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Validated All-in-One™ qPCR Primer for BAD(NM_032989.3) Search again
Product ID:
HQP150272
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
BBC2, BCL2L8
Gene Description:
BCL2 associated agonist of cell death
Target Gene Accession:
NM_032989.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
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].
Gene References into function
- expression in normal, hyperplastic and carcinomatous human prostate
- Protein kinase A RIalpha antisense inhibition of PC3M prostate cancer cell growth: Bcl-2 hyperphosphorylation, Bax up-regulation, and Bad-hypophosphorylation
- results suggest that direct interaction of Bad with pro-survival members of the Bcl-2 family contributes to the progress of Sindbis virus-induced apoptosis
- BAD cleavage and apoptosis in tumor cells in response to raloxifene
- effects of paclitaxel on BAD phosphorylation in ovarian cancer cells
- role of PI3-kinase-dependent phosphorylation and altered transcription in cytokine-mediated neutrophil survival
- study suggests that the cleavage of 14-3-3 protein during apoptosis promotes cell death by releasing the associated Bad protein from the 14-3-3 protein and facilitates Bad translocation to the mitochondria and its interaction with Bcl-x(L)
- BAD-mediated sensitivity of prosstatic cancer cells to TRAIL depends on the phosphorylation status of BAD WT and tBAD.
- BAD is a substrate for pim-2 oncogene proto-oncogene
- Mutation of BAD within the BH3 domain modulates its apoptotic function.
- Bad is increased in quercetin-treated nasopharyngeal carcinoma cells
- Bad gene is occasionally mutated in colon cancer
- constitutively active Rac1 is shown to stimulate the phosphorylation of Bad, thereby suppressing drug-induced caspase activation and apoptosis in human lymphoma cells; Rac1 activation leads to Bad phosphorylation specifically at serine-75
- mechanisms that regulate the conversion of BAD from an anti-death to a pro-death factor include alternative splicing that produces N-terminally truncated BAD(S)and conversion by caspases into a pro-death fragment that resembles the short splice variant
- degraded during Chlamydia trachomatis infection
- A recombinant fusion protein linking human granulocyte-macrophage colony-stimulating factor to the N-terminus of the proapoptotic protein BAD delivers BAD into tumor cells, where it restores the apoptotic pathway.
- AR and IGF1 cooperate to prevent apoptosis by activating a specific PKC-p90(rsk)-dependent pathway, which leads to Bad and Bax inactivation.
- Pak1-dependent Raf-1 phosphorylation regulates its mitochondrial localization, phosphorylation of BAD, and Bcl-2 association
- BAD induces apoptosis upon detecting the coincidence of G2/M phase and growth factor deprivation
- Bax, Bad, and Bim are upregulated, while Bcl-2 is downregulated in human neuroblastoma cells treated with propargylamine
- Bcl-xL mRNA overexpression may suggest poor prognosis in NSCLC.
- There was no somatic mutation of BH3 domains of Bad, Bmf and Bcl-G genes in transitional cell carcinoma samples. The data presented here indicate that BH3 domain mutation of these genes is rare in TCCs and may not contribute to the pathogenesis of TCCs.
- the interaction of BAD with membranes is tied to binding of 14-3-3 protein and activation and membrane translocation of Bcl-XL
- Sequestration of BAD away from mitochondria provides C. trachomatis with mechanism to protect host cell from apoptosis via interaction of a C. trachomatis-encoded inclusion protein with host-cell phosphoserine-binding protein. (BAD protein)
- antiapoptotic signaling pathways activated by vasoactive intestinal polypeptide, epidermal growth factor, and phosphatidylinositol 3-kinase in prostate cancer cells converge on BAD
- Phosphorylation of BAD or inhibition of its translocation to the mitochondria are critical survival pathways in LNCaP tumor cells.
- Cytogenetic investigation of a nodal diffuse large B cell lymphoma carrying an IGH-BCL2-fusion revealed a homogeneously staining region at chromosome 1p21-22.
- doxorubicin-stimulated phosphorylation of Bad in cells expressing dominant negative p38 MAPK was impeded by the inhibition of PI3-kinase
- EGF protects prostate cancer cells from apoptosis by inducing BAD phosphorylation via redundant signaling pathways
- Bad translocation to mitochondria plays a critical role in Tetrahydrocannabinol-induced apoptosis in Jurkat cells.
- AKT-induced BAD phosphorylation and its subsequent cytoplasmic sequestration by 14-3-3zeta is a major mechanism responsible for the postponement of UVB-induced apoptosis in human keratinocytes.
- The high expression of bad in Hodgkin and Reed-Sternberg cells in most classical Hodgkin's lymphomas (HLs)indicates that this protein may play predominant role in the regulation of apoptosis in classical HLs.
