Analytical Data
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Gene name
HSP21
- Application
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Alternative Names
HSP21；Small heat shock Protein 21
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Species
E.coli
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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
Q5AHH4
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Expression Region
1-891aa
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AA Sequence
MSWFGFFDPDFDDFFGRPRKYATEVPPNFNPRKIAQGDNGKGQQVSRYGAGAGHPHRALARRDDFFDDFWKNFSSGKYFVGFDDNVKTTEESDKYVVSYDQENLSPDEVNVDFDKQENELIITVTQETEKDGTKKSSTFHSNLKFEKPVNFDDISAEIGEQGVQVTLPKVHADHEKIVNIPISKAAAKK
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Molecular Weight
21.4 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 (HSP) family, plays a crucial role in cellular protection and stress response, particularly under conditions of heat shock and oxidative stress. As a molecular chaperone, HSP21 is involved in the refolding of denatured proteins, prevention of protein aggregation, and adaptation to various environmental stressors. Its significance has been highlighted in several organisms ranging from yeast to higher plants, where it contributes to improved tolerance against abiotic stresses. Recent studies have focused on the recombinant expression of HSP21 in various expression systems, aiming to understand its functional mechanisms and to harness its protective properties for biotechnological applications. This includes exploring its potential in enhancing crop resilience to climate change, as well as its therapeutic implications in human health, particularly in diseases related to protein misfolding. The ability to produce HSP21 as a recombinant protein has opened avenues for in-depth biochemical analyses and the development of novel stress-resistant plant varieties, underscoring its importance in both basic and applied research.
