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HSPE1 Antibody

  • 货号:
    CSB-PA977270
  • 规格:
    ¥2024
  • 图片:
    • Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using HSP10 antibody.
    • Immunofluorescence analysis of NIH/3T3 cells, using HSP10 antibody.
    • Western blot analysis of extracts from NIH/3T3 cells, using HSP10 antibody.
    • Western blot analysis of extracts from COS7 cells (Lane 2), using HSP10 antiobdy. The lane on the left is treated with systhesized peptide.
  • 其他:

产品详情

  • 产品名称:
    Rabbit anti-Homo sapiens (Human) HSPE1 Polyclonal antibody
  • Uniprot No.:
    P61604
  • 基因名:
    HSPE1
  • 宿主:
    Rabbit
  • 反应种属:
    Human,Mouse,Rat
  • 免疫原:
    Synthesized peptide derived from Human HSP10.
  • 免疫原种属:
    Homo sapiens (Human)
  • 克隆类型:
    Polyclonal
  • 纯化方式:
    The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
  • 浓度:
    It differs from different batches. Please contact us to confirm it.
  • 产品提供形式:
    Liquid
  • 应用范围:
    ELISA,WB,IHC,IF
  • 推荐稀释比:
    Application Recommended Dilution
    WB 1:500-1:3000
    IHC 1:50-1:100
    IF 1:100-1:500
  • Protocols:
  • 储存条件:
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 货期:
    Basically, 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.

产品评价

靶点详情

  • 功能:
    Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.
  • 基因功能参考文献:
    1. elevated expression of HSP10 protein inhibits apoptosis and associates with poor prognosis of astrocytoma PMID: 29028811
    2. miR-146a, miR-146b, and miR-155 are exerting anti-inflammatory properties by down-regulating IL-6 and IL-8, and influencing the expression of HSP10 in the activated endothelium PMID: 28662100
    3. High expression of HSP10 is negatively associated with estrogen receptor/progesterone receptor status and might be a novel independent biomarker for poor prognosis in invasive ductal breast carcinoma. PMID: 27993580
    4. EPF induces the differentiation of regulatory T cells and increases their immunosuppressive activities. PMID: 27840373
    5. Cpn10 has a role in the spatial regulation of NPAT signaling PMID: 26429916
    6. Hsp10 has a role in nuclear localization and lung cells response to cigarette smoke PMID: 25355063
    7. Data show that that in presence of 300 mg/mL Ficoll the thermodynamic stability of each cpn10 monomer increases by over 30%, whereas the interfaces are stabilized by less than 10%. PMID: 21375247
    8. HSP10 protein was detected only in oocytes from human preantral follicles, whereas in antral follicles, it was localised in oocytes, granulosa cells, theca cells and stroma cells. PMID: 19903031
    9. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. PMID: 11898127
    10. The low stability of the monomeric unit suggests that folding and assembly reactions for cpn10 are coupled. PMID: 12220543
    11. Cpn10 and placental lactogen are capable of stimulating the synthesis of type I collagen by human osteoblasts in culture PMID: 12703979
    12. Identification of amino acids important for the assembly of the cpn10 heptamer. PMID: 14525625
    13. complex mechanisms are involved in the protection by hsp10 against simulated ischemia and reoxygenation-induced myocyte death PMID: 15059967
    14. The HSP10 plays a role in bone marrow cell differentiation other than being a mitochondrial co-chaperonin. PMID: 15590416
    15. Chaperonin 10 and calgranulin A are identified as markers for diagnosis and screening of endometrial carcinoma. PMID: 15816004
    16. the cpn10 interfaces can adapt to structural alterations without loss of either subunit-subunit affinity or heptamer specificity PMID: 15978542
    17. biophysical analysis of dissociation equilibrium for the heptameric co-chaperonin proteins 10 from Aquifex aeolicus and human mitochondria PMID: 16100270
    18. proteomic analysis of possible role of heat shock protein 10 in colorectal cancer PMID: 16502466
    19. Results describe the time-resolved folding and assembly mechanism of the heptameric co-chaperonin protein 10 (cpn10) in vitro. PMID: 16979655
    20. Investigation of single-nucleotide variations in the Hsp10 gene and their disease-causing potential. PMID: 17072495
    21. In this review, we revise the involvement of Hsp10 in signal transduction pathways and its possible role in cancer etiology. PMID: 17278877
    22. Data show that Hhsp10 formed fibrils from only the acidic unfolded state and Core peptide regions of these protein fibrils were determined by proteolysis followed by a combination of Edman degradation and mass spectroscopy analyses. PMID: 18329043
    23. The effects of cpn 10 on cells of the oligodendrocyte lineage, were assessed. PMID: 18465204
    24. In patients with serous ovarian carcinomas, gene expression analysis coupled with immunohistochemistry allowed the identification of HSP10 as an independent factor of progression-free survival. PMID: 18500265
    25. Results describe a novel function of chaperonin 10 as a general differentiation factor, not limited to erythroid cells, and show how this biological effect is mediated by GSK-3alpha/beta. PMID: 19142874
    26. HSP10 was identified as a new autoantigen in both autoimmune pancreatitis and fulminant type 1 diabetes. PMID: 19520060

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  • 亚细胞定位:
    Mitochondrion matrix.
  • 蛋白家族:
    GroES chaperonin family
  • 数据库链接:

    HGNC: 5269

    OMIM: 600141

    KEGG: hsa:3336

    STRING: 9606.ENSP00000233893

    UniGene: Hs.1197