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Catalog Number: (PRSI92-391)
Supplier: ProSci Inc.
Description: Ganglioside GM2 activator (GM2A) is a small glycolipid transport protein which acts as a substrate specific co-factor for the lysosomal enzyme beta -hexosaminidase A (HEXB). HEXB together with GM2A, catalyses the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. GM2A accommodate several single chain phospholipids and fatty acids, is a lipid transfer protein that stimulates the enzymatic processing of gangliosides, and also T-cell activation through lipid presentation. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.
UOM: 1 * 50 µG


Catalog Number: (BOSSBS-12862R-A647)
Supplier: Bioss
Description: The B subunit of cholera toxin (CtxB) binds to a GM1-ganglioside receptor, a ubiquitous glycolipid cell surface receptor. This binding is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin A subunit into cells. The beta chain has no toxic activity by itself. The holotoxin consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. The A subunit contains two chains, A1 and A2, linked by a disulfide bridge. The A subunit (and Cholera toxin) activates the adenylate cyclase enzyme in cells of the intestinal mucosa leading to increased levels of intracellular cAMP.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12862R-CY7)
Supplier: Bioss
Description: The B subunit of cholera toxin (CtxB) binds to a GM1-ganglioside receptor, a ubiquitous glycolipid cell surface receptor. This binding is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin A subunit into cells. The beta chain has no toxic activity by itself. The holotoxin consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. The A subunit contains two chains, A1 and A2, linked by a disulfide bridge. The A subunit (and Cholera toxin) activates the adenylate cyclase enzyme in cells of the intestinal mucosa leading to increased levels of intracellular cAMP.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12862R-A350)
Supplier: Bioss
Description: The B subunit of cholera toxin (CtxB) binds to a GM1-ganglioside receptor, a ubiquitous glycolipid cell surface receptor. This binding is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin A subunit into cells. The beta chain has no toxic activity by itself. The holotoxin consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. The A subunit contains two chains, A1 and A2, linked by a disulfide bridge. The A subunit (and Cholera toxin) activates the adenylate cyclase enzyme in cells of the intestinal mucosa leading to increased levels of intracellular cAMP.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12862R-A488)
Supplier: Bioss
Description: The B subunit of cholera toxin (CtxB) binds to a GM1-ganglioside receptor, a ubiquitous glycolipid cell surface receptor. This binding is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin A subunit into cells. The beta chain has no toxic activity by itself. The holotoxin consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. The A subunit contains two chains, A1 and A2, linked by a disulfide bridge. The A subunit (and Cholera toxin) activates the adenylate cyclase enzyme in cells of the intestinal mucosa leading to increased levels of intracellular cAMP.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12862R-FITC)
Supplier: Bioss
Description: The B subunit of cholera toxin (CtxB) binds to a GM1-ganglioside receptor, a ubiquitous glycolipid cell surface receptor. This binding is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin A subunit into cells. The beta chain has no toxic activity by itself. The holotoxin consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. The A subunit contains two chains, A1 and A2, linked by a disulfide bridge. The A subunit (and Cholera toxin) activates the adenylate cyclase enzyme in cells of the intestinal mucosa leading to increased levels of intracellular cAMP.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12862R-A750)
Supplier: Bioss
Description: The B subunit of cholera toxin (CtxB) binds to a GM1-ganglioside receptor, a ubiquitous glycolipid cell surface receptor. This binding is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin A subunit into cells. The beta chain has no toxic activity by itself. The holotoxin consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. The A subunit contains two chains, A1 and A2, linked by a disulfide bridge. The A subunit (and Cholera toxin) activates the adenylate cyclase enzyme in cells of the intestinal mucosa leading to increased levels of intracellular cAMP.
UOM: 1 * 100 µl


Catalog Number: (345759-100)
Supplier: Merck Millipore (Oncogene)
Description: Anti-Ganglioside Rabbit Polyclonal Antibody
UOM: 1 * 100 µl


Catalog Number: (345758-100)
Supplier: Merck Millipore (Oncogene)
Description: Anti-Ganglioside Rabbit Polyclonal Antibody
UOM: 1 * 100 µl


