6868 Results for: "lacnac MP glycoside"

Supplier: TCI America

Molecular Weight: 593.54
Purity/Analysis Method: >95.0% (HPLC)
Form: Crystal
Storage Temperature: <0°C
Molecular Formula: C24H35NO16

Supplier: TCI America

CAS Number: 159922-54-0
Molecular Formula: C24H35NO15
Molecular Weight: 577.54
Purity/Analysis Method: >95.0% (HPLC)
Form: Crystal
Storage Temperature: <0°C

Supplier: TCI America

Molecular Weight: 577.54
Purity/Analysis Method: >95.0% (HPLC)
Form: Crystal
Storage Temperature: <0°C
Molecular Formula: C24H35NO15

Supplier: TCI America

CAS Number: 1072896-38-8
Molecular Formula: C24H35NO16
Molecular Weight: 593.54
Purity/Analysis Method: >97.0% (HPLC)
Form: Crystal
Storage Temperature: <0°C

Supplier: TCI America

Molecular Weight: 530.53
Form: Crystal
Color: White
Storage Temperature: <0°C
Molecular Formula: C23H34N2O12

Supplier: TCI America

Molecular Weight: 530.53
Storage Temperature: <0°C
Molecular Formula: C23H34N2O12

Supplier: AFG BIOSCIENCE LLC

2-Azidoethyl LacNAc ≥95%

Supplier: Prosci

CHST1 catalyzes the transfer of sulfate to position 6 of galactose (Gal) 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 Gal residues are sulfated. It 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.

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

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: 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

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: MP Biomedicals

Agar is a polysaccharide complex extracted by bleaching and hot water treatment of agarocytes from the red alga Rhodophyceae, and usually consisting of the genera Gelidium, Acanthopeltis, Ceramium, Pterocladia and Gracilaria. The algae are typically found in the Pacific and Indian Oceans and in the Sea of Japan. It is primarily composed of two different units: Agarose and Agaropectin; Agarose is a neutral gelling component which is composed of a linear polymer of alternating D-galactose and 3,6-anhydrogalactose units. Agaropectin is a non-gelling component which consists of D-1,3-glycosidically linked D-galactose units, some of which are sulfated at the 6th position.
Agar is specially purified for use in preparing solid culture media for microbiological and bacteriological applications.

Supplier: AFG BIOSCIENCE LLC

N-Acetyl-3-O-β-D-galactopyranosyl-β-D-galactosamine methyl glycoside ≥95%

Supplier: Bioss

Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.

Supplier: Proteintech

POFUT1 (protein O-fucosyltransferase 1), also known as GDP-fucose protein O-fucosyltransferase, is an enzyme that catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in EGF domains and plays a crucial role in Notch signaling.

Supplier: New England Biolabs (NEB)

Endoglycoceramidase I (EGCase I) catalyzes the hydrolysis of the β-glycosidic linkage between oligosaccharides and ceramides in various glycosphingolipids.

Supplier: Genetex

GBA3, or cytosolic beta-glucosidase (EC 3.2.1.21), is a predominantly liver enzyme that efficiently hydrolyzes beta-D-glucoside and beta-D-galactoside, but not any known physiologic beta-glycoside, suggesting that it may be involved in detoxification of plant glycosides (de Graaf et al., 2001 [PubMed 11389701]). GBA3 also has significant neutral glycosylceramidase activity (EC 3.2.1.62), suggesting that it may be involved in a nonlysosomal catabolic pathway of glucosylceramide metabolism (Hayashi et al., 2007 [PubMed 17595169]).[supplied by OMIM]

Supplier: Prosci

MPG functions in the hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.

Supplier: Prosci

MPG functions in the hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.

Supplier: Bioss

Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.

Supplier: Bioss

Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.