PDIA3 Human
Protein Disulfide Isomerase A3 Human Recombinant
Cat. No.
BT915
Source
Escherichia Coli.
Synonyms
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
PDIA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 518 amino acids (25-505 a.a.) and having a molecular wieght of 58.5 kDa. The PDIA3 is fused to 37 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Introduction
PDIA3, a protein disulfide isomerase, resides in the endoplasmic reticulum and collaborates with chaperones calreticulin and calnexin to facilitate proper folding of newly synthesized glycoproteins. This interaction with lectins forms complexes that assist in protein folding by promoting disulfide bond formation in glycoprotein substrates. PDIA3 expression is observed in the lumbar spinal cord of rats subjected to peripheral lesions during the neonatal period. Additionally, it interacts with the thiazide-sensitive sodium-chloride cotransporter in the kidney and is upregulated in response to glucose deprivation. Furthermore, PDIA3 is an integral component of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which plays a crucial role in the formation of the final antigen conformation and its subsequent export from the endoplasmic reticulum to the cell surface.
Description
Recombinant human PDIA3, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 518 amino acids (residues 25-505). With a molecular weight of 58.5 kDa, this PDIA3 variant includes a 37 amino acid His-Tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile filtered.
Formulation
The PDIA3 protein solution is formulated in a buffer containing 20mM Tris-HCl (pH 8), 1mM DTT, 0.1M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of PDIA3 is determined to be greater than 95.0% by SDS-PAGE analysis.
Synonyms
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMSDV LELTDDNFES RISDTGSAGL MLVEFFAPWC GHCKRLAPEY EAAATRLKGI VPLAKVDCTA NTNTCNKYGV SGYPTLKIFR DGEEAGAYDG PRTADGIVSH LKKQAGPASV PLRTEEEFKK FISDKDASIV GFFDDSFSEA HSEFLKAASN LRDNYRFAHT NVESLVNEYD DNGEGIILFR PSHLTNKFED KTVAYTEQKM TSGKIKKFIQ ENIFGICPHM TEDNKDLIQG KDLLIAYYDV DYEKNAKGSN YWRNRVMMVA KKFLDAGHKL NFAVASRKTF SHELSDFGLE STAGEIPVVA IRTAKGEKFV MQEEFSRDGK ALERFLQDYF DGNLKRYLKS EPIPESNDGP VKVVVAENFD EIVNNENKDV LIEFYAPWCG HCKNLEPKYK ELGEKLSKDP NIVIAKMDAT ANDVPSPYEV RGFPTIYFSP ANKKLNPKKY EGGRELSDFI SYLQREATNP PVIQEEKPKK KKKAQEDL.
Product Science Overview
Structure and Function
PDIA3 consists of four thioredoxin-like domains: a, b, b′, and a′. The a and a′ domains contain Cys-Gly-His-Cys active site motifs and are catalytically active. The bb′ domains contain a binding site for calnexin (CNX), which is composed of positively charged, highly conserved residues that interact with the negatively charged residues of the CNX P domain .
PDIA3 is primarily localized in the endoplasmic reticulum (ER) and interacts with lectin chaperones such as calreticulin and calnexin to modulate the folding of newly synthesized glycoproteins. Complexes of lectins and PDIA3 mediate protein folding by promoting the formation of disulfide bonds in their glycoprotein substrates .
Biological Role
PDIA3 plays a significant role in various biological processes, including:
- Protein Folding: It assists in the proper folding of proteins within the ER by catalyzing the formation and rearrangement of disulfide bonds .
- Antigen Presentation: PDIA3 is a core component of the major histocompatibility complex class I (MHC I) peptide loading complex, where it functions as an essential folding chaperone for TAPBP. This process is crucial for the presentation of antigens to cytotoxic T cells in adaptive immunity .
- Cellular Stress Response: PDIA3 is involved in the cellular response to ER stress and helps maintain cell redox homeostasis .
Clinical Significance
Recombinant PDIA3
Recombinant PDIA3 is produced using recombinant DNA technology, which involves inserting the PDIA3 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant form is used in various research and therapeutic applications, including studies on protein folding, cancer progression, and immune response .
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