HSF1 Protein, Human, Recombinant (His)

Heat shock factor protein 1, also known as heat shock transcription factor 1, HSF1, and HSTF1, is a cytoplasm and nucleus protein that belongs to the HSF family. HSF1 is the major transcription factor of HSPs (heat shock proteins) in response to various stresses. Wild type HSF1 (heat shock transcriptional factor 1) is normally inactive. HSF1 / HSTF1 is a DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. HSF1 / HSTF1 protects cells and organisms against various types of stress, either by triggering a complex response that promotes cell survival or by triggering cell death when stress-induced alterations cannot be rescued. HSF1 / HSTF1 is the key protein in regulating the stress response. It can be activated under heat, oxidative, or other stress conditions. Dominant-positive and dominant-negative HSF1 are two types of HSF1 mutants. Both of them gain DNA binding activity in the absence of stress. Also, dominant-positive HSF1 acquires transcriptional activity, which dominant-negative HSF1 does not acquire. HSF1 / HSTF1 was also reported to contribute to cell resistance against genotoxic stress, such as that caused by doxorubicin, an anticancer drug in common clinical use.

Pack Size	Availability	Price/USD	Quantity
100 μg	5 days	$ 600.00

Description

Species	Human
Expression System	E. coli
Tag	His
Accession Number	Q00613-1
Synonyms	HSTF1, heat shock transcription factor 1
Construction	A DNA sequence encoding the human HSF1 isoform long (Q00613-1) (Asp 2-Ser 529) was expressed, with a polyhistide tag at the N-terminus.
Protein Purity	> 70 % as determined by SDS-PAGE
Molecular Weight	Approxiamtely 58.6 kDa

Endotoxin	Please contact us for more information.
Formulation	Lyophilized from sterile PBS, pH 7.0Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution	A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage	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.
Shipping	In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background	Heat shock factor protein 1, also known as heat shock transcription factor 1, HSF1, and HSTF1, is a cytoplasm and nucleus protein that belongs to the HSF family. HSF1 is the major transcription factor of HSPs (heat shock proteins) in response to various stresses. Wild type HSF1 (heat shock transcriptional factor 1) is normally inactive. HSF1 / HSTF1 is a DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. HSF1 / HSTF1 protects cells and organisms against various types of stress, either by triggering a complex response that promotes cell survival or by triggering cell death when stress-induced alterations cannot be rescued. HSF1 / HSTF1 is the key protein in regulating the stress response. It can be activated under heat, oxidative, or other stress conditions. Dominant-positive and dominant-negative HSF1 are two types of HSF1 mutants. Both of them gain DNA binding activity in the absence of stress. Also, dominant-positive HSF1 acquires transcriptional activity, which dominant-negative HSF1 does not acquire. HSF1 / HSTF1 was also reported to contribute to cell resistance against genotoxic stress, such as that caused by doxorubicin, an anticancer drug in common clinical use.