Recombinant Human HSF1 protein is a Human Full Length protein, expressed in Escherichia coli, with >75% purity and suitable for SDS-PAGE, WB.
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Key facts
- Purity
- >75% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE, WB
- Biologically active
- No
Amino acid sequence
M G S S H H H H H H S S G L V P R G S H M D L P V G P G A A G P S N V P A F L T K L W T L V S D P D T D A L I C W S P S G N S F H V F D Q G Q F A K E V L P K Y F K H N N M A S F V R Q L N M Y G F R K V V H I E Q G G L V K P E R D D T E F Q H P C F L R G Q E Q L L E N I K R K V T S V S T L K S E D I K I R Q D S V T K L L T D V Q L M K G K Q E C M D S K L L A M K H E N E A L W R E V A S L R Q K H A Q Q Q K V V N K L I Q F L I S L V Q S N R I L G V K R K I P L M L N D S G S A H S M P K Y S R Q F S L E H V H G S G P Y S A P S P A Y S S S S L Y A P D A V A S S G P I I S D I T E L A P A S P M A S P G G S I D E R P L S S S P L V R V K E E P P S P P Q S P R V E E A S P G R P S S V D T L L S P T A L I D S I L R E S E P A P A S V T A L T D A R G H T D T E G R P P S P P P T S T P E K C L S V A C L D K N E L S D H L D A M D S N L D N L Q T M L S S H G F S V D T S A L L D L F S P S V T V P D M S L P D L D S S L A S I Q E L L S P Q E P P R P P E A E N S S P D S G K Q L V H Y T A Q P L F L L D P G S V D T G S N D L P V L F E L G E G S Y F S E G D G F A E D P T I S L L T G S E P P K A K D P T V S
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes ab78795 can be used as a WB positive control in conjunction with ab82586. |
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Target data
Function
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), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:11447121, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:18451878, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7760831, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107, PubMed:9499401, PubMed:9535852, PubMed:9727490). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:11583998, PubMed:16278218, PubMed:9727490). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7935471, PubMed:8455624, PubMed:8940068, PubMed:9499401, PubMed:9727490). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925). (Microbial infection) Plays a role in latent human immunodeficiency virus (HIV-1) transcriptional reactivation. Binds to the HIV-1 long terminal repeat promoter (LTR) to reactivate viral transcription by recruiting cellular transcriptional elongation factors, such as CDK9, CCNT1 and EP300.
Alternative names
HSTF1, HSF1, Heat shock factor protein 1, HSF 1, Heat shock transcription factor 1, HSTF 1
Recommended products
Recombinant Human HSF1 protein is a Human Full Length protein, expressed in Escherichia coli, with >75% purity and suitable for SDS-PAGE, WB.
Key facts
- Purity
- >75% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- Tag free
- Applications
- SDS-PAGE, WB
- Biologically active
- No
- Accession
- Q00613-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 0.29% Sodium chloride, 0.242% Tris, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Sequence info
Amino acid sequence
- M G S S H H H H H H S S G L V P R G S H M D L P V G P G A A G P S N V P A F L T K L W T L V S D P D T D A L I C W S P S G N S F H V F D Q G Q F A K E V L P K Y F K H N N M A S F V R Q L N M Y G F R K V V H I E Q G G L V K P E R D D T E F Q H P C F L R G Q E Q L L E N I K R K V T S V S T L K S E D I K I R Q D S V T K L L T D V Q L M K G K Q E C M D S K L L A M K H E N E A L W R E V A S L R Q K H A Q Q Q K V V N K L I Q F L I S L V Q S N R I L G V K R K I P L M L N D S G S A H S M P K Y S R Q F S L E H V H G S G P Y S A P S P A Y S S S S L Y A P D A V A S S G P I I S D I T E L A P A S P M A S P G G S I D E R P L S S S P L V R V K E E P P S P P Q S P R V E E A S P G R P S S V D T L L S P T A L I D S I L R E S E P A P A S V T A L T D A R G H T D T E G R P P S P P P T S T P E K C L S V A C L D K N E L S D H L D A M D S N L D N L Q T M L S S H G F S V D T S A L L D L F S P S V T V P D M S L P D L D S S L A S I Q E L L S P Q E P P R P P E A E N S S P D S G K Q L V H Y T A Q P L F L L D P G S V D T G S N D L P V L F E L G E G S Y F S E G D G F A E D P T I S L L T G S E P P K A K D P T V S
- Accession
- Q00613
- Protein length
- Full Length
- Nature
- Recombinant
Specifications
- Form
- Liquid
- Additional notes
Purified by using conventional chromatography techniques
General info
- Function
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), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:11447121, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:18451878, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7760831, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107, PubMed:9499401, PubMed:9535852, PubMed:9727490). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:11583998, PubMed:16278218, PubMed:9727490). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7935471, PubMed:8455624, PubMed:8940068, PubMed:9499401, PubMed:9727490). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925).
- Sequence similarities
Belongs to the HSF family.
- Post-translational modifications
Phosphorylated (PubMed:10359787, PubMed:11583998, PubMed:26159920, PubMed:9499401). Phosphorylated in unstressed cells; this phosphorylation is constitutive and implicated in the repression of HSF1 transcriptional activity (PubMed:16278218, PubMed:8940068, PubMed:8946918, PubMed:9121459). 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:10747973, PubMed:12646186, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9535852). 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).
- Subcellular localisation
- Nucleus, Nucleoplasm, Cytoskeleton, Spindle pole, Microtubule organizing center, Centrosome
Storage
- Shipped at conditions
- Blue Ice
- Appropriate short-term storage conditions
- -20°C
- Appropriate long-term storage conditions
- -20°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
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2 product images
SDS-PAGE - Recombinant Human HSF1 protein (ab78795)
15% SDS-PAGE showing ab78795 at approximately 59kDa (3μg).
Western blot - Recombinant Human HSF1 protein (ab78795)
All lanes: Anti-HSF1 antibody (ab82586) at 1/1000 dilution
All lanes: Western blot - Recombinant Human HSF1 protein (ab78795) at 0.01 µg
SecondaryAll lanes: Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (Goat Anti-Rabbit IgG H&L (HRP) preadsorbed ab97080) at 1/5000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Exposure time: 30s
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