BCL (pThr56) antibody

Details for Product No. ABIN965647
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Antigen
Epitope
pThr56
(1)
Reactivity
Human
(3)
Host
Rabbit
(3)
Application
Immunohistochemistry (IHC)
(3)
Pubmed 5 references available
Quantity 100 μg
Options
Shipping to United States (Change)
Availability Will be delivered in 5 to 7 Business Days
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Catalog No. ABIN965647
385.00 $
Plus shipping costs $45.00

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen The antiserum was produced against synthesized phosphopeptide derived from human BCL-2 around the phosphorylation site of threonine 56 (G-H-TP-P-H).
Specificity BCL-2 (phospho-Thr56) antibody detects endogenous levels of BCL-2 only when phosphorylated at threonine 56.
Application Notes IHC: 1:50-1:100.
Restrictions For Research Use only
Format Liquid
Concentration 100ug/100ul.
Buffer Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 50% glycerol
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
Product cited in: Ling, Tornos, Perez-Soler: "Phosphorylation of Bcl-2 is a marker of M phase events and not a determinant of apoptosis." in: The Journal of biological chemistry, Vol. 273, Issue 30, pp. 18984-91, 1998 (PubMed).

Siegert, Robbins: "Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250." in: Molecular and cellular biology, Vol. 19, Issue 1, pp. 846-54, 1999 (PubMed).

Yamamoto, Ichijo, Korsmeyer: "BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M." in: Molecular and cellular biology, Vol. 19, Issue 12, pp. 8469-78, 2000 (PubMed).

Deng, Xiao, Lang et al.: "Novel role for JNK as a stress-activated Bcl2 kinase." in: The Journal of biological chemistry, Vol. 276, Issue 26, pp. 23681-8, 2001 (PubMed).

Huang, Cidlowski: "Phosphorylation status modulates Bcl-2 function during glucocorticoid-induced apoptosis in T lymphocytes." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 16, Issue 8, pp. 825-32, 2002 (PubMed).

Validation Images
Did you look for something else?
back to top