The purity of this product is reported as the total protein content as determined by UV absorbance. The minimum protein content is 95% (on an anhydrous basis), with the remaining 5–10% consists buffer salts such as sodium acetate and sodium chloride. Minor trace impurities may include residual proteins such as ovalbumin. Electrophoretic analysis shows lysozyme as the predominant protein, indicating relatively high purity. A quantitative purity value is not available.
Fortfahren mit
L6876
Lysozym aus Hühnereiweiss
powder or granules, ≥39,000 units/mg protein
Synonym(e):
Mucopeptid-N-Acetylmuramoylhydrolase, Muramidase
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| Ihnen/SKU | Verfügbarkeit | Preis |
|---|---|---|
1 g | Warenkorb auf Verfügbarkeit prüfen | CHF 80.80 |
5 g | Warenkorb auf Verfügbarkeit prüfen | CHF 287.00 |
10 g | Warenkorb auf Verfügbarkeit prüfen | CHF 323.00 |
25 g | Warenkorb auf Verfügbarkeit prüfen | CHF 1'180.00 |
100 g | Warenkorb auf Verfügbarkeit prüfen | CHF 4'420.00 |
Über diesen Artikel
CAS-Nummer:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
235-747-3
MDL number:
Specific activity:
≥39,000 units/mg protein
Biological source:
chicken egg white
Technischer Dienst
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Unterstützung erhaltenbiological source
chicken egg white
Quality Segment
form
powder or granules
specific activity
≥39,000 units/mg protein
mol wt
single-chain 14.3 kDa
technique(s)
cell based assay: suitable
input
bacteria and yeast sample(s)
suitability
suitable for cell lysis
UniProt accession no.
application(s)
cell analysis
storage temp.
room temp
Gene Information
chicken ... LYZ(396218)
Application
Lysozym aus Hühnereiweiß wird für die Extraktion von genomischer DNA aus Bakterienzellen eingesetzt.[1] Es wird als externer Standard für die MALDI-TOF (Matrix-Assistierter Laser-Desorption-Ionisierung-Flugzeitmassenspektrometer)-Massenanalyse eingesetzt.
Enzym bricht die Zellwände von Bakterien, wird verwendet um Sphäroplasten vorzubereiten.
Biochem/physiol Actions
Lysozym hydrolysiert β(1→4)-Bindungen zwischen N-Acetylmuraminsäure und N-Acetyl-D -Glucosamin-Resten in Peptidoglycan und zwischen N-Acetyl-D -Glucosamin-Resten in Chitodextrin. Gram-positive Zellen sind sehr anfällig für diese Hydrolyse, da ihre Zellwände einen hohen Peptidoglycan-Anteil haben.
Lysozym hydrolysiert β(1→4)-Bindungen zwischen N-Acetylmuraminsäure und N-Acetyl-D -Glucosamin-Resten in Peptidoglycan und zwischen N-Acetyl-D -Glucosamin-Resten in Chitodextrin. Gram-positive Zellen sind sehr anfällig für diese Hydrolyse, da ihre Zellwände einen hohen Peptidoglycan-Anteil haben. Gram-negative Bakterien sind auf Grund einer äußeren Membran und eines geringeren Peptidoglycan-Anteils weniger anfällig. Allerdings können diese Zellen in Gegenwart von EDTA, welches Chelate mit Metallionen in der äußeren bakteriellen Membran bildet, hydrolysiert werden.
Das Enzym ist über einen breiten pH-Bereich aktiv (6.0 bis 9.0). Bei pH 6.2 wird eine maximale Aktivität über einen größeren Ionenstärken-Bereich (0.02 bis 0.100 M), verglichen mit pH 9,2 (0.01 bis 0.06 M), beobachtet.
Das Enzym ist über einen breiten pH-Bereich aktiv (6.0 bis 9.0). Bei pH 6.2 wird eine maximale Aktivität über einen größeren Ionenstärken-Bereich (0.02 bis 0.100 M), verglichen mit pH 9,2 (0.01 bis 0.06 M), beobachtet.
Features and Benefits
Lysozym aus Hühnereiweiß ist ein vielseitiges Enzym mit einzigartigen Eigenschaften, die es wirksam für zahlreiche Anwendungen machen, einschließlich Aufbrechen der Bakterienzellwand, genomische DNA-Extraktion und externer Standard für die Massenanalyse. Es ist zuverlässig, in einem breiten pH-Wertbereich aktiv und in zahlreichen Packungsgrößen erhältlich.
Other Notes
Eine Einheit lysiert 0,6 μg Micrococcus lysodeikticus pro Minute durch turbidimetrischen Nachweis bei 600 nm, wenn sie in Puffer bei 25 °C und pH 6,2 suspendiert wird.
