Analytical Data
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Gene name
DNAJC5G
- Application
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Alternative Names
DNAJC5GDnaJ homolog subfamily C member 5G; Cysteine string protein-gamma; CSP-gamma
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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
Q8N7S2
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Expression Region
1-189aa
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AA Sequence
MSTVKEAAHR LSKSEMSLYA VLDLKKGASP EDFKKSYSHS ALLPHPPFEY HLGRKLALRY HPDKNPGNAQ AAEIFKEINA AHAILSDSKK RKIYDQHGSL GIYLYDHFGE EGVRYYFILN SCWFKTLVIL CTLLTCCCFC CCCCFCCGAL KPPPEQDSGR KYQQNVQSQP PRSGAKCDFR SEENSEDDF
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Molecular Weight
21.4 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
DNAJC5G, a member of the DNAJ/Hsp40 protein family, plays a crucial role in cellular stress response and protein folding mechanisms. Its function is particularly relevant in the context of neurodegenerative diseases, where protein misfolding and aggregation are central pathological features. Research has shown that DNAJC5G is involved in the chaperone activity that aids in the correct folding of proteins, thus preventing toxic aggregations. Given its potential therapeutic implications, recombinant DNAJC5G has become an important focus for scientists aiming to explore its structure-function relationship and its interactions with misfolded proteins. Studies have demonstrated that the loss or malfunction of DNAJC5G can contribute to cellular toxicity, making it a candidate for intervention strategies in diseases like Alzheimer's and Parkinson's. The production of recombinant DNAJC5G allows for detailed biochemical studies, which can elucidate its role in maintaining proteostasis under stress conditions. Understanding the molecular mechanisms of DNAJC5G may lead to novel approaches in designing therapeutic agents that enhance its chaperone activity, ultimately contributing to the development of treatments for neurodegenerative disorders linked to protein misfolding and aggregation.
