Analytical Data
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Gene name
DNAJC12
- Application
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Alternative Names
JDP1; J Domain Protein 1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UKB3
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Expression Region
Met1~Lys183
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Molecular Weight
28kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
DNAJC12, a member of the DnaJ/Hsp40 protein family, plays a crucial role in the regulation of protein folding and degradation processes within cells. It acts as a co-chaperone, interacting with heat shock proteins to facilitate the proper folding of newly synthesized proteins and the refolding of misfolded proteins, thus maintaining cellular protein homeostasis. Research has highlighted its potential involvement in crucial cellular processes such as stress response, cell differentiation, and apoptosis. Aberrant expression or mutations in DNAJC12 have been linked to various diseases, including neurodegenerative disorders and cancer, making it a subject of significant interest in biomedical research. Moreover, understanding the molecular mechanisms regulated by DNAJC12 can provide insights into therapeutic strategies targeting protein misfolding diseases. Scientists have increasingly focused on characterizing recombinant DNAJC12 protein to elucidate its structure-function relationships and interaction networks. Such studies are essential for developing targeted therapies to mitigate the detrimental effects caused by dysfunctional protein handling.
