Recombinant Human Lysozyme C (LYZ) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04252P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Lysozyme C (LYZ) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04252P
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Product Overview

Description Recombinant Human Lysozyme C (LYZ) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P61626
Target Symbol LYZ
Synonyms 1 4 beta N acetylmuramidase C; 1; 4-beta-N-acetylmuramidase C; EC 3.2.1.17; LYSC_HUMAN; Lysosyme; Lysozyme (renal amyloidosis); Lysozyme C; Lysozyme C precursor; LYZ; LZM; Renal amyloidosis
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
Expression Range 19-148aa
Protein Length Full Length of Mature Protein
Mol. Weight 30.7kDa
Research Area Tags & Cell Markers
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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
  • FAQs

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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.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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