Purity ≥95% (SDS-PAGE) Endotoxin level <0.1 EU/μg Function Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity. Also binds GPC1 in lipid rafts. Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).
规格
产品名称
Recombinant Human Amyloid Precursor Protein
别名
淀粉样前体蛋白(APP)重组蛋白
英文别名
ABPP | Alzheimer disease amyloid protein | Amyloid precursor protein | Amyloid-beta A4 protein | APP | APPI | Cerebral vascular amyloid peptide | CVAP | PN-II | PreA4 | Protease nexin-II | A4 amyloid protein | A4_HUMAN | AAA | ABETA | ABPP | AD1 | AICD-50
100 - 125 kDa, under reducing conditions; 100 - 125 kDa, under non-reducing conditions.
分子类型
蛋白质
产品线
生物产品
储存与运输
物理形态
冻干(Lyophilized)
储存缓冲液
Lyophilized from 10mM PBS, 5% Trehalose, 5% Mannitol, pH 7.4
复溶
Reconstitute in sterile water to a concentration of 0.1-0.5 mg/ml.
储存条件
-20°C储存,避免反复冻融
运输条件
超低温运输
稳定性与储存
在 -20~-80℃ 下可保存 1 年以上。收货后建议分装。避免冷冻/解冻循环。
图片
Recombinant Human Amyloid Precursor Protein (rp142805) - SDS-PAGE 3 μg/lane of Recombinant Human Amyloid Precursor Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing the band at 100 - 125 kDa.