Analytical Data
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Gene name
DNAJB8
- Application
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Alternative Names
DJ6; DnaJ (Hsp40) homolog; subfamily B; member 8; DnaJ homolog subfamily B member 8; Dnajb8; DNJB8_HUMAN; mDj6; MGC33884; OTTHUMP00000216243
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NHS0
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Expression Region
1-232aa
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Molecular Weight
41.7 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
DNAJB8, a member of the DNAJ (Hsp40) protein family, has garnered significant attention in the context of cellular stress responses and protein homeostasis. This co-chaperone plays a pivotal role in modulating the activity of Hsp70, enhancing the protein folding process crucial for maintaining cellular functions under stress conditions, such as heat shock or oxidative stress. Moreover, DNAJB8 has been implicated in various pathological conditions, including neurodegenerative diseases and cancer, where protein misfolding and aggregation are prevalent. Its involvement in these diseases highlights its potential as a therapeutic target. Recent studies have focused on the characterization of DNAJB8 recombinant proteins to better understand its structure-function relationship and to explore its role in cellular mechanisms. Understanding the biochemical properties of DNAJB8, including its interaction with other chaperones and substrates, could provide insights into its potential applications in therapeutic strategies aimed at ameliorating protein misfolding disorders. Additionally, the development of DNAJB8 recombinant proteins enhances the ability to produce high-yield, functional proteins for various research applications, including drug development and biomarker discovery. Overall, the study of DNAJB8 recombinant proteins represents a promising avenue for advancing our comprehension of molecular chaperones in health and disease.
