Analytical Data
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Gene name
HSF4
- Application
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Alternative Names
HSF4；Heat shock factor Protein 4
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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
Q9ULV5
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Expression Region
1-492aa
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AA Sequence
MQEAPAALPT EPGPSPVPAF LGKLWALVGD PGTDHLIRWS PSGTSFLVSD QSRFAKEVLP QYFKHSNMAS FVRQLNMYGF RKVVSIEQGG LLRPERDHVE FQHPSFVRGR EQLLERVRRK VPALRGDDGR WRPEDLGRLL GEVQALRGVQ ESTEARLREL RQQNEILWRE VVTLRQSHGQ QHRVIGKLIQ CLFGPLQAGP SNAGGKRKLS LMLDEGSSCP TPAKFNTCPL PGALLQDPYF IQSPLPETNL GLSPHRARGP IISDIPEDSP SPEGTRLSPS SDGRREKGLA LLKEEPASPG GDGEAGLALA PNECDFCVTA PPPLPVAVVQ AILEGKGSFS PEGPRNAQQP EPGDPREIPD RGPLGLESGD RSPESLLPPM LLQPPQESVE PAGPLDVLGP SLQGREWTLM DLDMELSLMQ PLVPERGEPE LAVKGLNSPS PGKDPTLGAP LLLDVQAALG GPALGLPGAL TIYSTPESRT ASYLGPEASP SP
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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
HSF4 (Heat Shock Factor 4) is a member of the heat shock factor family, which plays a crucial role in the cellular stress response, particularly under conditions of heat stress. The importance of HSF4 is highlighted by its involvement in regulating the expression of heat shock proteins (HSPs), which are essential for protein folding, repair, and degradation processes, thereby maintaining cellular homeostasis. Research into HSF4 has gained traction due to its significant implications in various biological processes, including development and differentiation, particularly in the eye and lens. Mutations or dysregulation of HSF4 have been linked to congenital cataracts and other ocular disorders, underscoring its role in lens transparency and integrity. Furthermore, HSF4 has been implicated in cancer biology, where its expression may affect tumorigenesis and the adaptive response of cancer cells to environmental stressors. Understanding the structure, function, and regulation of HSF4 is crucial for elucidating its mechanisms in both normal physiology and disease states. Recent advances in recombinant protein technology have enabled the detailed analysis of HSF4, facilitating studies on its interactions and functional roles. This research is vital for developing therapeutic strategies that target HSF4-related pathways, potentially offering new avenues for treating heat stress-related conditions and eye diseases.
