Recombinant Human PEA15 Protein

Name: Recombinant Human PEA15 Protein
Brand: Beta LifeScience
SKU: BL-1870NP
Availability: InStock

BL-1870NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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

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Product Overview

Description	Recombinant Human Phosphoprotein Enriched in Astrocytes of 15 kDa is produced by our E.coli expression system and the target gene encoding Met1-Ala130 is expressed.
Accession	Q15121
Synonym	Astrocytic Phosphoprotein PEA-15; 15 kDa Phosphoprotein Enriched in Astrocytes; Phosphoprotein Enriched in Diabetes; PED; PEA15
Gene Background	Astrocyticphosphoprotein PEA-15 (PEA15) is a death effector domain (DED)-containing protein. PEA15 is mainly expressed in the central nervous system, principally in astrocytes. Increased PEA15 levels affect tumorigenesis and cancer progression. PEA15 is overexpressed in breast cancers and gliomas as well as in type 2 diabetes. PEA15 blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. PEA15 also inhibits RPS6KA3 activities by holding it in the cytoplasm. In addition, PEA15 inhibits both TNFRSF6 and TNFRSF1A mediated CASP8 activity and apoptosis. At present, PEA15 expression is also a significant prognostic marker in ovarian cancer.
Molecular Mass	15.3 KDa
Apmol Mass	12—16 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm. Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface.
Subcellular Location	Cytoplasm. Note=Associated with microtubules.
Database References	HGNC: 8822 OMIM: 603434 KEGG: hsa:8682 STRING: 9606.ENSP00000353660 UniGene: PMID: 29072691 PP4 regulates breast cancer cell survival and identifies a novel PP4c-PEA15 signalling axis in the control of breast cancer cell survival. PMID: 27317964 PEA15 expression was not significantly correlated with ovarian cancer antineoplastic drug resistance. PMID: 27669502 Data suggest the role of the phospholipase C epsilon-Protein kinase D-PEA15 protein-ribosomal S6 kinase-IkappaB-NF-kappa B pathway in facilitating inflammation and inflammation-associated carcinogenesis in the colon. PMID: 27053111 Integrin alpha5beta1 and p53 convergent pathways in the control of anti-apoptotic proteins PEA-15 and survivin in high-grade glioma. PMID: 26470725 High PED expression is associated with esophageal carcinoma. PMID: 25775393 The nuclear translocation of SApErk1/ 2 apart from PEA-15 as an important mechanism to reverse senescence phenotype. PMID: 25725291 Latent HCMV infection of CD34 + cells protects cells from FAS-mediated apoptosis through the cellular IL-10/PEA-15 pathway. PMID: 25957098 New therapeutic targets based around PEA-15 and its associated interactions are now being uncovered and could provide novel avenues for treatment strategies in multiple diseases. PMID: 24657708 PED/PEA-15 overexpression is sufficient to block hydrogen peroxide-induced apoptosis in Ins-1E cells through a PLD-1 mediated mechanism PMID: 25489735 Omi/HtrA2 overexpression promotes hepatocellular carcinoma cell apoptosis and the ped/pea-15 expression level causes this difference of the Omi/HtrA2 pro-apoptotic marker in the various hepatocellular carcinoma cell lines PMID: 25484138 Results suggest that neurochemical adaptations of brain FADD, as well as its interaction with PEA-15, could play a major role to counteract the known activation of the mitochondrial apoptotic pathway in major depression PMID: 25075716 Data show that phosphoprotein enriched in astrocytes of 15 kDa (PEA-15) influences dephosphorylation of epidermal growth factor receptor (EGFR) via extracellular signal-regulated kinases ERK1/2 sequestration in the cytoplasm. PMID: 25796184 Tumor suppressor PEA15 is a regulator of genome integrity and is an integral component of the DNA damage response pathway. PMID: 24710276 Up-regulated chaperone-mediated autophagy activity characteristic of most types of cancer cell enhances oncogenesis by shifting the balance of PED function toward tumor promotion. PMID: 24477641 Our findings highlight the importance of pPEA-15 as a promising target for improving the efficacy of paclitaxel-based therapy in ovarian cancer. PMID: 23543364 PEA-15 binding protects ERK2 from dephosphorylation, thus setting the stage for immediate ERK activity upon its release from the PEA-15 inhibitory complex PMID: 23575685 study demonstrates that the PEA-15 protein decreases proliferation, clonogenicity, and invasiveness, but increases resistance to apoptosis in colorectal carcinoma cells PMID: 23481023 The article hypothesizes that only unphosphorylated PEA-15 can act as a tumor-suppressor and that phosphorylation alters the interaction with binding partners to promote tumor development. PMID: 22694972 NMR chemical shift perturbation and backbone dynamic studies at the fast ps-ns timescale of PED/PEA-15, in its free form and in the complex with ERK2. PMID: 22820249 The 67 kD laminin receptor is a novel PED/PEA-15 