|Other Names||Guanylyl cyclase-activating protein 1, GCAP 1, Guanylate cyclase activator 1A, GUCA1A, C6orf131, GCAP, GCAP1, GUCA1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1567b was selected from the C-term region of human GCAP1 . 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.|
|Synonyms||C6orf131, GCAP, GCAP1, GUCA1|
|Function||Stimulates retinal guanylyl cyclase when free calcium ions concentration is low and inhibits guanylyl cyclase when free calcium ions concentration is elevated (PubMed:19459154). This Ca(2+)-sensitive regulation of retinal guanylyl cyclase is a key event in recovery of the dark state of rod photoreceptors following light exposure.|
|Cellular Location||Membrane; Lipid-anchor.|
|Tissue Location||Retina; cone outer and inner segments, in particular, in disk membrane regions, and to a lesser extent rod inner and outer segments|
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Guanylate cyclase-activating protein is a l Ca(2+)-binding protein that upregulates synthesis of cGMP in photoreceptors. The known mammalian GCAPs are more than 90% similar, consisting of 201 to 205 amino acids, and containing 3 identically conserved Ca(2+)-binding sites. The GUCA1A gene, also termed GCAP1, is transcribed into a single 1.7-kb mRNA species detectable only in the retina. In a 4-generation British family with typical clinical features of autosomal dominant cone dystrophy a tyr99-to-cys mutation) in the GUCA1A gene has been identified. Another family with a pro50-to-leu mutation in GUCA1A demonstrated phenotypic variability ranging from mild photophobia to rod-cone dystrophy. The mutant protein could activate guanylate cyclase 1 (GUCY2D) and displayed similar calcium sensitivity to wildtype protein. However, there was a marked increase in the susceptibility to protease degradation and a reduction in the thermal stability of the pro50-to-leu mutation, which may depress cellular concentration and thereby contribute to retinal cell mortality.
Pennesi, M.E., et al., Proc. Natl. Acad. Sci. U.S.A. 100(11):6783-6788 (2003).Payne, A.M., et al., Hum. Mol. Genet. 7(2):273-277 (1998).Subbaraya, I., et al., J. Biol. Chem. 269(49):31080-31089 (1994).
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