DnaK E.coli

DnaK (HSP70) E.Coli Recombinant
Cat. No.
BT15341
Source
Escherichia Coli.
Synonyms
HSP-70, HSP70, DnaK, , Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
Appearance
Sterile filtered colorless solution.
Purity

Greater than 85.0% 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.
Shipped with Ice Packs
In Stock

Description

Recombinant Dnak produced in E.Coli is a single, non-glycosylated polypeptide chain containing 638 amino acids and having a molecular mass of 69 kDa.

Product Specs

Introduction
DnaK, the bacterial HSP70 chaperone, plays a crucial role in protein folding and stress response. Originally discovered for its involvement in bacteriophage lambda DNA replication in E. coli, DnaK assists in the proper folding of newly synthesized polypeptides and prevents the aggregation of proteins damaged by cellular stress.
Description
This recombinant DnaK protein, expressed in E. coli, is a single polypeptide chain consisting of 638 amino acids. It is non-glycosylated and has a molecular weight of 69 kDa.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
This DnaK protein is supplied in a buffer composed of 25mM Tris-HCl (pH 7.5), 100mM NaCl, 5mM DTT, and 10% Glycerol.
Stability
For short-term storage (2-4 weeks), keep the vial refrigerated at 4°C. For extended storage, freeze the protein at -20°C. To maximize long-term stability, consider adding a carrier protein like 0.1% HSA or BSA. Minimize repeated freeze-thaw cycles to preserve protein integrity.
Purity
The purity of this protein is greater than 85% as determined by SDS-PAGE analysis.
Synonyms
HSP-70, HSP70, DnaK, , Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
Source
Escherichia Coli.
Amino Acid Sequence
MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVTNPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVLKKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIINEPTAAALAYGLDKGTGNRTI AVYDLGGGTFDISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYLVEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKVTRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKEPRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPTKHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMPQIEVTFDIDADGILHVSAKD KNSGKEQKITIKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGDHLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLMEIAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK.

Product Science Overview

Introduction

DnaK, also known as HSP70, is a highly conserved molecular chaperone found in Escherichia coli (E. coli). It plays a crucial role in protein homeostasis by assisting in the folding of newly synthesized polypeptides, preventing the aggregation of misfolded proteins, and aiding in the refolding of stress-denatured proteins .

Structure and Function

DnaK is a member of the HSP70 family of heat shock proteins, which are characterized by their ability to bind and hydrolyze ATP. The protein consists of three main domains:

  1. N-terminal ATPase domain: Responsible for ATP binding and hydrolysis.
  2. Substrate-binding domain: Binds to exposed hydrophobic regions of unfolded or partially folded proteins.
  3. C-terminal domain: Plays a role in the regulation of the chaperone activity.

The ATPase activity of DnaK is essential for its function as a chaperone. The binding and hydrolysis of ATP induce conformational changes in DnaK, allowing it to interact with substrate proteins and facilitate their proper folding .

Role in E. Coli

In E. coli, DnaK is involved in various cellular processes, including:

  • Protein Folding: DnaK assists in the folding of newly synthesized proteins and prevents the aggregation of misfolded proteins.
  • Stress Response: During stress conditions, such as heat shock, DnaK helps in the refolding of denatured proteins and protects cells from stress-induced damage .
  • Regulation of Gene Expression: DnaK plays a role in regulating the activity of the heat shock sigma factor σ32, which controls the expression of heat shock proteins .
Recombinant DnaK

Recombinant DnaK is produced by cloning the dnaK gene from E. coli into an expression vector and expressing the protein in a suitable host system. This allows for the production of large quantities of DnaK for research and industrial applications. Recombinant DnaK retains the functional properties of the native protein and is used in studies related to protein folding, stress response, and chaperone activity .

Applications

Recombinant DnaK has several applications in research and biotechnology:

  • Protein Folding Studies: Used to study the mechanisms of protein folding and the role of chaperones in this process.
  • Stress Response Research: Helps in understanding the cellular response to stress and the role of chaperones in protecting cells from damage.
  • Biotechnological Applications: Used in the production of recombinant proteins to improve their yield and stability by preventing aggregation and misfolding.

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