- Mycobacterium leprae inhibits apoptosis in THP-1 cells by downregulation of Bad and Bak and upregulation of Mcl-1 gene expression.
- Raf-1 and B-Raf promote protein kinase C theta interaction with BAD.
- dissociation of Bad from Bcl-xL and an increase in the intracellular level of Bcl-xL are responsible for development of acquired TRAIL resistance
- Akt/Bad pathway generates a progressive resistance to apoptosis, at a time HTLV-I genes expression is silenced.
- Expression of p-BAD was increased in the colorectal cancer cells and may possibly alter the cell death regulation during colorectal tumorigenesis.
- p53 can form a complex with dephosphorylated Bad thereby converting it to a pro-apoptotic player.
- GATA1 and GFI1B interplay to regulate bcl-X protein transcription.
- BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between BECN1 and BAX and Bcl-2.
- The functional and physical interaction between Bcl-X(L) and a BH3-like domain in BECN1 was studied.
- The presence of wild type PRV US3, but not of the point-mutated PRV US3, results in phosphorylation of the pro-apoptotic Bad protein in PRV-infected HEp-2 cells.
- Bcl-2 induces the expression of matrix metalloproteinases in renal cell tumors grown in the orthotopic sites, though no appreciable effects were observed in vitro.
- Lysophosphatidic acid prevents apoptosis of Caco-2 colonic neoplasms via activation of mitogen-activated protein kinase and phosphorylation of BAD.
- data presented here indicate that BH3 domain mutation of the proapoptotic genes Bad, Bmf and Bcl-G is rare in laryngeal squamous cell carcinoma and may not contribute to the apoptosis-resistance mechanisms of laryngeal squamous cell carcinoma
- a novel role for BAD in cell cycle regulation dependent upon its phosphorylation state and independent of the BAD/BCL2 interaction and apoptosis.
- decreased expression of p-BAD in malignant gastric epithelial cells suggested loss of p-BAD expression may play a role in gastric tumorigenesis; data also suggest BAD mutation may not be a direct target of inactivation in gastric tumorigenesis
- reelin binds to apoE receptors activating the PI3 K/Akt pathway causing phosphorylation of BAD which protects cells from apoptosis
- AG490 enhances UCN-01-induced cytotoxicity in p53 defective cell lines by suppression of BAD phosphorylation and induction of BAX and PARP cleavage
- Raf-1 in beta-cells led to a striking loss of Bad phosphorylation at serine 112 and an increase in the protein levels of both Bad and Bax
- In the absence of serum, the suppression of either Bad, Bim or Bid expression delayed cell death under several stress conditions
- Bad and Bim are major B-RAF responsive proteins regulating apoptosis in melanoma cells.
- EGF signals via p38 MAPK to increase phosphorylation of BADser112 and thereby limit trophoblast apoptosis.
- Activated extracellular signal-regulated kinase in epithelial cells infected with N. gonorrheae targeted Bad and Bim for downregulation at the protein level.
- C-RAF activation promotes BAD poly-ubiquitylation in a phosphorylation-dependent fashion, and increases the turn-over of this protein through proteasomal degradation.
- caspases activate a previously unrecognized proapoptotic function of HER-2 by releasing a Bad-like cell death effector
- miR-15b and miR-16 could play a role in the development of MDR in gastric cancer cells at least in part by modulation of apoptosis via targeting BCL2.
- B-Raf-initiated inactivation of Bad and Bim only partly contributes to the anti-apoptotic activities of this oncogene and that other points within the cell death machinery are also targeted by deregulated ERK signaling
- Bad and Bid proteins have roles in survival for patients with stage II and III colon cancers
- mRNA expressions of Hsp70, Hsp32 and Bax significantly increased in mononuclear blood cells after marathon running, whereas Hsp27 and Bad mRNA expression levels showed no significant changes.
- HDGF knock-down was found to induce the expression of the pro-apoptotic protein Bad and also inactivate ERK and Akt, which in turn led to dephosphorylation of Bad at Ser-112, Ser-136, and activation of the intrinsic apoptotic pathway.
- JAK2 promotes cell survival by signaling through the Pim/BAD/BCL-xL pathway
- PTH induction of apoptosis is mediated by translocation of mitochondria to the perinuclear region, dephosphorylation of Akt, dephosphorylation of Bad and its movement to the mitochondria, release of cytochrome c and Smac/Diablo, activating casp3.
- two different pathways mediated by downstream products of arachidonic acid metabolism converge in Bad phosphorylation emphasizes the relevance of this strategy for the regulation of macrophage survival to peroxynitrite at the inflammatory sites.
- The study provides the first evidence that AF1q plays a critical role in the regulation of apoptosis and drug resistance.