Analytical Data
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Gene name
HSP21
- Application
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Alternative Names
25.3 kDa heat shock protein, chloroplastic
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Species
Arabidopsis thaliana
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P31170
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Expression Region
44-227aa
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Molecular Weight
28.4 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
HSP21, a member of the heat shock protein family, plays a crucial role in cellular protection against stress conditions, including heat shock, oxidative stress, and other physiological challenges. This small heat shock protein, which is highly conserved across different species, is primarily localized in the mitochondria and is known for its ability to assist in protein folding and prevent aggregation, thus maintaining cellular homeostasis. Recent studies have highlighted the potential therapeutic applications of HSP21, particularly in neurodegenerative diseases and age-related disorders, where protein misfolding is a common pathological feature. The recombinant production of HSP21 has gained significant attention for both research and therapeutic purposes, as it allows for the exploration of its functional properties and the development of protein-based treatments. Understanding the structure-function relationship of HSP21 through recombinant techniques can provide insights into its mechanism of action and enhance its efficacy as a molecular chaperone. Furthermore, the study of HSP21's interactions with other cellular proteins could reveal new targets for drug development and contribute to the advancement of treatments for diseases associated with protein misfolding and aggregation.
