shi Yan Wai Ke Za Zhi 19:46-47(2002) Cloning and expression of arresten in Escherichia coli and Pachia pastoris.He A.B.Construction of recombinant plasmid and prokaryotic expression in E. coli and biological activity analysis of human placenta arresten gene.Zheng J.P., Tang H.Y., Chen X.J., Yu B.F., Xie J., Wu T.C.Hepatobiliary Pancreat. Dis. Int. 5:74-79(2006) Human alpha1 type IV collagen NC1 domain exhibits distinct antiangiogenic activity mediated by alpha1beta1 integrin.Sudhakar A., Nyberg P., Keshamouni V.G., Mannam A.P., Li J., Sugimoto H., Cosgrove D., Kalluri R.J. Clin. Invest. 115:2801-2810(2005) Characterization of the anti-angiogenic properties of arresten, an alpha1beta1 integrin-dependent collagen-derived tumor suppressor.Nyberg P., Xie L., Sugimoto H., Colorado P., Sund M., Holthaus K., Sudhakar A., Salo T., Kalluri R.Exp. Cell Res. 314:3292-3305(2008) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link.Than M.E., Henrich S., Huber R., Ries A., Mann K., Kuhn K., Timpl R., Bourenkov G.P., Bartunik H.D., Bode W.Proc. Natl. Acad. Sci. U.S.A. 99:6607-6612(2002) Mutations in Col4a1 cause perinatal cerebral hemorrhage and porencephaly.Gould D.B., Phalan F.C., Breedveld G.J., van Mil S.E., Smith R.S., Schimenti J.C., Aguglia U., van der Knaap M.S., Heutink P., John S.W.M.Science 308:1167-1171(2005) Novel mutations in three families confirm a major role of COL4A1 in hereditary porencephaly.Breedveld G., de Coo I.F., Lequin M.H., Arts W.F.M., Heutink P., Gould D.B., John S.W.M., Oostra B., Mancini G.M.S.J. Med. Genet. 43:490-495(2006) Role of COL4A1 in small-vessel disease and hemorrhagic stroke.Gould D.B., Phalan F.C., van Mil S.E., Sundberg J.P., Vahedi K., Massin P., Bousser M.G., Heutink P., Miner J.H., Tournier-Lasserve E., John S.W.M.N. Engl. J. Med. 354:1489-1496(2006) COL4A1 mutation in Axenfeld-Rieger anomaly with leukoencephalopathy and stroke.Sibon I., Coupry I., Menegon P., Bouchet J.P., Gorry P., Burgelin I., Calvas P., Orignac I., Dousset V., Lacombe D., Orgogozo J.M., Arveiler B., Goizet C.Ann. Neurol. 62:177-184(2007) COL4A1 mutations and hereditary angiopathy, nephropathy, aneurysms, and muscle cramps.Plaisier E., Gribouval O., Alamowitch S., Mougenot B., Prost C., Verpont M.C., Marro B., Desmettre T., Cohen S.Y., Roullet E., Dracon M., Fardeau M., Van Agtmael T., Kerjaschki D., Antignac C., Ronco P.N. Engl. J. Med. 357:2687-2695(2007) A sulfilimine bond identified in collagen IV.Vanacore R., Ham A.-J.L., Voehler M., Sanders C.R., Conrads T.P., Veenstra T.D., Sharpless K.B., Dawson P.E., Hudson B.G.Science 325:1230-1234(2009) COL4A1 mutation in a patient with sporadic, recurrent intracerebral hemorrhage.Vahedi K., Kubis N., Boukobza M., Arnoult M., Massin P., Tournier-Lasserve E., Bousser M.G.Stroke 38:1461-1464(2007) COL4A1 mutation in two preterm siblings with antenatal onset of parenchymal hemorrhage.de Vries L.S., Koopman C., Groenendaal F., Van Schooneveld M., Verheijen F.W., Verbeek E., Witkamp T.D., van der Worp H.B., Mancini G.Ann. Neurol. 65:12-18(2009) Novel COL4A1 mutations associated with HANAC syndrome a role for the triple helical CB3 domain.Plaisier E., Chen Z., Gekeler F., Benhassine S., Dahan K., Marro B., Alamowitch S., Paques M., Ronco P.Am. J. Med. Genet. A 152:2550-2555(2010) Ophthalmological features associated with COL4A1 mutations.Coupry I., Sibon I., Mortemousque B., Rouanet F., Mine M., Goizet C.Arch. Ophthalmol. 128:483-489(2010) A dominantly inherited mutation in collagen IV A1 (COL4A1) causing childhood onset stroke without porencephaly.Shah S., Kumar Y., McLean B., Churchill A., Stoodley N., Rankin J., Rizzu P., van der Knaap M., Jardine P.Eur. J. Paediatr. Neurol. 14:182-187(2010) Sequence variants in COL4A1 and COL4A2 genes in Ecuadorian families with keratoconus.Karolak J.A., Kulinska K., Nowak D.M., Pitarque J.A., Molinari A., Rydzanicz M., Bejjani B.A., Gajecka M.Mol. Vis. 17:827-843(2011) +Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of COL4A1 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 COL4A1 purchase

MBS954904 is a recombinant protein targeting COL4A1. Also known as Recombinant Human Collagen alpha-1(IV) chain (COL4A1), partial. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for COL4A1. 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-1(IV) chain isoform 2
NCBI Official Synonym Full Names
collagen type IV alpha 1
NCBI Official Symbol
COL4A1
NCBI Official Synonym Symbols
BSVD; RATOR
UniProt Protein Name
Collagen alpha-1(IV) chain
Protein Family
UniProt Gene Name
COL4A1
UniProt Entry Name
CO4A1_HUMAN
NCBI Protein Information
collagen alpha-1(IV) chain

NCBI Summary for COL4A1

This gene encodes a type IV collagen alpha protein. Type IV collagen proteins are integral components of basement membranes. This gene shares a bidirectional promoter with a paralogous gene on the opposite strand. The protein consists of an amino-terminal 7S domain, a triple-helix forming collagenous domain, and a carboxy-terminal non-collagenous domain. It functions as part of a heterotrimer and interacts with other extracellular matrix components such as perlecans, proteoglycans, and laminins. In addition, proteolytic cleavage of the non-collagenous carboxy-terminal domain results in a biologically active fragment known as arresten, which has anti-angiogenic and tumor suppressor properties. Mutations in this gene cause porencephaly, cerebrovascular disease, and renal and muscular defects. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2014]
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UniProt Comments for COL4A1

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.

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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