Analytical Data
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Gene name
HSPB2
- Application
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Alternative Names
HSPB2;Heat shock Protein beta-2
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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
MGSSHHHHHH SSGLVPRGSH MGSHMSGRSV PHAHPATAEY EFANPSRLGE QRFGEGLLPE EILTPTLYHG YYVRPRAAPA GEGSRAGASE LRLSEGKFQA FLDVSHFTPD EVTVRTVDNL LEVSARHPQR LDRHGFVSRE FCRTYVLPAD VDPWRVRAAL SHDGILNLEA PRGGRHLDTE VNEVYISLLP APPDPEEEEE AAIVEP
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Molecular Weight
23 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
HSPB2, a member of the small heat shock protein (sHSP) family, has garnered attention due to its essential role in cellular stress responses, particularly in muscle tissues. These proteins function as molecular chaperones, helping to prevent protein aggregation and maintain cellular homeostasis under stress conditions, such as heat shock or oxidative stress. Mutations in HSPB2 have been linked to various myopathies, particularly hereditary muscle diseases, highlighting its importance in muscle health and function. Research on the recombinant expression of HSPB2 is crucial for elucidating its functional properties and understanding the mechanisms underlying its protective effects in muscle cells. By producing HSPB2 in a recombinant system, scientists can study its structure, folding, and interactions with other proteins, paving the way for potential therapeutic applications. Furthermore, exploring the role of HSPB2 in muscle pathology may offer insights into developing strategies for treating muscle-related disorders. Overall, the investigation of HSPB2 through recombinant protein research holds significant promise for advancing our knowledge of muscle biology and enhancing therapeutic approaches for associated diseases.
