Recombinant Mouse Bcl2 antagonist of cell death(Bad)

Code CSB-YP736816MO
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Source Yeast
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Code CSB-EP736816MO
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Source E.coli
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Code CSB-EP736816MO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP736816MO
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Source Baculovirus
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Code CSB-MP736816MO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Bad
Uniprot No. Q61337
Alternative Names Bad; Bbc6Bcl2-associated agonist of cell death; BAD; Bcl-2-binding component 6; Bcl-xL/Bcl-2-associated death promoter; Bcl2 antagonist of cell death
Species Mus musculus (Mouse)
Expression Region 1-204
Target Protein Sequence MGTPKQPSLA PAHALGLRKS DPGIRSLGSD AGGRRWRPAA QSMFQIPEFE PSEQEDASAT DRGLGPSLTE DQPGPYLAPG LLGSNIHQQG RAATNSHHGG AGAMETRSRH SSYPAGTEED EGMEEELSPF RGRSRSAPPN LWAAQRYGRE LRRMSDEFEG SFKGLPRPKS AGTATQMRQS AGWTRIIQSW WDRNLGKGGS TPSQ
Protein Length full length protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Data

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. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.
Gene References into Functions
  1. This study shows for the first time that genetic knockout of Bad provides epileptic seizure protection in Kcna1-/- mice, a genetic model of epilepsy with sudden unexplained death. PMID: 29171006
  2. BAD knockout reduced epileptiform activity, and this effect was lost upon knockout or pharmacological inhibition of KATP channels. PMID: 29368690
  3. Bad is dispensable for TNF-mediated cell death. PMID: 25611386
  4. Results suggest that regulation of the proapoptotic activity of BAD plays a key role in the pathogenic mechanisms resulting in primary pigmented nodular adrenocortical disease tumor formation. PMID: 24865460
  5. fasting may increase the uptake beta-hydroxybutyrate by decreasing BAD in the brain during hypoglycemia PMID: 25043191
  6. Results indicate the downstream targets of insulin, cyclin D1, BAD, alpha-MHC, and GATA-4, elucidate a molecular mechanism of insulin in promoting cell proliferation and differentiation. PMID: 24020834
  7. our study suggests that Bad and Bmf co-regulate lymphocyte homeostasis and limit spontaneous transformation by mechanisms that may not exclusively be linked to the induction of lymphocyte apoptosis. PMID: 22430207
  8. Results reveal that IKK inhibits TNFalpha-induced apoptosis through two distinct but cooperative mechanisms: activation of the survival factor NF-kappaB and inactivation of the proapoptotic BH3-only BAD protein. PMID: 23332762
  9. RNAi-mediated silencing of STAT1 in soft tissue sarcoma (STS) cells was sufficient to increase expression of the apoptotic mediators Fas and Bad and to elevate the sensitivity of STS cells to Fas-mediated apoptosis PMID: 22805310
  10. BAD modulates counterregulatory responses to hypoglycemia and protective glucoprivic feeding PMID: 22162752
  11. the regulation of BAD by uremic toxins and report the sensitization of vascular smooth muscle cells to apoptosis upon BAD induction was explored. PMID: 22172950
  12. Tonicity-induced COX-2 expression and PGE2 synthesis in the renal medulla entails phosphorylation and inactivation of the pro-apoptotic protein Bad, thereby counteracting apoptosis in renal medullary epithelial cells. PMID: 21716255
  13. Caspase-3 is activated by the BAD-BAX cascade resulting in long term depression induction in the hippocampus. PMID: 21609830
  14. JNK1 is required for erythropoietin-mediated cell survival through phosphorylation and inactivation of the pro-apoptotic, Bcl-2 homology domain 3 (BH3)-only Bcl-associated death protein (Bad). PMID: 21095239
  15. Bad protein cooperate with bim protein in certain apoptotic responses and in the suppression of g-irradiation-induced thymic lymphoma.(Bad protein) PMID: 20431598
  16. Data show that loss of Bmf reduced the pressure to inactivate p53, whereas Bad deficiency did not, identifying Bmf as a novel component of the p53-independent tumor suppressor pathway triggered by c-Myc. PMID: 19965635
  17. The beta-arrestin 1-dependent ERK1/2 activation engaged by GLP-1 mediates the Ser-112 phosphorylation of Bad. PMID: 19915011
  18. The interaction of Bad with lipid rafts is a dynamic process regulated by IL-4 and involved in the control of apoptosis. PMID: 11907096
  19. activation by therapeutic inhibition of epidermal growth factor receptor and transactivation by insulin-like growth factor receptor PMID: 12011069
  20. Bcl-x(L) and Bcl-w target protein phosphatase 1alpha to Bad PMID: 12115603
