APP (基因名), Amyloid-beta A4 protein (蛋白名), A4_PIG.
Pig APP/ Amyloid-beta A4 protein CLIA Kit
ABPP, APP, Alzheimer disease amyloid A4 protein homolog, Amyloid precursor protein, Amyloid-beta precursor protein
Natural and recombinant pig Amyloid-beta A4 protein
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons (By similarity). Amyloid-beta associates with HADH2 (By similarity). Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER (By similarity). Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding (By similarity). Amyloid-beta protein 40 interacts with S100A9 (By similarity). CTF-alpha product of APP interacts with GSAP (By similarity). Interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides (By similarity). The C99 fragment also interacts with SORL1 (By similarity). Interacts with PLD3 (By similarity). Interacts with VDAC1 (By similarity). Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2 (By similarity). Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity). Interacts with LRRK2 (By similarity).
N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).
Gamma-secretase C-terminal fragment 59 Nucleus Cytoplasm Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated Thr-743 form is localized to the nucleus (By similarity).
MLPGLALVLL | AAWTARALEV | PTDGNAGLLA | EPQVAMFCGK | LNMHMNVQNG |
KWESDPSGTK | TCIGTKEGI | LQYCQEVYPE | LQITNVVEAN | QPVTIQNWCK |
RSRKQCKTHT | HIVIPYRCLV | G EFVSDALL | VPDKCKFLHQ | ERMDVCETHL |
HWHTVAKETC | SEKSTNLHDY | GMLLPCGIDK | FR GVEFVCC | PLAEESDNID |
SADAEEDDSD | VWWGGADTDY | ADGSEDKVVE | VAEEEEVADV | EEE EAEDDE |
DDEDGDEVEE | EAEEPYEEAT | ERTTSIATTT | TTTTESVEEV | VREVCSEQAE |
TGPC RAMIS | RWYFDVTEGK | CAPFFYGGCG | GNRNNFDTEE | YCMAVCGSVM |
SQSLLKTTQE | HLPQD PVKL | PTTAASTPDA | VDKYLETPGD | ENEHAHFQKA |
KERLEAKHRE | RMSQVMREWE | EAERQA KNL | PKADKKAVIQ | HFQEKVESLE |
QEAANERQQL | VETHMARVEA | MLNDRRRLAL | ENYITAL QA | VPPRPRHVFN |
MLKKYVRAEQ | KDRQHTLKHF | EHVRMVDPKK | AAQIRSQVMT | HLRVIYER M |
NQSLSLLYNV | PAVAEEIQDE | VDELLQKEQN | YSDDVLANMI | SEPRISYGND |
ALMPSLTET | KTTVELLPVN | GEFSLDDLQP | WHPFGVDSVP | ANTENEVEPV |
DARPAADRGL | TTRPGSGLTN | IKTEEISEV | KMDAEFRHDS | GYEVHHQKLV |
FFAEDVGSNK | GAIIGLMVGG | VVIATVIVIT | L VMLKKKQY | TSIHHGVVEV |
DAAVTPEERH | LSKMQQNGYE | NPTYKFFEQM | QN
"Hereditary cerebral hemorrhage with amyloidosis associated with the E693K mutation of APP."
"Association studies testing for risk for late-onset Alzheimer's disease with common variants in the beta-amyloid precursor protein (APP)."
"Contrasting, species-dependent modulation of copper-mediated neurotoxicity by the Alzheimer's disease amyloid precursor protein."
"Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid."
"Homodimerization of amyloid precursor protein and its implication in the amyloidogenic pathway of Alzheimer's disease."
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