SlyD E.Coli

FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant
Cat. No.
BT2075
Source
Escherichia Coli.
Synonyms
FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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.
Shipped with Ice Packs
In Stock

Description

SlyD Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids and having a molecular mass of 21 kDa.

Product Specs

Introduction
SlyD, with accession number NP_755987, is a putative folding helper protein found in the cytosol of Escherichia coli. It possesses an N-terminal prolyl isomerase domain belonging to the FKBP family and a C-terminal tail that is likely unstructured. SlyD plays a crucial role in the biosynthesis of the metal cluster within [NiFe]-hydrogenase enzymes and exhibits multiple activities, including that of a peptidyl-prolyl isomerase.
Description
Recombinant SlyD, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 196 amino acids. It has a molecular weight of 21 kDa.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The SlyD protein solution is supplied in 20mM Tris buffer at pH 7.5.
Stability
For optimal storage, keep at 4°C if the entire vial will be used within 2-4 weeks. For longer-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Biological Activity
The specific activity is measured to be greater than 220 nmoles per minute per mg. Specific activity is defined as the amount of enzyme required to cleave 1 μmole of suc-AAFP-pNA per minute at 25°C in Tris-HCl buffer at pH 8.0 using chymotrypsin.
Purity
Purity is determined to be greater than 95.0% by the following methods: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) (b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE)
Synonyms
FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.
Source
Escherichia Coli.
Amino Acid Sequence
MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH.

Product Science Overview

Introduction

FKBP-type peptidyl-prolyl cis-trans isomerases (PPIases) are a class of enzymes that play a crucial role in protein folding by catalyzing the cis-trans isomerization of proline residues in polypeptides. These enzymes are also known as immunophilins due to their ability to bind immunosuppressive drugs like FK506 (tacrolimus) and rapamycin. The recombinant expression of these enzymes in Escherichia coli (E. coli) has been a significant area of research due to their potential applications in biotechnology and medicine.

Structure and Function

FKBP-type PPIases are characterized by their FK506-binding domain, which is responsible for their isomerase activity. This domain facilitates the conversion of proline residues between their cis and trans conformations, a process essential for proper protein folding and function. The isomerase activity of these enzymes is crucial for various cellular processes, including signal transduction, protein trafficking, and stress responses .

Recombinant Expression in E. coli

The recombinant expression of FKBP-type PPIases in E. coli involves the insertion of the gene encoding the enzyme into an expression vector, which is then introduced into the bacterial cells. This allows for the production of large quantities of the enzyme, which can be purified and studied in detail. The use of E. coli as a host organism is advantageous due to its rapid growth, well-characterized genetics, and ease of manipulation .

Applications and Significance

The recombinant FKBP-type PPIases expressed in E. coli have several important applications:

  1. Biotechnology: These enzymes are used in the production of recombinant proteins, where their isomerase activity helps in achieving proper protein folding and stability.
  2. Medicine: FKBP-type PPIases are targets for immunosuppressive drugs used in organ transplantation and autoimmune diseases. Understanding their structure and function can aid in the development of new therapeutic agents.
  3. Stress Tolerance: Studies have shown that the expression of FKBP-type PPIases can impart stress tolerance to E. coli cells, making them more resilient to environmental stresses such as high temperature and salinity .

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