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elevated expression of HSP10 protein inhibits apoptosis and associates with poor prognosis of astrocytoma
miR (show MLXIP Antibodies)-146a, miR (show MLXIP Antibodies)-146b, and miR (show MLXIP Antibodies)-155 are exerting anti-inflammatory properties by down-regulating IL-6 (show IL6 Antibodies) and IL-8 (show IL8 Antibodies), and influencing the expression of HSP10 in the activated endothelium
High expression of HSP10 is negatively associated with estrogen receptor (show ESR1 Antibodies)/progesterone receptor (show PGR Antibodies) status and might be a novel independent biomarker for poor prognosis in invasive ductal breast carcinoma.
EPF induces the differentiation of regulatory T cells and increases their immunosuppressive activities.
Hsp10 and Hsp60 (show HSPD1 Antibodies) 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 has a role in the spatial regulation of NPAT (show NPAT Antibodies) signaling
Hsp10 has a role in nuclear localization and lung cells response to cigarette smoke
Hsp10 and Hsp90 (show HSP90 Antibodies) 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%.
heat shock protein 10 is a Sirtuin 3 (show SIRT3 Antibodies) substrate
Hsp10 exerts anti-inflammatory activity by inhibiting Toll (show TLR4 Antibodies)-like receptor signaling possibly by interacting with extracellular Hsp60 (show HSPD1 Antibodies)
interaction between HSPE1 and HSPD1 (show HSPD1 Antibodies) 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
, 10 kDa heat shock protein, mitochondrial
, chaperonin 10
, early-pregnancy factor
, heat shock 10kD protein 1 (chaperonin 10)
, chaperonin 10 kDa
, chaperonin, 10 kDa
, chaperonin-10 kDa
, Heat shock 10 kD protein 1 (chaperonin 10)
, heat shock 10 kDa protein 1 (chaperonin 10)
, heat shock protein 10
, heat shock 10kD protein
, heat shock 10kDa protein 1
, heat shock 10kDa protein 1 (chaperonin 10)
, 10 kd chaperonin
, co-chaperonin 10, mitochondrial
, co-chaperonin GroES
, mitochondrial heat shock protein Hsp10
, chaperonin GroS
, Hsp10 10 kDa chaperonin GROES
, 10 kDa chaperonin GROES Hsp10
, mitochondrial chaperonin 10