Recombinant Mouse Heat shock protein HSP 90-alpha(Hsp90aa1)

Code CSB-YP010802MO
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Source Yeast
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Code CSB-EP010802MO
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Source E.coli
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Code CSB-EP010802MO-B
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Source E.coli
Conjugate 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.
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Code CSB-BP010802MO
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Source Baculovirus
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Code CSB-MP010802MO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Hsp90aa1
Uniprot No. P07901
Alternative Names Hsp90aa1; Hsp86; Hsp86-1; HspcaHeat shock protein HSP 90-alpha; Heat shock 86 kDa; HSP 86; HSP86; Tumor-specific transplantation 86 kDa antigen; TSTA
Species Mus musculus (Mouse)
Expression Region 2-733
Target Protein Sequence PEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR YESLTDPSKL DSGKELHINL IPSKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE KEEEKEKEEK ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF DLFENRKKKN NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK CLELFTELAE DKENYKKFYE QFSKNIKLGI HEDSQNRKKL SELLRYYTSA SGDEMVSLKD YCTRMKENQK HIYFITGETK DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK TLVSVTKEGL ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK AEADKNDKSV KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID EDDPTVDDTS AAVTEEMPPL EGDDDTSRME EVD
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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.
Form 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.
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution 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.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life 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.
Lead Time 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.
Notes 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.

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Target Background

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 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. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. 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. In the first place, they 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. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Mediates the association of TOMM70 with IRF3 or TBK1 in mitochodria outer membrane which promotes host antiviral response.
Gene References into Functions
  1. 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
  2. Fusion of human SGT1 (hSGT1) to NOD1 LRR significantly enhanced the solubility, and the fusion protein was stabilized by coexpression of mouse Hsp90alpha. PMID: 27591899
  3. The major capsid protein of the mouse polyomavirus VP1 binds microtubules, HSP90, promotes their acetylation and blocks the host cell cycle. PMID: 27885808
  4. Artificially maintaining Hsp90alpha or knocking down Aarsd1L expression interferes with the differentiation of C2C12 myotubes. PMID: 26884463
  5. Immune-mediated destruction of ovarian follicles associated with the presence of HSP90 antibodies. PMID: 25653208
  6. identify that Hsp90alpha at the transition neck region represents a signalling platform on which IRS-1 interacts with intracellular downstream signalling molecules involved in IGF-1 receptor signalling. PMID: 25359884
  7. The study demonstrated that HSP90alpha plays an important role in the biogenesis of fetal PIWI-interacting RNAs (piRNA), which act against the transposon activities, in mouse male germ cells. PMID: 25262350
  8. deficiency does not affect immunoglobulin gene hypermutation and class switch but causes enhanced MHC class II antigen presentation PMID: 22855849
  9. study identified the essential role of Hsp90 in iNOS gene transactivation PMID: 21430289
  10. Hsp90alpha may be required to maintain and to activate these regulators and/or to disassemble the synaptonemal complex that holds homologous chromosomes together PMID: 21209834
  11. extracellular Hsp90alpha promotes angiogenesis in an MMP-2-dependent manner. PMID: 20937816
  12. Hsp90-ovalbumin peptide complexes bind to scavenger receptor expressed by endothelial cells (SREC-I) on the surface of antigen presenting cells. PMID: 20686127
  13. Endogenous HSP90 is essential for cross-presentation of both soluble and cell-associated antigens in dendritic cells. PMID: 20668218
  14. KLF4 inhibition by antisense oligonucleotides markedly decreased the constitutive expression of HSP90 (HSP84 and HSP86). PMID: 19669938
  15. Following exposure to elevated temperatures, higher amounts of Hsp90alpha are inside the nucleus, but not within the nucleoli. PMID: 12713799
  16. Heat shock protein 90 is an endogenous protein enhancer of inducible nitric-oxide synthase PMID: 12855682
  17. by induction of HSP90A c-Myc may control the activity of multiple signal pathways involved in cellular transformation PMID: 14724288
  18. HSPB1 pathway is important during trophoblast stem cell differentiation PMID: 17267699
  19. Hsp90 promotes activation of the Fanconi anemia pathway through regulation of intracellular turnover and trafficking of FANCA PMID: 17327415
  20. Unlike Hsp90beta, Hsp90alpha is not associated with regulation of the antiapoptotic response of immune cells. PMID: 17475835
  21. Blocking Hsp90 disrupts IGF-I and IL-6-induced proangiogenic signaling cascades by targeting IGF-IR and STAT3 in pancreatic cancer PMID: 17975158
  22. These results demonstrate a substantial role for hsp90 in chaperoning of antigenic peptides in direct and indirect presentation. PMID: 18216248
  23. Melusin directly binds to Hsp90, a ubiquitous chaperone involved in regulating several signaling pathways. PMID: 18474241
  24. mammalian Unc45b is a cytosolic protein that forms a stable complex with Hsp90, selectively binds the unfolded conformation of the myosin motor domain, and promotes motor domain folding PMID: 18478096
  25. A possible role of Hsp86 in mouse suprachiasmatic nucleus is association with circadian rhythms. PMID: 18480550
  26. Hsp90 regulates cPLA(2)alpha-mediated arachidonic acid release that involves association of a p54 kinase with cPLA(2)alpha upon okadaic acid stimulation PMID: 18550790
  27. hsp90 facilitates MHC class I antigen processing through epitope production in a complex of the 26 S proteasome PMID: 18703510
  28. the complex role played by Hsp90 in regulating signal transduction pathways in normal tissues as well as in cancer cells. PMID: 18840695

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Subcellular Location Nucleus. Cytoplasm. Melanosome. Cell membrane. Mitochondrion.
Protein Families Heat shock protein 90 family
Database Links

KEGG: mmu:15519

STRING: 10090.ENSMUSP00000021698

UniGene: Mm.1843

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