HSF1 Protein, Human (His)

HSF1, a stress-inducible transcription factor, orchestrates the heat shock response by activating heat shock genes through binding to heat shock elements (HSEs). In unstressed cells, it remains inactive in a multichaperone complex. Upon stress, HSF1 undergoes homotrimerization, binds to HSEs, and activates HSP gene transcription. It also participates in various cellular functions, including regulation of mitotic progression, repression of c-fos gene, and negative regulation of non-homologous end joining repair. Additionally, HSF1 plays a role in HIV-1 transcriptional reactivation. HSF1 Protein, Human (His) is the recombinant human-derived HSF1 protein, expressed by E. coli , with N-His, N-6*His labeled tag. The total length of HSF1 Protein, Human (His) is 528 a.a., with molecular weight of ~67 kDa.

HSF1, a stress-responsive and DNA-binding transcription factor, is a central orchestrator of the heat shock response (HSR), leading to the transcriptional activation of a multitude of heat shock proteins (HSPs) crucial for cellular protection against damage. In unstressed conditions, HSF1 resides in a HSP90-containing multichaperone complex, maintaining an inactivated monomeric state. Upon exposure to stress, particularly heat, HSF1 undergoes homotrimerization and activates the transcription of HSP genes by binding to heat shock elements (HSEs) in their promoters. This transition is reversible, and during the recovery phase of the HSR, HSF1 returns to its unactivated form. Beyond transcriptional activation, HSF1 participates in various cellular processes, including chromatin-associated complex formation with TTC5/STRAP and p300/EP300, repression of Ras-induced c-fos gene transcription, regulation of pre-mRNA processing, nuclear export of stress-induced mRNA, and modulation of mitotic progression. Additionally, in the context of microbial infection, HSF1 plays a role in the reactivation of latent human immunodeficiency virus (HIV-1) transcription by binding to the HIV-1 long terminal repeat promoter.

Human

E. coli

N-His;N-6*His

Q00613-1 (D2-S529)

3297  [NCBI]

DLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGSVDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS

Approximately 67 kDa

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  Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized a 0.2 μm filtered solution of PBS, pH 7.0.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.