Cité dans 2 publications.
Cet anticorps anti-BAD Polyclonal Lapin (ABIN362001) détecte spécifiquement BAD dans IHC.
L’anticorps est réactif avec des échantillons de Humain, Souris et Rat.
The antibody detects endogenous level of BAD only when phosphorylated at serine136.
Purification
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific phosphopeptide. The antibody against non-phosphopeptide was removedby chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Immunogène
Peptide sequence around phosphorylation site of pSer136 (S-R-S (p) -A-P) derived from Mouse BAD. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
BAD
Reactivité: Humain, Souris
WB, ELISA, IHC, FACS
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
Western blotting: 1:500-1:1000 Immunohistochemistry: 1:50-1:100
Restrictions
For Research Use only
Format
Liquid
Concentration
1 mg/mL
Buffer
Phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
4 °C/-20 °C
Stockage commentaire
Store at -20 °C for long term preservation (recommended). Store at 4 °C for short term use.
Otsuki, Sugiyama, Amano, Yasui, Sakagami: "Negative regulation of NaF-induced apoptosis by Bad-CAII complex." dans: Toxicology, Vol. 287, Issue 1-3, pp. 131-6, (2011) (PubMed).
Matsuda, Takano, Kageyama, Hatakeyama, Shakunaga, Kitajima, Yamazaki, Hattori: "Silencing of caspase-8 and caspase-3 by RNA interference prevents vascular endothelial cell injury in mice with endotoxic shock." dans: Cardiovascular research, Vol. 76, Issue 1, pp. 132-40, (2007) (PubMed).
Antigène
BAD
(BCL2-Associated Agonist of Cell Death (BAD))
Autre désignation
BAD
Sujet
The protein encoded by BAD gene is a member of the BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin were found to be involved in the regulation of this protein. Alternative splicing of this gene results in two transcript variants which encode the same isoform.