Recombinant Human Protein Phosphatase 1 Regulatory Subunit 15A (PPP1R15A) Protein (His)

Name: Recombinant Human Protein Phosphatase 1 Regulatory Subunit 15A (PPP1R15A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00022P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Protein Phosphatase 1 Regulatory Subunit 15A (PPP1R15A) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O75807
Target Symbol	PPP1R15A
Synonyms	Apoptosis associated protein; GADD 34; Growth arrest and DNA damage inducible 34; Growth arrest and DNA damage-inducible protein GADD34; Myeloid differentiation primary response protein MyD116 homolog; Ppp1r15a; PR15A_HUMAN; Protein phosphatase 1 regulatory (inhibitor) subunit 15A; Protein phosphatase 1 regulatory subunit 15A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFLKAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFLKAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPPPPWAPPRLPLRLQRRLKRPETPTHDPDPETPLKARKVRFSEKVTVHFLAVWAGPAQAARQGPWEQLARDRSRFARRITQAQEELSPCLTPAARARAWARLRNPPLAPIPALTQTLPSSSVPSSPVQTTPLSQAVATPSRSSAAAAAALDLSGRRG
Expression Range	40-674aa
Protein Length	Partial
Mol. Weight	73.2 kDa
Research Area	Cell Biology
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	Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'.
Subcellular Location	Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families	PPP1R15 family
Database References	HGNC: 14375 OMIM: 611048 KEGG: hsa:23645 STRING: 9606.ENSP00000200453 UniGene: PMID: 29632131 Compared with normal controls, the wild type TT and allele T of rs611251 of PPP1R15A showed higher frequency in gastric carcinoma, nasopharyngeal carcinomas and lymphomas. PMID: 29186961 Inhibition of IRE1 modifies the hypoxic regulation of GADD34 family gene expression in cultured glioma cells. PMID: 29227599 GADD34 constitutes a mechanistic link between endoplasmic reticulum stress and mTOR inactivation, therefore promotes cell survival during endoplasmic reticulum stress. PMID: 27992581 reduction of GADD34 expression significantly suppressed tumor, and resulted in decreased accumulation of MDSCs and T-cells, and inhibition of GADD34 reduced secretion of vascular epithelial growth factor alpha and transforming growth factor beta by MDSCs PMID: 27630304 ANXA11 rs1049550 and PPP1R15A rs557806 may improve the identification of mCRC patients sensitive to bevacizumab regimens, and further validation is required in large cohorts PMID: 27177629 Data of this study strengthen the evidence of an unfolded protein response during the course of RA and provide an insight of the potential interest in GADD34 as a relevant marker for RA. PMID: 26829377 The results suggest that dephosphorylation of eIF2a by GADD34 plays an important role in doxorubicin resistance of MCF-7/ADR cells. PMID: 26743901 The reactive oxygen species-generating NADPH oxidase-4 (Nox4) is induced downstream of ATF4, binds to a PP1-targeting subunit GADD34 at the endoplasmic reticulum, and inhibits PP1 activity to increase eIF2alpha phosphorylation and ATF4 levels. PMID: 26742780 stress pathways lead to the induction of the protein GADD34, which appears to provide protection against the toxic effects of the secreted virulence factors in Pseudomonas aeruginosa infection PMID: 26083346 The data highlight independent interactions of PP1 and eIF2alpha with GADD34, demonstrating that GADD34 functions as a scaffold both in vitro and in cells PMID: 26095357 GADD34 may play a neuroprotective role against amyloid-beta toxicity. PMID: 25204313 GADD34 enhances autophagy and suppresses apoptosis stimulated by LPS combined with amino acid deprivation through regulation of mTOR signaling pathway in macrophages. PMID: 25659802 Data indicate that protein phosphatase 1 subunit GADD34 directly interacts with eukaryotic translation initiation factor 2 subunit alpha (eIF2alpha). PMID: 26100893 GADD34 was increased in neurons of human Alzheimer's disease (AD) brains. Additionally, this finding was also observed in oligodendrocytes in human AD brains. GADD34 could be a therapeutic target for preventing ER stress in neuronal cells in AD. PMID: 26142647 GADD34 promotes cell survival and adaptation to increased extracellular osmolarity by increasing the uptake of small neutral amino acids via the amino acid transporter SNAT2. PMID: 26041779 Nuclear export of HTLV-1 basic leucine-zipper factor (HBZ) is essential for its interaction with GADD34 and increased phosphorylation of S6 kinase, which is an established downstream target of the mTOR pathway. PMID: 23708656 GADD34 phosphorylation on tyrosine 262 modulates endoplasmic reticulum stress signaling and cell fate. PMID: 24092754 Low GADD34 expression is associated with malignant mesothelioma. PMID: 23412101 the association of with ER modulates intracellular trafficking and proteasomal degradation of GADD34, and in turn, its ability to modify ER morphology PMID: 21518769 The data suggest that EBNA3C interacts with Gadd34, activating the upstream component of the UPR-unfolded protein response (eIF2alpha phosphorylation) while preventing downstream UPR events (XBP1 activation and ATF6 cleavage). PMID: 20040105 The role of the PP1/GADD34 complex in the molecular cascade is to the translocation of CRT to the outer leaflet of the plasma membrane. PMID: 19901557 SNF5/INI1 protein facilitates the function of the growth arrest and DNA damage-inducible protein and modulated protein phosphatase-1 activity PMID: 12016208 GADD 34 may play an important role in melanoma progression PMID: 12168790 the GADD34-mediated cellular stress response is suppressed by BAG-1 PMID: 12724406 Human Gadd34 lacking the viral homology domain does not interfere with normal Gadd34-induced apoptosis in cultured cells. This suggests that viral similarity sequences may be required for Gadd34-mediated functions other than apoptosis. PMID: 12813455 These findings suggest that phenethylisothiocyanate creates an oxidative cellular environment that induces DNA damage and GADD153, 34 and 45 gene activation, which in turn helps trigger apoptosis PMID: 14635187 GADD34-PP1c recruited by Smad7 inhibits TGFbeta-induced cell cycle arrest. PMID: 14718519 the up-regulation of GADD34 in response to global ischaemia in the human brain plus its influence on protein synthesis and DNA repair suggests that this protein may have the potential to influence cell survival PMID: 15541008 GADD34 may perform important functions in cardiac tissue in response to ischaemia. PMID: 16337513 During conditions of cell stress, GADD34 forms a stable complex with tuberous sclerosis complex (TSC) 1/2, causes TSC2 dephosphorylation, and inhibits signaling by mammalian target of the rapamycin (mTOR). PMID: 17273797 mechanisms that control GADD34 levels in human cells PMID: 18794359 GADD34 translation is regulated by a unique 5'UTR uORF mechanism to ensure proper GADD34 expression during eIF2alpha phosphorylation PMID: 19131336 Infectious bronchitis virus has developed a combination of two mechanisms, i.e., blocking PKR activation and inducing GADD34 expression, to maintain de novo protein synthesis in IBV-infected cells and, meanwhile, to enhance viral replication. PMID: 19776135

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.