Recombinant Human Protein Disulfide-Isomerase A3 (PDIA3) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-03996P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Protein Disulfide-Isomerase A3 (PDIA3) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-03996P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description Recombinant Human Protein Disulfide-Isomerase A3 (PDIA3) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P30101
Target Symbol PDIA3
Synonyms 58 kDa glucose regulated protein; 58 kDa glucose-regulated protein; 58 kDa microsomal protein; Disulfide isomerase ER 60; Disulfide isomerase ER-60; Endoplasmic reticulum resident protein 57; Endoplasmic reticulum resident protein 60; ER p57; ER protein 57; ER protein 60; ERp 57; ERp57; ERp60; ERp61; Glucose Regulated Protein 58 Kd; GRP 57; GRP 58; GRP57; HsT17083; p58; PDIA 3; PDIA3; PDIA3_HUMAN; Phospholipase C alpha; PI PLC; Protein disulfide isomerase A3; Protein disulfide isomerase family A member 3; Protein disulfide-isomerase A3
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence SDVLELTDDNFESRISDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASIVGFFDDSFSEAHSEFLKAASNLRDNYRFAHTNVESLVNEYDDNGEGIILFRPSHLTNKFEDKTVAYTEQKMTSGKIKKFIQENIFGICPHMTEDNKDLIQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDAGHKLNFAVASRKTFSHELSDFGLESTAGEIPVVAIRTAKGEKFVMQEEFSRDGKALERFLQDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKLNPKKYEGGRELSDFISYLQREATNPPVIQEEKPKKKKKAQEDL
Expression Range 25-505aa
Protein Length Full Length of Mature Protein
Mol. Weight 59.3 kDa
Research Area Signal Transduction
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

Subcellular Location Endoplasmic reticulum. Endoplasmic reticulum lumen. Melanosome.
Protein Families Protein disulfide isomerase family
Database References
Tissue Specificity Detected in the flagellum and head region of spermatozoa (at protein level). Expressed in liver, stomach and colon (at protein level). Expressed in gastric parietal cells and chief cells (at protein level).

