| Description | MOG (35-55), human is a component of CNS myelin. MOG (35-55), human is different from mMOG (35-55) by a proline for serine substitution at position 42. MOG (35-55), human is also immunogenic via bind to H-2b class II MHC and recognized by T cells, but not encephalitogenic, and is only partially MOG (35-55), human is a component of CNS myelin. MOG (35-55), human is different from mMOG (35-55) by a proline for serine substitution at position 42. MOG (35-55), human is also immunogenic via bind to H-2b class II MHC and recognized by T cells, but not encephalitogenic, and is only partially cross-reactive with mMOG35–55. MOG (35-55), human induces minimal clinical signs of EAE relative to the rodent peptide[1][2]... Read More | Apelin-36(human) is an endogenous orphan G protein-coupled receptor APJ agonist, with an EC50 of 20 nM. Apelin-36(human) shows high affinity to human APJ receptors expressed in HEK 293 cells (pIC50=8.61). Apelin-36 has been linked to two major types of biological activities: cardiovascular and Apelin-36(human) is an endogenous orphan G protein-coupled receptor APJ agonist, with an EC50 of 20 nM. Apelin-36(human) shows high affinity to human APJ receptors expressed in HEK 293 cells (pIC50=8.61). Apelin-36 has been linked to two major types of biological activities: cardiovascular and metabolic. Apelin-36(human) inhibits the entry of some HIV-1 and HIV-2 into the NP2/CD4 cells expressing APJ[1][2][3][4]... Read More | Aprotinin is a bovine pancreatic trypsin inhibitor (BPTI) inhibitor which inhibits trypsin and chymotrypsin with Kis of 0.06 pM and 9 nM, respectively | JAMM protein inhibitor 2 (compound 180) is a potent JAMM protease inhibitor with IC50s of 10 µM, 46 µM and 89 µM for thrombin, Rpn11 and MMP2, respectively. JAMM protein inhibitor 2 can be used for researching anticancer[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] |