5870 Results for: "Chondroitin+sulfate&amp"

Supplier: Bioss

Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Transfers sulfate to the C4 hydroxyl of beta1,4-linked GalNAc that is substituted with a beta-linked glucuronic acid at the C-3 hydroxyl. No activity toward dermatan.

Supplier: Prosci

GALNAC4S-6ST is a sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc (4,6-SO (4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc (4SO4)-GlcA (2SO4)-GalNAc (6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. GALNAC4S-6ST may also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo.

Supplier: AFG Bioscience

Rat CSPG5 (Chondroitin Sulfate Proteoglycan 5) ELISA Kit

Supplier: Bioss

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. May play a role in the maintenance of naive T-lymphocytes in the spleen.

Supplier: AFG Bioscience

Human MCSP (Melanoma Associated Chondroitin Sulfate Proteoglycan) ELISA Kit

Supplier: Bioss

Chondroitin sulphate proteoglycans (CSPGs) are upregulated in the central nervous system after injury, specifically around the lesion site where the glial scar forms. CSPGs have been shown to be closely involved in this neuronal growth inhibition, specifically through their sugar chains.Chondroitin sulphate proteoglycans may also play a role in the repair of spinal cord injury.

Supplier: ALADDIN SCIENTIFIC

Chondroitin sulfate C sodium salt

Supplier: Bioss

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.

Supplier: Boster Biological Technology

For quantitative detection of mouse Ncan in cell culture supernatants, serum and plasma (heparin, EDTA, citrate).

Supplier: Bioss

Chondroitinase is a 522 amino acid protein that localizes to the lysosome and functions as an exohydrolase that is essential for the degradation of glycosaminoglycans, keratan sulfate and chondroitin 6-sulfate. Using calcium as a cofactor, Chondroitinase, which exists as a disulfide linked oligomer, catalyzes the hydrolysis of the 6-sulfate group on target substrates. Defects in the gene encoding Chondroitinase are the cause of mucopolysaccharidosis type 4A (MPS4A), an autosomal recessive lysosomal storage disease that is characterized by the intracellular accumulation of keratan sulfate and chondroitin-6-sulfate and is associated with dental anomalies, short stature and, in some cases, death in the second or third decade of life.

Supplier: Bioss

Chondroitinase is a 522 amino acid protein that localizes to the lysosome and functions as an exohydrolase that is essential for the degradation of glycosaminoglycans, keratan sulfate and chondroitin 6-sulfate. Using calcium as a cofactor, Chondroitinase, which exists as a disulfide linked oligomer, catalyzes the hydrolysis of the 6-sulfate group on target substrates. Defects in the gene encoding Chondroitinase are the cause of mucopolysaccharidosis type 4A (MPS4A), an autosomal recessive lysosomal storage disease that is characterized by the intracellular accumulation of keratan sulfate and chondroitin-6-sulfate and is associated with dental anomalies, short stature and, in some cases, death in the second or third decade of life.

Supplier: Bioss

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.

Supplier: Bioss

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.

Supplier: Bioss

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.

Supplier: Bioss

Chondroitinase is a 522 amino acid protein that localizes to the lysosome and functions as an exohydrolase that is essential for the degradation of glycosaminoglycans, keratan sulfate and chondroitin 6-sulfate. Using calcium as a cofactor, Chondroitinase, which exists as a disulfide linked oligomer, catalyzes the hydrolysis of the 6-sulfate group on target substrates. Defects in the gene encoding Chondroitinase are the cause of mucopolysaccharidosis type 4A (MPS4A), an autosomal recessive lysosomal storage disease that is characterized by the intracellular accumulation of keratan sulfate and chondroitin-6-sulfate and is associated with dental anomalies, short stature and, in some cases, death in the second or third decade of life.

Supplier: Bioss

Chondroitinase is a 522 amino acid protein that localizes to the lysosome and functions as an exohydrolase that is essential for the degradation of glycosaminoglycans, keratan sulfate and chondroitin 6-sulfate. Using calcium as a cofactor, Chondroitinase, which exists as a disulfide linked oligomer, catalyzes the hydrolysis of the 6-sulfate group on target substrates. Defects in the gene encoding Chondroitinase are the cause of mucopolysaccharidosis type 4A (MPS4A), an autosomal recessive lysosomal storage disease that is characterized by the intracellular accumulation of keratan sulfate and chondroitin-6-sulfate and is associated with dental anomalies, short stature and, in some cases, death in the second or third decade of life.

