Analytical Data
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Gene name
DNAJC5
- Application
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Alternative Names
(Ceroid-lipofuscinosis neuronal protein 4)(Cysteine string protein)(CSP)
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Species
Human
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Source
E. coli
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Tag
N- MBP & C- His-Avi
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H3Z4
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Expression Region
1-198aa
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Molecular Weight
69.9 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
DNAJC5, also known as cysteine-string protein alpha (CSPα), is a crucial member of the DNAJ heat shock protein family, primarily involved in the regulation of protein folding and trafficking within cells. Dysfunctions in DNAJC5 have been linked to various neurodegenerative disorders, particularly the early-onset form of dementia associated with the accumulation of misfolded proteins. The study of DNAJC5 recombinant proteins has gained significance in understanding its role in cellular stress responses, protein quality control, and synaptic function. Researchers are particularly interested in elucidating the molecular mechanisms by which DNAJC5 interacts with other chaperones and client proteins to prevent aggregation and facilitate proper protein function. Additionally, since mutations in DNAJC5 have been associated with specific pathologies, including a form of hereditary spastic paraplegia, developing recombinant DNAJC5 allows for detailed investigations into the consequences of these mutations at the biochemical and cellular levels. Overall, the research on DNAJC5 recombinant proteins is pivotal for uncovering therapeutic targets and strategies for diseases linked to protein misfolding and aggregation, thereby contributing to the broader field of neurobiology and potentially leading to novel interventions in neurodegenerative diseases.
