Recombinant Bacillus licheniformis N-acetylmuramoyl-L-alanine amidase CwlM(cwlM) CSB-EP339780BQT
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Autolysin;Cell wall hydrolase
Species: (Organism)
Bacillus licheniformis
Gene Names:
cwlM
Tag info:
N-terminal 6xHis-SUMO-tagged
Target Protein AA Sequence:
MVKIFIDPGHGGSDTGASANGLQEKQLTLQTALALRNMLLNEYQNVSVLLSRTSDQTVSLTQRTNAANSWGADYFLSIHMNAGGGTGFEDYIYPGVGAPTTTYRDIMHEEILKVVDFRDRGKKTANFHVLRETAMPALLTENGFVDNTNDAEKLKSSAFIQSIARGHANGLARAFNLSKNAAALYKVQIAAFRTKANADSLAAQAEAKGFDALVIYRDSLYKVQIGAFSSKENAEALVQQAKNAEFDTFIYQE
Expression Region:
1-253aa
Subcellular Location:
Secreted
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
43.6 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:
Others
Function:
Hydrolyzes the cell wall of M.luteus more efficiently than that of B.licheniformis and B.subtilis. The C-terminal region, including the repeats, determines substrate specificity.
Involvement in disease:
Relevance:
Hydrolyzes the cell wall of M.luteus more efficiently than that of B.licheniformis and B.subtilis. The C-terminal region, including the repeats, determines substrate specificity.
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:
N-acetylmuramoyl-L-alanine amidase 3 family
Reference:
Genetic structure, isolation and characterization of a Bacillus licheniformis cell wall hydrolase.Kuroda A., Sugimoto Y., Funahashi T., Sekiguchi J.Mol. Gen. Genet. 234:129-137(1992)
