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  4. Recombinant Mouse Heat shock protein HSP 90-beta (Hsp90ab1)

Recombinant Mouse Heat shock protein HSP 90-beta (Hsp90ab1)

  • 货号：
    CSB-YP010808MO
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 货号：
    CSB-EP010808MO
  • 规格：
  • 来源：
    E.coli
  • 其他：
  • 货号：
    CSB-EP010808MO-B
  • 规格：
  • 来源：
    E.coli
  • 共轭：
    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：
  • 货号：
    CSB-BP010808MO
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 货号：
    CSB-MP010808MO
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
  • Uniprot No.：
  • 别名：
    Hsp90ab1; Hsp84; Hsp84-1; Hspcb; Heat shock protein HSP 90-beta; Heat shock 84 kDa; HSP 84; HSP84; Tumor-specific transplantation 84 kDa antigen; TSTA
  • 种属：
    Mus musculus (Mouse)
  • 蛋白长度：
    Full Length of Mature Protein
  • 表达区域：
    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 DKEDEEKPKI 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 DEDEVTAEEP SAAVPDEIPP LEGDEDASRM EEVD
  • 蛋白标签：
    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.
  • 产品提供形式：
    Lyophilized powder
    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.
  • 复溶：
    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.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    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.
  • 货期：
    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.
  • 注意事项：
    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.

产品评价

靶点详情

  • 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.
  • 基因功能参考文献：
    1. The results demonstrate that in renal cells, NHE1 is associated with several regulatory proteins including Hsp90, and that Hsp90 affects its function possibly through altered phosphorylation of the protein via the AKT kinase. PMID: 28483634
    2. Hsp90 is highly expressed on the cell surface of melanoma cells, and synthetic agents that target Hsp90 are promising cancer therapeutic drugs PMID: 27575453
    3. Data show that docetaxel, rapamycin and tanespimycin multi-drug loaded micelles targeted against HSP90 and the PI3K/AKT/mTOR pathway in prostate cancer. PMID: 28350865
    4. genes respond to HSP90 inhibition in a manner dependent on their genomic location with regard to strain-specific endogenous retroviruses-insertion sites. PMID: 28134929
    5. PABPN1 interacts with and is stabilized by heat shock protein 90. PMID: 26414348
    6. These findings demonstrate a critical role of Hsp90 in lipopolysaccharide (LPS) signaling, and a potential involvement of the heat shock response in LPS-induced preconditioning. PMID: 24646925
    7. Phosphoproteomics, protein expression inference and signaling pathway prediction analysis of P2RX7 signaling mediators pointed to HSPA2 and HSP90 proteins. PMID: 25700737
    8. Hsp90 inhibition plays a key role in preventing the recurrence of HCC, and the combination of ablation with targeted therapy holds great potential to improve prognosis and survival of HCC patients. PMID: 25403416
    9. These findings demonstrate CKII induces polymerization of soluble TDP-43 into filaments and Hsp90 promotes TDP-43 filament depolymerization. PMID: 24595055
    10. Reveal an opposite role of Hsp70 and Hsp90 in regulating TGF-beta signaling by implicating CHIP-mediated Smad3 ubiquitination and degradation. This study provides a new insight into understanding the regulation of the TGF-beta signaling by chaperones. PMID: 24613385
    11. A novel role for Hsp90 in controlling PPARgamma stability and cellular differentiation, is reported. PMID: 24096869
    12. inhibition exerts an anti-inflammatory effect in murine models of colitis PMID: 23321985
    13. Hsp90 activity is necessary to control the expression, activity or location of specific kinases and motor proteins during the axon specification and axon elongation processes. PMID: 24286867
    14. Alcohol-induced cilia stimulation occurs through the increased association of HSP90 with miR-122 target gene endothelial nitric oxide synthase (eNOS). PMID: 23078267
    15. Results suggest that heat shock protein 90 inhibitor radicicol inhibited 3T3-L1 preadipocyte differentiation through affecting the PDK1/Akt pathway. PMID: 23727383
    16. Perturbation of the HSP70-HSP90 heat-shock protein axis stimulates degradation of endothelial VEGFR2. PMID: 23139789
    17. Hsp90 expression is up-regulated in injured arteries and colocalizes with the apoptosis inhibitor, survivin, in vascular smooth muscle cell in vitro and in vivo. PMID: 22841823
    18. HSP90 is expressed in the vast majority of pancreatic endocrine tumors and inhibition of HSP90 results in a significant reduction of cell viability, cell cycle arrest, and increased apoptosis PMID: 22194440
    19. HSP90 may modulate myogenic differentiation and may be involved in cell survival. PMID: 21739150
    20. This study concluded that hsp90 plays a primary role in maturation of iNOS protein by interacting with the apoenzyme in cells and then driving heme insertion in an ATP-dependent manner. PMID: 21357526
    21. involved in translocation of a chaperoned antigen from endosome to proteasome for cross-presentation by dendritic cells PMID: 21421737
    22. The beneficial effects of HDAC6 targeting are also achieved by inhibition of the HDAC6-regulated protein heat shock protein 90. Inhibition of HSP90 enhances the suppressive functions of Foxp3+ Tregs. PMID: 21444725
    23. This results in the transcriptional repression of Hsp90beta, under GSH-deficient conditions which may play a role in arsenic-mediated pathogenesis. PMID: 18996350
    24. Heat shock protein 84 from C57BL/6 mice modulates higher cellular glucocorticoid-glucocorticoid receptor responsiveness. PMID: 20332616
    25. This study is the first report identifying four genetic variations of the murine hsp84 gene: 226A>C, 996G>C, 1483G>C, and 2000G>T. PMID: 19845467
    26. Data show that inhibition of Hsp90 engages a p53-dependent pathway to apoptosis. PMID: 19805107
    27. Hsp90 binding to Galpha12 helps target Galpha12 to lipid rafts PMID: 12117999
    28. peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein PMID: 12482853
    29. mineralocorticoid receptor and HSP84 mediate Src activation by aldosterone PMID: 15251441
    30. in the cytoplasm linker histones are bound to a complex containing NASP and HSP90 whose ATPase activity is stimulated by binding NASP PMID: 15533935
    31. The antiapoptotic activity of Bcl-2 was greatly affected by knocking-out specifically Hsp90beta using the RNA interference approach. PMID: 16166581
    32. Hsp90beta is distinct from Hsp90alpha in regulation of the cellular function of immune cells. PMID: 17475835
    33. A possible role of Hsp84 in mouse suprachiasmatic nucleus is association with circadian rhythms. PMID: 18480550
    34. 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
    35. analyzed meiotic maturation in wild-type oocytes treated with a specific inhibitor of Hsp90, 17-allylamino-17-demethoxy-geldanamycin, and observed similar defects PMID: 19158073
    36. Findings suggest that Hsp90 inhibitors might represent a novel means of promoting T cell tolerance. PMID: 19586661

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  • 亚细胞定位：
    Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane. Dynein axonemal particle.
  • 蛋白家族：
    Heat shock protein 90 family
  • 数据库链接：

    KEGG: mmu:15516

    STRING: 10090.ENSMUSP00000024739

    UniGene: Mm.2180