SMIM4 Protein, Human (Cell-Free, His)

The SMIM4 protein plays a critical role in the assembly and stability of the mitochondrial ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is responsible for oxidative phosphorylation A key component of the mitochondrial electron transport chain (ETC). It mediates early complex III biogenesis, regulating the levels of electron transport chain proteins in response to changing energy demands. SMIM4 Protein, Human (Cell-Free, His) is the recombinant human-derived SMIM4 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of SMIM4 Protein, Human (Cell-Free, His) is 70 a.a., with molecular weight of 11.5 kDa.

SMIM4 is essential for the assembly and stability of the mitochondrial ubiquinol-cytochrome c reductase complex, also known as complex III or the cytochrome b-c1 complex. This multisubunit transmembrane complex plays a crucial role in the mitochondrial electron transport chain (ETC), which, in turn, drives oxidative phosphorylation. Beyond its involvement in the early biogenesis of complex III, SMIM4 participates in the regulation of electron transport chain protein levels, contributing to the dynamic adjustment of energy supply in response to changes in energy demand. Additionally, SMIM4 plays a role in the initial steps of cytochrome c oxidase complex (complex IV) assembly. It forms associations with the mitochondrial ribosome and interacts with UQCC6, facilitating the synthesis and membrane insertion of MT-CYB. Notably, SMIM4 is a key component of the COMB (coordinator of mitochondrial CYTB biogenesis) complex, working in concert with UQCC1, UQCC2, UQCC4, UQCC5, and UQCC6 to regulate MT-CYB synthesis and promote its effective integration into the mitochondrial membrane.

Human

E. coli Cell-free

N-10*His

Q8WVI0 (M1-E70)

440957

MFTRAQVRRILQRVPGKQRFGIYRFLPFFFVLGGTMEWIMIKVRVGQETFYDVYRRKASERQYQRRLEDE

11.5 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.