Caveolin-1 Recombinant Protein | CAV1 recombinant protein

Recombinant Dog Caveolin-1

Cat. Num. AAA949563

• Gene Names: CAV1; caveolin 1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Caveolin-1; Recombinant Dog Caveolin-1; Vesicular integral-membrane protein VIP21; CAV1 recombinant protein

• 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: 1-178aa; Isoform Alpha
• Sequence: MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMAEEMSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPFFEAVGKIFSNIRINMQKET
• Sequence Length: 178

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for CAV1 recombinant protein

Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway.

References

VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles.Kurzchalia T.V., Dupree P., Parton R.G., Kellner R., Virta H., Lehnert M., Simons K.J. Cell Biol. 118:1003-1014(1992) Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells.Sargiacomo M., Sudol M., Tang Z., Lisanti M.P.J. Cell Biol. 122:789-807(1993) Comparative analyses of multi-species sequences from targeted genomic regions.Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G., Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C., Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S., Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J., Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q., Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N., Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S., Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E., Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A., Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E., Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D., Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B., Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A., Haussler D., Green P., Miller W., Green E.D.Nature 424:788-793(2003) Caveolae and sorting in the trans-Golgi network of epithelial cells.Dupree P., Parton R.G., Raposo G., Kurzchalia T.V., Simons K.EMBO J. 12:1597-1605(1993) Oligomeric structure of caveolin implications for caveolae membrane organization.Sargiacomo M., Scherer P.E., Tang Z., Kubler E., Song K.S., Sanders M.C., Lisanti M.P.Proc. Natl. Acad. Sci. U.S.A. 92:9407-9411(1995) Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae.Dietzen D.J., Hastings W.R., Lublin D.M.J. Biol. Chem. 270:6838-6842(1995) Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe.Scherer P.E., Tang Z., Chun M., Sargiacomo M., Lodish H.F., Lisanti M.P.J. Biol. Chem. 270:16395-16401(1995) Caveolin-1 expression inhibits Wnt/beta-catenin/Lef-1 signaling by recruiting beta-catenin to caveolae membrane domains.Galbiati F., Volonte D., Brown A.M., Weinstein D.E., Ben-Ze'ev A., Pestell R.G., Lisanti M.P.J. Biol. Chem. 275:23368-23377(2000)

NCBI and Uniprot Product Information

• NCBI GI #: 50979110
• NCBI GeneID: 403980
• NCBI Accession #: NP_001003296.1
• NCBI GenBank Nucleotide #: NM_001003296.1
• UniProt Accession #: P33724; A0M8U8
• Molecular Weight: 22.6 kDa
• NCBI Official Full Name: caveolin-1
• NCBI Official Symbol: CAV1
• NCBI Official Synonym Symbols: caveolin 1
• NCBI Protein Information: caveolin-1
• UniProt Protein Name: Caveolin-1
• Protein Family: Caveolin
• UniProt Gene Name: CAV1
• UniProt Synonym Gene Names: CAV
• UniProt Entry Name: CAV1_CANLF

Uniprot Description

Caveolin-1: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Involved in the costimulatory signal essential for T-cell receptor (TCR)- mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3- dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. Homooligomer. Interacts with GLIPR2, NOSTRIN, SNAP25 and syntaxin. Interacts with rotavirus A NSP4. Interacts (via the N- terminus) with DPP4; the interaction is direct. Interacts with CTNNB1, CDH1 and JUP. Interacts with BMX and BTK. Expressed in muscle and lung, less so in liver, brain and kidney. Belongs to the caveolin family. 2 isoforms of the human protein are produced by alternative initiation.

Protein type: Motility/polarity/chemotaxis; Adaptor/scaffold; Nuclear receptor co-regulator

Cellular Component: acrosomal membrane; apical plasma membrane; basolateral plasma membrane; caveola; cell cortex; cilium; cytosol; endosome; focal adhesion; Golgi membrane; integral to plasma membrane

Molecular Function: ATPase binding; identical protein binding; nitric-oxide synthase binding; protease activator activity; protein binding; protein binding, bridging; protein complex scaffold; protein heterodimerization activity; protein kinase binding; Rac GTPase binding; receptor binding; structural molecule activity

Biological Process: angiogenesis; calcium ion transport; cellular response to starvation; cholesterol homeostasis; cytosolic calcium ion homeostasis; inactivation of MAPK activity; lactation; mammary gland involution; MAPKKK cascade; membrane depolarization; negative regulation of BMP signaling pathway; negative regulation of cytokine and chemokine mediated signaling pathway; negative regulation of endothelial cell proliferation; negative regulation of epithelial cell differentiation; negative regulation of nitric oxide biosynthetic process; negative regulation of nitric-oxide synthase activity; negative regulation of peptidyl-serine phosphorylation; negative regulation of pinocytosis; negative regulation of protein binding; negative regulation of protein ubiquitination; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transforming growth factor beta receptor signaling pathway; negative regulation of tyrosine phosphorylation of Stat5 protein; nitric oxide homeostasis; positive regulation of metalloenzyme activity; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein binding; positive regulation of protein ubiquitination; positive regulation of toll-like receptor 3 signaling pathway; positive regulation of vasoconstriction; protein homooligomerization; receptor internalization; receptor mediated endocytosis of virus by host; regulation of blood coagulation; regulation of fatty acid metabolic process; regulation of smooth muscle contraction; regulation of the force of heart contraction by chemical signal; response to bacterium; response to calcium ion; response to estrogen stimulus; response to hypoxia; response to progesterone stimulus; sequestering of lipid; skeletal muscle development; T cell costimulation; triacylglycerol metabolic process; vasculogenesis; vasoconstriction; vesicle organization and biogenesis