Analytical Data
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Gene name
JTB
- Application
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Alternative Names
JTB; Protein JTB
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Species
Brugia malayi
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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
O77049
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Expression Region
31-105aa
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Molecular Weight
24.4 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
Related Products
Protein Description
JTB, or J-Protein T-Domain Binding, is a crucial protein in cellular processes, notably in chaperone-mediated protein folding and stress responses. It belongs to the Hsp40 family, which is characterized by its ability to interact with heat shock proteins and play a pivotal role in protein homeostasis. Research on JTB has gained momentum due to its implications in various diseases, including neurodegenerative disorders and cancer, where protein misfolding and aggregation are common pathological features. Recent studies have focused on the structural and functional characterization of JTB, utilizing advanced techniques like cryo-electron microscopy and X-ray crystallography to elucidate its interactions with client proteins and co-chaperones. Understanding JTB's role in cellular mechanisms can provide insights into potential therapeutic targets, particularly in the context of diseases associated with protein misfolding. The ongoing research aims to develop JTB-based strategies for enhancing cellular resilience to stress and improving the effectiveness of therapeutic agents, thereby paving the way for novel interventions in diseases linked to protein dysregulation.
