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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

Synonym(s):

Glycyl-glycine Endopeptidase

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About This Item

CAS Number:
9011-93-2
Enzyme Commission number:
3.4.24.75 (BRENDA, IUBMB)
MDL number:
MFCD00131556
UNSPSC Code:
12352204
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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
A P Desbois et al.
European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology, 30(8), 1015-1021 (2011-02-12)
Drug-resistant staphylococci constitute a serious problem that urgently requires the discovery of new therapeutic agents. There has been a resurgence in interest in using lysostaphin (a specific anti-staphylococcal enzyme) as a treatment for infections caused by these important pathogens. However
Martin Bjerregård Pedersen et al.
Journal of immunology (Baltimore, Md. : 1950), 184(4), 1931-1945 (2010-01-08)
The binding of Abs to microbial surfaces followed by complement activation constitutes an important line of defense against infections. In this study, we have investigated the relationship between complement activation and the binding of human IgM Abs to surfaces with
M Fenton et al.
Journal of applied microbiology, 111(4), 1025-1035 (2011-08-05)
To develop an efficient purification strategy for the bacteriophage lysin CHAP(K) . To evaluate its antibacterial spectrum(,) enzymatic properties, optimal reaction conditions and lytic activity against live Staphlyococcus aureus. Recombinant CHAP(K) was purified to homogeneity by cation exchange chromatography, with
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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