Weitere Informationen über Enzyme für die Analyse komplexer Kohlenhydrate finden Sie unter www.sigma-aldrich.com/enzymeexplorer
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Dieser Artikel | |||
|---|---|---|---|
| description powder or granules, ≥39,000 units/mg protein | description powder (crystalline), 70000-140000 U/mg | description 10 mg/mL | description aseptically filled |
| technique(s) cell based assay: suitable | technique(s) cell based assay: suitable | technique(s) cell based assay: suitable | technique(s) - |
| Gene Information chicken ... LYZ(396218) | Gene Information chicken ... LYZ(396218) | Gene Information chicken ... LYZ(396218) | Gene Information chicken ... LYZ(396218) |
| specific activity ≥39,000 units/mg protein | specific activity 70000-140000 U/mg | specific activity - | specific activity - |
| biological source chicken egg white | biological source chicken egg white | biological source chicken egg white | biological source - |
| application(s) cell analysis | application(s) cell analysis | application(s) cell analysis | application(s) - |
| form powder or granules | form powder (crystalline) | form liquid | form powder |
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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Lagerklasse
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Would it be possible to confirm the purity of this product? I am interested in this rather than it's enzymic activity and can't find this information. Thank you
1 answer-
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We previously stored lysozyme at -20 °C, as indicated in the previous product information sheet. Should the product now be stored at room temperature instead? How long can it be stored when resuspended and keptat -20°?
1 answer-
In powder form, this product may be stored at room temperature. Prepared solutions are stable for at least 1 month at 2-8 °C. The solution stability when stored at -20 °C has not been investigaed. However, product L3790, a 10 mg/mL Lysozym solution in 25 mM sodium acetate pH 4.5 with 50% glycerol, is stable for at least 1 year at -20 °C. Please see the links below to review additional information available in the product datasheet of each product.
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We typically store our lyophilized lysozyme at -20C, but one recent order (shipped at room temperature) was left at room temperature, sealed, for several weeks. Will it still be active?
1 answer-
This product is stored and shipped at ambient temperature. In the powder form, this material is quite robust and does not require controlled temperature storage. This item is stable at room temperature until the lot specific expiration date.
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I have ordered this product and stored in -70 degree C. But there is no dilution preparation method available here. Can you please tell me hot to prepare that.
1 answer-
This product may be prepared in 10 mM Tris-HCl, pH 8.0 at 10 mg/mL. The material is also soluble in water at 10 mg/mL. Aqueous solutions are stable for at least one month when stored at 2-8 °C. Please see the link below to review additional information available in the product datasheet:
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/938/215/l6876dat-ms.pdfHelpful?
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What's the best buffer and pH for the preparation of lysozyme stock solution, and can I incubate it at room temperature for 1 day?
1 answer-
This product can be resuspended in 350 µL of STET buffer (10 mM Tris-HCl, pH 8.0, with 0.1 M NaCl,
1 mM EDTA, and 5% [w/v] TRITON® X-100). The enzyme is active over a broad pH range (6.0 to 9.0). At pH 6.2, maximal activity is observed over a wider range of ionic strengths (0.02 to 0.100 M) than at pH 9.2 (0.01 to 0.06 M).During this assay, the end-user should Incubate E. coli (strain ATCC 37017) bearing the pBR322 plasmid overnight in Terrific Broth (Cat. No. T0918) with 25 µg/mL tetracycline (Cat. No. T3383) and 25 µg/mL ampicillin (Cat. No. A9518). The
optimal pH for E. coli cell lysis is 8.0 ± 0.1.16For more information please read through the product data sheet: https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/938/215/l6876dat-ms.pdf
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What is the amino acid sequence of Product L6876, Lysozyme from chicken egg white?
1 answer-
Lysozyme is a single chain polypeptide of 129 amino acids. The amino acid sequence of chicken egg white Lysozyme is described in the Journal of Biological Chemistry, 238, 2698-2707 (1963).
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Under what conditions can Product L6876, Lysozyme from chicken egg white, be used to lyse E. coli?
1 answer-
The following procedure is for the lysis of E. coli. It may be used as a guideline for other species.1. Incubate E. coli (strain ATCC 37017) bearing the pBR322 plasmid overnight in Terrific Broth (Product No. T 0918) with 25 μg/ml tetracycline (Product No T 3383) and 25 μg/ml ampicillin (Product No. A 9518).2. Centrifuge 1-2 ml samples of the overnight culture.3. Resuspend the pellets in 350 μl of STET buffer (10 mM Tris-HCl, pH 8.0, with 0.1 M NaCl, 1 mM EDTA, and 5% [w/v] TRITON® X-100).4. Add 25 μl of a freshly prepared lysozyme solution (500,000 units/ml in 10 mM Tris-HCl, pH 8.0).5. Mix by vortexing for 3 seconds.6. Incubate the lysis mixture for 30 minutes at 37 °C7. After incubation, place the tube containing the lysis mixture in a boiling water bath for exactly 40 seconds.8. Centrifuge the lysis mixture at 14,000 x g.9. Remove the pellet (cell debris) from the tube using a sterile toothpick.10. Plasmid DNA from the supernatant may then be purified and analyzed.
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How can Product L6876, Lysozyme from chicken egg white, be reconstituted and can stock solutions be prepared?
1 answer-
For the lysis procedure, use a freshly prepared solution of 500,000 units/ml in 10 mM Tris-HCl, pH 8.0. The product is also soluble in water (10 mg/ml) yielding a clear to slightly hazy colorless solution. Aqueous solutions should be stable for at least one month when stored between 2-8 °C.
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What is the Department of Transportation shipping information for this product?
1 answer-
Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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Can Product L6876, Lysozyme from chicken egg white, be inactivated by heat?
1 answer-
Solutions of Lysozyme may be inactivated by boiling for 40 seconds at 100°C at an alkaline pH.
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