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

Caspase 4, Apoptosis-Related Cysteine Peptidase (CASP4) (Internal Region) Peptide

Details for Product No. ABIN1382242, Supplier: Log in to see
Protein Name
  • CASP4
  • ICE(rel)II
  • ICEREL-II
  • ICH-2
  • Mih1/TX
  • TX
  • Casp11
  • Caspl
  • ich-3
  • CASP1
  • CASP13
Protein Region
Internal Region
Origin
Human
7
1
1
1
1
1
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-Caspase 4 antibody (Caspase 4, Apoptosis-Related Cysteine Peptidase) (Middle Region) (ABIN1030900)
Characteristics 15 amino acids near the center of human caspase-4.
Human
Research Area Apoptosis/Necrosis
Application Notes Caspase-4 peptide is used for blocking the activity of caspase-4.
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 Scobie, Rainey, Bradley et al.: "Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, Issue 9, pp. 5170-4, 2003 (PubMed).

Bradley, Mogridge, Mourez et al.: "Identification of the cellular receptor for anthrax toxin." in: Nature, Vol. 414, Issue 6860, pp. 225-9, 2001 (PubMed).

Kamens, Paskind, Hugunin et al.: "Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases." in: The Journal of biological chemistry, Vol. 270, Issue 25, pp. 15250-6, 1995 (PubMed).