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L1667

Sigma-Aldrich

Lysozyme human

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

Synonym(s):

Lysobac r Lysozyme, Mucopeptide N-acetylmuramoylhydrolase, Muramidase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... LYZ(4069)

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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. Lysozyme is mapped to human chromosome 12q15 and corresponds to a molecular weight of 16.5kDa. It is a positively charged and a C-type lysozyme with α and β structural domains.

Application

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

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. It is a potential anti-inflammatory factor and also has anti-fungal and anti-viral functionality. In inflammatory bowel disease, lysozyme is highly expressed in colonic tissue. Point mutations in lysozyme is implicated in the pathogenesis of hereditary non-neuropathic renal amyloidosis.

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

Packaging

Package size based on protein content

Unit Definition

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.

Legal Information

Lysobac is a trademark of InVitria

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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A novel lysozyme mutation Phe57Ile associated with hereditary renal amyloidosis
Yazaki M, et al.
Kidney International, 63(5), 1652-1657 (2003)
Suppression of human arthritis synovial fibroblasts inflammation using dexamethasone-carbon nanotubes via increasing caveolin-dependent endocytosis and recovering mitochondrial membrane potential
Lee YK, et al.
International journal of nanomedicine, 12(5), 5761-5761 (2017)
Inflammatory bowel disease: an impaired barrier disease
Jager S, et al.
Langenbeck'S Archives of Surgery / Deutsche Gesellschaft Fur Chirurgie, 398(1), 1-12 (2013)
Thermodynamics and binding mechanism of polyphenon-60 with human lysozyme elucidated by calorimetric and spectroscopic techniques
Yasmeen S, et al.
The Journal of Chemical Thermodynamics, 110(5), 79-86 (2017)
Huahua He et al.
Frontiers in bioengineering and biotechnology, 8, 118-118 (2020-03-27)
Human lysozyme (hLYZ), known for its bacteriolytic activity, is widely applied in the food and pharmaceutical industries as an antimicrobial agent. However, its extensive application was limited by its low large-scale production efficiency. In this study, a combinational method of

Protocols

This enzymatic rate determination may be used for Lysozyme products. It is not to be used to assay recombinant or insoluble Lysozyme on agarose.

This enzymatic rate determination may be used for Lysozyme products. It is not to be used to assay recombinant or insoluble Lysozyme on agarose.

This enzymatic rate determination may be used for Lysozyme products. It is not to be used to assay recombinant or insoluble Lysozyme on agarose.

This enzymatic rate determination may be used for Lysozyme products. It is not to be used to assay recombinant or insoluble Lysozyme on agarose.

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