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HSPE1 encodes a major heat shock protein which functions as a chaperonin. Zusätzlich bieten wir Ihnen Heat Shock 10kDa Protein 1 (Chaperonin 10) Kits (34) und Heat Shock 10kDa Protein 1 (Chaperonin 10) Proteine (26) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 164 products:
Cow (Bovine) Polyclonal HSPE1 Primary Antibody für ICC, IF - ABIN2481936
Vélez-Granell, Arias, Torres-Ruíz, Bendayan: Molecular chaperones in pancreatic tissue: the presence of cpn10, cpn60 and hsp70 in distinct compartments along the secretory pathway of the acinar cells. in Journal of cell science 1994
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Cow (Bovine) Polyclonal HSPE1 Primary Antibody für ICC, IF - ABIN2481937
Morton, Hegh, Clunie: Immunosuppression detected in pregnant mice by rosette inhibition test. in Nature 1974
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Cow (Bovine) Polyclonal HSPE1 Primary Antibody für ICC, IF - ABIN2481930
Cavanagh, Morton: The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10. in European journal of biochemistry / FEBS 1994
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Cow (Bovine) Polyclonal HSPE1 Primary Antibody für ICC, IF - ABIN2481935
Minto, Galli, Gianazza, Eberini, Legname, Fossati, Modena, Marcucci, Mascagni, Ghezzi, Fratelli: Mycobacterial Cpn10 promotes recognition of the mammalian homologue by a mycobacterium-specific antiserum. in Biochimica et biophysica acta 1998
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Chicken Polyclonal HSPE1 Primary Antibody für WB - ABIN2785819
Ralph, Brenchley, Summers, Rosa, Swindell, Jayson: Heparanase gene haplotype (CGC) is associated with stage of disease in patients with ovarian carcinoma. in Cancer science 2007
Data show that chaperonin (zeige HSPD1 Antikörper) Cpn10(1) (At3g60210) is active only upon formation of hetero-oligomers with chaperonin (zeige HSPD1 Antikörper) Cpn20 (At5g20720).
provide evidence that CPN20 functions through antagonizing the ABAR-WRKY40 coupled pathway, and ABA relieves this pathway of repression by inhibiting the ABAR-CPN20 interaction to activate ABAR-WRKY40 interaction
findings show that CPN20 functions negatively in the ABAR-WRKY40 coupled ABA signaling independently of its co-chaperonin (zeige HSPD1 Antikörper) role, and provide a new insight into the role of co-chaperones in the regulation of plant responses to environmental cues.
CPN20 silencing decreases iron superoxide dismutases activity in chloroplast.
Data indicate that on addition of the heat-shock proteins GroEL (zeige GroEL Antikörper)-GroES molecular chaperone (zeige HSP90AA1 Antikörper) system, the folding of the nascent chemokine receptor (zeige CCR1 Antikörper) type 5 (CCR5 (zeige CCR5 Antikörper)) was significantly enhanced.
Cpn10 has a role in the spatial regulation of NPAT (zeige NPAT Antikörper) signaling
Hsp10 has a role in nuclear localization and lung cells response to cigarette smoke
Hsp10 and Hsp90 (zeige HSP90 Antikörper) may be involved in large bowel carcinogenesis.
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%.
Hereditary spastic paraplegia SPG13 (zeige HSPD1 Antikörper) is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60 (zeige HSPD1 Antikörper).
The low stability of the monomeric unit suggests that folding and assembly reactions for cpn10 are coupled.
Cpn10 and placental lactogen (zeige CSH1 Antikörper) are capable of stimulating the synthesis of type I collagen by human osteoblasts in culture
Identification of amino acids important for the assembly of the cpn10 heptamer.
complex mechanisms are involved in the protection by hsp10 against simulated ischemia and reoxygenation-induced myocyte death
heat shock protein 10 is a Sirtuin 3 (zeige SIRT3 Antikörper) substrate
Hsp10 exerts anti-inflammatory activity by inhibiting Toll (zeige TLR4 Antikörper)-like receptor signaling possibly by interacting with extracellular Hsp60 (zeige HSPD1 Antikörper)
interaction between HSPE1 and HSPD1 (zeige HSPD1 Antikörper) in the reproductive tract and in capacitating spermatozoa
This gene encodes a major heat shock protein which functions as a chaperonin. Its structure consists of a heptameric ring which binds to another heat shock protein in order to form a symmetric, functional heterodimer which enhances protein folding in an ATP-dependent manner. This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2. Naturally occurring read-through transcription occurs between this locus and the neighboring locus MOBKL3.
10 kDa chaperonin
, chaperonin 10 kDa
, chaperonin, 10 kDa
, chaperonin-10 kDa
, heat shock 10kDa protein 1
, heat shock 10kDa protein 1 (chaperonin 10)
, 10 kd chaperonin
, co-chaperonin 10, mitochondrial
, chaperonin 10
, 10 kDa heat shock protein, mitochondrial
, co-chaperonin GroES
, mitochondrial heat shock protein Hsp10
, chaperonin GroS
, Hsp10 10 kDa chaperonin GROES
, 10 kDa chaperonin GROES Hsp10
, heat shock protein 10
, heat shock 10kD protein 1 (chaperonin 10)
, early-pregnancy factor
, heat shock 10kD protein
, heat shock 10 kDa protein 1 (chaperonin 10)
, mitochondrial chaperonin 10
, Heat shock 10 kD protein 1 (chaperonin 10)