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GM2A encodes a small glycolipid transport protein which acts as a substrate specific co-factor for the lysosomal enzyme beta-hexosaminidase A. Zusätzlich bieten wir Ihnen GM2 Ganglioside Activator Antikörper (155) und GM2 Ganglioside Activator Kits (19) und viele weitere Produktgruppen zu diesem Protein an.
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Review of GM2A mutations causing GM2 activator protein deficiency and GM2 gangliosidosis-AB variant.
Studies indicate that sphingolipid activator proteins (SAPs) and anionic lipids are essential stimulators to reach physiological rates of lysosomal sphingolipid degradation.
this study has established the potential role of GM2A in breast cancer progression
Mobilization of membrane lipids by GM2AP was also inhibited in the presence of cholesterol or SM, as revealed by surface plasmon resonance studies
Gene polymorphisms of MD2 and GM2A were associated with the occurrence or severity of neonatal necrotizing enterocolitis.
In vitro assays with the isolated H1 or H2 homodimers (beta-alpha hybrid construct of beta-hexosaminidase A subunits) confirmed that neither was capable of human GM2AP-dependent hydrolysis of GM2 ganglioside.
impact of GM2AP on glucose metabolism
Treatment of meniscal explants with IL-1RA inhibited the expression of many catabolic genes following a single bout of high dynamic strain.
these results provide novel insights into the physiological functions of GM2AP in obesity.
GM2 activator protein exerts strong and broad inhibitory effects on the hydrolysis of phospholipids carried out by plant and microbial phospholipases D
Two new structures of GM2-AP with bound lipids, showing two different lipid-binding modes within the apolar pocket
elucidation of mode of action on gangioside GM2
alpha-subunit loop structure is required for GM2 activator protein binding by beta-hexosaminidase A
glycosphingolipids, particularly GM2, form a complex with CD82, and this complex interacts with Met and thereby inhibits HGF-induced Met tyrosine kinase activity, as well as integrin to Met cross-talk
The most interesting finding was the association of the GM2-AP with the acrosomal apparatus in early spermatids. A modest to intense staining was observed in some acrosomal granules and acrosomal caps. The GM2-AP seemed to disappear from acrosomal caps in the later stage of spermatids, in which the nucleus became elongated and condensed.
The trafficking of prosaposin and GM2 activator protein to the lysosome in sertoli cells is dependent on sortilin.
This gene encodes a small glycolipid transport protein which acts as a substrate specific co-factor for the lysosomal enzyme beta-hexosaminidase A. Beta-hexosaminidase A, together with GM2 ganglioside activator, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. Mutations in this gene result in GM2-gangliosidosis type AB or the AB variant of Tay-Sachs disease. Alternative splicing results in multiple transcript variants.
GM2 ganglioside activator protein
, ganglioside GM2 activator
, GM2 ganglioside activator
, GM2 activator protein
, cerebroside sulfate activator protein
, shingolipid activator protein 3
, sphingolipid activator protein 3