BAD recombinant protein

BAD recombinant protein

Cat. Num. AAA515218

• Gene Names: BAD; BBC2; BCL2L8
• Applications: Western Blot
• Synonyms: BAD; BAD recombinant protein; BBC2; BCL2L8

• Host: Sf9 insect cells
• Form/Format: 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
• Sequence Length: 986

• Applicable Applications for BAD recombinant protein: Western Blot (WB)
• Type: Recombinant Fusion Protein
• Species: Human
• Tag Information: GST tag
• Expression System: Sf9 insect cells using baculovirus
• Source Note: Recombinant full-length human BAD was expressed by baculovirus in Sf9 insect cells
• Preparation and Storage: Store product at -70 degree C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

SDS-PAGE

Related Product Information for BAD recombinant protein

Recombinant full-length human BAD was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag.

Scientific Background: BAD is a member of the BCL-2 family of proteins that are known to be regulators of programmed cell death. BAD is a pro-apoptotic protein that forms a heterodimer complex with BCL-xL and BCL-2 which reverses the prosurvival activity of these proteins (1). The proapoptotic activity of BAD is regulated through its phosphorylation and this inhibits the pro-apoptosis function of BAD. Protein kinases such as AKT, RAF and RSK1 can phosphorylate BAD and RSK1-induced phosphorylation of BAD at ser112 suppresses BAD-mediated apoptosis in neurons. BAD inhibits G(1) to S phase transition in MCF7 breast cancer cells and overexpression of BAD inhibits cell growth as well as cyclin D1 expression (2).

Product Categories/Family for BAD recombinant protein

Apoptosis Proteins; Signaling Proteins - Apoptosis Proteins

References

1.Yang E, et al: Bad, a heterodimeric partner for Bcl-X(L) and Bcl-2, displaces Bax and promotes cell death. Cell 80: 285-291, 1995.
2.Fernando R, et al: Breast cancer cell proliferation is inhibited by BAD: regulation of cyclin D1. J Biol Chem. 2007 Sep 28;282(39):28864-73.

NCBI and Uniprot Product Information

• NCBI GI #: 197116382
• NCBI GeneID: 572
• NCBI Accession #: NP_116784.1
• NCBI GenBank Nucleotide #: NM_032989
• UniProt Accession #: Q92934; O14803; Q6FH21
• Molecular Weight: ~47 kDa
• NCBI Official Full Name: Homo sapiens BCL2-associated agonist of cell death (BAD), transcript variant 2, mRNA
• NCBI Official Synonym Full Names: BCL2-associated agonist of cell death
• NCBI Official Symbol: BAD
• NCBI Official Synonym Symbols: BBC2; BCL2L8
• NCBI Protein Information: bcl2 antagonist of cell death; bcl2-L-8; BCL2-binding protein; bcl-2-like protein 8; BCL2-binding component 6; bcl-2-binding component 6; BCL-X/BCL-2 binding protein; BCL2-antagonist of cell death protein; bcl-XL/Bcl-2-associated death promoter
• UniProt Protein Name: Bcl2 antagonist of cell death
• Protein Family: Bcl2-associated agonist of cell death
• UniProt Gene Name: BAD
• UniProt Synonym Gene Names: BBC6; BCL2L8; BAD; Bcl2-L-8
• UniProt Entry Name: BAD_HUMAN

NCBI Description

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. [provided by RefSeq, Jul 2008]

Uniprot Description

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.

Subunit structure: Forms heterodimers with the anti-apoptotic proteins, Bcl-X(L), Bcl-2 and Bcl-W. Also binds protein S100A10

By similarity. The Ser-75/Ser-99 phosphorylated form binds 14-3-3 proteins

By similarity. Interacts with AKT1 and PIM3. Ref.4 Ref.11 Ref.15

Subcellular location: Mitochondrion outer membrane. Cytoplasm. Note: Upon phosphorylation, locates to the cytoplasm.

Tissue specificity: Expressed in a wide variety of tissues.

Domain: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.

Post-translational modification: 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. Ref.2 Ref.11 Ref.12 Ref.13 Ref.14Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99. Ref.18

Sequence similarities: Belongs to the Bcl-2 family.

Sequence caution: The sequence AAB36516.1 differs from that shown. Reason: Frameshift at positions 64 and 91.