| Catalog# |
CI91 |
| Source |
Human cells |
| Description |
Recombinant Human LYZ is produced by our mammalian expression system in human cells. The target protein is expressed with sequence (Lys19-Val148) of Human LYZ fused with a polyhistidine tag at the C-terminus. |
| Names |
Lysozyme C，1,4-beta-N-acetylmuramidase C，LYZ，LZM |
| Accession # |
P61626 |
| Formulation |
Supplied as a 0.2 μM filtered solution of 20mM TrisHCl, 150mM NaCl,10% Glycerol,pH7.5 |
| Shipping |
The product is shipped on dry ice/ice packs. |
| Storage |
Store at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles. |
| Purity |
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. |
| Endotoxin |
Less than 0.1 ng/µg (1 IEU/µg). |
| Amino Acid Sequence |
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWC NDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV VDHHHHHH
|
| Background |
lysozyme C is a secreted protein and belongs to the glycosyl hydrolase 22 family. Lysozymes have primarily a bacteriolytic function, damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides. |
