HSF1 Antibody
Description
Product Specs
Product Science Overview
Heat Shock Transcription Factor-1 (HSF1) is a crucial protein that plays a significant role in the cellular response to stress. It is highly conserved across eukaryotes and is the primary mediator of transcriptional responses to proteotoxic stress. This article delves into the background, structure, function, and significance of HSF1, particularly focusing on the mouse anti-human HSF1 antibody.
HSF1 consists of several domains that regulate its binding and activity . The key domains include:
- DNA-Binding Domain (DBD): This N-terminal domain is the most conserved region in the HSF protein family. It recognizes the sequence nGAAn on target DNA, which constitutes heat shock elements (HSEs) for active HSF1 trimers to bind.
- Oligomerization Domain (Leucine Zipper Domains): These regions are responsible for oligomerization between HSF1 monomers. Under non-stress conditions, spontaneous HSF1 activation is negatively regulated by the interaction between these domains.
- Regulatory Domain (RD): Situated between the oligomerization domains, the RD regulates the Trans-Activation Domain (TAD) through negative control by repressing TAD in the absence of stress.
- Trans-Activation Domain (TAD): This C-terminal region contains two TADs (TAD1 and TAD2) that are crucial for HSF1’s transcriptional activation.
HSF1 functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR). Upon exposure to heat and other stress stimuli, HSF1 undergoes homotrimerization and activates HSP gene transcription through binding to site-specific HSEs present in the promoter regions of HSP genes . This leads to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage.
In unstressed cells, HSF1 is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form. Upon heat shock stress, HSF1 forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, thereby increasing cell survival .
The mouse anti-human HSF1 antibody is an IgG1 κ monoclonal antibody that detects the HSF1 protein of mouse, rat, and human origin. It is used in various applications such as Western Blot (WB), Immunoprecipitation (IP), Immunofluorescence (IF), Immunohistochemistry (IHC), and Enzyme-Linked Immunosorbent Assay (ELISA) .
HSF1 is involved in several critical cellular processes beyond the heat shock response. It plays a role in the regulation of lifespan, development, and metabolism. HSF1 also has important functions in non-stress regulation, such as activating transcription of transcription factor FOXR1, which in turn activates transcription of heat shock chaperones HSPA1A and HSPA6, and the antioxidant NADPH-dependent reductase DHRS2 .
Moreover, HSF1 has been implicated in various diseases, including cancer. Genetic elimination of HSF1 has been shown to protect mice from tumors induced by mutations in the RAS oncogene or a hot spot mutation in the tumor suppressor gene P53 . HSF1 promotes apoptotic cell death of pachytene spermatocytes exposed to thermal stress, indicating its role in quality control during spermatogenesis .