Catalog Number: (345757-100)
Supplier: Merck Millipore (Oncogene)
Description: Anti-Ganglioside Rabbit Polyclonal Antibody
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13695R)
Supplier: Bioss
Description: The Src family of protein tyrosine kinases (Src-PTKs) is important in the regulation of growth and differentiation of eukaryotic cells. The activity of Src-PTKs in cells of different types is negatively controlled by Csk. Csk binding protein (Cbp), also designated phosphoprotein associated with glycosphingo-lipid-enriched microdomains (GEMs) or PAG, is a ubiquitously expressed transmembrane phosphoprotein that binds specifically to the SH2 domain of Csk. Cbp is involved in the membrane localization of Csk and in Csk-mediated inhibition of c-Src. In the plasma membrane, Cbp is exclusively localized in the GM1 ganglioside-enriched detergent-insoluble membrane domain, which is important in receptor-mediated signaling. Cbp is a component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13695R-CY7)
Supplier: Bioss
Description: The Src family of protein tyrosine kinases (Src-PTKs) is important in the regulation of growth and differentiation of eukaryotic cells. The activity of Src-PTKs in cells of different types is negatively controlled by Csk. Csk binding protein (Cbp), also designated phosphoprotein associated with glycosphingo-lipid-enriched microdomains (GEMs) or PAG, is a ubiquitously expressed transmembrane phosphoprotein that binds specifically to the SH2 domain of Csk. Cbp is involved in the membrane localization of Csk and in Csk-mediated inhibition of c-Src. In the plasma membrane, Cbp is exclusively localized in the GM1 ganglioside-enriched detergent-insoluble membrane domain, which is important in receptor-mediated signaling. Cbp is a component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13695R-CY5)
Supplier: Bioss
Description: The Src family of protein tyrosine kinases (Src-PTKs) is important in the regulation of growth and differentiation of eukaryotic cells. The activity of Src-PTKs in cells of different types is negatively controlled by Csk. Csk binding protein (Cbp), also designated phosphoprotein associated with glycosphingo-lipid-enriched microdomains (GEMs) or PAG, is a ubiquitously expressed transmembrane phosphoprotein that binds specifically to the SH2 domain of Csk. Cbp is involved in the membrane localization of Csk and in Csk-mediated inhibition of c-Src. In the plasma membrane, Cbp is exclusively localized in the GM1 ganglioside-enriched detergent-insoluble membrane domain, which is important in receptor-mediated signaling. Cbp is a component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13695R-HRP)
Supplier: Bioss
Description: The Src family of protein tyrosine kinases (Src-PTKs) is important in the regulation of growth and differentiation of eukaryotic cells. The activity of Src-PTKs in cells of different types is negatively controlled by Csk. Csk binding protein (Cbp), also designated phosphoprotein associated with glycosphingo-lipid-enriched microdomains (GEMs) or PAG, is a ubiquitously expressed transmembrane phosphoprotein that binds specifically to the SH2 domain of Csk. Cbp is involved in the membrane localization of Csk and in Csk-mediated inhibition of c-Src. In the plasma membrane, Cbp is exclusively localized in the GM1 ganglioside-enriched detergent-insoluble membrane domain, which is important in receptor-mediated signaling. Cbp is a component of the regulatory mechanism controlling the activity of membrane-associated Src-PTKs.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11725R)
Supplier: Bioss
Description: Glutathione S-transferases (GSTs) function to conjugate reduced glutathione to many exogenous and endogenous hydrophobic electrophiles. Although it shares the carboxy and amino-terminal glutathione S-transferase domains, GDAP1 is characterized as a GST-like protein because it contains an extended GST domain II and a predicted transmembrane domain, two characteristics which are unusual for GST family members. GDAP1 may function in a signal transduction pathway that is responsible for ganglioside-induced neurite differentiation and also may play a role in protecting myelin membranes from free-radical damage. Mutations in the gene encoding GDAP1 is the cause of many forms of Charcot-Marie-Tooth disease, a common inherited disorder of the peripheral nervous system that is characterized by reduced nerve conduction velocities, slow progressive distal muscle atrophy and absent deep tendon reflexes.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12862R)
Supplier: Bioss
Description: The B subunit of cholera toxin (CtxB) binds to a GM1-ganglioside receptor, a ubiquitous glycolipid cell surface receptor. This binding is widely accepted to initiate toxin action by triggering uptake and delivery of the toxin A subunit into cells. The beta chain has no toxic activity by itself. The holotoxin consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. The A subunit contains two chains, A1 and A2, linked by a disulfide bridge. The A subunit (and Cholera toxin) activates the adenylate cyclase enzyme in cells of the intestinal mucosa leading to increased levels of intracellular cAMP.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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