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当前位置: 首页 > 产品中心 > Flow_cytometry > Cusabio/HSP90AA1 Antibody/100μl/CSB-RA011087A2HU
商品详细Cusabio/HSP90AA1 Antibody/100μl/CSB-RA011087A2HU
Cusabio/HSP90AA1 Antibody/100μl/CSB-RA011087A2HU
Cusabio/HSP90AA1 Antibody/100μl/CSB-RA011087A2HU
商品编号: CSB-RA011087A2HU
品牌: Cusabio
市场价: ¥7000.00
美元价: 3500.00
产地: 美国(厂家直采)
公司:
产品分类: 流式抗体
公司分类: Flow_cytometry
联系Q Q: 3392242852
电话号码: 4000-520-616
电子邮箱: info@ebiomall.com
商品介绍

HSP90AA1 Antibody

Datasheet
CodeCSB-RA011087A2HU
SizeUS$350
Image
  • Western BlotPositive WB detected in: Jurkat whole cell lysateAll lanes: Hsp90 alpha antibody at 1.9μg/mlSecondaryGoat polyclonal to rabbit IgG at 1/50000 dilutionPredicted band size: 85, 99 KDaObserved band size: 90 KDa

  • IHC image of CSB-RA011087A2HU diluted at 1:190 and staining in paraffin-embedded human testis tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • Immunofluorescence staining of NIH/3T3 cells with CSB-RA011087A2HU at 1:63, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG (H+L).

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Product Details

Uniprot No. P07900
Target NamesHSP90AA1
Alternative NamesHeat shock 86 kDa antibody; Heat shock protein 90kDa alpha cytosolic class A member 1 antibody; Heat shock protein 90kDa alpha cytosolic class B member 1 antibody; Heat shock protein HSP 90 alpha antibody; Heat shock protein HSP 90 beta antibody; Heat shock protein HSP 90-alpha antibody; HS90A_HUMAN antibody; HSP 84 antibody; HSP 86 antibody; Hsp 90 antibody; HSP86 antibody; HSP90A antibody; HSP90AA1 antibody; HSP90AB1 antibody; HSP90B antibody; HSPC1 antibody; HSPC2 antibody; HSPCAL1 antibody; HSPCAL4 antibody; Renal carcinoma antigen NY-REN-38 antibody
Species ReactivityHuman
ImmunogenA synthesized peptide derived from human HSP90AA1
Immunogen SpeciesHomo sapiens (Human)
ConjugateNon-conjugated
ClonalityMonoclonal
IsotypeRabbit IgG
Clone No.4D1
Purification MethodAffinity-chromatography
ConcentrationIt differs from different batches. Please contact us to confirm it.
BufferRabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
FormLiquid
Tested ApplicationsELISA, WB, IHC, IF
Recommended Dilution
ApplicationRecommended Dilution
WB1:500-1:5000
IHC1:50-1:200
IF1:20-1:200
ProtocolsELISA ProtocolWestern Blotting(WB) ProtocolImmunohistochemistry (IHC) ProtocolImmunofluorescence (IF) Protocol
Troubleshooting and FAQsAntibody FAQs
StorageUpon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead TimeBasically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Data

