DnaJ Human

DnaJ (HSP40) Human Recombinant
Cat. No.
BT14390
Source
Escherichia Coli.
Synonyms
HSP-40, HSP40, DnaJ, DNAJB1, HSPF1, Hdj1, DnaJ homolog subfamily B member 1, Heat shock 40 kDa protein 1, Heat shock protein 40, DnaJ protein homolog 1, HDJ-1, Sis1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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.
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Description

HSP40 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 1-340) and fused to a 20 aa His Tag at N-terminus, containing a total of 360 amino acids and having a molecular mass of 40.2 kDa.
The HSP40 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Human DnaJ homolog subfamily A member 1 (DNAJA1), also known as Hsp40, is a heat shock protein that plays a critical role in protein folding and cellular stress response. It functions as a cochaperone with Hsp70, assisting in the folding of newly synthesized proteins, refolding of misfolded proteins, and prevention of protein aggregation.
Description
DnaJ Human Recombinant protein is produced in E.Coli. It is a single, non-glycosylated polypeptide chain containing amino acids 1-340 and fused to a 20 aa His tag at the N-terminus, resulting in a total of 360 amino acids. The molecular mass of the protein is 40.2 kDa.
Purification of the DnaJ protein is achieved using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
The protein solution is supplied in 20mM Tris-HCl buffer with a pH of 8.0. It also contains 2mM DTT, 0.2mM PMSF, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the protein can be stored at 4°C. For extended storage, it is recommended to freeze the protein at -20°C.
Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage.
Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
HSP-40, HSP40, DnaJ, DNAJB1, HSPF1, Hdj1, DnaJ homolog subfamily B member 1, Heat shock 40 kDa protein 1, Heat shock protein 40, DnaJ protein homolog 1, HDJ-1, Sis1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGKDYYQTLG LARGASDEEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE AYDVLSDPRK REIFDRYGEE GLKGSGPSGG SGGGANGTSF SYTFHGDPHAMFAEFFGGRN PFDTFFGQRN GEEGMDIDDP FSGFPMGMGG FTNVNFGRSR SAQEPARKKQ DPPVTHDLRV SLEEIYSGCT KKMKISHKRL NPDGKSIRNE DKILTIEVKK GWKEGTKITF PKEGDQTSNN IPADIVFVLK DKPHNIFKRD GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE GLPLPKTPEK RGDLIIEFEV IFPERIPQTS RTVLEQVLPI.

Product Science Overview

Introduction

DnaJ, also known as Heat Shock Protein 40 (HSP40), is a member of the heat shock protein family. These proteins play a crucial role in cellular processes by aiding in protein folding, transport, and assembly. The human recombinant form of DnaJ (HSP40) is a synthesized version of this protein, which is used in various research and therapeutic applications.

Structure and Function

DnaJ (HSP40) proteins are characterized by the presence of a J-domain, which is essential for their function. The J-domain interacts with the ATPase domain of HSP70, another heat shock protein, to stimulate its activity. This interaction is vital for the protein’s role as a molecular chaperone, helping to prevent protein aggregation and assisting in the proper folding of nascent polypeptides .

Role in Cellular Processes

HSP40 proteins are involved in several critical cellular processes, including:

  • Protein Folding: HSP40 assists HSP70 in the folding of newly synthesized proteins and the refolding of misfolded proteins.
  • Protein Transport: It helps in the transport of proteins across cellular membranes.
  • Protein Degradation: HSP40 targets improperly folded proteins for degradation, thus maintaining cellular protein homeostasis .
Clinical Significance

The role of DnaJ (HSP40) in preventing protein aggregation is particularly significant in the context of neurodegenerative diseases. For instance, the isoform DNAJB6b has been shown to prevent tau aggregation in neuronal cells, which is a hallmark of Alzheimer’s disease . This makes HSP40 a potential target for therapeutic interventions in such conditions.

Recombinant HSP40

Recombinant human HSP40 is produced using bacterial expression systems, such as Escherichia coli. The recombinant protein is often tagged with a histidine tag to facilitate purification. It is supplied in various formulations, including carrier-free versions, to suit different research needs .

Applications

Recombinant HSP40 is used in a variety of research applications, including:

  • Protein Interaction Studies: To study the interaction between HSP40 and other proteins.
  • Drug Development: As a target for developing drugs aimed at treating diseases associated with protein misfolding.
  • Cellular Stress Response Research: To understand the cellular mechanisms involved in stress responses .

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THE BIOTEK
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