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>   首页   >   产品   >   一抗   >   癌症   >   Anti-CD156c Antibody   

Anti-CD156c Antibody

     
  • 1 - Anti-CD156c Antibody AP51935
    Western blot analysis of CD156c expression in HEK293T (A), H446 (B), mouse lung (C), rat testis (D) whole cell lysates. (Predicted band size: 84 kD; Observed band size: 80 kD)
  • 3 - Anti-CD156c Antibody AP51935
    Immunofluorescent analysis of CD156c staining in NIH3T3 cells. Formalin-fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 5-10 minutes and blocked with 3% BSA-PBS for 30 minutes at room temperature. Cells were probed with the primary antibody in 3% BSA-PBS and incubated overnight at 4 °C in a hidified chamber. Cells were washed with PBST and incubated with a AF488-conjugated secondary antibody (green) in PBS at room temperature in the dark. Phalloidin - AF594 was used to stain Actin filaments (red). DAPI was used to stain the cell nuclei (blue).
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Product Information
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, IF/IC
Primary Accession O14672
Reactivity Human, Mouse, Rat, Pig, Bovine
Host Rabbit
Clonality Polyclonal
Calculated MW 84142 Da
Additional Information
Gene ID 102
Other Names KUZ; MADM; Disintegrin and metalloproteinase domain-containing protein 10; ADAM 10; CDw156; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease; CD156c
Target/Specificity KLH-conjugated synthetic peptide encompassing a sequence within the center region of human CD156c. The exact sequence is proprietary.
Dilution WB~~WB (1/500 - 1/1000)
IF/IC~~N/A
Format Liquid in 0.42% Potassium phosphate, 0.87% Sodium chloride, pH 7.3, 30% glycerol, and 0.01% sodium azide.
StorageStore at -20 °C.Stable for 12 months from date of receipt

For Research Use Only. Not For Use In Diagnostic Procedures.

Protein Information
Name ADAM10 (HGNC:188)
Synonyms KUZ, MADM
Function Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins, including adhesion proteins, growth factor precursors and cytokines being essential for development and tissue homeostasis (PubMed:11786905, PubMed:12475894, PubMed:20592283, PubMed:24990881, PubMed:26686862, PubMed:28600292, PubMed:31792032, PubMed:31792032). Associates with six members of the tetraspanin superfamily TspanC8 which regulate its exit from the endoplasmic reticulum and its substrate selectivity (PubMed:26686862, PubMed:28600292, PubMed:31792032, PubMed:34739841, PubMed:37516108). Cleaves the membrane-bound precursor of TNF at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha- secretase cleavage of amyloid precursor protein (APP) (PubMed:11786905, PubMed:26686862, PubMed:29224781, PubMed:34739841, PubMed:33731436). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Also controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Required for the development of type 1 transitional B cells into marginal zone B cells, probably by cleaving Notch (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (PubMed:26876177). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (PubMed:24990881). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146). Regulates leukocyte transmigration as a sheddase for the adherens junction protein VE- cadherin/CDH5 in endothelial cells (PubMed:28600292).
Cellular Location Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, clathrin-coated vesicle. Cell projection, axon {ECO:0000250|UniProtKB:O35598}. Cell projection, dendrite {ECO:0000250|UniProtKB:O35598}. Cell junction, adherens junction. Cytoplasm Note=Is localized in the plasma membrane but is also expressed in the Golgi apparatus and in clathrin-coated vesicles derived likely from the Golgi (PubMed:12475894). During long term depression, it is recruited to the cell membrane by DLG1 (PubMed:23676497). The immature form is mainly located near cytoplasmic fibrillar structures, while the mature form is predominantly located at zonula adherens and the cell membrane (PubMed:30463011). The localization and clustering of mature ADAM10 to zonula adherens is regulated by AFDN, TSPAN33, PLEKHA7 and PDZD11 (PubMed:30463011).
Tissue Location Expressed in the brain (at protein level) (PubMed:23676497). Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver (PubMed:11511685, PubMed:9016778).
Research Areas

REFERENCES

Rosendahl M.S.,et al.J. Biol. Chem. 272:24588-24593(1997).
Howard L.,et al.Biochem. J. 317:45-50(1996).
McKie N.,et al.Biochem. Biophys. Res. Commun. 230:335-339(1997).
Gutwein P.,et al.FASEB J. 17:292-294(2003).
Vincent B.,et al.J. Biol. Chem. 276:37743-37746(2001).

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