HSF1 pSer303 Rabbit Polyclonal Antibody

Specifications

Product Data
Applications	IHC, WB
Recommend Dilution	Western Blot: 1/500~1/1000. Immunohistochemistry on Paraffin Sections: 1/50~1/100.
Reactivity	Human
Host	Rabbit
Clonality	Polyclonal
Immunogen	The antiserum was produced against synthesized phosphopeptide derived from Human HSF1 around the phosphorylation site of Serine 303 (P-P-Sp-P-P).
Specificity	This antibody detects endogenous levels of HSF1 only when phosphorylated at Serine 303.
Formulation	PBS (without Mg2+ and Ca2+), pH 7.4 containing 150mM NaCl, 0.02% Sodium Azide and 50% Glycerol. State: Aff - Purified State: Liquid purified IgG fraction.
Concentration	lot specific
Purification	Affinity Chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Conjugation	Unconjugated
Storage Condition	Store the antibody at -20°C. Avoid repeated freezing and thawing.
Gene Name	heat shock transcription factor 1
Database Link	Entrez Gene 3297 Human UniProt ID Q00613
Background	All organisms respond to elevated temperatures and a variety of environmental stresses by rapid synthesis of heat shock RNAs and proteins. The regulation of heat shock gene transcription is mediated by the transcriptional activator, heat shock factor (HSF), which binds to heat shock response elements (HSEs). These HSEs are found as three repeats of a 5-nucleotide {nGAAn} module, arranged in alternating orientation and present upstream of all heat shock genes. The HSEs are highly conserved among species yet HSF purified from yeast, Drosophila and human have different molecular weights and the proteins do not show significant immunological cross reaction. Two HSFs have been identified in human cells, HSF 1 and HSF 2, which bind to the same HSEs and have 38% sequence identity. These factors are activated by distinct stimuli, HSF 1 is responsive to classical stress signals such as heat, heavy metals and oxidative reagents, whereas HSF 2 is activated during hemin-mediated differentiation of human erythroleukemia cells. HSF 1 exists constitutively in the cytoplasm and the nucleus of unstressed cells as a monomer which lacks DNA binding activity. Through an unknown signal generated during stress, HSF 1 becomes activated to a nuclear localized, trimeric state which binds to DNA. The phosphorylation of HSF 1 is necessary for maximal transcription of heat shock genes.
Synonyms	HSTF1, HSF-1
Reference Data

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