Recombinant Human PTGES3 Protein

Beta LifeScience SKU/CAT #: BL-1842PS

Recombinant Human PTGES3 Protein

Beta LifeScience SKU/CAT #: BL-1842PS
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Product Overview

Tag N/A
Host Species Human
Synonym TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.
Background PTGES3 takes part as a cochaperone and is involved in signal transduction. PTGES3 is a molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexess. PTGES3 is necessary for appropriate functioning of the glucocorticoid and other steroid receptors.PTGES3 localizes to genomic response elements in a hormone-dependent method and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.
Description Recombinant Human PTGES3 expressed in E.Coli is a single,non-glycosylated polypeptide chain containing 160a.a. (1-160 a.a.) and having a molecular weight of 18.6 kDa.PTGES3 is purified by convential chromatogrpahy techniques.
Source E.coli
AA Sequence MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE.
Purity >95.0% as determined by SDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Formulation The PTGES3 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT & 10% Glycerol.
Stability Recombinant protein is stable for 12 months at -70°C
Usage For Research Use Only
Storage Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

Target Details

Target Function Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway.
Subcellular Location Cytoplasm.
Protein Families P23/wos2 family
Database References

Gene Functions References

  1. The Hsp90 independence of the interaction between p23 and p53 DNA-binding domain, together with the competition of p23 versus DNA for p53, raises the intriguing possibility that p23, like other small charged proteins, may affect p53 in hitherto unknown ways. PMID: 29334217
  2. dysregulation of GR, MR, FKBP5, and PTGES3 in autistic spectrum disorder (ASD) and suggest a possible role of inflammation in altered GR function in ASD. PMID: 25912394
  3. increased p23 expression may allow cells to acquire a more aggressive phenotype, contributing to disease progression PMID: 25241147
  4. Even if p23 predominantly binds the Hsp90 dimer, p23 is also able to interact with Hsp90 oligomers, shifting the Hsp90 dimer-oligomers equilibrium toward dimer. PMID: 26151834
  5. FKBP4, p23, and Aha1 cooperatively regulate the progression of hAgo2 through the chaperone cycle. PMID: 23741051
  6. p23 recruits PHD2 to the HSP90 machinery to facilitate HIF-1alpha hydroxylation PMID: 23413029
  7. The effects of p23 on androgen receptor (AR) activity are at least partly HSP90 independent, a mutant form of p23, unable to bind HSP90, increases AR activity. PMID: 22899854
  8. p23 co-chaperone protects the aryl hydrocarbon receptor from degradation PMID: 22759865
  9. As an anti-apoptotic factor, p23 is able to be a potential target for anti-leukemic therapy. PMID: 22677230
  10. Patients with severe Alzheimer disease displayed a consistent reduction in brain p23 levels. Cleavage product p19 was not seen in AD brain samples. PMID: 21691801
  11. a small increase in the expression of p23 amplifies ER-binding genome wide and, in combination with ER, elicits an invasive phenotype in breast cancer PMID: 22074947
  12. In cytosol only one protein called p23 hsp90 binds to Bax but the binding protein does not affect the subcellular localization and pro-apoptotic activity of Bax. PMID: 22277657
  13. Data show that cytosolic prostaglandin E synthase 2 is found in microglia, neurons, and endothelium of control human middle frontal gyrus and that its levels decrease in pyramidal cells of Alzheimer's disease brains. PMID: 19001348
  14. The p23 cochaperone of Hsp90, which plays a major role in glucocorticoid receptor folding and function, associates with influenza virus polymerase. PMID: 21853119
  15. the N-terminal domain of human Hsp90 triggers binding to the cochaperone p23 PMID: 21183720
  16. High levels of Hsp90 cochaperone p23 promote tumor progression in breast cancer by increasing lymph node metastases and drug resistance. PMID: 20847343
  17. the interaction of the Hsp90-p23 complex with hTERT is critical for regulation of the nuclear localization of telomerase PMID: 19751963
  18. Data show that the small molecule celastrol inhibits the Hsp90 chaperoning machinery by inactivating the co-chaperone p23, resulting in a more selective destabilization of steroid receptors. PMID: 19996313
  19. localizes in vivo to genomic response elements in a hormone-dependent manner, disrupting receptor-mediated transcriptional activation in vivo and in vitro PMID: 12077419
  20. TEP1, hTR, hsp90, p23, and dyskerin remained at high and unchanged levels throughout up- or down regulation of telomerase activity. PMID: 12135483
  21. acts in vivo to stabilize hsp90 binding to client protein [hsp90 cochaperone p23] PMID: 14507910
  22. A role proposed for co-chaperone p23 is to lock individual subunits of Hsp90 in an ATP-dependent conformational state that has a high affinity for client proteins. PMID: 16403413
  23. p23 differentially regulates ER target genes and is involved in the control of distinct cellular processes in breast tumor development PMID: 16809759
  24. Carbonyl reductase-1 (CBR1), microsomal prostaglandin E synthase-1 and 2 (mPGES-1, mPGES-2), cytosolic prostaglandin E synthase (cPGES), aldoketoreductase (AKR1C1) and prostaglandin F synthase (AKR1C3) were all expressed in hair follicles. PMID: 17697149
  25. all three terminal prostaglandin synthases, mPGES-1, mPGES-2, and cPGES, are over-expressed in human gliomas PMID: 19347995
  26. Overexpression of Delta p23 resulted in a decrease in hTERT levels, and a down-regulation in telomerase activity. PMID: 19740745

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.

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