|Other Names||Recoverin, Cancer-associated retinopathy protein, Protein CAR, RCVRN, RCV1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1565c was selected from the Center region of human Recoverin . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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.|
|Function||Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.|
|Tissue Location||Retina and pineal gland.|
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Provided below are standard protocols that you may find useful for product applications.
Recoverin belongs to a high-affinity calcium-binding family that includes neuronal calcium sensor-1, visinin-like proteins (VILIPs), guanylate cyclase-activating proteins (GCAPs), and Kv-channel interacting proteins (KchIPs). Features common to this family include four calcium-binding EF-hand domains, and an N-terminal myristoylation sequence. This family of proteins has been implicated in a broad range of cellular signaling functions, including phototransduction and neurotransmitter release, lipid metabolism, gene expression, and ion channel regulation. Myristoylation, the post-translational addition of a fatty acid tail, has been shown to have functional significance for other calcium-binding protein family members. Recoverin is subject to the posttranslational modification of myristoylation. Binding of calcium to recoverin elicits a change in conformation that exposes the buried hydrophobic myristoyl moiety to interaction with cell membranes and other cellular proteins.
Wiechmann, A., et al., Curr. Eye Res. 26(1):25-32 (2003).Matsubara, S., et al., Br. J. Cancer 74(9):1419-1422 (1996).Yamaji, Y., et al., Int. J. Cancer 65(5):671-676 (1996).McGinnis, J.F., et al., Mamm. Genome 4(1):43-45 (1993).Wiechmann, A.F., et al., Exp. Eye Res. 56(4):463-470 (1993).
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