ARG22258

anti-HSF1 antibody [10H8]

anti-HSF1 antibody [10H8] for Western blot,ICC/IF,Immunoprecipitation,ELISA,Gel supershift assays and Human,Monkey,Mouse,Rat,Bovine,Guinea pig,Hamster,Rabbit

Overview

Product Description Rat Monoclonal antibody [10H8] recognizes HSF1
Tested Reactivity Hu, Ms, Rat, Bov, Gpig, Hm, Mk, Rb
Tested Application ELISA, GSA, ICC/IF, IP, WB
Specificity Detects ~85kDa (unstressed cell lysates), and~95kDa (heat shocked cell lysates).
Host Rat
Clonality Monoclonal
Clone 10H8
Isotype IgG1
Target Name HSF1
Antigen Species Mouse
Immunogen Purified recombinant Mouse HSF1 protein
Epitope around aa. 378-395
Conjugation Un-conjugated
Alternate Names Heat shock transcription factor 1; Heat shock factor protein 1; HSF 1; HSTF 1; HSTF1

Application Instructions

Application Suggestion
Tested Application Dilution
ELISAAssay-dependent
GSAAssay-dependent
ICC/IF1:200
IPAssay-dependent
WB1:1000
Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.

Properties

Form Liquid
Purification Purification with Protein G.
Buffer PBS (pH 7.4), 0.09% Sodium azide and 50% Glycerol
Preservative 0.09% Sodium azide
Stabilizer 50% Glycerol
Concentration 1 mg/ml
Storage Instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Database Links

