Recombinant Human Heat shock protein HSP 90-beta (HSP90AB1)

中文名稱：

人HSP90AB1重組蛋白
貨號：

CSB-YP010808HU
說明書：

MSDS Datasheet
規格：
來源：

Yeast
其他：

中文名稱：

人HSP90AB1重組蛋白
貨號：

CSB-EP010808HU-B
說明書：

MSDS Datasheet
規格：
來源：

E.coli
共軛：

Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
其他：

中文名稱：

人HSP90AB1重組蛋白
貨號：

CSB-MP010808HU
說明書：

MSDS Datasheet
規格：
來源：

Mammalian cell
其他：

產品詳情
產品評價
相關產品
靶點詳情

產品詳情

純度：

>85% (SDS-PAGE)
基因名：

HSP90AB1
Uniprot No.：

P08238
別名：

90 kda heat shock protein beta HSP90 beta; D6S182; FLJ26984; Heat shock 84 kDa; Heat shock 90kD protein 1; beta ; Heat shock 90kDa protein 1 beta; Heat shock protein 90 alpha family class B member 1; Heat shock protein 90 kDa; Heat shock protein 90kDa alpha (cytosolic) class B member 1; Heat shock protein 90kDa alpha family class B member 1; Heat shock protein beta ; Heat shock protein HSP 90 beta ; Heat shock protein HSP 90-beta; HS90B_HUMAN; HSP 84; HSP 90; HSP 90 b; HSP 90b; HSP84; HSP90 BETA ; hsp90ab1; HSP90B; HSPC2; HSPCB
種屬：

Homo sapiens (Human)
蛋白長度：

Full Length of Mature Protein
表達區域：

2-724
氨基酸序列

PEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE DKDDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVAAEEP NAAVPDEIPP LEGDEDASRM EEVD
蛋白標簽：

Tag?type?will?be?determined?during?the?manufacturing?process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
產品提供形式：

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Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
復溶：

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
儲存條件：

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
保質期：

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
貨期：

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
注意事項：

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet ：

Please contact us to get it.

