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Thermo Fisher Scientific Phospho-HSF1 (Ser121) Polyclonal Antibody
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Thermo Fisher Scientific Phospho-HSF1 (Ser121) Polyclonal Antibody

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HSF1 단백질의 Ser121 인산화 부위를 인식하는 Rabbit Polyclonal 항체. Western blot 및 IHC(Paraffin)에서 검증됨. Human 및 Mouse 반응성. 항원 친화 크로마토그래피로 정제된 액상 항체로, -20°C에서 보관.

카탈로그번호
PA539718
판매단위
pk
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마지막 업데이트 2025. 07. 31. 오전 01:39
Thermo Fisher Scientific PA539718 Phospho-HSF1 (Ser121) Polyclonal Antibody 100 ug pk판매 단위 pk ·
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630,500원VAT 포함 693,550원

Thermo Fisher Scientific · Thermo Fisher Scientific Phospho-HSF1 (Ser121) Polyclonal Antibody

Applications and Tested Dilutions

Application Tested Dilution
Western Blot (WB) 1:500–1:1,000
Immunohistochemistry (Paraffin) (IHC (P)) 1:50–1:100

Product Specifications

항목 내용
Species Reactivity Human, Mouse
Host / Isotype Rabbit / IgG
Class Polyclonal
Type Antibody
Immunogen A synthetic phosphopeptide derived from human HSF1 around the phosphorylation site of Ser121 (V-T-SP-V-S)
Conjugate Unconjugated
Form Liquid
Concentration 1 mg/mL
Purification Antigen affinity chromatography
Storage Buffer Dulbecco’s PBS, pH 7.4, with 50% glycerol
Contains 0.02% sodium azide
Storage Conditions -20°C
Shipping Conditions Wet ice
RRID AB_2556269

Target Information

All organisms respond to elevated temperatures and various 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 composed of three repeats of a 5-nucleotide {nGAAn} module arranged in alternating orientation upstream of heat shock genes. Although HSEs are conserved among species, HSFs from yeast, Drosophila, and human differ in molecular weight and immunological cross-reactivity.

Two HSFs (HSF1 and HSF2) have been identified in human cells, sharing 38% sequence identity and binding to the same HSEs. HSF1 responds to classical stress signals such as heat, heavy metals, and oxidative reagents, while HSF2 is activated during hemin-mediated differentiation of human erythroleukemia cells. HSF1 exists constitutively in the cytoplasm and nucleus of unstressed cells as a monomer lacking DNA-binding activity. Upon stress, HSF1 becomes activated to a nuclear-localized trimeric form that binds DNA. Phosphorylation of HSF1 is essential for maximal transcription of heat shock genes.


For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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