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SDS-PAGE

Collagen alpha-1(IV) chain Recombinant Protein | COL4A1 recombinant protein

Recombinant Human Collagen alpha-1(IV) chain protein

Gene Names
COL4A1; BSVD; RATOR
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
Collagen alpha-1(IV) chain; Recombinant Human Collagen alpha-1(IV) chain protein; COL4A1 recombinant protein
Ordering
For Research Use Only!
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE.
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Sequence Positions
30-167aa; Partial
Sequence
GCAGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPQGPPGQKGDTGEPGLPGTKGTRGPPGASGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFAGNPGPPGLPGMKGDPGEILGHVP
Sequence Length
519
Preparation and Storage
Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

SDS-PAGE

SDS-PAGE
Related Product Information for COL4A1 recombinant protein
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 tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.
Product Categories/Family for COL4A1 recombinant protein
References
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.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
39.9 kDa
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
NCBI Protein Information
collagen alpha-1(IV) chain
UniProt Protein Name
Collagen alpha-1(IV) chain
Protein Family
UniProt Gene Name
COL4A1
UniProt Entry Name
CO4A1_HUMAN

NCBI Description

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]

Uniprot Description

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.

Research Articles on COL4A1

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Product Notes

The COL4A1 col4a1 (Catalog #AAA962953) is a Recombinant Protein produced from E Coli or Yeast or Baculovirus or Mammalian Cell and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 30-167aa; Partial. The amino acid sequence is listed below: GCAGSGCGKC DCHGVKGQKG ERGLPGLQGV IGFPGMQGPE GPQGPPGQKG DTGEPGLPGT KGTRGPPGAS GYPGNPGLPG IPGQDGPPGP PGIPGCNGTK GERGPLGPPG LPGFAGNPGP PGLPGMKGDP GEILGHVP. It is sometimes possible for the material contained within the vial of "Collagen alpha-1(IV) chain, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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