ADAM10 antibody

Catalog No. ABIN2664261

This Mouse Monoclonal antibody specifically detects ADAM10 in ICFC. It exhibits reactivity toward Human.

Quick Overview for ADAM10 antibody (ABIN2664261)

Target: ADAM10 (ADAM Metallopeptidase Domain 10 (ADAM10))

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This ADAM10 antibody is un-conjugated

Application: Intracellular Flow Cytometry (ICFC)

Clone: SHM14

Product Details anti-ADAM10 Antibody

Purification: The antibody was purified by affinity chromatography.

Isotype: IgG1 kappa

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Handling

Concentration: 0.5 mg/mL

Buffer: Phosphate-buffered solution, pH 7.2, containing 0.09 % sodium azide.

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: 4 °C

Storage Comment: The antibody solution should be stored undiluted between 2°C and 8°C.

Target Details for ADAM10

Target: ADAM10 (ADAM Metallopeptidase Domain 10 (ADAM10))

Alternative Name: CD156c

Background: CD156c, also known as a disintegrin and metalloproteinase domain-containing protein 10 (ADAM10), is a 748 amino acid type I membrane glycoprotein ubiquitously expressed on most cell types. It consists of multiple functional domains, including a N-terminal prodomain, catalytic domain, cysteine-rich domain, transmembranous domain, and cytoplasmic domain. It is secreted as a precursor protein and becomes as the activate/mature form through removing the ADAM10 prodomain by proprotein convertase 7 and furin. ADAM10 functions as metalloproteinase to cleave several molecules including Notch, pro-TNF-α, amyloid precursor protein, myelin basic protein, and type IV collagen. It mediates the release of several cell adhesion molecules such as vascular endothelial cadherin or L-selectin to regulate endothelial permeability and leukocyte transmigration. Dysregulation of ADAM activity may contribute to the pathogenesis of vascular diseases.

Pathways: Notch Signaling, EGFR Signaling Pathway