Gene Functions References

  1. Data suggest that disulfide bond switch in allosteric activation/inactivation of TGM2 is example of post-translational redox regulation that is reversibly and allosterically modulated by two proteins (ERp57 and TRX). (TGM2 = transglutaminase 2; ERp57 = endoplasmic reticulum resident protein 57; TRX = thioredoxin-1) PMID: 29305423
  2. Study demonstrated that the expression of PDIA3 is frequently upregulated at the mRNA and protein levels in diffuse gliomas. Its high expression was significantly correlated with high Ki-67, more TP53 mutations and poor survival outcome. These findings imply that high expression of PDIA3 plays an important role in diffuse glioma progression. PMID: 29207176
  3. summarize available knowledge of ERp57's functions in subcellular compartments and the roles of dysregulated ERp57 in various diseases. PMID: 28723413
  4. ERp57 is involved in sperm capacitation and spermatozoa-zona pellucida binding. PMID: 28175305
  5. Thiol isomerase ERp57 is mobilized to the surface of activated platelets via a process that requires actin polymerization. PMID: 27079884
  6. Findings suggested that miR-330-5p represents a potential tumor-suppressive miRNA and plays an important role in cutaneous malignant melanoma progression by suppressing TYR and PDIA3 expression. PMID: 27363653
  7. Our study found increased expression of ERp57 in chronic hepatitis B -hepatocellular carcinoma (HBV-HCC) genesis. Such altered expression could be related to HBV infection and high ERp57 expression may lead to poor prognosis of HBV-HCC patients. PMID: 28373975
  8. The interaction of different flavonoids with PDIA3 was investigated by quenching fluorescence analysis and the effects on protein activity were evaluated. PMID: 28044092
  9. Upregulation of PDIA3 promotes ovarian cancer cell proliferation and migration. PMID: 27492604
  10. Data show that knockdown of endoplasmic reticulum resident protein 57 (ERP57) expression resulted in increase in shikonin induced apoptosis, and suggest that ERP57 might be a therapeutic option for the treatment of acute myeloid leukemia. PMID: 27415599
  11. Amyotrophic lateral sclerosis-linked PDIA3 mutations disrupt motor neuron connectivity. PMID: 26869642
  12. These data indicate that the presence of autoantibodies to PDIA3 favors the development of an efficient and specific T-cell response against PDIA3 in colorectal cancer patients. PMID: 26772958
  13. ERp57 levels are increased in the airway epithelium of asthmatic patients and in mice with allergic airways disease. PMID: 26435004
  14. LEDGF/p75 Overexpression Attenuates Oxidative Stress-Induced Necrosis and Upregulates the Oxidoreductase ERP57/PDIA3/GRP58 in Prostate Cancer PMID: 26771192
  15. it is possible that the vimentin and PDIA3 could be the candidate biomarkers specific to Achyranthes saponin therapy for rheumatoid arthritis in synovial membrane. PMID: 26724776
  16. ERp57 specifically contributes to peripheral nerve regeneration, whereas its activity is dispensable for the survival of a specific neuronal population of the central nervous system. PMID: 26361352
  17. Data suggest that regulation of PDIA3 (protein disulfide isomerase associated 3 protein) expression by microRNA-330-5p is important in maintaining hair cycle through regulation of proliferation and migration capability of keratinocytes. PMID: 26402295
  18. miR148a inhibits the proliferation and promotes paclitaxelinduced apoptosis of ovarian cancer cells, and this may be partly attributed to direct targeting of PDIA3. PMID: 26004124
  19. results suggested that ER chaperone PDIA3 plays a pivotal role in FFA-induced hepatocyte steatosis and apoptosis. PMID: 26214517
  20. The sPLA2-hPDI model constitutes a valuable tool to facilitate further insights into this process and into the (patho)physiology of sPLA2s in relation to their action intracellularly. PMID: 25763817
  21. Its cross-reaction to GFAP antibodies seems to lead to a changed signaling in the cells triggering the protective effects. PMID: 25837926
  22. PDIA3 and PDIA6 gene expression is a neoplasm aggressiveness marker in primary ductal breast cancer. PMID: 26125904
  23. study identifies ERp57 as a new modulator of PrP levels and may help with understanding the consequences of ERp57 up-regulation observed in human disease PMID: 26170458
  24. Reported increased expression of ALDH3A1, PDIA3, and PRDX2 in pterygia using a proteomic approach. These proteins are presumed to have a protective role against oxidative stress-induced apoptosis. PMID: 25221425
  25. Suggest that ERp57-STAT3 regulation functions in radioresistance of laryngeal cancer. PMID: 25605256
  26. Increased expression of PDIA3 is associated with tumor progression and the clinical behavior of gallbladder carcinoma. PMID: 23782473
  27. Results demonstrated that Grp58 appears to regulate WNT signaling by targeting beta-catenin to augment cancer invasion. PMID: 25081282
  28. Increased expression of the AGR2 and ERp57 is associated with cancer. [review] PMID: 24490732
  29. ERp57 can regulate the expression of the mitochondrial calcium uniporter (MCU) and modulate mitochondrial calcium uptake PMID: 24815697
  30. Low ERp57 expression independently predicts a poor outcome for patients with cervical cancer. PMID: 23957851
  31. ERP57 was excreted in the early stages of chronic kidney disease, and its level in urine correlated with the degree of renal fibrosis, suggesting that the secretion of ERP57 represents one of the first signs of renal fibrosis onset and progression. PMID: 23781031
  32. Tg "adduct B" was identified as primarily engaging the endoplasmic reticulum oxidoreductases ERp57 and protein disulfide isomerase PMID: 24599957
  33. Low PDIA3 expression is associated with chemoresistant colon tumors. PMID: 23255428
  34. ERp57 appears as a multifunctional chaperone that can regulate diverse biological processes to maintain the homeostasis of breast cancer cells and promote the development of bone metastasis. PMID: 23625662
  35. ERp57 positively regulates H(+),K(+)-ATPase activity apart from its chaperoning function. PMID: 24188822
  36. Platelets lacking ERp57 have defective activation of the alphaIIbbeta3 integrin and platelet aggregation. The defect in aggregation was corrected by the addition of exogenous ERp57, implicating surface ERp57 in platelet aggregation. PMID: 24030382
  37. We postulate that apoB cleavage by ER-60 within the ER lumen could facilitate proteasomal degradation of the C-terminus of translocationally-arrested apoB. PMID: 23827315
  38. Nuclear ERp57 interacts in vivo with DNA fragments in melanoma cells and is potentially involved in the transcriptional regulation of its target genes. PMID: 23587917
  39. ERp57 regulates RalA signalling by acting as a redox-sensitive guanine-nucleotide dissociation inhibitor. PMID: 23226417
  40. Data indicate that the peptide-loading complex (PLC) consists maximally of 2x tapasin-ERp57/MHC I per TAP complex, but one tapasin-ERp57/MHC I in the PLC is essential and sufficient for antigen processing. PMID: 22923333
  41. Downregulation of ER60 protease is associated with inhibition of cell proliferation in breast cancer cells in vitro. PMID: 22266712
  42. PDIA3 may play in the progression of heart failure. PMID: 22503978
  43. the vitamin D receptor (VDR) and ERp57 are critical components for actions of 1,25 dihydroxy vitamin D 3 against DNA damage, but the VDR does not require normal DNA binding or classical ligand binding to mediate photoprotection. PMID: 22322599
  44. kinetic, extent and stability of the ERp57-CRT complex, using the surface plasmon resonance spectroscopy PMID: 21996511
  45. ERp57 has roles in multiple components of platelet function and arterial thrombus formation. PMID: 22168334
  46. These results suggest that increased level of hnRNP-H and PDIA3 expression in Dengue virus infected THP1 cells assist in the viral replication by suppressing the TNF-alpha production. PMID: 22207023
  47. PDIA3 and GRP78 are IL11 targets in invasive trophoblasts PMID: 21840908
  48. Grp58 is highly expressed in patients with serious cervical stromal penetration, and further supports the theory that Grp58 is critical for cervical AD progression. PMID: 21917082
  49. ERp57 participates in signal transduction from the cell surface, in regulatory processes taking place in the nucleus, and in multimeric protein complexes involved in DNA repair. (Review) PMID: 21837552
  50. Immunostaining for both ERp57-GFP and p65 after TNF-alpha treatment indicated that nuclear translocation of these two proteins occurs independently PMID: 21598303

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

Recently viewed