| Description | CD9-binding peptide TFA is a CD9-binding peptide. CD9-binding peptide TFA inhibits the binding of EWI-2 to CD9. CD9-binding peptide TFA exhibits selective anti-migratory and anti-invasive activities against cancer cells. CD9-binding peptide TFA can be used for the study of cancer[1] | β-Endorphin, human, a prominent endogenous peptide, existing in the hypophysis cerebri and hypothalamus, is an agonist of opioid receptor, with preferred affinity for µ-opioid receptor and δ-opioid receptor; β-Endorphin, human exhibits antinociception activity | Exoenzyme C3, clostridium botulinum, is a mono-ADP-ribosylating enzyme. Exoenzyme C3, clostridium botulinum specifically modifies RhoA, B, and C by transferring ADP-ribose to them, thereby inactivating these GTPases. Exoenzyme C3, clostridium botulinum can induce neuronal axonal and dendritic growthExoenzyme C3, clostridium botulinum, is a mono-ADP-ribosylating enzyme. Exoenzyme C3, clostridium botulinum specifically modifies RhoA, B, and C by transferring ADP-ribose to them, thereby inactivating these GTPases. Exoenzyme C3, clostridium botulinum can induce neuronal axonal and dendritic growth, inhibit macrophage migration, and regulate cytoskeletal dynamics. Exoenzyme C3, clostridium botulinum can be used in the research of spinal cord injury and diabetic painful neuropathy[1][2][3][4][5]... Read More | Laccase, Microorganisms (Denilite IIS) is a multi-copper oxidase (MCOs), which widely exists in microorganisms, plants and fungi, and can catalyze the oxidation of one electron of various phenolic compounds. Laccase can promote the oxidative coupling of single lignin, which plays an important role Laccase, Microorganisms (Denilite IIS) is a multi-copper oxidase (MCOs), which widely exists in microorganisms, plants and fungi, and can catalyze the oxidation of one electron of various phenolic compounds. Laccase can promote the oxidative coupling of single lignin, which plays an important role in the formation and biodegradation of lignin, and also has the potential to cross-link food polymers[1]... Read More | L-Lactate dehydrogenase, Microorganism (LAD) is a redox enzyme. L-Lactate dehydrogenase catalyzes the reduction of pyruvate to L-lactate by NADH in vivo with absolute enantiospecificity[1] |