Analytical Data
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Gene name
HSBP1
- Application
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Alternative Names
HSBP1;HSF1BP;Heat shock factor-binding Protein 1
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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
O75506
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Expression Region
1-75aa
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AA Sequence
MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQK
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Molecular Weight
35.5kDa
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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
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Protein Description
HSBP1, or heat shock factor-binding protein 1, is a crucial regulatory protein implicated in the cellular response to stress, particularly heat shock. This protein interacts with heat shock factor 1 (HSF1), a key transcription factor that activates the expression of heat shock proteins (HSPs) in response to various stressors. The synthesis of HSPs is essential for protecting cells from damage caused by stress, aiding in protein folding, and preventing misfolding and aggregation. Studies have shown that HSBP1 plays a significant role in modulating the activity of HSF1, thereby influencing the cellular stress response and impacting various physiological processes, including development, aging, and disease progression. Recent research has focused on the recombinant expression of HSBP1 to investigate its structure, function, and interactome in detail. Understanding the functional dynamics of HSBP1 through recombinant technologies can provide insights into its regulatory mechanisms and potential roles in diseases such as cancer and neurodegeneration, where the heat shock response is often perturbed. The exploration of HSBP1 as a target for therapeutic interventions is an emerging area of interest, as modulation of this protein may enhance cellular resilience under stress and improve outcomes in stress-related diseases. Thus, the study of HSBP1 through recombinant protein technology is pivotal for advancing our comprehension of stress response pathways and developing novel therapeutic strategies.