Supplier: Boster Biological Technology

For quantitative detection of human NCAN in cell culture supernatants, serum and plasma (heparin, EDTA, citrate).

Supplier: Bioss

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.

Supplier: Bioss

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.

Supplier: Bioss

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.

Supplier: Bioss

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.

Supplier: Bioss

Chondroitinase is a 522 amino acid protein that localizes to the lysosome and functions as an exohydrolase that is essential for the degradation of glycosaminoglycans, keratan sulfate and chondroitin 6-sulfate. Using calcium as a cofactor, Chondroitinase, which exists as a disulfide linked oligomer, catalyzes the hydrolysis of the 6-sulfate group on target substrates. Defects in the gene encoding Chondroitinase are the cause of mucopolysaccharidosis type 4A (MPS4A), an autosomal recessive lysosomal storage disease that is characterized by the intracellular accumulation of keratan sulfate and chondroitin-6-sulfate and is associated with dental anomalies, short stature and, in some cases, death in the second or third decade of life.

Supplier: Bioss

Catalyzes the transfer of sulfate to position 6 of galactose residues of keratan. It has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal galactose residues are sulfated. It also may function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. It participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Aggrecan is the major proteoglycan of human articular cartilage. The core protein is substituted by a number of keratan sulfate and chondroitin sulfate glycosaminoglycan chains. Whereas chondroitin sulfate is widely distributed throughout the body, keratan sulfate is primarily expressed in cartilage (joints, trachea, intervertebral discs) and cornea.

Supplier: Bioss

Chondroitinase is a 522 amino acid protein that localizes to the lysosome and functions as an exohydrolase that is essential for the degradation of glycosaminoglycans, keratan sulfate and chondroitin 6-sulfate. Using calcium as a cofactor, Chondroitinase, which exists as a disulfide linked oligomer, catalyzes the hydrolysis of the 6-sulfate group on target substrates. Defects in the gene encoding Chondroitinase are the cause of mucopolysaccharidosis type 4A (MPS4A), an autosomal recessive lysosomal storage disease that is characterized by the intracellular accumulation of keratan sulfate and chondroitin-6-sulfate and is associated with dental anomalies, short stature and, in some cases, death in the second or third decade of life.

Supplier: Bioss

Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix.

Supplier: Prosci

XYLT2 is an isoform of xylosyltransferase, which belongs to a family of glycosyltransferases. This enzyme transfers xylose from UDP-xylose to specific serine residues of the core protein and initiates the biosynthesis of glycosaminoglycan chains in proteoglycans including chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate. The enzyme activity, which is increased in scleroderma patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis.The protein encoded by this gene is an isoform of xylosyltransferase, which belongs to a family of glycosyltransferases. This enzyme transfers xylose from UDP-xylose to specific serine residues of the core protein and initiates the biosynthesis of glycosaminoglycan chains in proteoglycans including chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate. The enzyme activity, which is increased in scleroderma patients, is a diagnostic marker for the determination of sclerotic activity in systemic sclerosis. 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: MilliporeSigma

NG2 is a high molecular weight, integral membrane chondroitin sulfate proteoglycan. It is found on the surfaces of an unusual class of glial cells within the developing and mature central nervous system that have the properties of oligodendrocyte precursor cells (i.e., O-2A progenitor cells). NG2 is also found on the surfaces of chondroblasts, proliferating capillary endothelial cells, some human melanoma cell lines, and on leukemic blasts in childhood acute lymphoblastic leukemia. The NG2 proteoglycan is likely to play a role in regulation of cell motility, axon outgrowth and the cellular responses to platelet-derived growth factor.

Supplier: Bioss

Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix.

Supplier: Genetex

Rabbit polyclonal to CSGALNACT2 (Internal)

Supplier: Bioss

Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix.