Katalognummer: 209 - 101-M697
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 100 µg
101-M697
u-Plasminogen Activator (uPA) is a serine protease that converts plasminogen to plasmin, with roles in a variety of normal and pathological processes that include cell migration and tissue destruction. uPA is a potent marker of invasion and metastasis in a variety of human cancers including breast, stomach, colon, bladder, ovarian, brain, and endometrium.
101-M571
MIF (or macrophage migration inhibitory factor) was the first lymphokine/cytokine to be recognized in the pregenomics era. Regardless, it is one of the least understood of all inflammatory mediators. Human MIF is a 12.5 kDa, 115 amino acid (aa) nonglycosylated polypeptide that is synthesized without a signal sequence. Secretion occurs nonclassically via an ABCA1 transporter. The initiating Met is removed, leaving Pro as the first amino acid. The molecule consists of two αhelices and six βstrands, four of which form a βsheet. The two remaining βstrands interact with other MIF molecules, creating a trimer. Structure-function studies suggest MIF is bifunctional with segregated topology. The N-and C-termini mediate enzyme activity (in theory). Phenylpyruvate tautomerase activity (enol to keto) has been demonstrated and is dependent upon Pro at position #1. Amino acids 50-65 have also been suggested to contain thiol protein oxidoreductase activity. MIF has proinflammatory cytokine activity centered around aa’s 49-65. On fibroblasts, MIF induces, IL1, IL8, and MMP expression; on macrophages, MIF stimulates NO production and TNF-α release following IFNγ activation. MIF apparently acts through CD74 and CD44, likely in some form of trimeric interaction. Human MIF is active on mouse cells. Human MIF is 90%, 94%, 95%, and 90% aa identical to mouse, bovine, porcine, and rat MIF, respectively.
101-M572
Müllerian inhibiting substance (MIS), also named antiMüllerian hormone (AMH), is a tissuespecific TGFβ superfamily growth factor. Its expression is restricted to the Sertoli cells of fetal and postnatal testis, and to the granulosa cells of postnatal ovary. The human MIS gene encodes a 553 amino acid residue (aa) prepropeptide containing a signal a sequence (1-24), a proregion (25-455), and the carboxylterminal bioactive protein (446-553). MIS is synthesized and secreted as a disulfidelinked homodimeric proprotein. Proteolytic cleavage is required to generate the Nterminal pro region and the C-terminal bioactive protein, which remain associated in a noncovalent complex. Recombinant C-terminal MIS has been shown to be bioactive. However, the complex with the N-terminal pro region showed enhanced activity. The Cterminal region contains the seven canonical cysteine residues found in TGF-β superfamily members. These cysteine residues are involved in interand intramolecular disulfide bonds, which forms the cysteine knot structure. Human and mouse MIS share 73% and 90% aa sequence identity in their pro region and Cterminal region, respectively. MIS induces Mullerian duct (female reproductive tract) regression during sexual differentiation in the male embryo. Posnatally, MIS has been shown to regulate gonadal functions. MIS inhibits Leydig cell proliferation and is a regulator of the initial and cyclic recruitment of ovarian follicles. MIS has also been found to have antiproliferative effects on breast, ovarian and prostate tumor cells.
101-M590
NOV belongs to the CCN (CTGF/CYR61/NOV) family of secreted proteins that share a common multimodular organization. Each protein contains an IGFBP domain, a von Willebrand factor type C domain, a thrombospondin type I domain and a cysteine knot domain. NOV interacts with several proteins and is involved in both internal and external cell signaling.

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