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Validated All-in-One™ qPCR Primer for CBL(NM_005188.3) Search again
Product ID:
HQP114862
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
C-CBL, CBL2, FRA11B, NSLL, RNF55
Gene Description:
Cbl proto-oncogene
Target Gene Accession:
NM_005188.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The cbl oncogene was first identified as part of a transforming retrovirus which induces mouse pre-B and pro-B cell lymphomas. As an adaptor protein for receptor protein-tyrosine kinases, it positively regulates receptor protein-tyrosine kinase ubiquitination in a manner dependent upon its variant SH2 and RING finger domains. Ubiquitination of receptor protein-tyrosine kinases terminates signaling by marking active receptors for degradation.
Gene References into function
- novel E3 ubiquitin-protein ligase; role in regulation of immune response - review
- Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
- The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met
- Negative regulation of Lck by Cbl ubiquitin ligase
- Cbl-b protein and CIN85 downregulate receptor tyrosine kinases
- Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors.
- complexation with ArgBP2 mediates ubiquitination and degradation of c-Abl
- c-Cbl-dependent EphA2 protein degradation is induced by ligand binding.
- MLL-CBL fusion was the result of an interstitial deletion in patients with de novo acute myeloid leukemia (FAB-M1).
- Ron tyrosine kinase receptor desensitization mediated by c-Cbl and its binding partner Grb2.
- c-cbl binds to hSpry2, and this interaction is critical for its physiological function in a signal-specific context
- Cbl has a role, via its ubiquitin ligase activity, as a negative regulator of activated Vav
- Lower expression of cbl is associated with acute myeloid leukemia-M2 and higher expression of cbl is associated with acute myeloid leukemia-M5
- the c-Cbl/CD2AP complex binds to activated Flt-1 and plays a crucial role in its endocytosis and subsequent degradation.
- Recruitment of CBL to lipid rafts mediates signals important for actin reorganization in growing neurites.
- Sts-1 and Sts-2 bind to Cbl and inhibit endocytosis of receptor tyrosine kinases
- CBL has a role in down-regulation of Lyn and Fyn in osteoblast differentiation induced by constitutive FGFR2 activation
- c-Cbl has a role in EGFR trafficking
- Differences in ubiquitin-binding may reflect distinct regulatory functions of c-Cbl and Cbl-b.
- c-Cbl-dependent ubiquitination of p75NTR involved in the regulation of p75NTR signalling.
- c-Cbl guides the epidermal growth factor receptor into clathrin-coated pits by two distinct modes of Eps15 recruitment
- Grb2-mediated recruitment of the functional RING domain of Cbl to the EGFR is essential and sufficient to support receptor endocytosis
- mediates ubiquitination and lysosomal degradation of PAR(2) to irrevocably terminate its signaling
- the alpha5 integrin subunit has a role in the induction of apoptosis triggered by FGFR2 activation in osteoblasts, and a Cbl-dependent mechanism is involved in the coordinated regulation of cell apoptosis induced by alpha5 integrin degradation
- Data show that infected cell protein 0 (ICP0) binds CIN85 in a reciprocal manner and that the complexes pulled down by ICP0 also contain Cbl.
- dynamin, Cbl, and Src coordinately participate in signaling complexes that are important in the assembly and remodeling of the actin cytoskeleton, leading to changes in osteoclast adhesion, migration, and resorption
- Results suggest a novel function for c-Cbl, microtubule binding and stabilization.
- Cbl promotes clustering of endocytic adaptor proteins.
- EGF-R fate is controlled by a checkpoint downstream of receptor ubiquitination whose regulation by the Cbl RF tail may require Sprouty2 degradation.
- CD21 activation triggered Cbl tyrosine phosphorylation, which interacts with SH2 domains of p85 subunit, SH2 domains of Crk-L and with tyrosine phosphorylated Syk kinase. CD21 activation triggers dissociation of Cbl-Vav complex.
- the SH3 domain of betaPix specifically interacts with a proline-arginine motif (PxxxPR) present within the ubiquitin ligase Cbl and Pak1 kinase. Cbl and Pak1 compete for binding to betaPix.
