ATP2A2 Protein, Human, Recombinant (C-His) is expressed in E. coli expression system with C-6xHis tag. The predicted molecular weight is 55.2 kDa and the accession number is P16615.
ABCC1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 35.9 kDa and the accession number is P33527.
G-protein coupled receptor kinase 2 (GRK2), also referred as Adrenergic, beta, receptor kinase 1 (ADRBK1), is a ubiquitous member of the G protein-coupled receptor kinase (GRK) family that appears to play a central, integrative role in signal transduction cascades. GRK2 can phosphorylate a growing number of non-GPCR substrates and associate with a variety of proteins related to signal transduction, thus suggesting that this kinase could also have diverse 'effector' functions. GRK2 has been reported to interact with a variety of signal transduction proteins related to cell migration such as MEK, Akt, PI3Kgamma or GIT. Interestingly, the levels of expression and activity of this kinase are altered in a number of inflammatory disorders (as rheumatoid arthritis or multiple sclerosis), thus suggesting that GRK2 may play an important role in the onset or development of these pathologies. The important physiological function of GRK2 as a modulator of the efficacy of GPCR signal transduction systems is exemplified by its relevance in cardiovascular physiopathology as well as by its emerging role in the regulation of chemokine receptors. Besides its canonical role in the modulation of the signalling mediated by many G protein-coupled receptors (GPCR), this protein can display a very complex network of functional interactions with a variety of signal transduction partners, in a stimulus, cell type, or context-specific way.
NAD(P)+transhydrogenase (NNT) is located in the inner mitochondrial membrane and catalyzes a reversible hydride transfer between NAD(H) and NADP(H) that is coupled to proton translocation between the intermembrane space and mitochondrial matrix. NNT activity has an essential role in maintaining the NADPH supply for antioxidant defense and biosynthetic pathways. Structurally, NNT is composed of three domains; domains I and III are hydrophilic and have binding sites for NAD and NADP, respectively, while domain II is hydrophobic and is a transmembrane pathway through which protons translocate. NNT forms dimers, whose monomers act in an anti-phase way; domain III (NADP(H)- binding) flips, allowing proton translocation across the inner mitochondrial membrane one moment and favoring hydride transfer between NAD(H) and NADP(H) the next. And NNT pathophysiological roles after the discovery of a spontaneous Nnt mutation in C57BL 6J mice. And Nnt silencing reduced the growth of cancer cell lines, suggesting that NNT might be a therapeutic target in some cancers.
Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably responsible for energy coupling to the transport system.
ATP4A Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 54.6 kDa and the accession number is P20648.
Required for corrinoid utilization. Probably part of the ABC transporter complex BtuCDF involved in cobalamin (vitamin B12) import. Probably responsible for energy coupling to the transport system.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). Can transport lactose, melibiose, lactulose or the analog methyl-1-thio-beta,D-galactopyranoside (TMG), but not sucrose or fructose. The substrate specificity is directed toward the galactopyranosyl moiety of the substrate. Lactose permease Protein, E. coli, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 34.4 kDa and the accession number is P02920.
ATP5F1B Protein, Rat, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 59.2 kDa and the accession number is P10719.
ATP5D is a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase consists of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). ATP5D gene encodes the delta subunit of the catalytic core.