GeneID: 15499 Mouse HSF1

GeneID: 3297 Human HSF1

GeneID: 506235 Bovine HSF1

Gene Symbol Hsf1
Gene Full Name heat shock factor 1
Background The product of this gene is a heat-shock transcription factor. Transcription of heat-shock genes is rapidly induced after temperature stress. Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of this gene. [provided by RefSeq, Jul 2008]
Function DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. [UniProt]
Cellular Localization Cytoplasm, Nucleus
Calculated MW ~85 kDa (unstressed cell lysates), and ~95 kDa (heat shocked cell lysates).
PTM Phosphorylated (PubMed:9499401, PubMed:10359787, PubMed:11583998, PubMed:26159920). Phosphorylated in unstressed cells; this phosphorylation is constitutive and implicated in the repression of HSF1 transcriptional activity (PubMed:8946918, PubMed:8940068, PubMed:9121459, PubMed:16278218). Phosphorylated on Ser-121 by MAPKAPK2; this phosphorylation promotes interaction with HSP90 proteins and inhibits HSF1 homotrimerization, DNA-binding and transactivation activities (PubMed:16278218). Phosphorylation on Ser-303 by GSK3B/GSK3-beta and on Ser-307 by MAPK3 within the regulatory domain is involved in the repression of HSF1 transcriptional activity and occurs in a RAF1-dependent manner (PubMed:8946918, PubMed:8940068, PubMed:9121459, PubMed:9535852, PubMed:10747973, PubMed:12646186). Phosphorylation on Ser-303 and Ser-307 increases HSF1 nuclear export in a YWHAE- and XPO1/CRM1-dependent manner (PubMed:12917326). Phosphorylation on Ser-307 is a prerequisite for phosphorylation on Ser-303 (PubMed:8940068). According to PubMed:9535852, Ser-303 is not phosphorylated in unstressed cells. Phosphorylated on Ser-419 by PLK1; phosphorylation promotes nuclear translocation upon heat shock (PubMed:15661742). Hyperphosphorylated upon heat shock and during the attenuation and recovery phase period of the heat shock response (PubMed:11447121, PubMed:12659875, PubMed:24581496). Phosphorylated on Thr-142; this phosphorylation increases HSF1 transactivation activity upon heat shock (PubMed:12659875). Phosphorylation on Ser-230 by CAMK2A; this phosphorylation enhances HSF1 transactivation activity upon heat shock (PubMed:11447121). Phosphorylation on Ser-326 by MAPK12; this phosphorylation enhances HSF1 nuclear translocation, homotrimerization and transactivation activities upon heat shock (PubMed:15760475, PubMed:27354066). Phosphorylated on Ser-320 by PRKACA/PKA; this phosphorylation promotes nuclear localization and transcriptional activity upon heat shock (PubMed:21085490). Phosphorylated on Ser-363 by MAPK8; this phosphorylation occurs upon heat shock, induces HSF1 translocation into nuclear stress bodies and negatively regulates transactivation activity (PubMed:10747973). Neither basal nor stress-inducible phosphorylation on Ser-230, Ser-292, Ser-303, Ser-307, Ser-314, Ser-319, Ser-320, Thr-323, Ser-326, Ser-338, Ser-344, Ser-363, Thr-367, Ser-368 and Thr-369 within the regulatory domain is involved in the regulation of HSF1 subcellular localization or DNA-binding activity; however, it negatively regulates HSF1 transactivation activity (PubMed:25963659). Phosphorylated on Ser-216 by PLK1 in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex inducing HSF1 degradation, and hence mitotic progression (PubMed:18794143). Dephosphorylated on Ser-121, Ser-307, Ser-314, Thr-323 and Thr-367 by phosphatase PPP2CA in an IER5-dependent manner, leading to HSF1-mediated transactivation activity (PubMed:26754925).
Sumoylated with SUMO1 and SUMO2 upon heat shock in a ERK2-dependent manner (PubMed:12646186, PubMed:12665592). Sumoylated by SUMO1 on Lys-298; sumoylation occurs upon heat shock and promotes its localization to nuclear stress bodies and DNA-binding activity (PubMed:11514557). Phosphorylation on Ser-303 and Ser-307 is probably a prerequisite for sumoylation (PubMed:12646186, PubMed:12665592).
Acetylated on Lys-118; this acetylation is decreased in a IER5-dependent manner (PubMed:26754925). Acetylated on Lys-118, Lys-208 and Lys-298; these acetylations occur in a EP300-dependent manner (PubMed:24581496, PubMed:27189267). Acetylated on Lys-80; this acetylation inhibits DNA-binding activity upon heat shock (PubMed:19229036). Deacetylated on Lys-80 by SIRT1; this deacetylation increases DNA-binding activity (PubMed:19229036).
Ubiquitinated by SCF(BTRC) and degraded following stimulus-dependent phosphorylation at Ser-216 by PLK1 in mitosis (PubMed:18794143). Polyubiquitinated (PubMed:24581496). Undergoes proteasomal degradation upon heat shock and during the attenuation and recovery phase period of the heat shock response (PubMed:24581496).

Images (3) Click the Picture to Zoom In

  • ARG22258 anti-HSF1 antibody [10H8] WB image

    Western blot: Human Heat Shocked HeLa cell lysates stained with ARG22258 anti-HSF1 antibody [10H8].

  • ARG22258 anti-HSF1 antibody [10H8] ICC/IF image

    Immunocytochemistry: 2% Formaldehyde (20 min at RT) fixed Heat Shocked HeLa cells stained with ARG22258 anti-HSF1 antibody [10H8] (green) at 1:100 dilution (12 hours at 4°C). Counterstain: DAPI (blue) nuclear stain at 1:40000 for 120 min at RT. Magnification: 100x. Left: DAPI (blue) nuclear stain, Middle: Primary antibody, Right: Composite.

  • ARG22258 anti-HSF1 antibody [10H8] ICC/IF image

    Immunocytochemistry: 2% Formaldehyde (20 min at RT) fixed Heat Shocked HeLa cells stained with ARG22258 anti-HSF1 antibody [10H8] (red) at 1:100 dilution (12 hours at 4°C). Counterstain: DAPI (blue) nuclear stain at 1:40000 for 120 min at RT. Magnification: 20x. Left: DAPI (blue) nuclear stain, Middle: Primary antibody, Right: Composite.