Analytical Data
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Gene name
HSP27
- Application
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Alternative Names
SAFB;HAP;HET;SAFB1;Scaffold attachment factor B1
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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
Q16082
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Expression Region
1-182aa
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AA Sequence
MSGRSVPHAHPATAEYEFANPSRLGEQRFGEGLLPEEILTPTLYHGYYVRPRAAPAGEGSRAGASELRLSEGKFQAFLDVSHFTPDEVTVRTVDNLLEVSARHPQRLDRHGFVSREFCRTYVLPADVDPWRVRAALSHDGILNLEAPRGGRHLDTEVNEVYISLLPAPPDPEEEEEAAIVEP
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Molecular Weight
47.2kDa
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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
HSP27, or heat shock protein 27, is a small molecular chaperone that plays a crucial role in cellular stress responses, protein folding, and protection against apoptosis. Research into recombinant HSP27 protein has gained momentum due to its potential therapeutic applications in various diseases, particularly in neurodegenerative disorders, cancer, and cardioprotection. Studies have shown that HSP27 can modulate cellular pathways involved in inflammation and oxidative stress, highlighting its importance in cellular homeostasis under adverse conditions. The generation of recombinant HSP27 protein enables detailed functional analyses, including its chaperone activity, interactions with other proteins, and its protective role in various cellular models. Moreover, the expression of recombinant HSP27 in model organisms or cell lines facilitates exploration of its mechanisms of action and could lead to the development of novel therapeutic strategies aimed at enhancing HSP27 expression or mimicking its activity. Understanding the structural and functional properties of HSP27 through recombinant technology is essential for harnessing its biological functions and improving outcomes in diseases where protein misfolding and stress response are key factors. Consequently, the study of recombinant HSP27 is not only fundamental for basic science but also holds promise for innovative approaches to treating complex diseases associated with protein homeostasis.
