You are viewing an incomplete version of our website. Please click to reload the website as full version.

ADAM Metallopeptidase Domain 10 (ADAM10) (C-Term) Peptide

Details for Product No. ABIN1382004, Supplier: Log in to see
Protein Name
  • adam10
  • wu:fc03d12
  • ADAM10
  • LOC100219653
  • Adam10
  • 1700031C13Rik
  • MADM
  • kuz
  • kuzbanian
  • AD10
  • CD156c
  • HsT18717
  • ad10
  • cd156c
  • madm
  • xadam10
  • ADAM-10
  • ADAM 10
Protein Region
C-Term
Origin
Human
2
2
2
2
Application
Blocking Peptide (BP)
Supplier
Log in to see
Supplier Product No.
Log in to see
Request

Showcase your results, aid the scientific community, and receive a full refund.

Contribute a validation

Learn more

Blocked Antibody anti-ADAM10 antibody (ADAM Metallopeptidase Domain 10) (C-Term) (ABIN1030219)
Characteristics 17 amino acids near the carboxy terminus of human ADAM10.
Human
Research Area Proteolysis / Ubiquitin, Metalloprotease, Extracellular Matrix, Apoptosis/Necrosis, Alzheimer's Disease, Proteases
Application Notes ADAM10 peptide is used for blocking the activity of ADAM10.
Restrictions For Research Use only
Format Liquid
Concentration 200 μg/mL
Buffer PBS pH 7.2 (10 mM NaH2PO4, 10 mM Na2HPO4, 130 mM NaCl) containing 0.1 % bovine serum albumin and 0.02 % 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 -20 °C
Expiry Date 12 months
Background publications Hu, Benedict, Wu et al.: "Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, Issue 8, pp. 4386-91, 1998 (PubMed).

Li, Nijhawan, Budihardjo et al.: "Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade." in: Cell, Vol. 91, Issue 4, pp. 479-89, 1997 (PubMed).

Rosendahl, Ko, Long et al.: "Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases." in: The Journal of biological chemistry, Vol. 272, Issue 39, pp. 24588-93, 1997 (PubMed).