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CBL Antibody

Purified Mouse Monoclonal Antibody (Mab)

     
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  • 1 - CBL Antibody AM8590b
    All lanes : Anti-CBL Antibody at 1:2000 dilution Lane 1: K562 whole cell lysate Lane 2: Jurkat whole cell lysate Lane 3: Raji whole cell lysate Lane 4: SK-BR-3 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-mouse IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 100 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P22681
Reactivity Human
Host Mouse
Clonality monoclonal
Isotype IgG2b,k
Clone Names 1762CT401.80.60
Calculated MW 99633 Da
Additional info
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
StorageMaintain 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.
PrecautionsCBL Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
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. 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.
Cellular Location Cytoplasm. Cell membrane. Note=Colocalizes with FGFR2 in lipid rafts at the cell membrane
Research Areas

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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