Human CCM-2, His-Tag recombinant Protein
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CCM-2, malcavernin, cerebral cavernous malformation 2, OSM, C7orf22, PP10187
Description of Human CCM-2, His-Tag
Cerebral cavernous malformations (CCMs) are sporadically acquired or inherited vascular lesions of the central nervous system consisting of clusters of dilated thin-walled blood vessels that predispose individuals to seizures and stroke. Familial CCM is caused by mutations in KRIT1 (CCM1) or in malcavernin (CCM2). The roles of the CCM proteins in the pathogenesis of the disorder remain largely unknown. It was shown that the CCM1 gene product, KRIT1, interacts with the CCM2 gene product, malcavernin. Analogous to the established interactions of CCM1 and beta1 integrin with ICAP1, the CCM1/CCM2 association is dependent upon the phosphotyrosine binding (PTB) domain of CCM2. A familial CCM2 missense mutation abrogates the CCM1/CCM2 interaction, suggesting that loss of this interaction may be critical in CCM pathogenesis. CCM2 and ICAP1 bound to CCM1 via their respective PTB domains differentially influence the subcellular localization of CCM1. The data indicate that the genetic heterogeneity observed in familial CCM may reflect mutation of different molecular members of a coordinated signaling complex. The CCM-2 is fused to a N-terminal His-tag (6x His).
Testing in Progress.
The lyophilized CCM-2 is soluble in water and most aqueous buffers and should be reconstituted in water or PBS.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEEEGKKGKK PGIVSPFKRV FLKGEKSRDK KAHEKVTERR PLHTVVLSLP ERVEPDRLLS DYIEKEVKYL GQLTSIPGYL NPSSRTEILH FIDNAKRAHQ LPGHLTQEHD AVLSLSAYNV KLAWRDGEDI ILRVPIHDIA AVSYVRDDAA HLVVLKTAQD PGISPSQSLC AESSRGLSAG SLSESAVGPV EACCLVILAA ESKVAAEELC CLLGQVFQVV YTESTIDFLD RAIFDGASTP THHLSLHSDD SSTKVDIKET YEVEASTFCF PESVDVGGAS PHSKTISESE LSASATELLQ DYMLTLRTKL SSQEIQQFAA LLHEYRNGAS IHEFCINLRQ LYGDSRKFLL LGLRPFIPEK DSQHFENFLE TIGVKDGRGI ITDSFGRHRR ALSTTSSSTT NGNRATGSSD DRSAPSEGDE WDRMISDISS DIEALGCSMD QDSA
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