|Other Names||Phospholipase A2, membrane associated, 184.108.40.206, GIIC sPLA2, Group IIA phospholipase A2, Non-pancreatic secretory phospholipase A2, NPS-PLA2, Phosphatidylcholine 2-acylhydrolase 2A, PLA2G2A, PLA2B, PLA2L, RASF-A|
|Target/Specificity||The synthetic peptide sequence is selected from aa 52-62 of HUMAN PLA2G2A|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||PLA2B, PLA2L, RASF-A|
|Function||Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:2925633). Thought to participate in the regulation of phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Independent of its catalytic activity, acts as a ligand for integrins (PubMed:18635536, PubMed:25398877). Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 (PubMed:18635536, PubMed:25398877). Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:25398877). Induces cell proliferation in an integrin-dependent manner (PubMed:18635536).|
|Cellular Location||Cell membrane; Peripheral membrane protein. Secreted|
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Provided below are standard protocols that you may find useful for product applications.
Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides.
Seilhamer J.J.,et al.J. Biol. Chem. 264:5335-5338(1989).
Kramer R.M.,et al.J. Biol. Chem. 264:5768-5775(1989).
Kramer R.M.,et al.Adv. Exp. Med. Biol. 275:35-53(1990).
Liang N.S.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Ebert L.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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