Analytical Data
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Gene name
JTB
- Application
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Alternative Names
JTB;Protein JTB
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O76095
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Expression Region
31-105aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSEAPVQEEKLSASTSNLPCWLVEEFVVA EECSPCSNFRAKTTPECGPTGYVEKITCSSSKRNEFKSCRSALMEQRL
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Molecular Weight
11 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
JTB, or J-domain containing protein B, is an essential component of the cellular machinery involved in protein folding and stress responses. Research on JTB has gained momentum due to its critical role in cellular homeostasis and its implications in various diseases, including neurodegenerative disorders and cancers. The JTB protein functions as a co-chaperone, interacting with heat shock proteins and facilitating the proper folding of nascent polypeptides under stress conditions. Understanding the structure and function of JTB, particularly in the context of its role in the heat shock protein 70 (Hsp70) system, is vital for elucidating the mechanisms of protein misfolding and aggregation. Scientists have utilized recombinant DNA technology to produce JTB in vitro, which allows for detailed studies of its structural properties, binding interactions, and functional dynamics. This research is crucial for developing targeted therapeutic strategies aimed at modulating JTB activity, potentially leading to novel treatments for conditions characterized by protein misfolding. The investigation into the JTB protein thus represents a significant frontier in cell biology and therapeutic development, shedding light on fundamental processes that sustain cellular integrity and contribute to the pathogenesis of various diseases.
