L1667

Lysozyme human

Lysobac^™, recombinant, expressed in rice, lyophilized powder, ≥100,000 units/mg protein

• Sinónimos: Lysobac^™ r Lysozyme, Mucopeptide N-acetylmuramoylhydrolase, Muramidase
• Número CAS: 12671-19-1
• UNSPSC Code: 12352204
• NACRES: NA.54
• Número CE: 3.2.1.17 (BRENDA, IUBMB)
• MDL number: MFCD00131557

Propiedades

• Nombre del producto: Lysozyme human, Lysobac^™, recombinant, expressed in rice, lyophilized powder, ≥100,000 units/mg protein
• biological source: human
• recombinant: expressed in rice
• assay: ≥90% (SDS-PAGE)
• form: lyophilized powder
• specific activity: ≥100,000 units/mg protein
• mol wt: 16.5 kDa
• technique(s): cell based assay: suitable
• suitability: suitable for cell lysis
• UniProt accession no.: P61626
• application(s): cell analysis
• shipped in: dry ice
• storage temp.: −70°C
• Quality Level: 200
• Gene Information: human ... LYZ(4069)

Descripción

Application

Lysozyme human has been used:

• in the interaction studies with polyphenon-60 by calorimetric and spectroscopic techniques[1]
• in the drug release assay of dexamethasone (DEX) - carbon nanotube based delivery system[2]
• in the surface plasmon resonance (SPR) for measuring its interaction with human angiotensin I-converting enzyme (ACE)[3]

Biochem/physiol Actions

Lysozyme is an antibacterial enzyme, which acts on the peptidoglycan layer at the on the N-acetylgluosamine (NAG) and N-acetylmuramic acid linkage, resulting in the lysis of microbial cells.[4] It is a potential anti-inflammatory factor and also has anti-fungal and anti-viral functionality.[5] In inflammatory bowel disease, lysozyme is highly expressed in colonic tissue.[6] Point mutations in lysozyme is implicated in the pathogenesis of hereditary non-neuropathic renal amyloidosis.[7]

Features and Benefits

Lysobac^™ is a breakthrough for bacterial cell lysis and can be used in diagnostic applications, bioprocessing and life science research. It is recombinant human lysozyme produced in an animal-free production system. Animal-free production eliminates the safety risk and inconsistent lot-to-lot performance of hen egg white lysozyme. Lysobac^™ has significantly higher bioactivity than hen egg white lysozyme. One gram replaces 4 grams of hen egg white lysozyme. It also delivers gentle cell lysis, unlike mechanical lysis which can cause protein shear and reduce protein yields by up to 20%.
Advantages:

• Improves Bacterial Fermentation Efficiency
• Greater bacterial lysis activity per mg.
• 1 gram of delivers more lysis activity than 4 grams of HEWL
• Animal-free and consistent leading to improved regulatory efficiency for drug manufacturing
• Improved recombinant protein yield compared to mechanical lysis
• Reduces cost of goods

General description

Lysozyme is present in tears, saliva and human milk. The human lysozyme expressed in rice grains is an excellent supplemental source of this antimicrobial protein.[4] Lysozyme is mapped to human chromosome 12q15 and corresponds to a molecular weight of 16.5kDa.[6] It is a positively charged and a C-type lysozyme[5] with α and β structural domains.[7]

Legal Information

rhLysozyme manufactured in the USA by InVitria.

Lysobac is a trademark of InVitria

Other Notes

One unit will lyse 0.6 μg of Micrococcus lysodeikticus per minute by turbidimetric detection at 600 nm when suspended in buffer at pH 6.2 at 25 °C.

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Packaging

Package size based on protein content

Información de seguridad

• Clase de almacenamiento: 11 - Combustible Solids
• wgk: WGK 3
• flash_point_f: Not applicable
• flash_point_c: Not applicable