Analytical Data
-
Gene name
DNAJB7
- Application
-
Alternative Names
DJ5; DnaJ (Hsp40) homolog subfamily B member 7; DnaJ homolog subfamily B member 7; DnaJ/Hsp40 homolog subfamily B; member 7; DNAJB7; DNJB7_HUMAN; HSC3; MGC138340; Novel DnaJ domain protein
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q7Z6W7
-
Expression Region
1-309aa
-
AA Sequence
MVDYYEVLGL QRYASPEDIK KAYHKVALKW HPDKNPENKE EAERKFKEVA EAYEVLSNDE KRDIYDKYGT EGLNGGGSHF DDECEYGFTF HKPDDVFKEI FHERDPFSFH FFEDSLEDLL NRPGSSYGNR NRDAGYFFST ASEYPIFEKF SSYDTGYTSQ GSLGHEGLTS FSSLAFDNSG MDNYISVTTS DKIVNGRNIN TKKIIESDQE REAEDNGELT FFLVNSVANE EGFAKECSWR TQSFNNYSPN SHSSKHVSQY TFVDNDEGGI SWVTSNRDPP IFSAGVKEGG KRKKKKRKEV QKKSTKRNC
-
Molecular Weight
61.8 kDa
-
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
DNAJB7, a member of the DnaJ/Hsp40 family of heat shock proteins, plays a critical role in protein folding and cellular stress responses. Its primary function is to assist in the proper folding of nascent polypeptides and the refolding of misfolded proteins, thereby maintaining cellular homeostasis. The significance of DNAJB7 has gained attention due to its involvement in various cellular processes, including chaperone-mediated protein quality control, which is vital for cell survival under stress conditions. Research has revealed that DNAJB7 may influence several diseases, including neurodegenerative disorders and cancer, by modulating the stability and aggregation of proteins associated with these conditions. The recombinant protein of DNAJB7 is being studied to elucidate its specific mechanisms of action, structural properties, and interactions with substrate proteins. Understanding the functional dynamics of DNAJB7 could provide insights into therapeutic strategies aimed at enhancing cellular resilience against stress and misfolded protein accumulation. Moreover, the potential of DNAJB7 as a biomarker for disease diagnosis and prognosis has prompted ongoing investigations into its role in disease mechanisms, making it a focus of significant interest in molecular biology and biomedicine. Through these research efforts, scientists aim to exploit the chaperone functions of DNAJB7 for developing novel therapeutic interventions that target protein misfolding diseases.
