Recombinant Lophura leucomelanos Lysozyme C(LYZ) CSB-EP013283LIQ
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
1,4-beta-N-acetylmuramidase
Species: (Organism)
Lophura leucomelanos (Kalij pheasant)
Gene Names:
LYZ
Tag info:
N-terminal 6xHis-SUMO-tagged
Target Protein AA Sequence:
KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKYESNFNTHATNRNTDGSTDYGILQINSRWWCNDGKTPGSRNLCHIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVSVWTRGCRL
Expression Region:
1-129aa
Subcellular Location:
Secreted
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
30.3 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Immunology
Function:
Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Involvement in disease:
Relevance:
Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. 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.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Glycosyl hydrolase 22 family
Reference:
"The amino acid sequence of lysozyme from kalij pheasant (Lophura leucomelana) egg-white."Araki T., Kudo K., Kuramoto M., Torikata T.Agric. Biol. Chem. 55:1701-1706(1991)
