Biotinylated Recombinant Chicken Lysozyme G, Biotinylated Protein (MBP&His-Avi)

Product Overview Description Biotinylated Recombinant Chicken Lysozyme G, Biotinylated 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 P27042 Target Symbol P27042 Species Gallus gallus (Chicken) Expression System E.coli Tag N-MBP&C-6His-Avi Target Protein Sequence GTGCYGSVSRIDTTGASCRTAKPEGLSYCGVRASRTIAERDLGSMNKYKVLIKRVGEALCIEPAVIAGIISRESHAGKILKNGWGDRGNGFGLMQVDKRYHKIEGTWNGEAHIRQGTRILIDMVKKIQRKFPRWTRDQQLKGGISAYNAGVGNVRSYERMDIGTLHDDYSNDVVARAQYFKQHGY Expression Range 27-211aa Protein Length Full Length of Mature Protein Mol. Weight 68.3 kDa Research Area Others 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 Subcellular Location Secreted. Protein Families Glycosyl hydrolase 23 family Database References KEGG: gga:395708 STRING: 9031.ENSGALP00000027012 UniGene: Gga.3357 Tissue Specificity Granulocyte compartment of myelomonocytic cells. Gene Functions References Improved algorithms for mapping protein surfaces using small organic molecules as molecular probes reproduced the binding of eight organic solvents to lysozyme as observed by NMR. PMID: 13677484 The pH dependence of the initial structure of the fully reduced hen egg white lysozyme in the presence of 90% (v/v) ethanol suggests that Asp and His residues may play an important role. PMID: 14718651 oxidative refolding of equilibrium intermediates of lysozyme stabilized in trifluoroethanol (TFE) and ethylene glycol PMID: 14741343 Site-specific glycosylation of lysozyme in the interfacial region of lysozyme-antibody complex is more effective to reduce the antigenicity than the mutation of single amino acids. PMID: 14741362 A prominent structural difference was observed in the loop region of residues Ser60-Leu75 as observed when a water molecule was replaced with a sodium atom PMID: 15039550 Nonrandom folding occurs in the early stage of the folding of reduced lysozyme, a finding which provides new insight into early-stage events in the folding process of reduced lysozyme. PMID: 15122914 Ni2+ quenches the fluorescence of Trp62 and Trp108 due to the binding of Ni2+ to the active site of lysozyme PMID: 15474459 data describe the early events in the folding of reduced mutated W62G lysozyme in detail PMID: 15733925 that expression of the lysozyme gene in undifferentiated monoblasts is low and a high level of gene expression requires both cell differentiation and lipopolysaccharide stimulation PMID: 15923188 potential energy surfaces have been generated for all the oligomers PMID: 16330266 The three-dimensional structure of hen egg-white lysozyme (HEWL) in a hexagonal crystal form has been determined and refined to 1.46 A resolution. PMID: 16552135