Hsp90 alpha/beta Antibody (YA356)(PBS only)
(Synonyms: HSP90AA1; HSP90A; HSPC1; HSPCA; Heat shock protein HSP 90-alpha; Heat shock 86 kDa; HSP 86; HSP86; Renal carcinoma antigen NY-REN-38; HSP90AB1; HSP90B; HSPC2; HSPCB; Heat shock protein HSP 90-beta; HSP 90; Heat shock 84 kDa; HSP 84; HSP84)Hsp90 alpha/beta Antibody (YA356) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Hsp90 alpha/beta.
-
Host:
Rabbit
-
Isotype:
IgG
-
Application:
WB, IHC-F, IHC-P, ICC/IF, IP
-
Reactivity :
Human, Mouse, Rat
-
Formulation:
Supplied in PBS, pH 7.4.
-
Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
|
IHC-P
IHC-P: Immunohistochemistry-Paraffin
|
IHC-F
IHC-F: Immunohistochemistry-Frozen
|
ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IP
IP: Immunoprecipitation
|
|---|---|---|---|---|---|
| Dilution Ratio | 1:500-1:1000 | 1:50-1:100 | 1:50-1:100 | 1:50-1:200 | 1:20 |
Product Details
Hsp90 alpha/beta Antibody (YA356) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Hsp90 alpha/beta.
-
Host Rabbit
-
Species ReactivityHuman, Mouse, Rat
-
Observed Molecular WeightObserved band size: 90 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
-
Calculated Molecular Weight Predicted band size: 85 kDa
Synthetic peptide corresponding to Human Hsp90 beta.The exact sequence is proprietary to MCE.
affinity purified
Non-conjugated
IgG
Product Properties
-
Appearance
Solution
-
Formulation
Supplied in PBS, pH 7.4.
-
Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
-
Shipping
Shipping with blue ice.
Verification Images
-
Western blot analysis of extracts from C6(lane 2(20ug) , NIH/3T3(lane 3(20ug) and Hela(lane 4(20ug) using Hsp90 alpha/beta Antibody (HY-P80714) Rabbit mAb. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P83730, 1/10000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature. -
Western blot analysis was performed on extracts from Mouse brain (lane 1, 15 μg), Rat brain (lane 2, 15 μg), C6 (lane 3, 15 μg), 3T3 (lane 4, 15 μg), Hela (lane 5, 15 μg), and K562 (lane 6, 15 μg) using Hsp90 alpha/beta Rabbit mAb.Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST at 4°C overnight.The primary antibody (1:4000 dilution) and the loading control antibody (beta-Actin, HY-P83730, 1:20000 dilution) were incubated in 5% non-fat milk in TBST for 1 hour at 37°C.Goat Anti-Rabbit IgG-HRP Secondary Antibody (1:20000 dilution) was then applied for 40 minutes at 37°C. -
Immunohistochemical analysis of paraffin-embedded mouse testis tissue using Hsp90 alpha/beta Antibody. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0) for 8 minutes. The tissues were blocked in QuickBlock for 20 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody at 1/100 dilution in 4℃ overnight. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded mouse testis tissue using Hsp90 alpha/beta Antibody. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0) for 8 minutes. The tissues were blocked in QuickBlock for 20 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody at 1/100 dilution in 4℃ overnight. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunocytochemistry analysis of Hela cells labeling Hsp90 alpha/beta Antibody (HY-P80714) at 1/50 dilution. Cells were fixed in 4% paraformaldehyde for 15 minutes at room temperature, permeabilized with 0.1% Triton X-100 for 10 minutes at room temperature, then blocked with BSA for Immunol Staining for 10 min at room temperature. Cells were then incubated with Hsp90 alpha/beta Antibody (HY-P80714) at 1/50 dilution in BSA for Immunol Staining at 4 ℃ Overnight. AF488-conjugated AffiniPure Goat Anti-Rabbit IgG H&L（HY-P8002, Green) was used as the secondary antibody at 1/1,000 dilution. PBS instead of the primary antibody was used as the secondary antibody only control. The Nuclear counterstain was DAPI (Blue). -
Immunocytochemistry analysis of Hela cells labeling Hsp90 alpha/beta Antibody (HY-P80714) at 1/100 dilution. Cells were fixed in 4% paraformaldehyde for 15 minutes at room temperature, permeabilized with 0.1% Triton X-100 for 10 minutes at room temperature, then blocked with BSA for Immunol Staining for 10 min at room temperature. Cells were then incubated with Hsp90 alpha/beta Antibody (HY-P80714) at 1/100 dilution in BSA for Immunol Staining at 4 ℃ Overnight. AF488-conjugated AffiniPure Goat Anti-Rabbit IgG H&L（HY-P8002, Green) was used as the secondary antibody at 1/1,000 dilution. PBS instead of the primary antibody was used as the secondary antibody only control. The Nuclear counterstain was DAPI (Blue).
