Recombinant Mouse Asialoglycoprotein receptor 2 (Asgr2),partial Reference: CSB-EP002208MO1_100 Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
Recombinant Mouse Asialoglycoprotein receptor 2 (Asgr2),partial Reference: CSB-EP002208MO1_20 Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
Recombinant Mouse Asialoglycoprotein receptor 2 (Asgr2),Partial Reference: CSB-EP002208MO1b3_1 Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
Recombinant Mouse Asialoglycoprotein receptor 2 (Asgr2),Partial Reference: CSB-EP002208MO1b3_100 Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
Recombinant Mouse Asialoglycoprotein receptor 2 (Asgr2),Partial Reference: CSB-EP002208MO1b3_20 Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.
Recombinant Human Agouti-signaling protein(ASIP),partial Reference: CSB-EP002212HU1_1 Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). In higher primates, agouti may affect the quality of hair pigmentation rather than its pattern of deposition. Could well play a role in neuroendocrine aspects of melanocortin action. May have some functional role in regulating the lipid metabolism with adipocytes.
Recombinant Human Agouti-signaling protein(ASIP),partial Reference: CSB-EP002212HU1_100 Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). In higher primates, agouti may affect the quality of hair pigmentation rather than its pattern of deposition. Could well play a role in neuroendocrine aspects of melanocortin action. May have some functional role in regulating the lipid metabolism with adipocytes.
Recombinant Human Agouti-signaling protein(ASIP),partial Reference: CSB-EP002212HU1_20 Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment). In higher primates, agouti may affect the quality of hair pigmentation rather than its pattern of deposition. Could well play a role in neuroendocrine aspects of melanocortin action. May have some functional role in regulating the lipid metabolism with adipocytes.
Recombinant Human Acetylserotonin O-methyltransferase(ASMT) Reference: CSB-EP002216HU_1 Isoform 1 catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin. Isoform 2 and isoform 3 lack enzyme activity.
Recombinant Human Acetylserotonin O-methyltransferase(ASMT) Reference: CSB-EP002216HU_100 Isoform 1 catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin. Isoform 2 and isoform 3 lack enzyme activity.
Recombinant Human Acetylserotonin O-methyltransferase(ASMT) Reference: CSB-EP002216HU_20 Isoform 1 catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin. Isoform 2 and isoform 3 lack enzyme activity.
Recombinant Human ATPase ASNA1(ASNA1) Reference: CSB-EP002218HU_1 ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmbrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by mbrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA mbrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the mbrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting . May be involved in insulin signaling.