Analytical Data
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Gene name
HSCB
- Application
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Alternative Names
HSCB;DNAJC20;HSC20;Iron-sulfur cluster co-chaperone Protein HscB
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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
Q8IWL3
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Expression Region
30-235aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAASQA GSNYPRCWNC GGPWGPGRED RFFCPQCRAL QAPDPTRDYF SLMDCNRSFR VDTAKLQHRY QQLQRLVHPD FFSQRSQTEK DFSEKHSTLV NDAYKTLLAP LSRGLYLLKL HGIEIPERTD YEMDRQFLIE IMEINEKLAE AESEAAMKEI ESIVKAKQKE FTDNVSSAFE QDDFEEAKEI LTKMRYFSNI EEKIKLKKIP L
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Molecular Weight
27 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
HSCB (Hsp70/Hsp90 organizing protein) is a significant molecular chaperone that plays a crucial role in the assembly and functioning of protein complexes, particularly in relation to the heat shock protein (HSP) family. This family is essential for maintaining cellular proteostasis, especially under stress conditions. HSCB interacts with HSP70 and HSP90, facilitating the proper folding and stabilization of client proteins, which include a variety of regulatory and signaling molecules involved in essential biological processes. Abnormalities in protein folding and chaperone function are associated with several diseases, including neurodegenerative disorders and cancers. Therefore, understanding the mechanisms by which HSCB operates and its implications in disease states is of significant interest in both basic and applied biomedical research. Efforts to characterize HSCB's structure, interactions, and regulatory pathways could potentially lead to therapeutic advancements, offering novel strategies for targeting diseases linked to protein misfolding or aggregation. This research underscores the broader significance of chaperone networks in cellular health and highlights HSCB as a promising candidate for further investigation in the context of proteostasis and disease.
