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L4402

Sigma-Aldrich

Lysostaphin from Staphylococcus staphylolyticus

BioUltra, ≥97% (SDS-PAGE), Protein 40-60 % by biuret, ≥2,000 units/mg protein

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Synonym(s):
Glycyl-glycine Endopeptidase
CAS Number:
9011-93-2
Enzyme Commission number:
3.4.24.75 (BRENDA, IUBMB)
MDL number:
MFCD00131556
NACRES:
NA.54

biological source

bacterial (Staphylococcus sp.)

Quality Level

300

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

Unit Definition

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.

Physical form

Contains potassium phosphate buffer salts and sodium chloride

Preparation Note

Affinity purified

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

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
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
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
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
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