FunctionMolecular 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
Gene References into Functions
  1. RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. PMID: 29662061
  2. The study shows that a conserved tryptophan in the middle domain senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation-pi interaction with a neighboring lysine. PMID: 29662162
  3. While activation in c-Src is strictly controlled by ATP-binding and phosphorylation, the authors find that activating conformational transitions are spontaneously sampled in Hsp90-dependent Src mutants. PMID: 28290541
  4. chemotherapy agents can induce HSP90AA1 expression in osteosarcoma cells. And HSP90AA1, acting as an important regulator of autophagy, is a critical factor in the development of osteosarcoma chemoresistance both in vitro and in vivo. HSP90AA1 provides a novel therapeutic target for improving osteosarcoma treatment. PMID: 30153855
  5. We confirm that miR-628-3p promotes apoptosis and inhibits migration in A549 cells by negatively regulating HSP90. Our results may reveal a novel strategy for lung cancer treatment PMID: 29888262
  6. Data recognize HSP90 as a novel binding partner of PKM2 in hepatocellular carcinoma (HCC) cells. HSP90 potentiates the glycolysis and proliferation, reduces the apoptosis and thus enhances the growth of HCC cells through PKM2 Thr-328 phosphorylation maintaining its stability. PMID: 29262861
  7. EGFR expression stratified most pronounced among HSP90low tumours, where the EGFRhigh phenotype was associated with longer survival PMID: 28765916
  8. the SGT1-HSP90 complex contributes to the E3 ligase activity of the CUL4A complex that is necessary for CENP-A ubiquitylation and CENP-A deposition at the centromere. PMID: 28816574
  9. our data suggested that Hsp90alpha could positively regulate the self-renewal of BCSCs by facilitating the nuclear translocation of c-Myc and EZH2 to maintain BMI1 expression. PMID: 28914785
  10. HSP90 contributes to cutaneous vasodilation via NOS-dependent mechanisms in young habitually active men during exercise in the heat. PMID: 28751373
  11. The association between the MEEVD C-terminal peptide from the heat shock protein 90 (Hsp90) and tetratricopeptide repeat A (TPR2A) domain of the heat shock organizing protein (Hop) is a useful prototype to study the fundamental molecular details about the Hop-Hsp90 interaction.Observed are conformational changes of the peptide and the protein receptor induced by binding. The binding free energy is 8.4 kcal/mol. PMID: 28723223
  12. Our findings demonstrate Hsp90 blockade leads to ICN1 destabilization, providing an alternative strategy to antagonize oncogenic Notch1 signaling with Hsp90-selective inhibitors PMID: 28143869
  13. Generated multiple mutant KRAS-driven cancer cell lines with acquired resistance to the purine-scaffold HSP90 inhibitor PU-H71. Report a Y142N missense mutation in the ATP-binding domain of HSP90alpha that co-occurred with amplification of the HSP90AA1 locus in resistant cells. PMID: 28032595
  14. ATM is the primary kinase responsible for phosphorylation of Hsp90alpha after exposure ionizing radiation. PMID: 27738310
  15. molecular modeling was employed to incorporate experimental data using partial constructs of the Hsp90 C-terminal domain. PMID: 27771574
  16. findings suggested that this mechanism may be exploited by the Hsp90-Cdc37 chaperone to recruit and protect intrinsically dynamic kinase clients from degradation PMID: 29267381
  17. The findings establish an active role for Tsc1 as a facilitator of Hsp90-mediated folding of kinase and non-kinase clients-including Tsc2-thereby preventing their ubiquitination and proteasomal degradation. PMID: 29127155
  18. Data indicate HSP90 inhibitors as a class of preferred drugs for treatment combination with immunotherapy. PMID: 28878208
  19. Data suggest that SOCS3 is an important signaling protein in CLL, and Hsp90 inhibitors represent an approach to target transcriptional repression in B cell lymphoproliferative disorders. PMID: 27107422
  20. FKBP51 is primarily localized in mitochondria and hTERT is totally nuclear, upon the onset of oxidative stress, FKBP51 (but not FKBP52) becomes mostly nuclear colocalizing with hTERT, and longer exposure times to peroxide favors hTERT export to mitochondria. PMID: 27233944
  21. High HSP90 expression is associated with Colorectal Cancers. PMID: 28870917
  22. High HSP90 expression is associated with prostate cancer. PMID: 28038472
  23. Data suggest HSP90AA1-dependent regulation of ATM-NBN-CHK2 and ATR-CHK1 axes influences cells capability to repair double-stranded DNA damage; mechanisms include phosphorylation, polyubiquitination, and proteasomal degradation/proteolysis. (HSP90AA1 = heat shock protein 90kDa alpha; ATM = ataxia telangiectasia mutated protein; NBN = nibrin; CHK = checkpoint kinase; ATR = ataxia telangiectasia and Rad3 related kinase) PMID: 28631426
  24. Data show that pyruvate kinase M2 (PKM2) directly interacted with mutant growth factor receptor (EGFR) and heat-shock protein 90 (HSP90), and thus stabilized EGFR by maintaining its binding with HSP90 and co-chaperones. PMID: 26500058
  25. Binding of FM807 to the N-terminus of Hsp90 disrupted Hsp90/client complexes, resulting in degradation of the Hsp90 client protein EGFR and inhibition of the downstream pathway. PMID: 28157708
