Recombinant human Hsp90 beta protein (Active) is a Human Full Length protein, in the 1 to 724 aa range, expressed in Baculovirus infected BTI-TN-5B1-4, with >90% purity and suitable for SDS-PAGE, ELISA, Inhib, WB, FuncS.
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- Advanced science (Weinheim, Baden-Wurttemberg, Germany) 10:e23020252023HSP90β Impedes STUB1-Induced Ubiquitination of YTHDF2 to Drive Sorafenib Resistance in Hepatocellular Carcinoma.Applications:Unspecified applicationReactive species:Unspecified reactive speciesYuning Liao,Yuan Liu,Cuifu Yu,Qiucheng Lei,Ji Cheng,Weiyao Kong,Yuanhui Yu,Xuefen Zhuang,Wenshuang Sun,Shusha Yin,Gengxi Cai,Hongbiao HuangPubMed 37515378
- Drug testing and analysis 13:903-9152021A cell-free bioassay for the detection of androgens.Applications:Unspecified applicationReactive species:Unspecified reactive speciesElliot R Cooper,Gillian Hughes,Alexia Kauff,Emma Sutherland,Zoe Ashley,Alison K HeatherPubMed 33709622
- Nanoscale 12:15857-158682020A method to measure the denatured proteins in the corona of nanoparticles based on the specific adsorption of Hsp90ab1.Applications:Unspecified applicationReactive species:Unspecified reactive speciesShang Liu,Xinbang Jiang,Xuejiao Tian,Zhenzhen Wang,Zhen Xing,Jiahui Chen,Junfeng Zhang,Chunming Wang,Lei DongPubMed 32696774
Key facts
- Purity
>90% SDS-PAGE
- Expression system
Baculovirus infected BTI-TN-5B1-4 cells
- Tags
Tag free
- Applications
SDS-PAGE, ELISA, Inhib, WB, FuncS
- Biologically active
Yes
Amino acid sequence
M P E E V H H G E E E V E T F A F Q A E I A Q L M S L I I N T F Y S N K E I F L R E L I S N A S D A L D K I R Y E S L T D P S K L D S G K E L K I D I I P N P Q E R T L T L V D T G I G M T K A D L I N N L G T I A K S G T K A F M E A L Q A G A D I S M I G Q F G V G F Y S A Y L V A E K V V V I T K H N D D E Q Y A W E S S A G G S F T V R A D H G E P I G R G T K V I L H L K E D Q T E Y L E E R R V K E V V K K H S Q F I G Y P I T L Y L E K E R E K E I S D D E A E E E K G E K E E E D K D D E E K P K I E D V G S D E E D D S G K D K K K K T K K I K E K Y I D Q E E L N K T K P I W T R N P D D I T Q E E Y G E F Y K S L T N D W E D H L A V K H F S V E G Q L E F R A L L F I P R R A P F D L F E N K K K K N N I K L Y V R R V F I M D S C D E L I P E Y L N F I R G V V D S E D L P L N I S R E M L Q Q S K I L K V I R K N I V K K C L E L F S E L A E D K E N Y K K F Y E A F S K N L K L G I H E D S T N R R R L S E L L R Y H T S Q S G D E M T S L S E Y V S R M K E T Q K S I Y Y I T G E S K E Q V A N S A F V E R V R K R G F E V V Y M T E P I D E Y C V Q Q L K E F D G K S L V S V T K E G L E L P E D E E E K K K M E E S K A K F E N L C K L M K E I L D K K V E K V T I S N R L V S S P C C I V T S T Y G W T A N M E R I M K A Q A L R D N S T M G Y M M A K K H L E I N P D H P I V E T L R Q K A E A D K N D K A V K D L V V L L F E T A L L S S G F S L E D P Q T H S N R I Y R M I K L G L G I D E D E V A A E E P N A A V P D E I P P L E G D E D A S R M E E V D
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application Inhib | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes ab80033 can be used as a WB positive control in conjunction with Anti-Hsp90 beta antibody [H90-10] ab53497. |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Associated Products
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Target data
Function
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059).
