L4402
Lysostaphin from Staphylococcus staphylolyticus
BioUltra, ≥97% (SDS-PAGE), Protein 40-60 % by biuret, ≥2,000 units/mg protein
Synonym(s):
Glycyl-glycine Endopeptidase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
biological source
bacterial (Staphylococcus sp.)
Quality Level
product line
BioUltra
Assay
≥97% (SDS-PAGE)
form
lyophilized powder
specific activity
≥2,000 units/mg protein
mol wt
25 kDa
composition
Protein, 40-60% biuret
concentration
40—60% protein
technique(s)
cell based assay: suitable
suitability
suitable for cell lysis
antibiotic activity spectrum
Gram-positive bacteria
application(s)
diagnostic assay manufacturing
Mode of action
cell wall synthesis | interferes
storage temp.
−20°C
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General description
Chemical structure: peptide
Package size based on protein content
Biochem/physiol Actions
Lysostaphin is a zinc endopeptidase with a molecular weight of approximately 25 kDa. Because lysostaphin cleaves the polyglycine cross-links in the peptidoglycan layer of the cell wall of Staphylococcus species it has been found useful for cell lysis and also as a potential anti-microbial therapeutic.
pH Optimum for activity: ~7.5
pH Optimum for activity: ~7.5
Physical form
Contains potassium phosphate buffer salts and sodium chloride
Preparation Note
Affinity purified
Other Notes
One unit will reduce the turbidity (A620) of a suspension of Staphylococcus aureus cells from 0.250 to 0.125 in 10 min at pH 7.5 at 37 °C in a 6.0 ml reaction mixture.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Johnny Gutierrez et al.
Open forum infectious diseases, 6(4), ofz090-ofz090 (2019-04-27)
Staphylococcus aureus (SA) bacteremia often requires a long treatment duration with antibiotics to prevent relapse due to the ability of SA to establish reservoirs of infection in sites such as heart and bone. These metastatic sites of infection cannot be
Thomas S Lawson et al.
Journal of clinical laboratory analysis, 25(5), 359-365 (2011-09-16)
Aspects of the fluorescence in situ hybridization (FISH) method for the detection of clinically important bacteria, such as Staphylococcus aureus, Staphylococcus epidermidis, and Escherichia coli, were investigated for optimization. Various approaches to optimizing the FISH procedure were taken and different
Igor Belyansky et al.
The American surgeon, 77(8), 1025-1031 (2011-09-29)
Mesh and wound infections during hernia repair are predominantly caused by Staphylococcus aureus. Human acellular dermis (HAD) is known to lose its integrity in the face of large bacterial loads. The goal of this study was to determine if lysostaphin
Shaw R Gargis et al.
Applied and environmental microbiology, 76(20), 6944-6946 (2010-08-24)
Resistance to lysostaphin, a staphylolytic glycylglycine endopeptidase, is due to a FemABX-like immunity protein that inserts serines in place of some glycines in peptidoglycan cross bridges. These modifications inhibit both binding of the recombinant cell wall targeting domain and catalysis
Yuliya Yurko et al.
Surgical innovation, 19(1), 20-26 (2011-07-12)
Naturally occurring antimicrobial peptides are possibly the "next frontier" in infection prevention. Binding them to mesh could reduce the rate of mesh infections. This study identifies an antimicrobial agent capable of significant antibacterial activity when bound to mesh. Lysozyme, human
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