Analytical Data
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Gene name
DNAJD1
- Application
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Alternative Names
DnaJ homolog subfamily C member 15. Cell growth-inhibiting gene 22 protein. Methylation-controlled J protein. MCJ
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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
Q9Y5T4
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Expression Region
1-150aa
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AA Sequence
MAARGVIAPVGESLRYAEYLQPSAKRPDADVDQQGLVRSLIAVGLGVAALAFAGRYAFRIWKPLEQVITETAKKISTPSFSSYYKGGFEQKMSRREAGLILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAAKINEAKDLLETTTKH
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Molecular Weight
42.24 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
DNAJD1, a member of the DnaJ heat shock protein family, plays a crucial role in protein folding and cellular stress response. This protein is characterized by the presence of a J-domain, which facilitates the recruitment of molecular chaperones to assist in the maturation of misfolded proteins. Research has shown that DNAJD1 is involved in critical biological processes, including mitochondrial function, and it has been implicated in various human diseases, particularly in neurodegenerative disorders and cancer. The study of recombinant DNAJD1 protein has gained momentum due to its potential therapeutic applications, as modulating its activity could enhance protein homeostasis in stressed cells. By generating recombinant DNAJD1, researchers aim to explore its functional mechanisms in protein folding and degradation pathways, assess its interactions with other chaperones, and evaluate its effects in cellular models of stress and disease. Understanding the structural and functional properties of recombinant DNAJD1 could pave the way for novel strategies in treating diseases characterized by protein misfolding and aggregation, thus underscoring its importance in the field of molecular biology and therapeutic development.
