Biotinylated Recombinant Chicken Lysozyme C (LYZ) Protein (MBP&His-Avi)

Name: Biotinylated Recombinant Chicken Lysozyme C (LYZ) Protein (MBP&His-Avi)
Brand: Beta LifeScience
SKU: BLC-06373P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Avi-tagged proteins, Biotinylated proteins, Featured biotinylated protein molecules, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Biotinylated Recombinant Chicken Lysozyme C (LYZ) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P00698
Target Symbol	LYZ
Species	Gallus gallus (Chicken)
Expression System	E.coli
Tag	N-MBP&C-6His-Avi
Target Protein Sequence	KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
Expression Range	19-147aa
Protein Length	Full Length of Mature Protein
Mol. Weight	62.1 kDa
Research Area	Cardiovascular
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. Has bacteriolytic activity against M.luteus.
Subcellular Location	Secreted.
Protein Families	Glycosyl hydrolase 22 family
Database References	KEGG: gga:396218 STRING: 9031.ENSGALP00000016177 UniGene: Gga.713
Tissue Specificity	In the egg white and polymorphonuclear leukocytes.

Gene Functions References

NG and NR inhibited the enzymatic activity of Hen Egg White Lysozyme (HEWL) and exhibited their affinity for the active site of HEWL. PMID: 29145059
Molecular docking results suggested the location of vandetanib (VDB) binding site near the LYZ active site while molecular dynamics simulation results suggested stability of VDB-LYZ complex. PMID: 28843881
Specific structural changes constitute the first steps in lysozyme unfolding by urea. PMID: 27573790
Molecular dynamics (MD) simulation results demonstrate that the "hard protein" lysozyme retains much of its secondary structure during adsorption, whereas BSA loses it almost completely. BSA has a considerably larger adsorption energy compared to that of lysozyme, which does not scale with chain length. Desorption simulations are carried out using classical steered MD. PMID: 27421144
The ability of an anion to slow down the water dynamics around lysozyme was found to have the following order: SCN- > Cl- > H2PO4- > NO3- approximately SO42-. This result indicates that the effects of anions on the dynamics of water around the lysozyme molecule are the opposite of those for bulk water. PMID: 27193313
Protein microcrystals magnetically aligned in D2O hydrogels were subjected to neutron diffraction measurements, and reflections were observed for the first time to a resolution of 3.4 A from lysozyme microcrystals ( approximately 10 x 10 x 50 microm). PMID: 27377379
Here, a single nanocrystal with a diffracting volume of only 0.14 microm(3), i.e. no more than 6 x 10(5) unit cells, provided sufficient information to determine the structure of a rare dimeric polymorph of hen egg-white lysozyme by electron crystallography. PMID: 28876237
Solutions of lysozyme in heavy water were studied by small-angle neutron scattering at concentrations of 40, 20 and 10 mg ml(-1) with and without the addition of precipitant, and at temperatures of 10, 20 and 30 degrees C. In addition to the expected protein monomers, dimeric and octameric species were identified in solutions at the maximum concentration and close to the optimal conditions for crystallization. PMID: 28695859
The enzyme activity of LYZ was inhibited by the addition of copper with catalytic residues Glu 35 and Asp 52 locating at the binding sites. This study helps to elucidate the molecular mechanism of the interaction between copper and lysozyme and provides reference for toxicological studies of copper. PMID: 27089183
At neutral pH, lysozyme retains its native conformation between 0 and 8 M urea over the entire range of temperatures studied. PMID: 27933780
Data show that hen lysozyme aggregates faster than the human lysozyme. PMID: 27825804
Different C-type lysozyme gene haplotypes are associated with egg hatchability and survival in Rhode Island Red layer chickens PMID: 27478034
Drospirenone had different effects on the local conformation of HSA and LYZ molecules. PMID: 26448295
At micro-second and coarser temporal resolutions, free energy landscape of hen egg white lysozyme exhibits hub-like topology with crystal structures occupying the dominant structural ensemble. PMID: 26057625
Data indicate that lysozyme significantly enhances the dewaterability of biosludge. PMID: 25462773
Data show that copper(II) inhibits self-association of hen egg white lysozyme (HEWL) at pH 12.75 both at 37 and 65 degrees C. PMID: 24806136
Under high pressure, the crystal structure of the enzyme undergoes several local and global changes accompanied by changes in hydration structure. PMID: 25849385
Structure of hen egg-white lysozyme determined from single shots of trapped microcrystals. PMID: 25849403
Egg white-lysozyme protein structure and stability revealed by X-ray crystallography. PMID: 25521080
Underdamped delocalized vibrational modes in the terahertz frequency domain are identified and shown to blue-shift and strengthen upon LYZ-triacetylchitotriose binding. PMID: 24893252