Alternative names
Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, HSPCB, HSPC2, HSP90B, HSP90AB1
Recommended products
Recombinant human Hsp90 beta protein (Active) is a Human Full Length protein, in the 1 to 724 aa range, expressed in Baculovirus infected BTI-TN-5B1-4, with >90% purity and suitable for SDS-PAGE, ELISA, Inhib, WB, FuncS.
Alternative names
Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, HSPCB, HSPC2, HSP90B, HSP90AB1
Key facts
- Purity
>90% SDS-PAGE
- Expression system
Baculovirus infected BTI-TN-5B1-4 cells
- Tags
Tag free
- Applications
SDS-PAGE, ELISA, Inhib, WB, FuncS
- Biologically active
Yes
- Biological activity
1. The reactions are in 33 mM Hepes pH7.2, 30 mM NaCl, 5 mM MgCl2, 1 mM DTT, 1.5 mM ATP in a 100 μl reaction at 37°C. It is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.
2. The protein concentrations (where applicable) were 2 μM Hsp90 (Hsp90 beta), 2 μM Ahsa1 (His tagged human Ahsa1), 4 μM p23 (cleaved human p23), 4 μM HOP (His-tagged human HOP).
3. Addition of a two-fold excess of p23 reduced Aha1-mediated Hsp90 stimulation by 30% (when using 2 μM Hsp90 and Aha1).
4. Addition of a two -fold excess of HOP completely eliminated Aha1-mediated ATPase stimulation as well as intrinsic Hsp90 ATPase activity.
- Accession
- P08238-1
- Animal free
No
- Species
Human
- Concentration
- Storage buffer
Constituents: 10% Glycerol (glycerin, glycerine), 1.015% Sodium chloride, 0.242% Tris, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00292% EDTA
Sequence info
Amino acid sequence
M P E E V H H G E E E V E T F A F Q A E I A Q L M S L I I N T F Y S N K E I F L R E L I S N A S D A L D K I R Y E S L T D P S K L D S G K E L K I D I I P N P Q E R T L T L V D T G I G M T K A D L I N N L G T I A K S G T K A F M E A L Q A G A D I S M I G Q F G V G F Y S A Y L V A E K V V V I T K H N D D E Q Y A W E S S A G G S F T V R A D H G E P I G R G T K V I L H L K E D Q T E Y L E E R R V K E V V K K H S Q F I G Y P I T L Y L E K E R E K E I S D D E A E E E K G E K E E E D K D D E E K P K I E D V G S D E E D D S G K D K K K K T K K I K E K Y I D Q E E L N K T K P I W T R N P D D I T Q E E Y G E F Y K S L T N D W E D H L A V K H F S V E G Q L E F R A L L F I P R R A P F D L F E N K K K K N N I K L Y V R R V F I M D S C D E L I P E Y L N F I R G V V D S E D L P L N I S R E M L Q Q S K I L K V I R K N I V K K C L E L F S E L A E D K E N Y K K F Y E A F S K N L K L G I H E D S T N R R R L S E L L R Y H T S Q S G D E M T S L S E Y V S R M K E T Q K S I Y Y I T G E S K E Q V A N S A F V E R V R K R G F E V V Y M T E P I D E Y C V Q Q L K E F D G K S L V S V T K E G L E L P E D E E E K K K M E E S K A K F E N L C K L M K E I L D K K V E K V T I S N R L V S S P C C I V T S T Y G W T A N M E R I M K A Q A L R D N S T M G Y M M A K K H L E I N P D H P I V E T L R Q K A E A D K N D K A V K D L V V L L F E T A L L S S G F S L E D P Q T H S N R I Y R M I K L G L G I D E D E V A A E E P N A A V P D E I P P L E G D E D A S R M E E V D
- Accession
- Protein length
Full Length
- Predicted molecular weight
90 kDa
- Amino acids
1 to 724
- Nature
Recombinant
Specifications
- Form
Liquid
- Additional notes
ab80033 is Affinity Purified, Endotoxin-free
General info
- Function
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059).
