Recombinant Human Lysozyme C Protein (C-6His)

Name: Recombinant Human Lysozyme C Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1607NP
Availability: InStock

BL-1607NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Lysozyme C is produced by our Mammalian expression system and the target gene encoding Lys19-Val148 is expressed with a 6His tag at the C-terminus.
Accession	P61626
Synonym	Lysozyme C;1;4-beta-N-acetylmuramidase C;LYZ;LZM
Gene Background	lysozyme C is a secreted protein and belongs to the glycosyl hydrolase 22 family. Lysozymes have primarily a bacteriolytic function, damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.
Molecular Mass	15.7 KDa
Apmol Mass	15 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 10% Glycerol, pH 7.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Subcellular Location	Secreted.
Protein Families	Glycosyl hydrolase 22 family
Database References	HGNC: 6740 OMIM: 105200 KEGG: hsa:4069 STRING: 9606.ENSP00000261267 UniGene: Hs.524579
Associated Diseases	Amyloidosis 8 (AMYL8)

Gene Functions References

The findings suggest that the F57I mutation affects the aggregation process of lysozyme resulting in the formation of cytotoxic species and that SAP is able to prevent cell death in the F57I flies by preventing accumulation of toxic F57I structures. PMID: 27428539
the location of specific mutations is an important factor in determining the native-state dynamical properties of human lysozyme PMID: 27926837
rhamnolipid (RL) secreted by Pseudomonas aeruginosa (PA) accelerates proteolysis of lysozyme. PMID: 27931094
Data show increased levels of lysozyme C (LYZ), lacritin (LACRT) and zinc-alpha-2 glycoprotein 1 (AZGP1) in pooled tear fluid sample from Graves' disease (GD) patients with moderate-to-severe Graves' orbitopathy (GO) compared with GD patients without clinical signs of GO. PMID: 28419103
lysozyme cannot be used as a marker of acinar differentiation in salivary tumors. However, lysozyme expression can be helpful to distinguish mammary analog secretory carcinoma from acinic cell carcinoma PMID: 27177644
The preliminary results from the milk yield and milk compositions from a naturally lactating transgenic cloned cow 0906 were also tested. These results provide a solid foundation for the large-scale production of rhLZ in the future. PMID: 26961596
The purpose of this study is to understand the oral mucosal immune status of cancer patients and to make clear whether antibacterial proteins such as salivary secretory immunoglobulin (SIgA) and lysozyme in saliva were influenced by patients' health status and certain medical treatment therapy. PMID: 27294141
Data show that hen lysozyme aggregates faster than the human lysozyme. PMID: 27825804
Data show that transgenic hens with stable expression of recombinant human lysozyme proteins can be created by microinjection of lentiviral vectors. PMID: 25706123
The determination of the structure of a low-population intermediate in the product release process by human lysozyme, is reported. PMID: 25575179
Accumulation of pathogenic lysozymes in the endoplasmic reticulum caused ER stress and the unfolded protein response mainly via the IRE1alpha pathway. PMID: 25659958
Hereditary amyloidosis associated with the p.Trp82Arg lysozyme variant in this new family is predominantly associated with mild upper gastrointestinal tract involvement and in some cases with inflammatory bowel disease. PMID: 25217048
Both mRNA and protein levels of lysozyme were significantly higher in patients with biofilm associated chronic rhinosinusitis (CRS) than those with CRS and no biofilm and controls. PMID: 24121782
Lzm-S can deposit in the systemic vasculature and kidneys in SS, where this deposition could lead to acute organ dysfunction. PMID: 24296430
Lysozyme functions as an antimicrobial peptide, with antibacterial activity. PMID: 16416029
the protective action of lysozyme on the nephrotoxic effects of advanced glycation end products depend on ability to prevent the production and release of inflammatory mediators, such as IL-6 and to reduce macrophage recruitment in the inflammatory sites. PMID: 24495950
Data suggest that the invariant loop of PliC (periplasmic inhibitor of c-type lysozyme) from Brucella abortus plays crucial role in inhibition of human c-type lysozyme via its insertion into the active site cleft of lysozyme. PMID: 24308818
The purpose of this study was to evaluate the effect of chronic alcohol intoxication and smoking on the concentration and output of salivary lysozyme. PMID: 23264227
When Lzm-S was located in close proximity to vascular smooth muscle cells, it could generate H(2)O(2) to produce lengthening in a human cell culture preparation. PMID: 22096116
