| Description | LL-37, acetylated, amidated is a cathelicidin peptide LL-37 acetylated on the N-terminus and amidated on the C-terminus. The single human cathelicidin peptide LL-37 has antimicrobial and anti-biofilm activity against multiple Gram-positive and Gram-negative human pathogens, and has wound-healing LL-37, acetylated, amidated is a cathelicidin peptide LL-37 acetylated on the N-terminus and amidated on the C-terminus. The single human cathelicidin peptide LL-37 has antimicrobial and anti-biofilm activity against multiple Gram-positive and Gram-negative human pathogens, and has wound-healing effects on the host[1]... Read More | Alcohol oxidase is a functional enzyme of methanol utilization pathway and can be isolated from yeast peroxisome[1] | M1145, a chimeric peptide, is a selective galanin receptor type 2 (GAL2) agonist, with a Ki of 6.55 nM. M1145 shows more than 90-fold higher affinity for GAL2 over GAL1 (Ki=587 nM) and a 76-fold higher affinity over GalR3 (Ki=497 nM). M1145 has an additive effect on the signal transduction of M1145, a chimeric peptide, is a selective galanin receptor type 2 (GAL2) agonist, with a Ki of 6.55 nM. M1145 shows more than 90-fold higher affinity for GAL2 over GAL1 (Ki=587 nM) and a 76-fold higher affinity over GalR3 (Ki=497 nM). M1145 has an additive effect on the signal transduction of galanin[1]... Read More | MCE NHS Magnetic Beads (200 nm, 10 mg/mL) contain N-hydroxysuccinimide (NHS) functional groups, which react with primary amines on proteins orother molecules to form stable amide linkages，can covalently immobilize proteins for the affinity purification of antibodies, antigens and MCE NHS Magnetic Beads (200 nm, 10 mg/mL) contain N-hydroxysuccinimide (NHS) functional groups, which react with primary amines on proteins orother molecules to form stable amide linkages，can covalently immobilize proteins for the affinity purification of antibodies, antigens and otherbiomolecules... Read More | TCTDSTNCYKAT is an engineered-variant peptide of antifreeze protein (AFP)[1] |