Human BAD Antibody : APC (Phospho-Ser112)

Référence OAAQ00150-10tests

Conditionnement : 10Tests

Marque : Aviva Systems Biology

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Human BAD Antibody : APC (Phospho-Ser112)

Human BAD Antibody : APC (Phospho-Ser112) (OAAQ00150)

Datasheets/ManualsPrintable datasheet for OAAQ00150
Product Info
Tested Species ReactivityHuman, Mouse, Rat
Predicted Species ReactivityMouse, Rat, and other homologues
Product FormatLiquid 1X PBS with 0.2% BSA and 0.09% sodium azide
ClonalityMonoclonal
CloneBADS112-B9
IsotypeRabbit IgG1L
HostRabbit
ConjugationAPC: Allophycocyanin
ApplicationFC
Reconstitution and StorageStore at 2-8°C
ImmunogenA synthetic phospho-peptide corresponding to residues surrounding Ser112 of human phospho BAD
PurificationProtein A+G
Target Post-Translational ModificationPhospho-Ser112
Application InfoFor flow cytometric staining, the suggested use of this reagent is 5 uL per million cells or 5 uL per 100 uL of staining volume. It is recommended that the reagent be titrated for optimal performance for each application.
ReferenceCzabotar PE., et al., (2014) Nat Rev Mol Cell Biol 15:49-63.
Polzien L., et al., (2009) J Biol Chem 284:28004-28020.
Masters SC., et al., (2001) Mol Pharmacol 60: 1325-1331.
Datta SR., et al., (1997) Cell 91:231-241.
Harada H., et al., (1999) Mol Cell 3:413-422.
Chiang CW et al., (2001) Blood 97:1289-1297.
Gene SymbolBAD
Gene Full NameBCL2 associated agonist of cell death
Alias SymbolsBBC2, BCL2L8
NCBI Gene Id572
Protein Namebcl2-associated agonist of cell death
Description of TargetHuman BCL-2-assocaited death promoter (BAD) regulates apoptosis by binding to anti-apoptotic members of BCL family including BCL-2, BCL-xL, and BCL-w. The BAD protein signal transduction activity is regulated by multiple kinases and phosphatases. Non-phosphorylated BAD protein selectively dimerizes with Bcl-xL and Bcl-2 displacing Bax, which is then free to initiate mitochondrial membrane permeability, initiating apoptosis. When phosphorylated, BAD is unable to heterodimerize with Bcl-2 or Bcl-xL and is sequestered into the cytosolic compartment by binding to 14-3-3 protein. BAD protein has been shown to phosphorylated at multiple sites. The phosphorylation of 3 serine residues (Ser112, Ser136 and Ser155) effects the activity of the BAD. Multiple kinases phosphorylate BAD at these serine site. Ribosomal protein S6 kinase alpha-1 (RPS6KA1/RSK) and cAMP-dependent protein kinase phosphorylated BAD at Ser112 while protein kinase B (PKB/Akt) phosphorylates BAD at Ser136 residue. Phosphorylation of BAD at Ser-155 is preferentially carried out by Protein Kinase A. Other BAD phosphorylation sites may regulation cellular localization of BAD. Phosphorylation of both Ser75 and Ser99 increases sequestration of BAD by 14-3-3 protein which leads to translocation of BAD from the mitochondria to the cytosol. This prevents BAD from binding to anti-apoptotic proteins. Phosphorylation at Ser99 also prevents BAD from binding to the hydrophobic groove of Bcl-2 and Bcl-XL.
Uniprot IDQ92934
Protein Accession #NP_004313.1
Nucleotide Accession #NM_004322.3