  26. Conventional as well as scaled molecular dynamics simulations further demonstrate that citrullination of selected Arg residues leads to progressive disruption of HSP90 tertiary structure, promoting exposure of R502/R510 to PAD modification and subsequent autoantibody binding. PMID: 27448590
  27. SYK is an HSP90 client protein, and B-cell receptor signaling-dependent phosphorylation of HSP90 on Y197 is required for this interaction. HSP90 promotes Burkitt lymphoma cell survival by maintaining tonic B-cell receptor signaling. PMID: 28064214
  28. Data indicate a chaperone function of nicotinamide mononucleotide adenylyl transferase 2 (NMNAT2), independent from its enzymatic activity, and NMNAT2 complexes with heat shock protein 90 (HSP90) to refold aggregated protein substrates. PMID: 27254664
  29. In the bound state, the Hsp90 dimer predominantly populates an open conformation, and transthyretin retains its globular structure. PMID: 28218749
  30. CD30 facilitates phosphorylation of heat shock factor 1, activates heat shock promoter element, and induces heat shock protein (HSP) 90. PMID: 27870927
  31. However, once the mumps virus L protein formed a mature polymerase complex with the P protein, Hsp90 activity was no longer required for the stability and activity of the L protein. PMID: 28053100
  32. HSP90 may be essential for stabilization and function of P2X7Rs through an action on the cysteine-rich domain of the cytoplasmic the C-terminus. PMID: 27301716
  33. HSP90AA1 and AB1 genes exhibit low expression in breast cancers highly sensitive to chemotherapy and may indicate the patients with higher probability of pathological complete response. PMID: 28051275
  34. the effect of HSP90 inhibition on IL-17-mediated cytokine and antimicrobial peptide expression in keratinocytes following heat treatment, was examined. PMID: 27279135
  35. epididymis secretory protein 4 had better specificity than CA125 in discriminating ovarian cancer, and endometrial cancer from benign gynecological diseases in southern China population PMID: 27302312
  36. Hsp90 has roles in the regulation of autophagy, such as toll-like receptor (TLR)-mediated autophagy, Ulk1-mediated mitophagy, and chaperone-mediated autophagy (CMA) [review] PMID: 26432328
  37. this study identified HSP90AA1 as a new potential biomarker for Behcet"s disease by comparing highly ranked genes from all the built network-derived gene lists, which was confirmed the with real-world clinical samples PMID: 27226232
  38. Data show that heat shock protein 90 (HSP90) inhibitor 17-DMAG caused loss of ret proto-oncogene protein (RET) and proto-oncogene protein erbB-3 (ERBB3) phosphorylation and lead to rapid cell death. PMID: 26595521
  39. Hsp103 associates with cochaperone proteins, such as Hop, Cdc37 and Aha1, similar to Hsp90. The extra domain reduces the ATP hydrolysis when compared to Hsp90 thereby acting as a negative regulator of the chaperones intrinsic ATPase activity. PMID: 23951259
  40. Data suggest that synergistic mechanism between heat shock protein 90 (Hsp90) inhibitor SNX-7081 and fludarabine nucleoside (2-FaraA) may provide an alternative treatment for chronic lymphocytic leukemia (CLL) patients with p53 protein mutations. PMID: 26556860
  41. The expression of HSP90A was increased in the HCC cells, serum, and tissues. Immunohistochemistry analysis on 76 clinical tissue samples also suggested the relevance between HSP90A expression and HCC metastatic behavior. PMID: 26704341
  42. Aarsd1 inhibits the activity of a paradigmatic Hsp90 client protein. PMID: 26884463
  43. study confirmed Hsp90 as an influenza virus A PB2 polymerase interacting protein, and established that Hsp90 interacts with both the E627 and 627K variants, but has established this interaction is species independent, and both mammalian and avian Hsp90 can bind to the PB2 protein PMID: 26616658
  44. Data show that high-affinity heat shock protein 90 (HSP90) binding conferred by the inhibitor backbone could be exploited for conjugate accumulation within tumor cells. PMID: 26271675
  45. In conjunction with HSP90, the cytoplasmic USP19 may play a key role in triage decision for the disease-related polyQ-expanded substrates, suggesting a function of USP19 in quality control of misfolded proteins by regulating their protein levels PMID: 26808260
  46. The region of aa 250-295 of BGLF4 is essential for the BGLF4/Hsp90 interaction. PMID: 26982469
  47. The thermodynamics of binding of Cyp-40 to Hsp90 shows remarkable temperature sensitivity in the physiological temperature range. PMID: 26330616
  48. HSP90 overexpression is a prognostic marker for cholangiocarcinoma. HSP90-targeted therapy may be an option for a subset of cholangiocarcinoma. PMID: 26141945
  49. From our screening methodology, we identified HCAb2 as a breast tumor specific heavy chain antibody targeting cell surface heat shock protein 90. PMID: 26334999
  50. Heat shock protein 90 is required for ex vivo neutrophil-driven autoantibody-induced tissue damage in experimental epidermolysis bullosa acquisita. PMID: 25739426

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Subcellular LocationNucleus, Cytoplasm, Melanosome, Cell membrane
Protein FamiliesHeat shock protein 90 family
Database Links

HGNC: 5253

OMIM: 140571

KEGG: hsa:3320

STRING: 9606.ENSP00000335153

UniGene: Hs.525600

品牌介绍
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