PDIA4 Human

Protein Disulfide Isomerase A4 Human Recombinant
Cat. No.
BT1234
Source
Escherichia Coli.
Synonyms
Endoplasmic reticulum resident protein 72, ERP70, ERP72.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTeks 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

PDIA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 646 amino acids (21-645 a.a.) and having a molecular weight of 72.9kDa. The PDIA4 is fused to 21a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Protein Disulfide Isomerase Family A Member 4 (PDIA4), found in the endoplasmic reticulum lumen, acts as a stress protein and belongs to the protein disulfide isomerase family. Its primary function involves rearranging protein disulfide bonds (S-S bonds). Additionally, both PDIA4 and PDIA3 exhibit protease, protein disulfide isomerase, and phospholipase activities, either individually or in combination.
Description
Recombinant human PDIA4, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 646 amino acids (specifically, amino acids 21 to 645) and has a molecular weight of 72.9 kDa. This PDIA4 variant is fused to a 21-amino acid His-Tag at its N-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The provided PDIA4 protein solution has a concentration of 1 mg/ml and is formulated in a buffer consisting of 20 mM Tris-HCl (pH 8), 1 mM DTT, 0.1 M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To further enhance long-term stability, consider adding a carrier protein like HSA or BSA (0.1%). Repeated freezing and thawing should be avoided.
Purity
SDS-PAGE analysis indicates a purity exceeding 90%.
Synonyms
Endoplasmic reticulum resident protein 72, ERP70, ERP72.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVAGAEGPDE DSSNRENAIE DEEEEEEEDD DEEEDDLEVK EENGVLVLND ANFDNFVADK DTVLLEFYAP WCGHCKQFAP EYEKIANILK DKDPPIPVAK IDATSASVLA SRFDVSGYPT IKILKKGQAV DYEGSRTQEE IVAKVREVSQ PDWTPPPEVT LVLTKENFDE VVNDADIILV EFYAPWCGHC KKLAPEYEKA AKELSKRSPP IPLAKVDATA ETDLAKRFDV SGYPTLKIFR KGRPYDYNGP REKYGIVDYM IEQSGPPSKE ILTLKQVQEF LKDGDDVIII GVFKGESDPA YQQYQDAANN LREDYKFHHT FSTEIAKFLK VSQGQLVVMQ PEKFQSKYEP RSHMMDVQGS TQDSAIKDFV LKYALPLVGH RKVSNDAKRY TRRPLVVVYY SVDFSFDYRA ATQFWRSKVL EVAKDFPEYT
FAIADEEDYA GEVKDLGLSE SGEDVNAAIL DESGKKFAME PEEFDSDTLR EFVTAFKKGK LKPVIKSQPV PKNNKGPVKV VVGKTFDSIV MDPKKDVLIE FYAPWCGHCK QLEPVYNSLA KKYKGQKGLV IAKMDATAND VPSDRYKVEG FPTIYFAPSG DKKNPVKFEG GDRDLEHLSK FIEEHATKLS RTKEEL.

Product Science Overview

Structure and Function

PDIA4 is synthesized as a 625 amino acid precursor, which includes a 20 amino acid signal sequence and a mature chain of 605 amino acids . The enzyme contains three thioredoxin domains, which are critical for its oxidoreductase and chaperone activities . These domains facilitate the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins .

Biological Significance

PDIA4 is primarily located in the endoplasmic reticulum (ER) lumen, where it assists in the proper folding of nascent proteins . It is a core component of the major histocompatibility complex class I (MHC I) peptide loading complex, functioning as an essential folding chaperone for TAPBP . Through its interaction with TAPBP, PDIA4 aids in the dynamic assembly of the MHC I complex with high-affinity antigens in the ER, playing a crucial role in antigen presentation to cytotoxic T cells in adaptive immunity .

Role in Disease

Recent studies have highlighted the involvement of PDIA4 in various diseases, particularly in cancer. PDIA4 has been reported to be involved in carcinogenesis and the progression of glioblastoma, a type of brain cancer . Its role in maintaining protein homeostasis and regulating redox states makes it a potential target for therapeutic interventions in cancer treatment .

Human Recombinant PDIA4

Human recombinant PDIA4 is produced using recombinant DNA technology, which involves inserting the human PDIA4 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study its structure, function, and role in disease processes .

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