Render Target: SSR
Render Timestamp: 2024-11-14T22:54:57.143Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-10-24 20:52:07.375
Product last modified at: 2024-10-11T14:30:08.990Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

OB-Cadherin (16G5) Mouse mAb #13577

Filter:
  • WB
  • IF
  • F

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 120
    Source/Isotype Mouse IgG1
    Application Key:
    • WB-Western Blotting 
    • IF-Immunofluorescence 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunofluorescence (Immunocytochemistry) 1:3200
    Flow Cytometry (Fixed/Permeabilized) 1:3200
    Flow Cytometry (Live) 1:3200

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    OB-Cadherin (16G5) Mouse mAb recognizes endogenous levels of total OB-cadherin protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant protein containing the extracellular cadherin domain 1 of OB-cadherin fused to maltose binding protein.

    Background

    Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).
    OB-cadherin (CDH11) is highly expressed in osteoblastic cell lines (9). Its upregulation during differentiation in cells of the osteo-lineage and the chondro-lineage implies a specific role in bone cell differentiation and bone formation (9,10).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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