免疫原
Synthesized peptide derived from human GLTL4 AA range: 144-194
特异性
This antibody detects endogenous levels of GLTL4 at Human/Mouse
组成
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
纯化工艺
The antibody was affinity-purified from mouse serum by affinity-chromatography using specific immunogen.
背景
catalytic activity:NADH + ubiquinone = NAD(+) + ubiquinol.,disease:Defects in MT-ND2 are a cause of Leber hereditary optic neuropathy (LHON) [MIM:535000]. LHON is a maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes.,disease:Defects in MT-ND2 may be associated with mitochondrial susceptibility to Alzheimer disease (AD) [MIM:502500].,function:Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.,similarity:Belongs to the complex I subunit 2 family.,
功能
catalytic activity:UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide.,cofactor:Calcium.,cofactor:Manganese.,domain:The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.,domain:There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.,function:May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.,online information:GlycoGene database,pathway:Protein modification; protein glycosylation.,similarity:Belongs