interacting protein. PED/PEA-15 overexpression increases 67LR-mediated cell adhesion and migration to laminin and extracellular matrix invasion. PMID: 21895963 the solution death effector domain (DED) structure of the PED/PEA-15 protein, a representative member of DED subfamily, using traditional NMR restraints with the addition of residual dipolar coupling restraints was refined. PMID: 22732408 PEA15 impairs cell migration and correlates with clinical features predicting good prognosis in neuroblastoma PMID: 22213050 Data show that knockdown of PEA-15 expression resulted in reversal of selumetinib-sensitive cells to resistant cells, implying that PEA-15 contributes to selumetinib sensitivity. PMID: 22144664 Vitamin D3 signalling in the brain enhances the function of phosphoprotein enriched in astrocytes--15 kD (PEA-15) PMID: 19382910 The protective effect of melatonin is likely mediated, in part, by inhibition of peroxynitrate-mediated nitrosative stress, which in turn relieves imbalance of mitochondrial HtrA2-PED signaling and endothelial cell death. PMID: 21198825 There was no significant difference in the frequency of three marker haplotype in the PEA15 gene in patient with schizophrenia. PMID: 20537721 The expressions of PED/PEA-15 and XIAP are elevated in hepatocellular carcinoma as compared with adjacent tissues and normal tissues. PMID: 20979872 PED/PEA-15 modulates Coxsackievirus-adenovirus receptor expression and adenoviral entry, by sequestering ERK1/2. PMID: 20406097 provide molecular basis of the PED/PEA-15 functional interactions and detailed surface for the design and development of PED/PEA-15 binders PMID: 20825483 Data show that PED and Rac1 interact and that this interaction modulates cell migration/invasion processes in cancer cells through ERK1/2 pathway. PMID: 20648624 The results show that HNF-4alpha serves as a scaffold protein for histone deacetylase activities, thereby inhibiting liver expression of genes including PED. PMID: 20396999 PEA-15 promotes autophagy in glioma cells in a JNK-dependent manner PMID: 20452983 Data show that PEA-15 prevents ERK1/2 localization to the plasma membrane, thereby inhibiting ERK1/2-dependent threonine phosphorylation of FRS2alpha to promote activation of the ERK1/2 MAP kinase pathway. PMID: 20032303 Results suggest that PEA-15 expression is likely to be associated with the tumorigenesis of alignant pleural mesothelioma. PMID: 19771552 role of mitogen-activated protein kinase family members in anti-apoptotic function PMID: 11790785 role in modulating tumor necrosis factor-related apoptosis-inducing ligand-induced death-inducing signaling complex PMID: 11976344 interaction with p90 ribosomal S6 kinase isoenzyme regulates its activity PMID: 12796492 phosphorylation by Akt regulates the antiapoptotic function of PED/PEA-15 at least in part by controlling the stability of PED/PEA-15 PMID: 12808093 apoptosis following Omi/HtrA2 mitochondrial release is mediated by reduction in ped/pea-15 cellular levels PMID: 15328349 PEA-15 is inhibited by adenovirus E1A and has a role in ERK nuclear export and Ras-induced senescence PMID: 15331596 The mechanism controlling PEA-15 binding to ERK/MAPK or FADD, and its subsequent role in cell proliferation and apoptosis is reported. PMID: 15916534 Raised expression of the antiapoptotic protein pea-15 increases susceptibility to chemically induced skin tumor development PMID: 16044159 Human breast cancer cells express high levels of PED and that AKT activity regulates PED protein levels. AKT-dependent increase of PED expression levels represents a key molecular mechanism for chemoresistance in breast cancer. PMID: 16061647 cytoplasmic sequestration of the activated form of ERK by PEA15 enables the action of E1A in ovarian neoplasms PMID: 16170361 Akt overactivation prevents the nuclear translocation of ERK1/2 and the AngII-induced proliferation through interaction with and stabilization of endogenous PEA-15. PMID: 16822839 These data reveal a new function for PEA-15 in the inhibitory control of astrocyte motility through a PKC delta-dependent pathway involving the constitutive expression of a catalytic fragment of PKC delta. PMID: 16987961 PEA15 overexpression represents a common defect in first degree relatives of patients with type 2 diabetes and is correlated with reduced insulin sensitivity in these individuals. PMID: 17021921 TPA increases PED/PEA-15 expression at the post-translational level by inducing phosphorylation at serine 116 and preventing ubiquitinylation and proteosomal degradation PMID: 17227770 In addition to sequestering protein kinases ERK1/2 in the cytoplasm, PEA-15 has the potential to modulate the activity of ERK2 in cells by competing directly with proteins that contain D-recruitment sites. PMID: 17658892

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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.

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