Background
-
Function
Hsp90 alpha/beta is a P07900: 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 that is linked to its ATPase activity which is essential for its chaperone 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. 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.
P08238: 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. 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.
[1][2][3][4][5][6][7][8][9][10]. -
Subcellular Localization
P07900: Nucleus; Cytoplasm; Melanosome; Cell membrane; Mitochondrion
P08238: Cytoplasm; Melanosome; Nucleus; Secreted; Cell membrane; Dynein axonemal particle; Cell surface -
Expression
Induction: P08238: By heat shock
-
Isoforms & Post-Translational Modification
P07900 has 2 isomers: P07900-1: 84660 Da (predicted); P07900-2: 98161 Da (predicted).
ISGylated;S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1;Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from the membrane and secretory pathways -
Subunit
P07900: Homodimer. Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1 (PubMed:15383005, PubMed:9195923). Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex (PubMed:29127155).
P08238: Monomer (PubMed:24880080). Homodimer (PubMed:18400751, PubMed:7588731). Forms a complex with CDK6 and CDC37 (PubMed:25486457, PubMed:9482106). -
Synonyms
HSP90AA1; HSP90A; HSPC1; HSPCA; Heat shock protein HSP 90-alpha; Heat shock 86 kDa; HSP 86; HSP86; Renal carcinoma antigen NY-REN-38; HSP90AB1; HSP90B; HSPC2; HSPCB; Heat shock protein HSP 90-beta; HSP 90; Heat shock 84 kDa; HSP 84; HSP84
-
Research Field
Signal Transduction
Documentation
References
[1]. Forsythe HL, et al. Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem. 2001 May 11;276(19):15571-4. [Content Brief]
[2]. Young JC, et al. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell. 2003 Jan 10;112(1):41-50. [Content Brief]
[3]. Yang J, et al. Molecular basis for TPR domain-mediated regulation of protein phosphatase 5. EMBO J. 2005 Jan 12;24(1):1-10. [Content Brief]
[4]. Martínez-Ruiz A, et al. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8525-30. [Content Brief]
[5]. Woodford MR, et al. The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding. Nat Commun. 2016 Jun 29;7:12037. [Content Brief]
[6]. Woodford MR, et al. Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients. EMBO J. 2017 Dec 15;36(24):3650-3665. [Content Brief]
[7]. Pearl LH, et al. Review: The HSP90 molecular chaperone-an enigmatic ATPase. Biopolymers. 2016 Aug;105(8):594-607. [Content Brief]
[8]. Verma S, et al. Hsp90: Friends, clients and natural foes. Biochimie. 2016 Aug;127:227-40. [Content Brief]
[9]. Chadli A, et al. GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway. Mol Cell Biol. 2006 Mar;26(5):1722-30. [Content Brief]
[10]. Retzlaff M, et al. Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep. 2009 Oct;10(10):1147-53. [Content Brief]
Powered by Bioz
