57543 Results for: "Gal+beta(1-3)GalNAc-alpha-Thr"

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: Apollo Scientific

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

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: Apollo Scientific

N-Acetyl-D-galactosamine ≥98%

Supplier: Thermo Fisher Scientific

CAS No.: 14215-68-0

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: 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

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

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: 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

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

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

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: 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: ProSci Inc.

C-Type Lectin Domain Family 10 Member A (CLEC10A) is a type II transmembrane C-type lectin that is expressed on immature myleloid dendritic cells and alternatively activated (tolerogenic) macrophages. CLEC10A/MGL binds and internalizes molecules with terminal nonsialylated GalNAc carbohydrates such as the Tn carcinoma antigen. CLEC10A/MGL also binds the GP envelope glycoprotein on Marburg and Ebola viruses and enhances viral entry and infectivity. It constitute a unique class of C-type lectins because of their specificity for galactose and its structural homologues. CLEC10A is thought to participate in the recognition of molecules from both altered self and pathogens due to its monosaccharide specificity for Gal and N-acetylgalactosamine (GalNAc). Human and rat carry a single gene for CLEC10A/MGL, while mouse has two closely related MGL1 and MGL2 genes.