Analytical Data
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Gene name
HSPB9
- Application
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Alternative Names
HSPB9;Heat shock Protein beta-9
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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
Q9BQS6
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Expression Region
1-159aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMQRVGNTFSNESRVASRCPSVGLAERNRVA TMPVRLLRDSPAAQEDNDHARDGFQMKLDAHGFAPEELVVQVDGQWLMVT GQQQLDVRDPERVSYRMSQKVHRKMLPSNLSPTAMTCCLTPSGQLWVRGQ CVALALPEAQTGPSPRLGSLGSKASNLTR
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Molecular Weight
20 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
HSPB9, a member of the heat shock protein 27 family, has garnered significant attention in recent years due to its crucial role in cellular stress responses and its potential implications in various diseases. This small molecular chaperone is primarily known for its involvement in protecting cells from apoptosis under stress conditions, including oxidative stress and abnormal protein aggregation. Studies have shown that HSPB9 is upregulated in various tissues in response to heat shock and oxidative stress, thereby highlighting its potential as a biomarker for stress-related diseases. Additionally, HSPB9 has been implicated in neurodegenerative disorders, such as Alzheimer's disease, where its regulatory effects on protein folding and aggregation can influence disease progression. The recombinant expression of HSPB9 enables detailed study of its structure-function relationship, providing valuable insights into its mechanism of action and potential therapeutic applications. Researchers are investigating the use of HSPB9 in neuroprotection, cancer therapy, and age-related diseases, emphasizing the need for a comprehensive understanding of its functional dynamics. Overall, the study of recombinant HSPB9 is pivotal for elucidating its roles in health and disease, paving the way for innovative strategies in treating stress-related pathologies.
