GALNT1 Mouse
Sf9, Insect cells.
Polypeptide N-acetylgalactosaminyltransferase 1, Polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, Protein-UDP acetylgalactosaminyltransferase 1, polypeptide N-acetylgalactosaminyltransferase 1.
Sterile filtered colorless solution.
Greater than 90.0% as determined by SDS-PAGE.
Description
GALNT1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 528 amino acids (41-559 a.a.) and having a molecular mass of 60.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
GALNT1 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) is a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) enzyme family. It catalyzes the first step in O-linked oligosaccharide biosynthesis, which involves transferring an N-acetyl-D-galactosamine residue to a serine or threonine residue on a protein. Galnt1 is involved in glycosylating proteins important for bone formation, including osteopontin and bone sialoprotein.
Recombinant Mouse GALNT1 is produced in Sf9 insect cells. It is a single-chain polypeptide containing 528 amino acids (residues 41-559), with a predicted molecular weight of 60.5 kDa. The protein migrates at approximately 50-70 kDa on SDS-PAGE due to glycosylation. The recombinant protein includes a C-terminal 9-amino acid His-tag. It is purified using proprietary chromatographic techniques.
Clear, colorless, and sterile-filtered solution.
The GALNT1 protein solution is provided at a concentration of 0.25 mg/ml in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Avoid repeated freeze-thaw cycles.
The purity of GALNT1 is determined to be greater than 90% by SDS-PAGE analysis.
Polypeptide N-acetylgalactosaminyltransferase 1, Polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, Protein-UDP acetylgalactosaminyltransferase 1, polypeptide N-acetylgalactosaminyltransferase 1.
Sf9, Insect cells.
ADPGLPAGDV LELVQKPHEG PGEMGKPVVI PKEDQEKMKE MFKINQFNLM ASEMIALNRS LPDVRLEGCK TKVYPDNLPT TSVVIVFHNE AWSTLLRTVH SVINRSPRHM IEEIVLVDDA SERDFLKRPL ESYVKKLKVP VHVIRMEQRS GLIRARLKGA AVSRGQVITF LDAHCECTAG WLEPLLARIK HDRRTVVCPI IDVISDDTFE YMAGSDMTYG GFNWKLNFRW YPVPQREMDR RKGDRTLPVR TPTMAGGLFS IDRDYFQEIG TYDAGMDIWG GENLEISFRI WQCGGTLEIV TCSHVGHVFR KATPYTFPGG TGQIINKNNR RLAEVWMDEF KNFFYIISPG VTKVDYGDIS SRLGLRRKLQ CKPFSWYLEN IYPDSQIPRH YFSLGEIRNV ETNQCLDNMA RKENEKVGIF NCHGMGGNQV FSYTANKEIR TDDLCLDVSK LNGPVTMLKC HHLKGNQLWE YDPVKLTLQH VNSNQCLDKA TEEDSQVPSI RDCTGSRSQQ WLLRNVTLPE IFHHHHHH .
Product Science Overview
Polypeptide N-Acetylgalactosaminyltransferase 1 (ppGaNTase 1) is an enzyme that plays a crucial role in the process of O-glycosylation. This enzyme is responsible for the transfer of N-acetylgalactosamine (GalNAc) from the nucleotide sugar UDP-GalNAc to the hydroxyl groups of serine or threonine residues on polypeptides. This modification is essential for the proper functioning of many proteins, particularly those involved in cell signaling and adhesion.
The enzyme ppGaNTase 1 belongs to a family of glycosyltransferases that initiate mucin-type O-glycosylation. The structure of ppGaNTase 1 includes a catalytic domain that binds to both the donor substrate (UDP-GalNAc) and the acceptor substrate (polypeptide). The enzyme catalyzes the formation of a glycosidic bond between GalNAc and the hydroxyl group of serine or threonine residues .
O-glycosylation is a post-translational modification that affects the stability, localization, and function of proteins. In particular, mucin-type O-glycosylation, initiated by ppGaNTase 1, is critical for the formation of mucins, which are glycoproteins that protect and lubricate the surfaces of epithelial tissues. This modification also plays a role in cell-cell communication and immune response .
The recombinant form of ppGaNTase 1 from mouse is produced using genetic engineering techniques. The gene encoding the enzyme is cloned into an expression vector, which is then introduced into a host cell, such as E. coli or mammalian cells. The host cells produce the enzyme, which is subsequently purified for research or therapeutic use .
Recombinant ppGaNTase 1 is used in various research applications to study the mechanisms of O-glycosylation and its effects on protein function. It is also used in the development of therapeutic strategies for diseases associated with aberrant glycosylation, such as cancer and congenital disorders of glycosylation .
