PDIA4 Human, Active

Protein Disulfide Isomerase A4 Human Recombinant, Active
Cat. No.
BT1323
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 21 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Protein disulfide isomerase A4 (PDIA4) is found within the endoplasmic reticulum lumen and acts as both a stress protein and a member of the protein disulfide isomerase family. It plays a crucial role in the catalytic rearrangement of disulfide bonds (S-S bonds) within proteins. Both PDIA4 and PDIA3 exhibit multifunctional properties, acting as proteases, protein disulfide isomerases, phospholipases, or a combination of these functions.
Description
Recombinant human PDIA4, expressed in E. coli, is a single polypeptide chain that lacks glycosylation. It comprises 646 amino acids, specifically residues 21 to 645, with a molecular weight of 72.9 kDa. The N-terminus of PDIA4 is fused to a 21 amino acid His-Tag. Purification is achieved through proprietary chromatographic methods.
Physical Appearance
The solution is colorless and has been sterilized through filtration.
Formulation
The PDIA4 protein solution is provided at 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 optimal storage, the product should be kept at 4°C if it will be used within 2-4 weeks. For extended storage, freezing at -20°C is recommended. To further enhance long-term stability, the addition of a carrier protein such as 0.1% HSA or BSA is advisable. It's important to avoid subjecting the product to repeated cycles of freezing and thawing.
Purity
The purity of the protein is determined to be greater than 90.0% based on SDS-PAGE analysis.
Biological Activity
The specific activity of the enzyme is measured to be greater than 10 A650/cm/min/mg. Enzymatic activity was confirmed by assessing the aggregation of insulin in the presence of DTT.
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 characterized by its N-terminal endoplasmic reticulum (ER) signal sequence, three catalytically active thioredoxin (TRX) domains, two TRX-like domains, and a C-terminal ER-retention sequence . These domains enable PDIA4 to function as a protein folding chaperone, ensuring that proteins achieve their correct conformation within the ER .

When bound to cyclophilin B, PDIA4 enhances the rate of immunoglobulin G (IgG) intermolecular disulfide bonding and antibody assembly . This function is particularly important in the immune response, as it ensures the proper assembly and functionality of antibodies.

Role in Disease

PDIA4 has been implicated in various diseases, particularly in cancer. Its overexpression has been associated with poor prognosis in glioblastoma multiforme (GBM), a highly aggressive brain tumor . PDIA4 promotes angiogenesis (the formation of new blood vessels) in GBM, which supports tumor growth and survival under harsh conditions . Additionally, PDIA4 has been found to confer resistance to anti-angiogenic therapy, making it a potential target for improving cancer treatment outcomes .

Recombinant PDIA4

Recombinant PDIA4 is produced using various expression systems, including E. coli, yeast, baculovirus, and mammalian cells . The recombinant form retains the enzymatic activity of the native protein, making it valuable for research and therapeutic applications. It is used in studies to understand the molecular mechanisms of protein folding and its role in diseases, as well as in the development of potential therapeutic interventions.

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THE BIOTEK
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