ADAM15 (基因名), Disintegrin and metalloproteinase domain-containing protein 15 (蛋白名), ADA15_HUMAN.
Human ADAM15/ Disintegrin and metalloproteinase domain-containing protein 15 ELISA Kit
Metalloprotease RGD disintegrin protein, Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15, Metargidin, MDC-15, ADAM 15, MDC15
Natural and recombinant human Disintegrin and metalloproteinase domain-containing protein 15
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Interacts with ITAGV-ITGB3 (vitronectin receptor). Interacts with SH3GL2 and SNX9; this interaction occurs preferentially with ADAM15 precursor, rather than the processed form, suggesting it occurs in a secretory pathway compartment prior to the medial Golgi. Interacts with ITAG9-ITGB1 (By similarity). Interacts specifically with Src family protein-tyrosine kinases (PTKs). Interacts with SH3PXD2A. Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC.
Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.
Endomembrane system Single-pass type I membrane protein Cell junction Adherens junction Cell projection Cilium Flagellum Cytoplasmic vesicle Secretory vesicle Acrosome The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity).
MRLALLWALG | LLGAGSPLPS | WPLPNIGGTE | EQQAESEKAP | REPLEPQVLQ |
DDLPISLKKV | LQTSLPEPLR | IKLELDGDSH | ILELLQNREL | VPGRPTLVWY |
QPDGTRVVSE | GHTLENCCYQ | GRVRGYAGSW | VSICTCSGLR | GLVVLTPERS |
YTLEQGPGDL | QGPPIISRIQ | DLHLPGHTCA | LSWRESVHTQ | KPPEHPLGQR |
HIRRRRDVVT | ETKTVELVIV | ADHSEAQKYR | DFQHLLNRTL | EVALLLDTFF |
RPLNVRVALV | GLEAWTQRDL | VEISPNPAVT | LENFLHWRRA | HLLPRLPHDS |
AQLVTGTSFS | GPTVGMAIQN | SICSPDFSGG | VNMDHSTSIL | GVASSIAHEL |
GHSLGLDHDL | PGNSCPCPGP | APAKTCIMEA | STDFLPGLNF | SNCSRRALEK |
ALLDGMGSCL | FERLPSLPPM | AAFCGNMFVE | PGEQCDCGFL | DDCVDPCCDS |
LTCQLRPGAQ | CASDGPCCQN | CQLRPSGWQC | RPTRGDCDLP | EFCPGDSSQC |
PPDVSLGDGE | PCAGGQAVCM | HGRCASYAQQ | CQSLWGPGAQ | PAAPLCLQTA |
NTRGNAFGSC | GRNPSGSYVS | CTPRDAICGQ | LQCQTGRTQP | LLGSIRDLLW |
ETIDVNGTEL | NCSWVHLDLG | SDVAQPLLTL | PGTACGPGLV | CIDHRCQRVD |
LLGAQECRSK | CHGHGVCDSN | RHCYCEEGWA | PPDCTTQLKA | TSSLTTGLLL |
SLLVLLVLVM | LGASYWYRAR | LHQRLCQLKG | PTCQYRAAQS | GPSERPGPPQ |
RALLARGTKQ | ASALSFPAPP | SRPLPPDPVS | KRLQAELADR | PNPPTRPLPA |
DPVVRSPKSQ | GPAKPPPPRK | PLPADPQGRC | PSGDLPGPGA | GIPPLVVPSR |
PAPPPPTVSS | LYL
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