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CCM2 encodes a scaffold protein that functions in the stress-activated p38 Mitogen-activated protein kinase (MAPK) signaling cascade. Additionally we are shipping CCM2 Proteins (8) and CCM2 Kits (2) and many more products for this protein.
Showing 10 out of 58 products:
Human Polyclonal CCM2 Primary Antibody for ELISA, WB - ABIN185733
Zawistowski, Stalheim, Uhlik, Abell, Ancrile, Johnson, Marchuk: CCM1 and CCM2 protein interactions in cell signaling: implications for cerebral cavernous malformations pathogenesis. in Human molecular genetics 2005
Studies suggest that the 3 proteins of the Cerebral Cavernous Malformations (CCM) complex KRIT1/CCM1 (show KRIT1 Antibodies), CCM2/malcavernin and CCM3/PDCD10 (show PDCD10 Antibodies) not only require one another for reciprocal stabilization, but also act as a platform for signal transduction.
a new mutation in MGC4607/CCM2 was identified in several family members with spinal and cutaneous angiomas.
both CCM2 and CCM3 (show PDCD10 Antibodies) are required for normal endothelial cell network formation.
Data find that several disease-associated missense mutations in CCM2 have the potential to interrupt the KRIT1 (show KRIT1 Antibodies)-CCM2 interaction by destabilizing the CCM2 PTB (show PTBP1 Antibodies) domain and that a KRIT1 (show KRIT1 Antibodies) mutation also disrupts this interaction
Prevalence, frequency and characterization of CCM1 (show KRIT1 Antibodies), CCM2 and CCM3 (show PDCD10 Antibodies) variants in cerebral cavernous malformation Spanish patients.
Cerebral cavernous malformation(CCM)s develop because of loss of heart of glass (HEG (show HEG1 Antibodies))-independent CCM2 signaling in murine transgenic endothelium of central nervous system after birth.
DNA sequencing and deletion/duplication testing of the CCM1 (show KRIT1 Antibodies), CCM2, and CCM3 (show PDCD10 Antibodies) genes in the proband revealed a CCM1 (show KRIT1 Antibodies) c.601CNG mutation.
CCM2 mutations are associated with cerebral cavernous malformation in some Japanese patients.
A previously undescribed deletion mutation in CCM2 gene exon 5 is described in an Italian family with multiple cerebral cavernous malformations and epilepsy.
structural characterization of CCM2
CCM2 expression and it's role during ovary and testis development
CCM2:MEKK3 (show MAP3K3 Antibodies)-mediated regulation of Rho-ROCK signalling is required for maintenance of neurovascular integrity, a mechanism by which CCM2 loss leads to disease.
Down-modulation of STK25 (show STK25 Antibodies), but not STK24 (show STK24 Antibodies), rescued medulloblastoma cells from NGF (show NGFB Antibodies)-induced TrkA (show NTRK1 Antibodies)-dependent cell death, suggesting that STK25 (show STK25 Antibodies) is part of the death-signaling pathway initiated by TrkA (show NTRK1 Antibodies) and CCM2.
The inducible deletion of Ccm2 in adult mice recapitulates the cerebral cavernous malformations-like brain lesions in humans.
Developmental timing of CCM2 loss influences cerebral cavernous malformations in mice.
Rac1/osmosensing scaffold for MEKK3 contributes via phospholipase C (show PLC Antibodies)-gamma1 to activation of the osmoprotective transcription factor NFAT5 (show NFAT5 Antibodies).
Pdcd10 (show PDCD10 Antibodies) has a different role in cerebral cavernous malformation than Ccm2 and Krit1 (show KRIT1 Antibodies)
The KRIT1 (show KRIT1 Antibodies)-CCM2 interaction regulates endothelial junctional stability and vascular barrier function by suppressing activation of the RhoA (show RHOA Antibodies)/ROCK signaling pathway.
CCM1 (show KRIT1 Antibodies) associates with CCM2, indicating that the genetic heterogeneity observed in familial cavernous malformation pathogenesis may reflect mutation of different molecular members of a coordinated signaling complex.
CCM1 (show KRIT1 Antibodies) and CCM2 have similar expression patterns during development and are involved in the same pathway important for central nervous system vascular development
This gene encodes a scaffold protein that functions in the stress-activated p38 Mitogen-activated protein kinase (MAPK) signaling cascade. The protein interacts with SMAD specific E3 ubiquitin protein ligase 1 (also known as SMURF1) via a phosphotyrosine binding domain to promote RhoA degradation. The protein is required for normal cytoskeletal structure, cell-cell interactions, and lumen formation in endothelial cells. Mutations in this gene result in cerebral cavernous malformations. Multiple transcript variants encoding different isoforms have been found for this gene.
, cerebral cavernous malformation 2
, cerebral cavernous malformations 2 protein
, cerebral cavernous malformation 2 homolog
, cerebral cavernous malformations protein 2 homolog
, osmosensing scaffold for MEKK3