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Mouse Cblb Antibody (C-term) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q3TTA7
Clone Names 110919009
Additional Information
Gene ID 208650
Other Names E3 ubiquitin-protein ligase CBL-B, 632-, Casitas B-lineage lymphoma proto-oncogene b, SH3-binding protein CBL-B, Signal transduction protein CBL-B, Cblb
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name Cblb
Function E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBL, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (PubMed:29237719).
Cellular Location Cytoplasm. Note=In adipocytes, translocates to the plasma membrane upon insulin stimulation
Research Areas
Citations (0)
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Background

E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. May also be involved in EGFR ubiquitination and internalization.

References

Wilson, B.G., et al. Cancer Cell 18(4):316-328(2010)Stromnes, I.M., et al. J. Clin. Invest. 120(10):3722-3734(2010)Naramura, M., et al. Proc. Natl. Acad. Sci. U.S.A. 107(37):16274-16279(2010)Teh, C.E., et al. Proc. Natl. Acad. Sci. U.S.A. 107(33):14709-14714(2010)Huang, H., et al. Immunity 33(1):60-70(2010)

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$ 277.78
Cat# BP19220b
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