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Caveolin-1 scaffolding domain peptide

Cell permeable eNOS blocker
 
ALX-153-064-M001 1 mg 175.00 USD
 
ALX-153-064-M005 5 mg 642.00 USD
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Cell permeable peptide that blocks eNOS (NOS III) activity and cellular nitric oxide (NO) release in vitro and reduces inflammation and tumorigenesis in vivo. Caveolin-1 interacts with several lipid-modified signalling ligands, such as EGFR, eNOS, G-protein α-subunits, PKCα, H-Ras, and Src, via the C1-SD82-101 sequence.

Product Specification

Alternative Name:Cavtratin, AP-Cav, Pen-C1-SD
 
Sequence:H-Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys-Asp-Gly-Ile-Trp-Lys-Ala-Ser-Phe-Thr-Thr-Phe-Thr-Val-Thr-Lys-Tyr-Trp-Phe-Tyr-Arg-OH
 
Formula:C228H335N61O49S
 
MW:4746.6
 
Purity:≥97% (HPLC)
 
Appearance:White lyophilized powder.
 
Solubility:Soluble in DMSO or acetonitrile:water (50:50).
 
Shipping:Ambient
 
Long Term Storage:-20°C
 
Use/Stability:Stock solutions are stable for up to 3 months when stored at -20°C.
 
Handling:Protect from light. Hygroscopic.
 

Product Literature References

Caveolin-1 regulates expression of junction-associated proteins in brain microvascular endothelial cells: L. Song, et al.; Blood 109, 1515 (2007), Abstract;
Dissecting the molecular control of endothelial NO synthase by caveolin-1 using cell-permeable peptides: P.N. Bernatchez, et al.; PNAS 102, 761 (2005), Abstract; Full Text
Caveolin-1 gene disruption promotes mammary tumorigenesis and dramatically enhances lung metastasis in vivo. Role of Cav-1 in cell invasiveness and matrix metalloproteinase (MMP-2/9) secretion: T.M. Williams, et al.; J. Biol. Chem. 279, 51630 (2004), Abstract; Full Text
Selective inhibition of tumor microvascular permeability by cavtratin blocks tumor progression in mice: J.P. Gratton, et al.; Cancer Cell 4, 31 (2003), Abstract;
In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation: M. Bucci, et al.; Nat. Med. 6, 1362 (2000), Abstract; Full Text
Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane: T. Okamoto, et al.; J. Biol. Chem. 273, 4519 (1998), Abstract; Full Text

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