We observed that expressing the destabilized F57I and D67H lysozymes triggers unfolded protein response activation, resulting in degradation of these variants. PMID: 21965601
increased production of the antibacterial enzyme lysozyme was found in collagenous colitis and lymphocytic colitis PMID: 21460390
The degree of residual structure of lysozyme correlates with the ability of the protein to form amyloid fibrils. PMID: 21574221
Lysozyme is up-regulated in Barrett's mucosa PMID: 21486364
There was no difference in the concentration of lysozyme in children with dental caries than that in controls. PMID: 19563039
Raised plasma lysozyme levels may be a useful biomarker of atherosclerotic cardiovascular disease and response to therapy. PMID: 20167661
a residue at the N-terminal of lysozyme is required for hydrogen bond networks with ordered water molecules and stabilization of the protein. PMID: 10561612
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme PMID: 11887182
Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. PMID: 11927576
Streptococcal inhibitor of complement inhibits two additional components of the mucosal innate immune system: secretory leukocyte proteinase inhibitor and lysozyme. PMID: 12183536
Detailed comparison between the 35 degree C and 4 degree C structures of lysozyme revealed for the first time that an active site lobe has a structural ability to obstruct the polysaccharide-binding cleft only by temperature lowering without a substrate. PMID: 12564923
Structural and folding dynamic properties of human lysozyme T70N variant PMID: 12709420
promyelocytic leukemia protein, but not Sp100, induced the accumulation of MEF in PML nuclear bodies and MEF and PML physically interacted, stimulating MEF transcriptional activity, resulting in the up-regulation of endogenous lysozyme expression. PMID: 14976184
Hydrostatic pressure (3.5 kbar at 57 degrees C, pH 7.4) was used to make amyloidogenic states of WT & variant(Ile56Thr & Asp67His) lysozymes by inducing a conformational state of lysozyme that aggregates readily upon decompression. PMID: 15155566
amyloidogenic variants, I56T and D67H, show a specific, partly unfolded intermediate state under physiologically relevant conditions PMID: 15713462
the ensemble of reduced denatured conformers initially collapses into a large number of unstructured intermediates with one or two disulphide bonds, the majority of which then fold to form the native-like three-disulphide intermediate, des-[77-95] PMID: 16023673
Data suggest that partial unfolding is an intrinsic property of the human lysozyme structure, and suggest that the readiness with which it occurs is a critical feature determining whether or not amyloid deposition occurs in vivo. PMID: 16126226
A novel form of systemic ALys amyloidosis, caused by compound heterozygosity in exon 2 (p.T70N) and exon 4 (p.W112R) of the lysozyme gene (LYZ), with both mutations being present on the same allele. PMID: 16329101
findings indicate that a complex interplay between reduced native-state stability, lower secretion levels, and protein aggregation propensity influences the types of mutation that give rise to familial forms of amyloid disease PMID: 16441658
report a case of hepatic rupture secondary to hereditary lysozyme amyloidosis that was successfully treated by liver transplantation PMID: 16799949
The distortion of the hydrophobic core at the alpha- and beta-interface putatively results in the formation of the initial "seed" for amyloid fibril. PMID: 17054380
The structure of the synthetic human lysozyme was confirmed by high-resolution x-ray diffraction, giving the highest-resolution structure (1.04 A) observed to date for this enzyme. PMID: 17360367
Clusterin, and perhaps other extracellular chaperones, could have a key role in curtailing the potentially pathogenic effects of the misfolding and aggregation of proteins that, like lysozyme, are secreted into the extracellular environment. PMID: 17407782
Thus, we provide a novel strategy for engineering the active site of enzymes. PMID: 17524359
The influence of mutant signal peptides on enzymatic activity of lysozyme at high pH or ionic strength were studied. PMID: 18029788
short-duration, high-intensity exercise increases the secretion rate of salivary Lysozyme despite no change in the saliva flow rate. PMID: 18344136
High salivary lysozyme levels are associated with the odds of hypertension. PMID: 18434581
Lysozyme activity in crevicular fluid and in unstimulated saliva correlated with periodontal pocket depth in donors and in patients with gingivitis or periodontitis. PMID: 19179970

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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