Recombinant Human PDIA3 Protein (C-6His)

Name: Recombinant Human PDIA3 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1448NP
Availability: InStock

BL-1448NP: Greater than 85% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Protein Disulfide-Isomerase A3 is produced by our Mammalian expression system and the target gene encoding Ser25-Leu505 is expressed with a 6His tag at the C-terminus.
Accession	P30101
Synonym	PDIA3 protein;Protein disulfide-isomerase A3;58 kDa glucose-regulated protein;Disulfide isomerase ER-60;ER protein 57
Gene Background	PDIA3 protein is also known as Protein disulfide-isomerase A3. It is a protein that in humans is encoded by the PDIA3 gene.PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.
Molecular Mass	55.3 KDa
Apmol Mass	60 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 10% Glycerol, pH 7.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 85% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Subcellular Location	Endoplasmic reticulum. Endoplasmic reticulum lumen. Melanosome.
Protein Families	Protein disulfide isomerase family
Database References	HGNC: 4606 OMIM: 602046 KEGG: hsa:2923 STRING: 9606.ENSP00000300289 UniGene: Hs.591095
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

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
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
summarize available knowledge of ERp57's functions in subcellular compartments and the roles of dysregulated ERp57 in various diseases. PMID: 28723413
ERp57 is involved in sperm capacitation and spermatozoa-zona pellucida binding. PMID: 28175305
Thiol isomerase ERp57 is mobilized to the surface of activated platelets via a process that requires actin polymerization. PMID: 27079884
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
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
The interaction of different flavonoids with PDIA3 was investigated by quenching fluorescence analysis and the effects on protein activity were evaluated. PMID: 28044092
Upregulation of PDIA3 promotes ovarian cancer cell proliferation and migration. PMID: 27492604
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
Amyotrophic lateral sclerosis-linked PDIA3 mutations disrupt motor neuron connectivity. PMID: 26869642
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
ERp57 levels are increased in the airway epithelium of asthmatic patients and in mice with allergic airways disease. PMID: 26435004
LEDGF/p75 Overexpression Attenuates Oxidative Stress-Induced Necrosis and Upregulates the Oxidoreductase ERP57/PDIA3/GRP58 in Prostate Cancer PMID: 26771192
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
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
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
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
results suggested that ER chaperone PDIA3 plays a pivotal role in FFA-induced hepatocyte steatosis and apoptosis. PMID: 26214517
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
Its cross-reaction to GFAP antibodies seems to lead to a changed signaling in the cells triggering the protective effects. PMID: 25837926
PDIA3 and PDIA6 gene expression is a neoplasm aggressiveness marker in primary ductal breast cancer. PMID: 26125904
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
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
Suggest that ERp57-STAT3 regulation functions in radioresistance of laryngeal cancer. PMID: 25605256
Increased expression of PDIA3 is associated with tumor progression and the clinical behavior of gallbladder carcinoma. PMID: 23782473
Results demonstrated that Grp58 appears to regulate WNT signaling by targeting beta-catenin to augment cancer invasion. PMID: 25081282
Increased expression of the AGR2 and ERp57 is associated with cancer. [review] PMID: 24490732
ERp57 can regulate the expression of the mitochondrial calcium uniporter (MCU) and modulate mitochondrial calcium uptake PMID: 24815697
Low ERp57 expression independently predicts a poor outcome for patients with cervical cancer. PMID: 23957851
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
Tg "adduct B" was identified as primarily engaging the endoplasmic reticulum oxidoreductases ERp57 and protein disulfide isomerase PMID: 24599957
Low PDIA3 expression is associated with chemoresistant colon tumors. PMID: 23255428
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
ERp57 positively regulates H(+),K(+)-ATPase activity apart from its chaperoning function. PMID: 24188822
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
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
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
ERp57 regulates RalA signalling by acting as a redox-sensitive guanine-nucleotide dissociation inhibitor. PMID: 23226417
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
Downregulation of ER60 protease is associated with inhibition of cell proliferation in breast cancer cells in vitro. PMID: 22266712
PDIA3 may play in the progression of heart failure. PMID: 22503978
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
kinetic, extent and stability of the ERp57-CRT complex, using the surface plasmon resonance spectroscopy PMID: 21996511
ERp57 has roles in multiple components of platelet function and arterial thrombus formation. PMID: 22168334
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
PDIA3 and GRP78 are IL11 targets in invasive trophoblasts PMID: 21840908
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
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
Immunostaining for both ERp57-GFP and p65 after TNF-alpha treatment indicated that nuclear translocation of these two proteins occurs independently PMID: 21598303

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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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