HSPE1 Antibody

Code CSB-PA10857A0Rb
Size US$166
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  • Immunohistochemistry of paraffin-embedded human kidney tissue using CSB-PA10857A0Rb at dilution of 1:100
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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) HSPE1 Polyclonal antibody
Uniprot No.
Target Names
HSPE1
Alternative Names
10 kDa chaperonin antibody; 10 kDa heat shock protein mitochondrial antibody; 10 kDa heat shock protein; mitochondrial antibody; CH10_HUMAN antibody; Chaperonin 10 antibody; Chaperonin 10 homolog antibody; CPN10 antibody; cpn10 homolog antibody; Early pregnancy factor antibody; Early-pregnancy factor antibody; EPF antibody; GROES antibody; GroES homolog antibody; Heat shock 10kD protein 1 chaperonin 10 antibody; Heat shock 10kDa protein 1 antibody; Heat shock 10kDa protein 1 chaperonin 10 antibody; Heat shock protein family E (Hsp10) member antibody; Heat-shock 10-kD protein antibody; Hsp10 antibody; Hspe1 antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human 10 kDa heat shock protein, mitochondrial protein (2-102AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated

The HSPE1 Antibody (Product code: CSB-PA10857A0Rb) is Non-conjugated. For HSPE1 Antibody with conjugates, please check the following table.

Available Conjugates
Conjugate Product Code Product Name Application
HRP CSB-PA10857B0Rb HSPE1 Antibody, HRP conjugated ELISA
FITC CSB-PA10857C0Rb HSPE1 Antibody, FITC conjugated
Biotin CSB-PA10857D0Rb HSPE1 Antibody, Biotin conjugated ELISA
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Tested Applications
ELISA, IHC
Recommended Dilution
Application Recommended Dilution
IHC 1:20-1:200
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
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.

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Target Background

Function
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.
Gene References into Functions
  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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Subcellular Location
Mitochondrion matrix.
Protein Families
GroES chaperonin family
Database Links

HGNC: 5269

OMIM: 600141

KEGG: hsa:3336

STRING: 9606.ENSP00000233893

UniGene: Hs.1197

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