Recombinatie Cpn10 monoklonaal antilichaam

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.

Cpn10

P61604

Human; Rat; Mouse

Recombinant human Cpn10 fragment

CPN; HSP; HSPE; HSPE1; CPN10; EPF; GROES; HSP10;10 kDa chaperonin;10 kDa heat shock protein;10 kDa heat shock protein mitochondrial; CH10; Chaperonin 10; Chaperonin 10 homolog; cpn10 homolog; Early pregnancy factor; Early-pregnancy factor; GroES homolog; Heat shock 10kD protein 1 chaperonin 10; Heat shock 10kDa protein 1; Heat shock 10kDa protein 1 chaperonin 10; Heat shock protein family E (Hsp10) member; Heat-shock 10-kD protein; mitochondrial

A193

Unconjugated

WB; IHC; IF

Signal Transduction; Metabolism

Protein A purified

1 mg/mL

WB 1:500-1:1000; IHC 1:200-1:1000; IF 1:50

PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant.

Ice bag

Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.

https://789.bio/eb/pNGSeamO

11 kDa

11 kDa

IgG, κ