- Remove All
- Your shopping cart is currently empty
LYG1 (Lysozyme G1) is a Protein Coding gene. It belongs to the glycosyl hydrolase 23 family. Glycoside hydrolases are a widespread group of enzymes that hydrolyze the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. LYG1 exhibits hydrolase activity, acting on glycosyl bonds (inferred); lysozyme activity (inferred). It is found in the extracellular region and may function in the cell wall macromolecule catabolic process, metabolic process, and peptidoglycan catabolic process. The lysozyme G gene structure has been largely conserved during vertebrate evolution, except at the 5' end of the gene, which varies in some exons.
Pack Size | Price | Availability | Quantity |
---|---|---|---|
100 μg | $700 | 7-10 days |
Biological Activity | Activity testing is in progress. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
Description | LYG1 (Lysozyme G1) is a Protein Coding gene. It belongs to the glycosyl hydrolase 23 family. Glycoside hydrolases are a widespread group of enzymes that hydrolyze the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. LYG1 exhibits hydrolase activity, acting on glycosyl bonds (inferred); lysozyme activity (inferred). It is found in the extracellular region and may function in the cell wall macromolecule catabolic process, metabolic process, and peptidoglycan catabolic process. The lysozyme G gene structure has been largely conserved during vertebrate evolution, except at the 5' end of the gene, which varies in some exons. |
Species | Human |
Expression System | Baculovirus Insect Cells |
Tag | C-His |
Accession Number | Q8N1E2 |
Synonyms | SALW1939,lysozyme G-like 1 |
Construction | A DNA sequence encoding the human LYG1 (Met 1-Phe194) (Q8N1E2) was expressed, with a C-terminal polyhistidine tag. Predicted N terminal: Ser 2 |
Protein Purity | > 90 % as determined by SDS-PAGE |
Molecular Weight | 20.82 kDa (predicted); 22 kDa (reducing condition, due to glycosylation) |
Endotoxin | < 1.0 EU/μg of the protein as determined by the LAL method. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM Tris, 500 mM NaCl, pH 7.4, 20% gly. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization. |
Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
Stability & Storage | It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping | In general, Lyophilized powders are shipping with blue ice. |
Research Background | LYG1 (Lysozyme G1) is a Protein Coding gene. It belongs to the glycosyl hydrolase 23 family. Glycoside hydrolases are a widespread group of enzymes that hydrolyze the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. LYG1 exhibits hydrolase activity, acting on glycosyl bonds (inferred); lysozyme activity (inferred). It is found in the extracellular region and may function in the cell wall macromolecule catabolic process, metabolic process, and peptidoglycan catabolic process. The lysozyme G gene structure has been largely conserved during vertebrate evolution, except at the 5' end of the gene, which varies in some exons. |
Copyright © 2015-2024 TargetMol Chemicals Inc. All Rights Reserved.