Data suggest that stabilization of lysozyme by mono- and oligo-saccharides can be accounted for by simplified statistical-thermodynamic model considering volume exclusion deriving from steric repulsion between enzyme and saccharides. PMID: 26000826
These results show that pressure suppresses protein nucleation, aggregation, and finally crystallization in supersaturated condensed lysozyme solutions. PMID: 25494777
The study explores fingerprinting the tertiary structure of electroadsorbed lysozyme at soft interfaces by electrostatic spray ionization ma.ss spectrometry PMID: 25156670
Aberrant disulfide bonds in non-amyloidogenic proteins (like HEWL), may strengthen non-covalent intermolecular forces among monomers and promote their aggregation. PMID: 24551048
This study compared the influence of Cu(II) ions and pH of the environment on the molecular structure of the native protein and its fibrils. PMID: 23786978
lysozyme C structure determined by X-ray crystallography method PMID: 23295480
This study analyzes binding structures of complexes of lysozyme and N-acetyl-beta-glucosamine trisaccharide, (NAG)(3). PMID: 23109228
The results of the three simulations show that the structural properties of fully thionated LYZ clearly differ from those of the native protein, while for partly thionated LYZ they only changed slightly compared with native LYZ. PMID: 22653637
Small-angle x-ray scattering studies on dense lysozyme solutions of high ionic strength as a function of temperature and pressure, are reported. PMID: 22713580
Both backbone amide and side chain methyl bond vectors in LYZ are relatively rigid in both the apo and chitotriose-bound states. PMID: 22593013
The tri-N-acetylglucosamine-bound state of the enzyme is less hydrated, more rigid, and less dynamic compared to the unbound state. PMID: 22732010
The study provides a quantitative description of the solvation properties of lysozyme in water/ethanol mixtures, which has been obtained by a simultaneous analysis of small-angle neutron scattering and differential scanning calorimetry experiments. PMID: 22225188
The study applied a protein mapping method to nine structures of hen egg-white lysozyme, and idenified ligand binding sites. PMID: 22092261
investigation of protein conformation/stability of lysozyme by comparison with analogs with varying degrees of ester linkages replacing amide/peptide linkages using molecular dynamics simulations PMID: 22093234
The study presents conformational responses of hen egg white lysozyme in the tetragonal crystal by X-ray diffraction experiments using a humidity-control apparatus, which provided air flow of 20-98%rh at 298 K. PMID: 21802827
The interaction between gold nanorods and lysozyme has been monitored using spectroscopic techniques. PMID: 21729718
These results demonstrate the enhanced chaperone activity of modified beta-casein and its protective effects on lysozyme refolding. PMID: 21802443
The orientation of lysozyme adsorbed to a negatively charged ligand surface was predicted by a rigid and a flexible model. PMID: 21689536
The whole hydration sites (HS) of lysozyme are composed of 195 single HSs and 38 clustered ones (CHS), and divided into 231 external HSs (EHS) and 2 internal ones (IHS). PMID: 21435773
The NMR results indicate that low-lying excited state conformers of hen lysozyme are characterized by slowly fluctuating local conformations around these cavities, attributed to the opportunities for water molecules to penetrate into the cavities. PMID: 21367514
fibril formation by hen egg white lysozyme PMID: 21483680
Data revealed that lysozyme with higher SDS concentrations showed superior thermodynamic stabilities over the ones with no or lower levels of SDS. PMID: 20674294
The reversible thermal unfolding of hen egg white lysozyme, was examined. PMID: 20923660
The interactions of lysozyme with caffeine (Caf), theophylline (Tph) and theobromine (Tbr) were investigated. PMID: 19823947
Results describe the size, shape, structure, and interactions of lysozyme in the ternary system lysozyme/DMSO/water at low protein concentrations. PMID: 20731407
Utilizing fluorescence correlation spectroscopy high spatial resolution of about the laser wavelength used, the molecular dynamics close to crystal surfaces was investigated for both tetragonal single crystals and needlelike spherulites. PMID: 20831338
Two model proteins, lysozyme and thaumatin, were used under unique flow conditions to differentially probe protein crystal nucleation and growth. PMID: 20713010
Single crystal X-ray diffraction shows that the rhenium tricarbonyl cation binds to hen egg lysozyme His15 in two significantly populated rotamer conformations. PMID: 20449250
Acetylation of the lysine residues promoted amyloid formation, resulting in more pronounced fibrils and a dramatic decline in the nucleation time. In contrast, citraconylation produced the opposite effect. PMID: 19945549
The obtained data suggested that LSZ embedment within the H(II) mesophase improved its thermal stability by hampering its helical structure destruction, apparently due to hydrogen bonding of the protein with monoolein polar heads. PMID: 19836212

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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.