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  4. Recombinant Danio rerio Heat shock protein HSP 90-alpha 1 (hsp90a.1), partial

Recombinant Danio rerio Heat shock protein HSP 90-alpha 1 (hsp90a.1), partial

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  • 中文名称：
    斑马鱼hsp90a.1重组蛋白
  • 货号：
    CSB-BP838557DIL
  • 规格：
    ￥3168
  • 图片：
    • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • 其他：

产品详情

  • 纯度：
    Greater than 85% as determined by SDS-PAGE.
  • 基因名：
    hsp90a.1
  • Uniprot No.：
  • 别名：
    hsp90a.1; hsp90; hsp90a; hsp90aa1; zgc:86652Heat shock protein HSP 90-alpha 1
  • 种属：
    Danio rerio (Zebrafish) (Brachydanio rerio)
  • 蛋白长度：
    Partial
  • 来源：
    Baculovirus
  • 分子量：
    27.9 kDa
  • 表达区域：
    151-355aa
  • 氨基酸序列
    HNDDEQYIWESAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEVAAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIK
    Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
  • 蛋白标签：
    N-terminal 10xHis-tagged and C-terminal Myc-tagged
  • 产品提供形式：
    Liquid or 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.
  • 缓冲液：
    Tris-based buffer，50% glycerol
  • 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：
    3-7 business days
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet & COA：
    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 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 key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.
  • 基因功能参考文献：
    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. The transcriptional up-regulation of unc45b, hsp90aa1.1 and smyd1b is specific to zebrafish mutants with myosin folding defects, and is not triggered in other zebrafish myopathy models PMID: 26631063
    3. Data indicate that heat shock protein 90alpha (Hsp90alpha1) function in myosin thick filament organization is potentially regulated by post-translational modification (PTM) involving phosphorylation and acetylation. PMID: 26562659
    4. The chaperone proteins Ahsa1 and Hsp90 promote severe craniofacial phenotypes in zebrafish model of HDR syndrome. PMID: 23720234
    5. Perturbation of the HSP70-HSP90 heat-shock protein axis stimulates degradation of endothelial VEGFR2. PMID: 23139789
    6. studies indicate that the hsp90alpha1 mutant phenotype is not simply due to disruption of myosin folding and assembly, suggesting that Hsp90alpha1 may play a role in the assembly and organization of other sarcomeric structures PMID: 20049323
    7. Mild perturbation of Hsp90 function at critical developmental stages may underpin the variable penetrance and expressivity of many developmental anomalies where the interaction between genotype and environment plays a major role. PMID: 17397257
    8. Steif/Unc-45b interacts with the chaperone Hsp90a in vitro. The two genes are co-expressed in the skeletal musculature. PMID: 17586488
    9. Embryonic heat shock reveals latent hsp90 translation in zebrafish. PMID: 18033674
    10. Loss of Hsp90a function leads to the downregulation of genes encoding sarcomeric proteins and upregulation of hsp90a and several other genes encoding proteins that may act with Hsp90a during sarcomere assembly. PMID: 18256191
    11. In response to stress or damage to the myofiber, Unc45b and Hsp90a dissociate from the Z line and transiently associate with myosin. PMID: 18347070

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  • 亚细胞定位：
    Melanosome. Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, sarcomere, A band. Cytoplasm, perinuclear region. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Shuttles between the Z line and A band in response to stress conditions and fibril damage.
  • 蛋白家族：
    Heat shock protein 90 family
  • 组织特异性：
    Strongly expressed in the early embryos within the somitic slow muscle progenitors, the adaxial cells that lie on either side of the notochord but not the notochord. Also expressed during the early differentiation of fast fibers. Detected in developing ca
  • 数据库链接：

    KEGG: dre:30591

    STRING: 7955.ENSDARP00000022302

    UniGene: Dr.75834