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Mouse Anti-BAD (Phospho-Ser112) Recombinant Antibody (CBYY-0141) (CBMAB-0142-YY)

This product is mouse antibody that recognizes BAD. The antibody CBYY-0141 can be used for immunoassay techniques such as: WB
See all BAD antibodies
Published Data

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBYY-0141
Antibody Isotype
IgG2b, κ
Application
ELISA, IP, IF, WB

Basic Information

Immunogen
Ser 112 phosphorylated Bad.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
BCL2 Associated Agonist Of Cell Death
Introduction
The protein encoded by this 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.
Entrez Gene ID
UniProt ID
Alternative Names
BCL2 Associated Agonist Of Cell Death; Bcl-XL/Bcl-2-Associated Death Promoter; Bcl2 Antagonist Of Cell Death; Bcl-2-Binding Component 6; Bcl-2-Like Protein 8; Bcl2-L-8; BCL2L8; BCL2-Antagonist Of Cell Death Protein;
Function
Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity).
Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.
Biological Process
Activation of cysteine-type endopeptidase activity Source: BHF-UCL
Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
ADP metabolic process Source: UniProtKB
Apoptotic process Source: UniProtKB
ATP metabolic process Source: UniProtKB
Cellular response to chromate Source: Ensembl
Cellular response to hypoxia Source: UniProtKB
Cellular response to lipid Source: Ensembl
Cellular response to mechanical stimulus Source: UniProtKB
Cellular response to nicotine Source: UniProtKB
Cerebral cortex development Source: Ensembl
Cytokine-mediated signaling pathway Source: Ensembl
Extrinsic apoptotic signaling pathway Source: UniProtKB
Extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
Extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
Glucose catabolic process Source: Ensembl
Glucose homeostasis Source: UniProtKB
Intrinsic apoptotic signaling pathway Source: UniProtKB
Intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
Pore complex assembly Source: UniProtKB
Positive regulation of apoptotic process Source: UniProtKB
Positive regulation of apoptotic process by virus Source: Ensembl
Positive regulation of autophagy Source: UniProtKB
Positive regulation of B cell differentiation Source: Ensembl
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Positive regulation of epithelial cell proliferation Source: UniProtKB
Positive regulation of glucokinase activity Source: UniProtKB
Positive regulation of granulosa cell apoptotic process Source: Ensembl
Positive regulation of insulin secretion Source: UniProtKB
Positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
Positive regulation of intrinsic apoptotic signaling pathway Source: Reactome
Positive regulation of intrinsic apoptotic signaling pathway in response to osmotic stress Source: Ensembl
Positive regulation of mitochondrial membrane potential Source: UniProtKB
Positive regulation of neuron death Source: Ensembl
Positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
Positive regulation of proteolysis Source: BHF-UCL
Positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
Positive regulation of T cell differentiation Source: Ensembl
Positive regulation of type B pancreatic cell development Source: UniProtKB
Protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
Regulation of mitochondrial membrane permeability Source: UniProtKB
Release of cytochrome c from mitochondria Source: GO_Central
Response to amino acid Source: Ensembl
Response to benzene Source: Ensembl
Response to calcium ion Source: Ensembl
Response to drug Source: Ensembl
Response to estradiol Source: Ensembl
Response to ethanol Source: Ensembl
Response to glucocorticoid Source: Ensembl
Response to glucose Source: Ensembl
Response to hydrogen peroxide Source: Ensembl
Response to oleic acid Source: Ensembl
response to progesterone Source: Ensembl
response to testosterone Source: Ensembl
Spermatogenesis Source: Ensembl
Suppression by virus of host apoptotic process Source: Ensembl
Type B pancreatic cell proliferation Source: UniProtKB
Cellular Location
Cytoplasm; Mitochondrion outer membrane. Colocalizes with HIF3A in the cytoplasm (By similarity). Upon phosphorylation, locates to the cytoplasm.
PTM
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. Phosphorylation at Ser-99 by PKB/AKT1 is almost completely blocked by the apoptotic C-terminus cleavage product of PKN2 generated by caspases-3 activity during apoptosis.
Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.
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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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