| Description | Cellulase refers to a family of enzymes which act in concert to hydrolyze cellulose. Trichoderma reesei has an extensively studied cellulase enzyme complex. This complex converts crystalline, amorphous, and chemically derived celluloses quantitatively to glucose.Cellulase has been used to degrade Cellulase refers to a family of enzymes which act in concert to hydrolyze cellulose. Trichoderma reesei has an extensively studied cellulase enzyme complex. This complex converts crystalline, amorphous, and chemically derived celluloses quantitatively to glucose.Cellulase has been used to degrade cello-oligosaccharides into glucose; to study the biodegradability of bioabsorbable bacterial cellulose (BBC) material. Cellulase from Trichoderma reesei has been used in a study to assess the differential regulation of the cellulase transcription factors XYR1, ACE2, and ACE. Cellulase from Trichoderma reesei has also been used in a study to investigate the liquefaction of hydrothermally pretreated wheat straw at high-solids content... Read More | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 8.38 | Inquire | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidicPurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence mechanism.A35R could block some stage of antigen processing or presentation in infected cells or interfere with regulation of apoptosis. In addition, the A35R function may be required for growth in certain cell types, e.g., macrophage, in vivo. It localizes to factories where viral DNA is located and it was shown to be a constitutive transcriptional activator in a large-scale yeast two-hybrid study... Read More | Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The HOLOenzyme may be used to determine tyrosine, phenylalanine and dihydroxyphenylalanine either manometrically or colorimetrically.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has been used in a study to purify and characterize tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has also been used in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase... Read More |