Recombinant Mouse Phorbol-12-Myristate-13-Acetate-Induced Protein 1 (PMAIP1) Protein (His)

Name: Recombinant Mouse Phorbol-12-Myristate-13-Acetate-Induced Protein 1 (PMAIP1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-11184P
Availability: InStock

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Pmaip1.

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Product Overview

Description	Recombinant Mouse Phorbol-12-Myristate-13-Acetate-Induced Protein 1 (PMAIP1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9JM54
Target Symbol	PMAIP1
Synonyms	Pmaip1; NoxaPhorbol-12-myristate-13-acetate-induced protein 1; Protein Noxa
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MPGRKARRNAPVNPTRAELPPEFAAQLRKIGDKVYCTWSAPDITVVLAQMPGKSQKSRMRSPSPTRVPADLKDECAQLRRIGDKVNLRQKLLNLISKLFNLVT
Expression Range	1-103aa
Protein Length	Full Length
Mol. Weight	15.6 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target Function	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.
Subcellular Location	Mitochondrion.
Protein Families	PMAIP1 family
Database References	KEGG: mmu:58801 STRING: 10090.ENSMUSP00000025399 UniGene: Mm.271878
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

Gene Functions References

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
data suggest that in the context of CLL NOXA may function as an oncomodulator PMID: 27479816
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
Noxa is involved in X-ray-induced lung injury. PMID: 27862899
Fluorizoline bind to prohibitin, inducing mitochondrial apoptotic pathway through NOXA and BIM upregulation. PMID: 26497683
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
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
Induction of noxa does not influence ischemic neuronal injury. PMID: 25299781
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
Noxa controls expansion of erythroid precursors and RBC production in vivo under conditions of induced anemia. PMID: 23975731
Noxa is targeted to the mitochondrial membrane where it neutralises Mcl-1 via its C-terminal BH3-domain. PMID: 23733106
Induction of senescence was only impaired in cells from the p21-/- puma-/- noxa-/- mice but abrogated in cells from the p53-/- mice. PMID: 23665218
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
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
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
The Bcl-2 proteins Noxa and Bcl-xL co-ordinately regulate oxidative stress-induced apoptosis. PMID: 22380599
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
Function of Noxa was at least in part neutralization of induced myeloid leukemia cell differentiation protein (Mcl-1) in neutrophils and progenitors. PMID: 21660046
in response to DNA-damage, Noxa efficiently induces apoptosis by "release" of Puma from Mcl-1. PMID: 21945433
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
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
This study reveals Noxa to be a crucial regulator of osteoclast apoptosis. PMID: 21689638
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
Here we showed that upon T cell activation, the proapoptotic molecule Noxa (encoded by Pmaip1) and its antagonist Mcl-1 were induced PMID: 20620942
Noxa(-/-) mice showed resistance to X-ray irradiation-induced gastrointestinal death, accompanied with impaired apoptosis. PMID: 12952892
Noxa is a major executor for axotomy-induced motor neuron death in the adult mouse, as a mediator located downstream of p53. PMID: 15703398
Noxa and Puma are important regulators of genotoxin-induced telencephalic neuron precursor cell death PMID: 16822983
functional eIF2alpha played an essential role in PS-341-induced Noxa expression PMID: 16928686
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
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
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
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
Bmi1 controls memory CD4(+) Th1/Th2 cell survival and functions through the direct repression of the Noxa gene. PMID: 18411339
The structure of the BH3 domains from the p53-inducible BH3-only protein Noxa in complex with Mcl-1 is reported. PMID: 18589438
Pmaip1 protein deficiency alone also increased B-lineage cells but did not accelerate lymphomagenesis. PMID: 19148184
Noxa-dependent cell death might contribute to particulate matter-induced alveolar epithelial dysfunction and the resulting inflammatory response PMID: 19237507

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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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