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SIKVAV (acetate) Sale

(Synonyms: Hexapeptide-10, Ser-Ile-Lys-Val-Ala-Val) 目录号 : GC49713

A laminin α1-derived peptide

SIKVAV (acetate) Chemical Structure

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100 mg
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500 mg
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1 g
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产品描述

SIKVAV is a laminin α1-derived peptide.1 It binds to α3, α6, and β1 integrins and induces adhesion of CAC2 adenoid cystic carcinoma cells when used at a concentration of 1 µg/ml. SIKVAV (100 µg/ml) stimulates the proliferation and migration of primary mouse fibroblasts, as well as induces the secretion of EGF, VEGF, TGF-β, and FGF in the same cells.2 Topical administration of a chitosan hydrogel containing SIKVAV promotes wound healing and angiogenesis in mice.

1.Freitas, V.M., Vilas-Boas, V.F., Pimenta, D.C., et al.SIKVAV, a laminin α1-derived peptide, interacts with integrins and increases protease activity of a human salivary gland adenoid cystic carcinoma cell line through the ERK 1/2 signaling pathwayAm. J. Pathol.171(1)124-138(2007) 2.Chen, X., Zhang, M., Chen, S., et al.Peptide-modified chitosan hydrogels accelerate skin wound healing by promoting fibroblast proliferation, migration, and secretionCell Transplant.26(8)1331-1340(2017)

Chemical Properties

Cas No. N/A SDF Download SDF
别名 Hexapeptide-10, Ser-Ile-Lys-Val-Ala-Val
Canonical SMILES OC[C@H](N)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](CCCCN)C(N[C@@H](C(C)C)C(N[C@@H](C)C(N[C@H](C(O)=O)C(C)C)=O)=O)=O)=O)=O.CC(O)=O
分子式 C28H53N7O8 • XC2H4O2 分子量 615.8
溶解度 DMF: insol,DMSO: insol,Ethanol: insol,PBS (pH 7.2): 2 mg/ml 储存条件 -20°C
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1 mg 5 mg 10 mg
1 mM 1.6239 mL 8.1195 mL 16.239 mL
5 mM 0.3248 mL 1.6239 mL 3.2478 mL
10 mM 0.1624 mL 0.812 mL 1.6239 mL
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Research Update

Enhancement of cell attachment and tissue integration by a IKVAV containing multi-domain peptide

Biochim Biophys Acta 2006 Sep;1760(9):1403-10.PMID:16860485DOI:10.1016/j.bbagen.2006.05.010.

Laminin contains a number of cell binding motifs including IKVAV and some that bind heparin. We developed a multi-domain synthetic peptide, LA2, which combines IKVAV sequences with a heparin-binding domain with the goal of improving cell attachment to otherwise non-adherent substrates. LA2 was used to coat polystyrene, ethyl vinyl acetate (EVA), expanded polytetrafluoroethylene (ePTFE), polycarbonate, titanium and stainless steel. In cell attachment studies, LA2 dramatically increased cell attachment to polystyrene and EVA compared to uncoated counterparts or those coated with SIKVAV. Similar increases were observed on ePTFE and titanium. On polystyrene, LA2 enhanced the attachment of endothelial cells, smooth muscle cells, epithelial cells, myoblasts, and osteoblast progenitor cells. Following adhesion, the cells underwent proliferation to form confluent monolayers with phenotypic morphologies. Using osteoblast progenitor cells (MC3T3 cells) grown on LA2/polystyrene, the cells exhibited an increased production of a differentiation marker, alkaline phosphatase. In vivo, LA2 improved tissue integration into ePTFE when implanted subcutaneously in rats. After 2 weeks, cells had penetrated deep into the LA2 coated ePTFE implant whereas little cell penetration was found in uncoated grafts. The implant sites exhibited little inflammation or other untoward effects. The results indicated that the LA2 peptide improved cell adhesion and tissue integration and might be useful in a number of tissue engineering applications.

Rat hepatocytes attach to laminin present in liver biomatrix proteins by an Mg(++)-dependent mechanism

Hepatology 1995 Aug;22(2):620-8.PMID:7635432DOI:10.1016/0270-9139(95)90588-x.

Laminin belongs to a family of proteins that contains at least seven variants. Together with fibronectin, it is the most important cell-adhesion protein. Recent data from various laboratories have suggested that liver sinusoidal laminins differ from Engelbert-Holmes-Swarm tumor laminin (laminin 1), because the former contain alpha 2 instead of alpha 1 chains. Therefore, we compared the adhesion of hepatocytes to laminin 1 and a matrix extracted with dilute acetic acid from liver biomatrix (LBP). We show that LBP contains laminin and that this extracellular matrix protein is the main adhesion protein. Close to 70% of the hepatocytes attach to LBP after 15 minutes of incubation at 37 degrees C. Cell adhesion was Mg++ and Mn(++)-dependent and Ca(++)- and insulin-independent. Ethylenediaminetetraacetic acid prevented cell adhesion in the presence of divalent cations. We show that synthetic cell-adhesion peptide sequences present in laminin 1 (RGD and YIGSR) or an antibody to the cell-binding domain (SIKVAV) of the alpha 1 chain do not prevent hepatocyte adhesion to LBP. We also show that the LBP has cell specificity; hepatocytes adhere to it preferentially when compared with other epithelial and mesenchymal cell lines. We suggest that because of the differences in chain composition of laminin 1 and liver sinusoidal laminins as well as the described differences in cell adhesion to the two substrata, further studies are needed to determine the actual composition of liver laminin and establish the chains and domains to which hepatocytes adhere.