HSF2 Protein, Human (His)

As a DNA-binding protein, HSF2 protein has specific affinity for the heat shock promoter element (HSE), thereby activating transcription. Notably, in higher eukaryotes, the ability of HSF2 to bind to HSE depends on the exposure of cells to heat shock. HSF2 Protein, Human (His) is the recombinant human-derived HSF2 protein, expressed by E. coli , with N-6*His labeled tag. The total length of HSF2 Protein, Human (His) is 126 a.a., with molecular weight of ~26.0 kDa.

The HSF2 protein serves as a DNA-binding factor with a distinct affinity for heat shock promoter elements (HSE), facilitating the activation of transcription. Notably, in higher eukaryotes, HSF2 demonstrates an intriguing behavior—it remains incapable of binding to HSE unless cells undergo heat shock conditions. Found predominantly as a homodimer in normal cellular states, HSF2 undergoes a transformative shift to a DNA-binding homotrimer configuration in response to cellular stress or heat shock. This trimeric form of HSF2 plays a critical role in initiating transcription, thereby regulating the expression of genes crucial for the cellular response to stress. The dynamic interplay between homodimeric and homotrimeric states underscores the nuanced regulatory function of HSF2 in orchestrating cellular responses to environmental challenges. (

Human

E. coli

N-6*His

Q03933 (S411-S536)

3298  [NCBI]

SENKGLETTKNNVVQPVSEEGRKSKSKPDKQLIQYTAFPLLAFLDGNPASSVEQASTTASSEVLSSVDKPIEVDELLDSSLDPEPTQSKLVRLEPLTEAEASEATLFYLCELAPAPLDSDMPLLDS

Approximately 26.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.