Analytical Data
-
Gene name
DnaJ
- Application
-
Alternative Names
DnaJ;Chaperone Protein DnaJ
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P25685
-
Expression Region
1-340aa
-
AA Sequence
MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI
-
Molecular Weight
65.0kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
DnaJ proteins are a crucial family of molecular chaperones that assist in protein folding and assembly within cells. Originating from studies of E. coli, DnaJ was identified as a key player in the heat shock response, where it stabilizes unfolded or misfolded proteins by facilitating their proper folding in conjunction with other chaperones, such as DnaK and GrpE. The DnaJ protein family has since been discovered in a wide range of organisms, highlighting its evolutionary conservation and fundamental role in cellular homeostasis. Research into DnaJ proteins has expanded to explore their involvement in various cellular processes, including stress response, signal transduction, and protein degradation pathways. Moreover, aberrations in DnaJ functions have been implicated in various diseases, including neurodegenerative disorders and cancer, making them a significant focus of therapeutic research. Understanding the specific mechanisms and interactions of DnaJ proteins is essential for developing potential interventions that target protein misfolding-related diseases. Advances in recombinant DNA technology have enabled the production of recombinant DnaJ proteins for functional studies, providing insights into their structure-function relationships and interaction networks. As our understanding of DnaJ proteins deepens, they continue to be a vital area of research in cell biology, molecular medicine, and biochemistry.
