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GroES encodes a major heat shock protein which functions as a chaperonin.
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elevated expression of HSP10 (zeige HSPE1 Antikörper) protein inhibits apoptosis and associates with poor prognosis of astrocytoma
miR (zeige MLXIP Antikörper)-146a, miR (zeige MLXIP Antikörper)-146b, and miR (zeige MLXIP Antikörper)-155 are exerting anti-inflammatory properties by down-regulating IL-6 (zeige IL6 Antikörper) and IL-8 (zeige IL8 Antikörper), and influencing the expression of HSP10 (zeige HSPE1 Antikörper) in the activated endothelium
High expression of HSP10 (zeige HSPE1 Antikörper) is negatively associated with estrogen receptor (zeige ESR1 Antikörper)/progesterone receptor (zeige PGR Antikörper) status and might be a novel independent biomarker for poor prognosis in invasive ductal breast carcinoma.
EPF (zeige HSPE1 Antikörper) induces the differentiation of regulatory T cells and increases their immunosuppressive activities.
Hsp10 (zeige HSPE1 Antikörper) and Hsp60 (zeige HSPD1 Antikörper) may be implicated in carcinogenesis from its very early steps in colorectal cancer.
Data indicate that on addition of the heat-shock proteins GroEL-GroES molecular chaperone system, the folding of the nascent chemokine receptor type 5 (CCR5) was significantly enhanced.
Cpn10 (zeige HSPE1 Antikörper) has a role in the spatial regulation of NPAT (zeige NPAT Antikörper) signaling
Hsp10 (zeige HSPE1 Antikörper) has a role in nuclear localization and lung cells response to cigarette smoke
Hsp10 (zeige HSPE1 Antikörper) 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 (zeige HSPE1 Antikörper) monomer increases by over 30%, whereas the interfaces are stabilized by less than 10%.
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
, 10 kDa heat shock protein, mitochondrial
, chaperonin 10
, early-pregnancy factor
, heat shock 10kD protein 1 (chaperonin 10)