5016 Results for: "3-Acetyl-6-methoxyindole"

Supplier: ProSci Inc.

ST6GALNAC5 belongs to a family of sialyltransferases that modify proteins and ceramides on the cell surface to alter cell-cell or cell-extracellular matrix interactions.ST6GALNAC5 belongs to a family of sialyltransferases that modify proteins and ceramides on the cell surface to alter cell-cell or cell-extracellular matrix interactions (Tsuchida et al., 2003 [PubMed 12668675]).

Supplier: Antibodies.com

Rabbit polyclonal antibody to AMPK1 (phospho Ser496) for WB, IHC and ELISA with samples derived from Human, Mouse and Rat.

Supplier: ProSci Inc.

Anti-B3GALNT1 Rabbit Polyclonal Antibody

Supplier: Abcam

Alexa Fluor® 555 Rabbit monoclonal [EPR5377] to Topoisomerase II alpha + Topoisomerase II beta/TOP2B.

Supplier: ProSci Inc.

ACAA1 is an enzyme operative in the beta-oxidation system of the peroxisomes. Deficiency of this enzyme leads to pseudo-Zellweger syndrome.Acetyl-Coenzyme A acyltransferase (ACAA1) is an enzyme operative in the beta-oxidation system of the peroxisomes. Deficiency of this enzyme leads to pseudo-Zellweger syndrome. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Abcam

Mouse monoclonal [2H6BE7] to ACAA1/Beta-ketothiolase.

Supplier: ProSci Inc.

FUNCTION: Involved in the production of GD3 and GT3 from GM3.
CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + beta-N-acetylneuraminyl-2,3-beta-D-galactosyl-R = CMP + beta-N-acetylneuraminyl-2,8-beta-N-acetylneuraminyl-2,3-beta-D-galactosyl-R.
SIMILARITY: Belongs to the glycosyltransferase 29 family.
PATHWAY: Glycosylation.
SUBCELLULAR LOCATION: Golgi apparatus; Golgi membrane; single-pass type II membrane protein

Supplier: MP Biomedicals

A modified tripeptide reversible protease inhibitor of trypsin-like proteases and some cysteine proteases including endoproteinase Lys-C, kallikrein, papain, thrombin, cathepsin B, cathepsins H and L, trypsin, calpain, trypsin and plasmin. Little to no inhibition is seen against pepsin, cathepsins A and D and alpha-chymotrypsin. When adjusted for molarity, all three salt forms are equally effective; however, the hydrochloride salt is usually less invasive in biological settings. Leupeptin, because of its aldehyde group, may act as a reducing agent and therefore interfere in protein determinations such as Lowry and, to a lesser extent, Bradford.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

CTBS is an evolutionarily conserved member of the glycosyl hydrolase 18 family of proteins. Localizing to the lysosome, CTBS plays a role in the degradation of asparagine-linked (Asn-linked) glycoproteins. Glycoproteins are translocated to lysosomes via endocytosis or autophagy where they are broken down by proteases and glycosidases. The catabolism of glycoproteins is an important step in the regular turnover of cellular contents and in maintaining the homeostasis of glycosylation. CTBS functions as a glycosidase that cleaves the reducing end GlcNAc from the core chitobiase unit of oligosaccharides. Before this reaction can occur, AGA (the lysosomal glycosylasparaginase) must first remove the Asn from the Asn-linked glycoprotein to expose the reducing end GlcNAc, thereby allowing CTBS to access the exposed moiety.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: ProSci Inc.

Platelet-Activating Factor Acetylhydrolase (PAFAH) is a secreted enzyme which belongs to the AB hydrolase superfamily and Lipase family and catalyzes the degradation of platelet-activating factor to biologically inactive products. PAFAH is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. PAFAH has been implicated in the development of atherosclerosis and has also been identified as a marker for cardiac disease. PAFAH might have a major physiologic effect in the presence of inflammatory bodily responses. PAFAH alters the action of PAF by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PAFAH has specificity for substrates with a short residue at the sn-2 position.

Supplier: Bioss

Belonging to the glycosyltransferase 14 family, GCNT7, also known as Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 7, is a 430 amino acid glycosyltransferase that is localized to the Golgi apparatus. Other members of this family include GCNT1, GCNT2, GCNT3, GCNT4 and GCNT6. GCNT1 has been shown to play an important regulatory role in the biosynthesis of mucin-type O-glycans, which serve as ligands in cell adhesion. Specifically, GCNT1 expression in leukocytes regulates the synthesis of core 2 O-glycans that carry sialyl-Lewis x (sLex) oligosaccharides, which confer high affinity binding to Selectin proteins. Since downregulation of Selectin ligand expression has been shown to inhibit tissue infiltration, glycosyltransferase 14 family members represent potential drug targets for the treatment of inflammatory disorders and other pathologies involving Selectin proteins.

Supplier: ProSci Inc.

ST8SIA2 is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. ST8SIA2 may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29The protein encoded by this gene is a type II membrane protein that is thought to catalyze the transfer of sialic acid from CMP-sialic acid to N-linked oligosaccharides and glycoproteins. The encoded protein may be found in the Golgi apparatus and may be involved in the production of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). This protein is a member of glycosyltransferase family 29.