Translocases,EC 7

Expression system: E. coli
Length: 1248-1531, Partial
Activity: Not Tested

Expression system: E. coli
Length: 314-756, Partial
Activity: Not Tested

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.

Expression system: E. coli
Length: 350-783, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-398, Full Length
Activity: Not Tested

Expression system: in vitro E. coli expression system
Length: 10-450, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-398, Full Length
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 48-529, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 350-710, Partial
Activity: Not Tested

SecA Protein, Helicobacter pylori, Recombinant (His) is expressed in E. coli. The accession number is B5Z7E8.

Expression system: E. coli
Length: 230-529, Partial
Activity: Not Tested

Expression system: E. coli
Length: 230-529, Partial
Activity: Not Tested

Expression system: E. coli
Length: 23-168, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-745, Full Length
Activity: ELISA

Expression system: E. coli
Length: 1-250, Partial
Activity: Not Tested

Expression system: E. coli
Length: 47-529, Full Length of Mature Protein
Activity: Not Tested