Analytical Data
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Gene name
HSPB6
- Application
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Alternative Names
HSPB6;Heat shock Protein beta-6
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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
O14558
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Expression Region
1-160aa
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AA Sequence
MEIPVPVQPS WLRRASAPLP GLSAPGRLFD QRFGEGLLEA ELAALCPTTL APYYLRAPSV ALPVAQVPTD PGHFSVLLDV KHFSPEEIAV KVVGEHVEVH ARHEERPDEH GFVAREFHRR YRLPPGVDPA AVTSALSPEG VLSIQAAPAS AQAPPPAAAK
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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
HSPB6, a member of the small heat shock protein (sHSP) family, has garnered significant interest in recent years due to its critical role in cellular stress responses and protein quality control. This protein is primarily expressed in embryonic and postnatal tissues, particularly in the heart and skeletal muscles, where it helps protect cells from stress-induced damage. Studies have indicated that HSPB6 functions as a molecular chaperone, preventing the aggregation of misfolded proteins and facilitating their proper refolding. Dysregulation or mutations in HSPB6 have been linked to various cardiac and neuromuscular diseases, highlighting its potential as a therapeutic target. The recombinant production of HSPB6 allows researchers to investigate its molecular properties, interactions with other proteins, and its functional role under pathological conditions. Understanding the mechanisms by which HSPB6 exerts its protective effects could open new avenues for the development of novel treatments for muscle degenerative diseases and cardiomyopathies. As such, research on HSPB6 recombinant proteins is poised to contribute valuable insights into cell survival mechanisms and the broader field of proteostasis.
