Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Bioss

PRKACA and PRKACB are members of the Ser/Thr protein kinase family and are a catalytic subunit of cAMP-dependent protein kinase. cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits.PKA alpha + beta (catalytic subunits) (phospho Thr198)

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Apollo Scientific

N-Acetyl-D-galactosamine

Supplier: Thermo Fisher Scientific

CAS No.: 14215-68-0

Supplier: Apollo Scientific

5-Bromo-4-chloro-3-indolyl N-acetyl-β-D-galactosaminide

Supplier: Apollo Scientific

N-Acetyl-D-galactosamine ≥98%

Supplier: Bioss

Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Isoform 2 may facilitate PARK2 transport into the mitochondria. In collaboration with PARK2, isoform 2 may enhance cell viability and protect cells from oxidative stress.

Supplier: Apollo Scientific

2-Azidoethyl 2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-galactopyranoside ≥98%

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Bioss

Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Isoform 2 may facilitate PARK2 transport into the mitochondria. In collaboration with PARK2, isoform 2 may enhance cell viability and protect cells from oxidative stress.

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Thermo Fisher Scientific

N-Acetyl-D-galactosamine 98%

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Bioss

Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

Supplier: Bioss

The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

Supplier: Biotium

Recognizes a disaccharide epitope, Gal1-3GalNAc, of Thomsen-Friedenreich (TF) antigen. It is specific for both anomeric forms of the disaccharide (TF and TF, including related structures on the glycolipid) and shows no cross-reactivity with sialylated glycophorin. The Thomsen-Friedenreich antigen acts as an oncofetal antigen, with low expression in normal adult tissues but increasing to fetal levels of expression in hyperplasia or malignancy. It is considered as a pan-carcinoma marker. This MAb is capable to agglutinate desialylated red blood cells. During metastasis, the ability of malignant cells to form multicellular aggregates via homotypic or heterotypic aggregation and their adhesion to the endothelium are critical. The tumor-associated carbohydrate Thomsen-Friedenreich antigen (Gal-GalNAc) is involved in tumor cell adhesion and tissue invasion. It also causes an immune response, and overexpression of the antigen causes cancer cells to be more sensitive to natural killer cell lysis. The Thomsen-Friedenreich antigen is suppressed in normal healthy cells and represents one of the few chemically well-defined antigens associated with tumor malignancy. The presence of the Thomsen-Friedenreich antigen on the surface of cancer cells may result from a divergence from the normal pathway for O-linked glycosylation in these cells, most likely caused by inappropriate localization of the enzymes involved in synthesis of the disaccharide.

Supplier: Biotium

Recognizes a disaccharide epitope, Gal1-3GalNAc, of Thomsen-Friedenreich (TF) antigen. It is specific for both anomeric forms of the disaccharide (TF and TF, including related structures on the glycolipid) and shows no cross-reactivity with sialylated glycophorin. The Thomsen-Friedenreich antigen acts as an oncofetal antigen, with low expression in normal adult tissues but increasing to fetal levels of expression in hyperplasia or malignancy. It is considered as a pan-carcinoma marker. This MAb is capable to agglutinate desialylated red blood cells. During metastasis, the ability of malignant cells to form multicellular aggregates via homotypic or heterotypic aggregation and their adhesion to the endothelium are critical. The tumor-associated carbohydrate Thomsen-Friedenreich antigen (Gal-GalNAc) is involved in tumor cell adhesion and tissue invasion. It also causes an immune response, and overexpression of the antigen causes cancer cells to be more sensitive to natural killer cell lysis. The Thomsen-Friedenreich antigen is suppressed in normal healthy cells and represents one of the few chemically well-defined antigens associated with tumor malignancy. The presence of the Thomsen-Friedenreich antigen on the surface of cancer cells may result from a divergence from the normal pathway for O-linked glycosylation in these cells, most likely caused by inappropriate localization of the enzymes involved in synthesis of the disaccharide.