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anti-Human CBLC Antibodies:
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Human Polyclonal CBLC Primary Antibody for IHC (p), ELISA - ABIN542717
Keane, Ettenberg, Nau, Banerjee, Cuello, Penninger, Lipkowitz: cbl-3: a new mammalian cbl family protein. in Oncogene 1999
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Human Polyclonal CBLC Primary Antibody for IHC (p), ELISA - ABIN542718
Kim, Tezuka, Suziki, Sugano, Hirai, Yamamoto: Molecular cloning and characterization of a novel cbl-family gene, cbl-c. in Gene 1999
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Methylmalonic aciduria with homocystinuria cblC is a multisystemic metabolic disease affecting cobalamin metabolism. The presence of retinal alterations in cblC is a common feature and it is reported to develop more frequently and into a more severe form in the early-onset phenotype, suggesting to some extent a correlation with the biochemical phenotype
Data suggest that ubiquitin ligase CBLC controls mostly network organization of the Golgi Apparatus.
Silencing of CBLC causes increased sensitivity to PARP1 inhibitor olaparib in breast cancer cell line models and that defective homologous recombination (HR) DNA repair is the likely cause.
the effects of two pathogenic missense mutations on the the catalytic activities of the human B12-processing chaperone CblC
This retrospective multicentre study evaluates clinical, biochemical and genetic findings in 88 cblC patients
The ubiquitin ligase activity of Cbl-c by the direct interaction of the LIM zinc coordinating domain of Hic5 is demonstrated.
the N terminus of Cbl-c contributes to the binding to the E2 and phosphorylation of Tyr-341 leads to a decrease in affinity and an increase in the E3 activity of Cbl-c
Data demonstrate that two E3 ligases of different classes, CBLC and AIP4, can interact and cooperate to down-regulate EGFR signaling.
c-Cbl is a negative regulator of hepatocyte growth factor/receptor tyrosine kinase Met signaling in B cells, mediating ubiquitination and, consequently, proteosomal degradation of Met, with a role in Met-mediated tumorigenesis.
Src is a preferential target of Cbl-c for degradation
ubiquitin protein ligase activity is regulated in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations
bCblC, a bovine B12 trafficking chaperone, catalyzes elimination of the glutathione ligand from GSCbl by using the reduced form of glutathione (GSH).
This gene encodes a member of the Cbl family of E3 ubiquitin ligases. Cbl proteins play important roles in cell signaling through the ubiquitination and subsequent downregulation of tyrosine kinases. Expression of this gene may be restricted to epithelial cells, and alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
Cas-Br-M (murine) ecotropic retroviral transforming sequence c
, Cas-Br-M (murine) ectropic retroviral transforming sequence c
, Cbl proto-oncogene, E3 ubiquitin protein ligase C
, RING finger protein 57
, SH3-binding protein CBL-3
, SH3-binding protein CBL-C
, signal transduction protein CBL-C
, Casitas B-lineage lymphoma c
, E3 ubiquitin-protein ligase CBL-C