|Other Names||Receptor activity-modifying protein 2, Calcitonin-receptor-like receptor activity-modifying protein 2, CRLR activity-modifying protein 2, RAMP2|
|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.|
|Function||Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL.|
|Cellular Location||Membrane; Single-pass type I membrane protein.|
|Tissue Location||Strongly expressed in lung, breast, immune system and fetal tissues.|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene is a member of the RAMP family of single-transmembrane-domain proteins, called receptor (calcitonin) activity modifying proteins (RAMPs). RAMPs are type I transmembrane proteins with an extracellular N terminus and a cytoplasmic C terminus. RAMPs are required to transport calcitonin-receptor-like receptor (CRLR) to the plasma membrane. CRLR, a receptor with seven transmembrane domains, can function as either a calcitonin-gene-related peptide (CGRP) receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. In the presence of this (RAMP2) protein, CRLR functions as an adrenomedullin receptor. The RAMP2 protein is involved in core glycosylation and transportation of adrenomedullin receptor to the cell surface.
Kuwasako, K., et al. Biochem. Biophys. Res. Commun. 392(3):380-385(2010)Michou, L., et al. Clin. Exp. Rheumatol. 26(6):1083-1086(2008)Qi, T., et al. Mol. Pharmacol. 74(4):1059-1071(2008)Luttrell, L.M. Mol. Biotechnol. 39(3):239-264(2008)Kuwasako, K., et al. J. Biol. Chem. 275(38):29602-29609(2000)Aldecoa, A., et al. FEBS Lett. 471 (2-3), 156-160 (2000)
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