- Sequence similarities
Belongs to the heat shock protein 90 family.
- Post-translational modifications
Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).
- Subcellular localisation
Nucleus
Storage
- Shipped at conditions
Blue Ice
- Appropriate short-term storage duration
1-2 weeks
- Appropriate short-term storage conditions
+4°C
- Appropriate long-term storage conditions
-20°C
- Aliquoting information
Upon delivery aliquot
- Storage information
Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Notes
ab80033 is endotoxin free. <0.1 EU/ml.
Supplementary info
This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Hsp90 beta also known as Hsp90AB1 or Hsp90 protein is a heat shock protein of approximately 90 kDa. It is a molecular chaperone found in most eukaryotic cells. Hsp90 beta helps in the proper folding stabilization and degradation of many proteins. Unlike its isoform Hsp90 alpha Hsp90 beta has a more stable expression and is not typically induced by stress. This protein is primarily localized in the cytosol but can also be present in other cellular compartments depending on the cellular state.
- Biological function summary
Hsp90 beta functions to maintain protein homeostasis and cellular integrity. It forms part of a multi-protein chaperone complex which includes cochaperones such as Hop Hsp70 and p23 necessary for its full functionality. Hsp90 beta supports the maturation of steroid hormone receptors kinases and other client proteins. It plays an important role in the cell cycle regulation through its interaction with various proteins ensuring proper cell division and growth.
- Pathways
Hsp90 beta is deeply involved in signal transduction and cellular stress response pathways. Its interaction with the Akt pathway is significant for cell survival signals. Hsp90 beta also participates in the MAP kinase pathway affecting cell growth and differentiation. The protein associates with multiple kinases including RAF and Src which are important for downstream signaling.
- Associated diseases and disorders
The dysregulation of Hsp90 beta is associated with cancer and neurodegenerative diseases. In cancer Hsp90 beta stabilizes many oncoproteins making it a potential therapeutic target for inhibiting tumor growth. It interacts with client proteins like the proto-oncogene c-Src promoting tumorigenesis. In neurodegenerative disorders such as Alzheimer's disease improper interaction between Hsp90 beta and tau proteins can contribute to disease progression impacting neuronal function.
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3 product images
SDS-PAGE - Recombinant human Hsp90 beta protein (Active) (ab80033)
SDS-PAGE of Hsp90 beta protein (ab80033).
Western blot - Recombinant human Hsp90 beta protein (Active) (ab80033)
All lanes: Western blot - Anti-Hsp90 beta antibody [H90-10] (Anti-Hsp90 beta antibody [H90-10] ab53497) at 1 µg/mL
All lanes: Western blot - Recombinant human Hsp90 beta protein (Active) (ab80033) at 0.1 µg
SecondaryAll lanes: Western blot - Goat Anti-Mouse IgG H&L (HRP) preadsorbed (Goat Anti-Mouse IgG H&L (HRP) preadsorbed ab97040) at 1/5000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size: 83 kDa
Exposure time: 8min
Western blot - Recombinant human Hsp90 beta protein (Active) (ab80033)
Blocking and dilution buffer: 5% NFDM/TBST.
All lanes: Western blot - Anti-Hsp90 antibody [EPR3953] (Anti-Hsp90 antibody [EPR3953] ab109248) at 1/1000 dilution
Lane 1: Western blot - Recombinant Human Hsp90 alpha protein (His tag) (Recombinant Human Hsp90 alpha protein (His tag) ab48801) at 0.015 µg
Lane 2: Western blot - Recombinant human Hsp90 beta protein (Active) (ab80033) at 0.015 µg
SecondaryAll lanes: Western blot - Goat Anti-Rabbit IgG H&L (HRP) (Goat Anti-Rabbit IgG H&L (HRP) ab97051) at 1/20000 dilution
Predicted band size: 85 kDa
Observed band size: 90 kDa
Exposure time: 5s
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