- results implicate CD45, Cbl, Cbl-b, src kinases and potentially other associated proteins as mediators of SDF-1alpha/CXCL12-induced cell migration of Jurkat T cells
- ubiquitin ligase of EGFR, namely c-Cbl, also mediates receptor modification with the ubiquitin-like molecule Nedd8
- By lysing primary hemopoietic cells at high pH, BCR-ABL1 protein-degradative activity was inhibited & association between BCR-ABL1 protein in complexes with adaptor proteins CBL, CRKL & GRB2 in primary chronic myeloid leukaemia material was demonstrated
- Twist haploinsufficiency results in decreased Cbl-mediated PI3K degradation in osteoblasts.
- Alix inhibits down-regulation of PDGFRbeta by modulating the interaction between c-Cbl and the receptor, thereby affecting the ubiquitination of the receptor
- Depletion of Cbl and Cbl-b E3 ubiquitin ligases by RNA interference, or overexpression of a Cbl dominant inhibitory mutant (Cbl-N), inhibited Spred-2 ubiquitination.
- The interaction between c-Cbl and SLAP in v-Abl-3T3 cells positively influenced c-Cbl-mediated spreading and adhesion of these cells
- corecruitment of c-Cbl and PLCgamma1 to VEGFR-2 serves as a mechanism to fine-tune the angiogenic signal relay of VEGFR-2
- novel mutations in c-CBL and CBL-b have been identified in human acute myeloid leukemia
- Cbl-dependent negative regulation of PDGFRbeta involves a dual mechanism that concurrently promotes ubiquitin-dependent lysosomal sorting of the receptor and competitively reduces the recruitment of a positive mediator of receptor signaling
- a role of Cbl dimerization in terminating signaling following activation of receptor tyroine kinase.
- a new role for CIN85 in regulating Syk protein levels in RBL-2H3 cells through the activation of the ubiquitin-proteasome pathway and provide a mechanism for this regulation involving c-Cbl ligase activity.
- STAP-2 associates with FAK and enhances its degradation, proteasome inhibitors block FAK degradation, and STAP-2 recruits an endogenous E3 ubiquitin ligase, Cbl, to FAK.
- myoferlin forms a complex with dynamin-2 and VEGFR-2, which prevents CBL-dependent VEGFR-2 polyubiquitination and proteasomal degradation.
- Given that phospholipase gamma 2 (PLC gamma 2) function is also influenced by c-Cbl hypophosphorylation, the ratio of PLC gamma 2 to c-Cbl
- recruiment to endosomes is regulated by epidermal growth factors and amphiregulin
- H-Ras interacts with Spry2-binding partners, c-Cbl and CIN85, in a Spry2-dependent manner.
- endogenous hSPRY2-mediated regulation of apoptosis requires c-Cbl and is manifested by the ability of hSPRY2 to sequester c-Cbl and thereby augment signaling via growth factor receptors
- Lyn activation is BCR-ABL independent, it is complexed with the Gab2 and c-Cbl adapter/scaffold proteins, and it mediates persistent Gab2 and BCR-ABL tyrosine phosphorylation in the presence or absence of imatinib.
- An obligatory, intrapeptidyl H-bond between the phosphotyrosine and the conserved asparagine or adjacent arginine is essential for binding and orientates peptides into a positively charged pocket on c-Cbl.
- two Cbls accounted for total receptor ubiquitination and that while c-Cbl and Cbl-b are each alone sufficient to effect EGFR degradation, both are involved in the physiological, EGF-mediated process of receptor downregulation.
- Results identify a molecular mechanism by which activated FGFR2 recruits Cbl in raft micro-domains to trigger PI3K ubiquitination and proteasome degradation, and reveal a role for PI3K/Akt in the control of osteoblast survival by FGFR2 signaling.
- c-Cbl is a critical regulator of the functional responses of memory T cell subsets; role in a mechanism controlling the functional heterogeneity of memory CD4 cells.
- Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation
- c-Cbl is a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis
- findings show that low levels of Lck caused a dramatic reduction in c-Cbl phosphorylation and a general reduction in protein ubiquitination after TCR stimulation
- TEAD1 and the ubiquitin ligase c-Cbl were identified as novel basal cell markers in prostate cancer
- Mapping minimally overlapping segmental UPD regions helps target the search for pathogenic mutations, including newly identified missense mutations in the proto-oncogene c-Cbl in 7 of 12 patients with UPD11q.
- c-Cbl mediates the ubiquitination of stimulated FcgammaRIIa