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CBL Antibody
Purified Mouse Monoclonal Antibody (Mab)
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- CITATIONS
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- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P22681 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | monoclonal |
| Isotype | IgG2b,k |
| Clone/Animal Names | 1762CT401.80.60 |
| Calculated MW | 99633 Da |
| Gene ID | 867 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase CBL, 6.3.2.-, Casitas B-lineage lymphoma proto-oncogene, Proto-oncogene c-Cbl, RING finger protein 55, Signal transduction protein CBL, CBL, CBL2, RNF55 |
| Target/Specificity | This CBL antibody is generated from a mouse immunized with a KLH conjugated synthetic peptide between 450-644 amino acids from human CBL. |
| Dilution | WB~~1:2000 |
| Format | Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | CBL Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | CBL |
|---|---|
| Synonyms | CBL2, RNF55 |
| Function | Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:17094949). Ubiquitinates SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates EGFR (PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin- protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor- alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity). |
| Cellular Location | Cytoplasm. Cell membrane. Cell projection, cilium. Golgi apparatus. Note=Colocalizes with FGFR2 in lipid rafts at the cell membrane |
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Provided below are standard protocols that you may find useful for product applications.
Background
Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3.
References
Blake T.J.,et al.Oncogene 6:653-657(1991).
Taylor T.D.,et al.Nature 440:497-500(2006).
Howlett C.J.,et al.Biochem. Biophys. Res. Commun. 257:129-138(1999).
Joazeiro C.A.,et al.Science 286:309-312(1999).
Donovan J.A.,et al.J. Biol. Chem. 269:22921-22924(1994).
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