  21. phosphorylation at serine 128 by activation of the JNK signaling pathway PMID: 12189144
  22. BAD phosphorylation protects cells from the deleterious effects of apoptotic stimuli and attenuates death pathway signaling by raising the threshold at which mitochondria release cytochrome c to induce cell death PMID: 12431371
  23. Bad apoptotic protein alone or in combination with bax apoptotic protein and the prostatic-specific promoter ARR(2)PB was an effective therapy for experimental prostatic neoplasms. PMID: 12490000
  24. Candida albicans phospholipomannan promotes survival of phagocytosed yeasts through modulation of of this protein's phosphorylation and macrophage apoptosis. PMID: 12551950
  25. HSV-1 US3 protein kinase blocks the caspases that cleave BAD at either residue 56 or 61 predicted to render the protein more proapoptotic or at residue 156, which would inactivate the protein. PMID: 12743316
  26. proapoptotic BAD suppresses tumorigenesis in the lymphocyte lineage PMID: 12876200
  27. combination of proteomics, genetics and physiology indicates an unanticipated role for BAD in integrating pathways of glucose metabolism and apoptosis PMID: 12931191
  28. PP2A dephosphorylation of pSer112 is the key initiating event regulating the activation of BAD during interleukin-3 withdrawal-induced apoptosis PMID: 12944463
  29. BAD is a substrate for pim-2 oncogene proto-oncogene PMID: 12954615
  30. regulation of Bad phosphorylation plays an active role in mediating anti-IgM-induced apoptosis of immature B cells PMID: 14585539
  31. JNK is required for IL-3-mediated cell survival through phosphorylation and inactivation of the proapoptotic Bcl-2 family protein BAD. PMID: 14967141
  32. Data show that the Bcl-2 homology 3 domain-only protein, Bad, is involved in cell death following IL-7 withdrawal from D1 cells, an IL-7-dependent murine thymocyte cell line. PMID: 15123689
  33. 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 PMID: 15231831
  34. alteration of lipid rafts is an early event in the apoptotic cascade indirectly induced by interleukin-4 deprivation via PP1alpha activation, dephosphorylation of cytoplasmic Bad, and caspase activation PMID: 15634756
  35. Bad phosphorylation is not essential for PKB-mediated survival signaling in hemopoietic cells PMID: 15843895
  36. Pak1-dependent Raf-1 phosphorylation regulates its mitochondrial localization, phosphorylation of BAD, and Bcl-2 association PMID: 15849194
  37. BAD induces apoptosis upon detecting the coincidence of G2/M phase and growth factor deprivation PMID: 15901741
  38. phosphorylation of BAD Serine 128 exerts cell-specific effects on apoptosis PMID: 15907327
  39. All three Pim kinase family members predominantly phosphorylate Bad on Ser112 and in addition are capable of phosphorylating Bad on multiple sites associated with the inhibition of the pro-apoptotic function of Bad in HEK-293 cells PMID: 16403219
  40. cellular cholesterol biosynthesis is critical for the activation and maintenance of the Akt-Bad cell survival cascade in response to growth factors such as insulin. PMID: 16513830
  41. These data establish a connection between calcium overload and mitochondria-mediated death pathways in outer hair cells and also suggest a dual role for BAD. PMID: 16521126
  42. the interaction of BAD with membranes is tied to binding of 14-3-3 protein and activation and membrane translocation of Bcl-XL PMID: 16603546
  43. Study shows, using spectroscopic methods, that the BH3-only proteins Bim, Bad and Bmf are unstructured in the absence of binding partners. PMID: 16645638
  44. Bad was not required for cell death following IL-3 withdrawal, suggesting changes to phosphorylation of Bad play only a minor role in apoptosis. PMID: 16705087
  45. Both gonadotropin releasing hormone andepidermal growth factor (EGF) caused rapid phosphorylation of BAD. PMID: 16741954
  46. The proapoptotic protein Bad is a key player in cell survival decisions, and is regulated post-translationally by several signaling networks. PMID: 17535812
  47. 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 PMID: 18006502
  48. These findings provide genetic proof of the bifunctional activities of BAD in both beta cell survival and insulin secretion. PMID: 18223655
  49. Thr-201 phosphorylation of Bad by JNK1 is required for PFK-1 activation PMID: 18469002
  50. BAD is the only BCL-2 family protein expressed in parietal cells PMID: 18779780

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Subcellular Location Mitochondrion outer membrane, Cytoplasm
Protein Families Bcl-2 family
Database Links

KEGG: mmu:12015

STRING: 10090.ENSMUSP00000025910

UniGene: Mm.4387

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