產品評價

靶點詳情

功能：

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. 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. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. 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. 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.
基因功能參考文獻：
1. The production of IFN-gamma by T cells stimulated with citrullinated HSP90beta demonstrates a bias toward TH1 immune responses that are likely involved in the pathogenesis of rheumatoid arthritis-interstitial lung disease. PMID: 29968330
2. the expressions of HSP90AB1 can predict prognosis in astrocytic tumors PMID: 27258564
3. We found that the nutrient value of the culturing medium and the length of induction had significant effect on Hsp90 production in Escherichia coli. Our fast, single-day purification protocol resulted in a stable, well-folded and pure sample that was resistant to degradation in a reproducible manner. PMID: 28651008
4. Data show that C allele of rs2282151 was associated with increased expression level of heat shock protein 90 alpha family class B member 1 (HSP90AB1). PMID: 27756247
5. Hsp90beta induced endothelial cell-dependent tumor angiogenesis by activating VEGFRs transcription. PMID: 28359326
6. The authors find that the interaction between sB-Raf and the Hsp90 chaperone system is based on contacts with the M domain of Hsp90, which contributes in forming the ternary complex with Cdc37 as long as the kinase is not stabilized by nucleotide. PMID: 27620500
7. High HSP90B expression is associated with laryngeal carcinoma. PMID: 27959448
8. The expression level of Hsp90AB1 in lung cancer tissues was significantly higher than that in normal lung tissue and was associated with lung cancer pathological type and overall survival in lung adenocarcinoma patients. PMID: 26903158
9. Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes. PMID: 26511315
10. HSP90AB1: Helping the good and the bad PMID: 26358502
11. These results suggest a means by which the hsp90beta interaction could prevent apo-sGCbeta1 from associating with its partner sGCalpha1 subunit while enabling structural changes to assist heme insertion into the H-NOX domain. PMID: 26134567
12. Casein kinase 2-mediated phosphorylation of Hsp90beta and stabilization of PXR is a key mechanism in the regulation of MDR1 expression. PMID: 25995454
13. This study identifies overexpression of HSP90 (especially isoform HSP90AB1) and its clients ATR, ATM, and NBS1 as promising markers for radioresistant, aggressive soft tissue sarcomas with particularly poor prognosis. PMID: 26044951
14. The proteins (HSP90b, TMS1 and L-plastin) in the current study may hold potential in differentiating between melanoma and benign nevi in diagnostically challenging cases. PMID: 25191796
15. The expression levels of Hsp90-beta and annexin A1 positively correlated and such co-overexpression of Hsp90-beta and annexin A1 contributed to lung cancer diagnosis. PMID: 25300907
16. Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells. PMID: 24466266
17. A novel mechanism for human carcinogenesis via methylation of HSP90AB1 by SMYD2. PMID: 24880080
18. Hsp90 is upregulated in systemic sclerosis (SSc) and is critical for TGF-beta signalling. PMID: 23661493
19. HSP70 was massively up-regulated in all mast cells three months after irradiation whereas HSP90AB1 was up-regulated only in a portion of mast cells PMID: 24670792
20. Study obtained a structural model of Hsp90 in complex with its natural disease-associated substrate, the intrinsically disordered Tau protein. Hsp90 binds to a broad region in Tau that includes the aggregation-prone repeats. PMID: 24581495
21. HSP90beta may positively regulate angiogenesis, not only as a protein chaperone, but also as an mRNA stabilizer for pro-angiogenic genes, such as BAZF, in a PRKD2 activity-dependent manner. PMID: 23515950
22. Here we describe the specific association of heat shock protein-90-beta (Hsp90beta) with EV71 viral particles by the co-purification with virions using sucrose density gradient ultracentrifugation and colocalization as shown by immunogold EM. PMID: 23711381
23. differences in expression caused by the -144 polymorphism in the HSP90beta promoter are associated with cellular inflammatory responses and the severity of organ injury PMID: 23516526
24. the transdominant effect of HSP90AB1 on capsid-spacer protein 1-mutant HIV infectivity suggests a potential role for this class of cellular chaperones in HIV core stability and uncoating. PMID: 23200770
25. The upregulation of Hsp90-beta was associated with poor post-surgical survival time and lymphatic metastasis of lung cancer patients PMID: 22929401
26. DNA sequencing of 101 human samples detects eight and seven unique single nucleotide polymorphisms (SNPs) at the HSP90AA1 and HSP90AB1 loci, respectively. PMID: 22185817
27. a possible role for HSP90AB1 in postentry HIV replication and may provide an attractive target for therapeutic intervention. PMID: 21602280
28. TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. PMID: 21689689
29. cyclophilin A and Hsp90 facilitate translocation of lethal factor(N) diphtheria toxin, but not of lethal factor, across endosomal membranes, and thus they function selectively in promoting translocation of certain proteins, but not of others PMID: 20946244
30. Results show that RPL4, RPLP0, and HSPCB were the most stable reference genes in ovarian tissues. PMID: 20705598
31. H. pylori induces the translocation of HSP90beta from the cytosol to the membrane and interaction of HSP90beta and Rac1, which leads to the activation of NADPH oxidase and production of ROS in gastric epithelial cells. PMID: 20451655
32. findings present novel Hsp90 mutants that render cells resistant to Hsp90 inhibitors; show that the resistance depends on the increased ATPase turnover due to enhanced interaction with Aha1 PMID: 20226818
33. Data show that the small molecule celastrol inhibits the Hsp90 chaperoning machinery by inactivating the co-chaperone p23, resulting in a more selective destabilization of steroid receptors. PMID: 19996313
34. Study points to a potential role for Hsp90beta in MSC biology. PMID: 19327008
35. PKC-epsilon is specifically required in the signaling pathway leading to the induction of hsp90 beta gene in response to heat shock. PMID: 14532285
36. hsp90beta is repressed by p53 in UV irradiation-induced apoptosis PMID: 15284248
37. Mutations at the phosphorylation sites of HSP90-beta modulate the interaction with arylhydrocarbon receptor (AhR) and may negatively regulate formation of the functional AhR complex in the steady-state cytosol. PMID: 15581363
38. Hydrogen-exchange mass spectrometry was used to study structural & conformational changes undergone by full-length Hsp90beta in solution upon binding of the co-chaperone Cdc37 & 2 Hsp90 ATPase inhibitors: Radicicol & the anticancer drug DMAG PMID: 17764690
39. Results suggest that HSP90 beta prevents auto-ubiquitination and degradation of its client protein c-IAP1, whose depletion would be sufficient to inhibit cell differentiation. PMID: 18239673
40. These data provide an explanation for apoptosome inhibition by activated leukemogenic tyrosine kinases and suggest that alterations in Hsp90beta-apoptosome interactions may contribute to chemoresistance in leukemias. PMID: 18591256
41. Presence of ovarian autoantibodies to human HSP90 in sera of women with infertility could be involved in human ovarian autoimmunity and thereby be a causative factor in early ovarian failure. PMID: 19022436
42. Results show that heat shock protein 90 beta is cleaved by activated caspase-10 under UVB irradiation. PMID: 19380486
43. celastrol may represent a new class of Hsp90 inhibitor by modifying Hsp90 C terminus to allosterically regulate its chaperone activity and disrupt Hsp90-Cdc37 complex. PMID: 19858214
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亞細胞定位：

Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane. Dynein axonemal particle.
蛋白家族：

Heat shock protein 90 family
數據庫鏈接：

HGNC: 5258

OMIM: 140572

KEGG: hsa:3326

STRING: 9606.ENSP00000325875

UniGene: Hs.509736