Analytical Data
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Gene name
DNAJC12
- Application
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Alternative Names
DNAJC12；JDP1;DnaJ homolog subfamily C member 12
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
1-198aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMDAILN YRSEDTEDYY TLLGCDELSS VEQILAEFKV RALECHPDKH PENPKAVETF QKLQKAKEIL TNEESRARYD HWRRSQMSMP FQQWEALNDS VKTSMHWVVR GKKDLMLEES DKTHTTKMEN EECNEQRERK KEELASTAEK TEQKEPKPLE KSVSPQNSDS SGFADVNGWH LRFRWSKDAP SELLRKFRNY EI
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Molecular Weight
26 kDa
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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
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Protein Description
DNAJC12, a member of the DnaJ family of heat shock proteins, plays a crucial role in the cellular stress response and protein folding. This protein functions as a co-chaperone, facilitating the proper folding of nascent polypeptides and the refolding of denatured proteins, thus maintaining proteostasis within cells. The research surrounding DNAJC12 has gained prominence due to its potential implications in various diseases, including neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies have shown that DNAJC12 interacts with several key proteins involved in cellular stress pathways, suggesting its significant role in mitigating the effects of stressors such as oxidative stress and misfolded proteins. Additionally, variations in the expression of DNAJC12 have been linked to cancer progression, making it a target of interest for therapeutic interventions. By exploring the mechanisms through which DNAJC12 operates and its interactions within the cellular environment, researchers aim to elucidate its contributions to health and disease. Recombinant DNAJC12 protein is being utilized in studies to better understand its functional properties, interactions, and the potential therapeutic applications that could arise from modulating its activity in various diseased states. Understanding DNAJC12's mechanisms could lead to novel strategies to combat diseases characterized by protein misfolding and aggregation, thereby highlighting its relevance in both basic and applied biomedical research.
