| Quantity | 5 mg, 10 mg | 5 mg, 10 mg, 25 mg, 50 mg | 10 mg, 25 mg, 50 mg, 100 mg | 10 mg, 50 mg, 100 mg | 10 KU |
| Description | HAEGT is the first N-terminal 1-5 residues of glucagon like peptide-1 (GLP-1) peptide, and the sequence is His-Ala-Glu-Gly-Thr. HAEGT acts as a competitive substrate for probing prime substrate binding sites of human dipeptidyl peptidase-IV (DPP-IV) 1, in which the N-terminal His-Ala is catalyzed HAEGT is the first N-terminal 1-5 residues of glucagon like peptide-1 (GLP-1) peptide, and the sequence is His-Ala-Glu-Gly-Thr. HAEGT acts as a competitive substrate for probing prime substrate binding sites of human dipeptidyl peptidase-IV (DPP-IV) 1, in which the N-terminal His-Ala is catalyzed cleavage by DPP-IV. HAEGT can be used in the research of diabetes, obesity[1]... Read More | Conalbumin (Ovotransferrin), also known as ovotransferrin, is a monomeric glycoprotein consisting of 686 amino acids, encoded by the avian transferrin gene in the oviduct, and a prominent component of chicken egg white. Exhibiting a unique glycosylation pattern that differentiates it from serum Conalbumin (Ovotransferrin), also known as ovotransferrin, is a monomeric glycoprotein consisting of 686 amino acids, encoded by the avian transferrin gene in the oviduct, and a prominent component of chicken egg white. Exhibiting a unique glycosylation pattern that differentiates it from serum transferrin, Conalbumin is a potent iron binder that plays a crucial role in iron transport to developing embryos. Additionally, it possesses a range of biological activities, including antimicrobial, antifungal, antiviral, anticancer, antioxidative, antihypertensive, and immunoregulatory properties, making it valuable in numerous applications such as infant formula ingredients, food additives, and agents for enhancing animal health... Read More | Gly-Gly-Phe-Gly is a peptide spacer and can be applied to Doxorubicin (HY-15142A) (DXR) conjugates[1] | Insulin (swine) is a porcine-derived insulin used in diabetes research[1] | PNGase F, a glycosidase, catalyzes the cleavage of an internal glycoside bond in an oligosaccharide. PNGase F removes nearly all N-linked oligosaccharides from glycoproteins. PNGase F can release N-glycans from glycoproteins in glycoanalytical workflows[1][2] |