26674 Results for: "5-Acetyl-2-chloro-6-methylnicotinonitrile&amp"

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

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3. [provided by RefSeq, Jul 2008].

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: Boster Bio

Rabbit IgG polyclonal antibody for DNA replication licensing factor MCM3(MCM3) detection. Tested with WB, IHC-P, ICC in Human;Mouse;Rat.

Supplier: Priorclave

Compact 40 benchtop and Compact 60 floor standing or benchtop autoclaves for the low volume user, with flexible operation usually only available in larger autoclave units. This flexibility is delivered by the TACTROL™ microprocessor control system, specially developed for laboratory autoclaves, with programming ranging from simple cycles to fully featured multi-program operation with logged records. All Priorclaves come complete with Biomaster antimicrobial coating, helping improved laboratory hygiene; it is effective against all bacteria and fungi including MRSA and therefore helps minimise the risk of cross contamination.

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: Antibodies.com

Human Sialidase-3 ELISA kit is a 90 minutes sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human Sialidase-3 in serum, plasma, and other biological fluids.

Supplier: Antibodies.com

Human NAA20 ELISA kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human NAA20 in serum, plasma, tissue homogenates, and other biological fluids.

Supplier: Antibodies.com

Mouse CD204 ELISA kit is a 90 minute sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of mouse CD204 in serum, plasma, and other biological fluids.

Supplier: Bioss

Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

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: Antibodies.com

Human NAGK ELISA kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human NAGK in serum, plasma, tissue homogenates, and other biological fluids.

Supplier: Antibodies.com

Human CD204 ELISA kit is a 90 minute sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human CD204 in serum, plasma, and other biological fluids.

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: Antibodies.com

Mouse Neu3 ELISA kit is a 90 minutes sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of mouse Neu3 in serum, plasma, and other biological fluids.

Supplier: Antibodies.com

Human NEU4 ELISA kit is a 90 minutes sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human NEU4 in serum, plasma, and other biological fluids.

Supplier: EPPENDORF

Eppendorf Safe-Lock Tubes BioBased 0,5 to 2,0 ml for secure sample storage and reducing carbon footprint. Made from 100% bio-based plastic, they feature a unique locking mechanism to protect samples and match fossil-based tubes performance without assay adjustments. Specifically designed for eco-conscious scientists seeking durability, ease of use, and environmental responsibility.

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: 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.