Recombinant Mouse Phorbol-12-myristate-13-acetate-induced protein 1 (Pmaip1)

Code
MSDS
Size Pls inquire
Source
Conjugate
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Product Details

Abbreviation
Pmaip1
Purity
>85% (SDS-PAGE)
Target Names
Pmaip1
Uniprot NO.
Species
Mus musculus (Mouse)
Source
Yeast
Expression Region
1-103
Target Protein Sequence
MPGRKARRNA PVNPTRAELP PEFAAQLRKI GDKVYCTWSA PDITVVLAQM PGKSQKSRMR SPSPTRVPAD LKDECAQLRR IGDKVNLRQK LLNLISKLFN LVT
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
full length protein
Tag Info
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.
Storage
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.
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.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Customer Reviews and Q&A

 Customer Reviews

Target Background

Function(From Uniprot)
Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BIM/BCL2L11 for binding to MCL1 and can displace BIM/BCL2L11 from its binding site on MCL1. Competes with BAK1 for binding to MCL1 and can displace BAK1 from its binding site on MCL1.
Gene References into Functions
  1. Findings indicate that prospero homeobox 1 (Prox1) regulated the differentiation of oligodendrocyte precursor cells via the regulation of phorbol-12-myristate-13-acetate-induced protein 1 (NOXA). PMID:29931031
  2. data suggest that in the context of CLL NOXA may function as an oncomodulator PMID:27479816
  3. knockdown of pmaip1 mimicked the phenotype of ph8(-/Y) by showing the decreased apoptosis during early differentiation of embryonic stem cells and promoted mesodermal and cardiac commitment. PMID:26866517
  4. Noxa is involved in X-ray-induced lung injury. PMID:27862899
  5. Fluorizoline bind to prohibitin, inducing mitochondrial apoptotic pathway through NOXA and BIM upregulation. PMID:26497683
  6. Overall, these data reveal a Noxa-mediated signaling pathway that couples lysosomal membrane permeabilization with mitochondrial outer membrane permeabilization and ultimate apoptosis during oxidative stress. PMID:23770082
  7. by preventing the consumption of IL-15, Bim limits the role of Noxa and Puma in causing the death of effector cells with less memory potential. PMID:25124553
  8. Induction of noxa does not influence ischemic neuronal injury. PMID:25299781
  9. the current findings indicate that Noxa is a novel regulator of early mitosis before 75% epiboly stage when it translates into a key mediator of apoptosis in subsequent embryogenesis. PMID:24608793
  10. Noxa controls expansion of erythroid precursors and RBC production in vivo under conditions of induced anemia. PMID:23975731
  11. Noxa is targeted to the mitochondrial membrane where it neutralises Mcl-1 via its C-terminal BH3-domain. PMID:23733106
  12. Induction of senescence was only impaired in cells from the p21-/- puma-/- noxa-/- mice but abrogated in cells from the p53-/- mice. PMID:23665218
  13. In acute viral infection, Noxa(-/-) mice had increased memory pool size & diversity but less cross-reactivity. Reduced T-cell apoptosis during chronic activation led to severe organ pathology & early death. PMID:23277490
  14. Results suggest that compromised induction of Unfolded Protein Response (UPR) and increased NOXA expression contributes to hypersensitivity of PERK(-/-) MEFs to ER stress-induced apoptosis. PMID:23068609
  15. The Noxa protein, even in combination with Bik, is not a potent suppressor of c-Myc-driven tumourigenesis or critical for chemotherapeutic drug-induced killing of Myc-driven tumours. PMID:22573037
  16. The Bcl-2 proteins Noxa and Bcl-xL co-ordinately regulate oxidative stress-induced apoptosis. PMID:22380599
  17. Data show that Noxa is induced in activated B cells, and its ablation provides a survival advantage both in vitro and in vivo. PMID:22144184
  18. Function of Noxa was at least in part neutralization of induced myeloid leukemia cell differentiation protein (Mcl-1) in neutrophils and progenitors. PMID:21660046
  19. in response to DNA-damage, Noxa efficiently induces apoptosis by "release" of Puma from Mcl-1. PMID:21945433
  20. Here the authors demonstrate that Noxa null baby mouse kidney cells are deficient in normal cytopathic response to lytic viruses, and that reconstitution of the knockout cells with wild-type Noxa restored normal cytopathic responses. PMID:21742363
  21. Investigation of downstream effectors used by tumor protein p53 to impair T cell lineage development finds many p53 targets are induced in ribosomal protein Rpl22-deficient thymocytes, including Noxa, Bax, p21waf, miR-34a, and PUMA. PMID:21690328
  22. This study reveals Noxa to be a crucial regulator of osteoclast apoptosis. PMID:21689638
  23. define the first physiologic function for Noxa and suggest that by repressing Noxa, induction of G arrest by p18INK4c bypasses a homeostatic cell-cycle checkpoint in intermediate plasma cells (iPCs) for PC differentiation PMID:21163929
  24. Here we showed that upon T cell activation, the proapoptotic molecule Noxa (encoded by Pmaip1) and its antagonist Mcl-1 were induced PMID:20620942
  25. Noxa(-/-) mice showed resistance to X-ray irradiation-induced gastrointestinal death, accompanied with impaired apoptosis. PMID:12952892
  26. Noxa is a major executor for axotomy-induced motor neuron death in the adult mouse, as a mediator located downstream of p53. PMID:15703398
  27. Noxa and Puma are important regulators of genotoxin-induced telencephalic neuron precursor cell death PMID:16822983
  28. functional eIF2alpha played an essential role in PS-341-induced Noxa expression PMID:16928686
  29. Puma and Noxa, the well-known p53-inducible proapoptotic members of the Bcl-2 family, differentially participate in dual pathways of the induction of apoptosis PMID:17024184
  30. The deleterious function in cerebral ischemia is specific for the NF-kappa B subunit RelA and may be mediated through Bim and Noxa. PMID:17167080
  31. Collectively, these results demonstrate that UVR activates the Bcl-2-regulated apoptotic pathway predominantly through activation of Noxa and, depending on cellular context, Puma. PMID:17283183
  32. A significant suppression of Noxa expression by the Suture may be a major reason why nerve suture induces survival and regeneration of nerve-injured motor neurons. PMID:17518541
  33. Bmi1 controls memory CD4(+) Th1/Th2 cell survival and functions through the direct repression of the Noxa gene. PMID:18411339
  34. The structure of the BH3 domains from the p53-inducible BH3-only protein Noxa in complex with Mcl-1 is reported. PMID:18589438
  35. Pmaip1 protein deficiency alone also increased B-lineage cells but did not accelerate lymphomagenesis. PMID:19148184
  36. Noxa-dependent cell death might contribute to particulate matter-induced alveolar epithelial dysfunction and the resulting inflammatory response PMID:19237507

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Subcellular Location
Mitochondrion.
Protein Families
PMAIP1 family
Tissue Specificity
Detected in thymocytes after irradiation with X-rays. Not detectable in untreated thymocytes (at protein level). Detected in embryonic neural precursor cells of the telencephalon Constitutively expressed at low levels in adult brain, testis, thymus, splee
Database Links
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