Adam15 (基因名), Disintegrin and metalloproteinase domain-containing protein 15 (蛋白名), ADA15_RAT.
Rat Adam15/ Disintegrin and metalloproteinase domain-containing protein 15 ELISA Kit
CRII-7, Metalloprotease RGD disintegrin protein, Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15, Metargidin, MDC-15, ADAM 15, Mdc15
Natural and recombinant rat 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 (By similarity). Interacts with ITAG9-ITGB1. 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 | LLGAGSPRPS | PPLPNIGGTE | EEQQASPERT | QSRSLENQVV |
QDSPPINLTE | VLQTGLPETL | RIGLELDGEN | HILELQQNRD | LVPGRPTLVW |
YQPDGTRMVS | EGHSLENCCY | RGRVQGRPSS | WVSLCACSGI | RGLVVLSPER |
SYTLELGPGD | LQRPLIVSRI | QDLLLPGHTC | APSWHAFVPT | EAAPDLLLEQ |
HHLRRLKRDV | VTETKIVELV | IVADNSEVRK | YPDFQQLLNR | TLEVALLLDT |
FFQPLNVRVA | LVGLEAWTQR | DLIEMSSNPA | VLLDNFLRWR | RTDLLPRLPH |
DSAQLVTVTS | FSGPMVGMAI | QNSICSPDFS | GGVNMDHSTS | ILGVASSIAH |
ELGHSLGLDH | DSPGNSCPCP | GPAPAKSCIM | EASTDFLPGL | NFSNCSRWAL |
EKALLDGMGS | CLFEWPPSRA | PMSSLCGNMF | VDPGEQCDCG | FPDECTDPCC |
DYFTCQLRPG | AQCASDGPCC | QNCKLQPAGW | QCRLPTDDCD | LPEFCLGDSS |
QCPPDIRLGD | GEPCASGEAV | CMHGRCASYT | RQCQSLWGPG | AQPAAPLCLQ |
TANTRGNAFG | SCGRSPSGSY | MPCNLRDAIC | GQLQCQWGRN | QPLLGSVQDQ |
LSEVLEANGT | QLNCSWVDLD | LGNDVAQPLL | ALPGTACGPG | LVCIGHRCQP |
VDLLGAQECR | SKCHGHGVCD | SSRHCHCDEG | WAPPDCMTQL | RATSSLTTGL |
LLSLLLLLVL | VLLGASYWYR | ARLHQRLCQL | KGSSCQYRAA | QSGPPERPGP |
PQRAQQMPGT | KQANVSFPVP | PSRPLPPNPV | PKKLQAELAD | RSNPPTRPLP |
ADPVVWRPKP | QGPTKPPPPR | KPLPANPQGR | PPLGDLPGPG | DGSLQLVVPS |
RPAPPPPAAS | SLYL
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