PDI Human
a) Analysis by RP-HPLC.
b) Analysis by SDS-PAGE.
Description
PDI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 502 amino acids and having a molecular mass of 56.6kDa. The PDI is fused to a 12 amino acid His tag at N-terminal and purified by proprietary chromatographic techniques.
Product Specs
MRGSGSHHHHHHAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKA
AGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVN
WLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNS
DVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIK
THILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITL
EEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEK
KNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFP
ASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
Product Science Overview
PDI is a multifunctional enzyme with both oxidoreductase and isomerase activities. It has two catalytic thioredoxin-like domains, each containing the canonical CGHC motif, and two non-catalytic domains . The enzyme catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold, allowing proteins to quickly find the correct arrangement of disulfide bonds in their fully folded state .
The primary function of PDI is to assist in the oxidative folding of proteins. This involves the oxidation of reduced cysteine residues in nascent proteins, leading to the formation of disulfide bridges that stabilize the protein’s native structure . PDI also acts as a chaperone, preventing the aggregation of misfolded proteins and assisting in their proper folding .
PDI is essential for the proper folding and maturation of many proteins, particularly those that are secreted or reside in the ER. It plays a critical role in maintaining cellular homeostasis and protein quality control. In addition to its role in protein folding, PDI is involved in various cellular processes, including the regulation of the unfolded protein response (UPR) and the degradation of misfolded proteins through the ER-associated degradation (ERAD) pathway .
The dysfunction of PDI has been implicated in several diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases. For example, the accumulation of misfolded proteins in the ER can lead to ER stress and contribute to the pathogenesis of diseases such as Alzheimer’s and Parkinson’s . In cancer, PDI is often overexpressed and contributes to the survival and proliferation of cancer cells by assisting in the folding of proteins required for tumor growth .
The production of human recombinant PDI involves the insertion of the human PDI gene into a suitable expression vector, which is then introduced into a host organism such as Escherichia coli or Saccharomyces cerevisiae. The host organism expresses the PDI protein, which can be purified and used for various research and therapeutic applications . Recombinant PDI is valuable for studying the enzyme’s structure and function, as well as for developing potential therapeutic interventions for diseases associated with PDI dysfunction.
