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Caveolin 1, Caveolae Protein, 22kDa (CAV1) Peptide

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Protein Name
(10), (7), (7), (5), (5), (4), (4), (2)
Control Peptide (CP)
Pubmed 5 references available
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Quantity 0.1 mg
Shipping to United States ( )
Specificity CAV1 Antibody Blocking Peptide
Purity 100 %
Background The scaffolding protein CAV1 is the main component of the caveolae plasma membranes found in most cell types. This protein links integrin subunits to the tyrosine kinase FYN, an initiating step in coupling integrins to the Ras-ERK pathway and promoting cell cycle progression. The CAV1 gene is a tumor suppressor gene candidate and a negative regulator of the Ras-p42/44 MAP kinase cascade.Synonyms: CAV1
Molecular Weight 2008.68 Da
Gene ID 857
NCBI Accession NP_001744
UniProt Q03135
Research Area Signaling
Application Notes Optimal working dilution should be determined by the investigator.
Restrictions For Research Use only
Reconstitution Restore with 0.1 mL DI water
Concentration 1.0 mg/mL
Buffer Lyophilized with 100 % acetonitrile
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Prior to reconstitution store at 2-8 °C. Following reconstitution store undiluted at 2-8 °C for one month or (in aliquots) at-20 °C for longer.
Background publications Zhong, Smart, Weksler et al.: "Caveolin-1 regulates human immunodeficiency virus-1 Tat-induced alterations of tight junction protein expression via modulation of the Ras signaling." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 28, Issue 31, pp. 7788-96, 2008 (PubMed).

Smith, Campos, Wandinger-Ness et al.: "Caveolin-1-dependent infectious entry of human papillomavirus type 31 in human keratinocytes proceeds to the endosomal pathway for pH-dependent uncoating." in: Journal of virology, Vol. 82, Issue 19, pp. 9505-12, 2008 (PubMed).

Di Vizio, Adam, Kim et al.: "Caveolin-1 interacts with a lipid raft-associated population of fatty acid synthase." in: Cell cycle (Georgetown, Tex.), Vol. 7, Issue 14, pp. 2257-67, 2008 (PubMed).

Lee, Woodman, Engelman et al.: "Palmitoylation of caveolin-1 at a single site (Cys-156) controls its coupling to the c-Src tyrosine kinase: targeting of dually acylated molecules (GPI-linked, transmembrane, or cytoplasmic) to caveolae effectively uncouples c-Src and caveolin-1 (TYR-14)." in: The Journal of biological chemistry, Vol. 276, Issue 37, pp. 35150-8, 2001 (PubMed).

Schlegel, Arvan, Lisanti: "Caveolin-1 binding to endoplasmic reticulum membranes and entry into the regulated secretory pathway are regulated by serine phosphorylation. Protein sorting at the level of the endoplasmic reticulum." in: The Journal of biological chemistry, Vol. 276, Issue 6, pp. 4398-408, 2001 (PubMed).

Catalog No. ABIN496191

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