Cerebral cavernous malformation 2 (CCM2) is an adaptor protein consisting of two domains. Structurally, it has two domains, N-terminal phospho­tyrosine-binding (PTB) domain and an independent domain named as Karet domain at the C-terminal end. It is mapped on human chromosome 7p. Its phosphotyrosine-binding (PTB) domain has the ability to bind proteins. It is expressed in vascular endothelium and neuroglial precursor cells during development and also observed in arterial endothelium, neurons, and some of the glial cells in adult neocortex.

CCM2 (NP_113631.1, 1 a.a. ~ 444 a.a) full-length human protein.

Sequence
MEEEGKKGKKPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVILAAESKVAAEELCCLLGQVFQVVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA

Cerebral cavernous malformation 2 (CCM2) is associated with several cellular pathways. It mainly behaves as a scaffold protein in the activation of GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) during hyperosmotic stress. It also participates in vascular integrity. CCM2 may play a role in vasculogenesis and angiogenesis during the development of the brain. Mutation in the gene is associated with familial cerebral cavernous malformations.

Solution in phosphate buffered saline, pH 7.4

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