Analytical Data
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Gene name
DNAJC8
- Application
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Alternative Names
DnaJ (Hsp40) homolog subfamily C member 8; DnaJ homolog subfamily C member 8; DNAJC 8; DNAJC8; DNJC8_HUMAN; HSPC315; HSPC331 ; SPF31 ; Splicing protein spf31
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75937
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Expression Region
1-253aa
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AA Sequence
MAASGESGTSGGGGSTEEAFMTFYSEVKQIEKRDSVLTSKNQIERLTRPGSSYFNLNPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKAFEAVDKAYKLLLDQEQKKRALDVIQAGKEYVEHTVKERKKQLKKEGKPTIVEEDDPELFKQAVYKQTMKLFAELEIKRKEREAKEMHERKRQREEEIEAQEKAKREREWQKNFEESRDGRVDSWRNFQANTKGKKEKKNRTFLRPPKVKMEQRE
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Molecular Weight
56.2 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
Related Products
Protein Description
DNAJC8, a member of the DnaJ/Hsp40 co-chaperone family, plays a crucial role in cellular protein homeostasis and stress response. Its involvement in chaperone-mediated protein folding and the maintenance of proteostasis makes it a significant subject of study in the context of neurodegenerative diseases, where protein misfolding and aggregation are common pathological features. Recent research has shown that mutations in the DNAJC8 gene are associated with severe neurological disorders, including early-onset Parkinson's disease and other movement disorders. Understanding the structure and function of DNAJC8, as well as its interactions with other chaperones and substrates, is essential for elucidating its biological role and potential therapeutic implications. The development of recombinant DNAJC8 proteins allows for the study of its chaperone activity, client protein interactions, and the molecular mechanisms underlying its protective effects against misfolded proteins. As researchers explore the therapeutic potential of targeting DNAJC8 in neurodegeneration, the insights gained may pave the way for novel strategies aimed at alleviating the burdens of these devastating diseases.
