ELISA, Dot Blot (DB), Immunohistochemistry (IHC), Immunofluorescence (IF)
Kreuzreaktivität (Details)
Expected species reactivity: Mouse, Rat
Aufreinigung
Antigen affinity purified
Immunogen
This phospho-Bad antibody was produced from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding pS99 of human Bad.
BAD
Reaktivität: Human
DB, IHC (p), IF
Wirt: Kaninchen
Polyclonal
RB06933
unconjugated
Applikationshinweise
Titration of the phospho-Bad antibody may be required due to differences in protocols and secondary/substrate sensitivity.\. Immunofluorescence: 1:200,Dot blot: 1:500,IHC (Paraffin): 1:50-1:100
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Buffer
In 1X PBS, pH 7.4, with 0.09 % sodium azide
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
-20 °C
Informationen zur Lagerung
Aliquot the phospho-Bad antibody and store frozen at -20°C or colder. Avoid repeated freeze-thaw cycles.
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Hintergrund
Bad 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 are found to be involved in the regulation of this protein. Bad is phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation.