You Searched For: N-Cbz-L-asparagine

Catalog Number: (BOSSBS-6800R-A555)

Supplier: Bioss

Description: Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-0473R-A680)

Supplier: Bioss

Description: Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. May also be activated by insulin. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialisation, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904). Acts as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses (PubMed:10051606, PubMed:10196349).

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-0473R-A750)

Supplier: Bioss

Description: Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. May also be activated by insulin. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialisation, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904). Acts as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses (PubMed:10051606, PubMed:10196349).

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-0473R-A555)

Supplier: Bioss

Description: Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. May also be activated by insulin. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904). Acts as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses (PubMed:10051606, PubMed:10196349).

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-12937R-A350)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Sale

Supplier: Merck

Description: L(+)-Asparagine, Sigma-Aldrich®

Supplier: MP Biomedicals

Description: Storage: Store at Room Temperature (15-30 °C). Store Desiccated.
L-Asparagine is used in cell culture media and is a component of MEM non-essential amino acids solution. L-Asparagine has been shown to enhance ornithine decarboxylase activity in cultured human colon adenocarcinoma Caco-2 cells and in cultured IEC-6 intestinal epithelial cells. Spore germination in Bacillus subtilis has been increased in the presence of L-asparagine. An isoxazoline RGD mimic platelet GPIIb/IIIa antagonist has been prepared by chiral synthesis with L-asparagine as a starting material. L-Asparagine has been utilized in the synthesis of 4-azalysine building blocks for application to combinatorial chemistry.

Catalog Number: (MOLE18373388-100G)

Supplier: Molekula

Description: L(+)-Asparagine monohydrate

UOM: 1 * 100 g

Sale

 This is a MarketSource item. Additional charges may apply

Catalog Number: (BOSSBS-12937R-CY5)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-0473R-CY5)

Supplier: Bioss

Description: Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. May also be activated by insulin. Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904). Acts as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses (PubMed:10051606, PubMed:10196349).

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-12937R-HRP)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-6800R-A488)

Supplier: Bioss

Description: Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-6800R-A350)

Supplier: Bioss

Description: Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-6800R-A647)

Supplier: Bioss

Description: Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-6800R-A680)

Supplier: Bioss

Description: Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-6800R-CY5)

Supplier: Bioss

Description: Component of the N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Loss of the DAD1 protein triggers apoptosis.

UOM: 1 * 100 µl

Sale