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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃.
- 保质期:
Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
- 英文名:
Recombinant Mouse Amyloid beta A4 protein (App)
- 库存:
200
- 供应商:
武汉华美生物工程有限公司
- 规格:
20μg
英文名称:
Recombinant Mouse Amyloid beta A4 protein (App)品名简称:
Recombinant Mouse App protein货号:
CSB-EP001950MOc7规格:
20μg价格:
1344LC-MS/Western Blot:
/SDS-PAGE:
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.纯度:
Greater than 95% as determined by SDS-PAGE.内毒素:
Not test生物活性:
/基因名:
AppUniprot No.:
P12023别名:
ABPP;APP;Alzheimer disease amyloid A4 protein homolog;Alzheimer disease amyloid protein;Amyloid precursor protein;Amyloid-beta (A4;Amyloid-beta A4 protein;Amyloidogenic glycoprotein;AG;S-APP-alpha;S-APP-beta;APP-C99;Beta-secretase C-terminal fragment;Beta-CTF;Abeta42;Beta-APP42;Abeta40;Beta-APP40;Alpha-secretase C-terminal fragment;Alpha-CTF;42;40;APP-C59;Amyloid intracellular domain 59;AID(59;Gamma-CTF(59;APP-C57;Amyloid intracellular domain 57;AID(57;Gamma-CTF(57;Amyloid intracellular domain 50;AID(50;Gamma-CTF(50种属:
Mus musculus (Mouse)蛋白长度:
Full Length of Mature Protein来源:
E.coli分子量:
91.8 kDa表达区域:
18-770aa氨基酸序列:
LEVPTDGNAGLLAEPQIAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDSVDSADAEEDDSDVWWGGADTDYADGGEDKVVEVAEEEEVADVEEEEADDDEDVEDGDEVEEEAEEPYEEATERTTSTATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCVPFFYGGCGGNRNNFDTEEYCMAVCGSVSTQSLLKTTSEPLPQDPDKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPHHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHPFGVDSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFGHDSGFEVRHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN蛋白标签:
C-terminal 6xHis-tagged产品提供形式:
Liquid or Lyophilized powder缓冲液:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.储存条件:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.保质期:
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.货期:
13-23 business days注意事项:
Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.功能1:
Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibit 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. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons. May be involved in copper homeostasis/oxidative stress through copper ion reduction. 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. ; Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse amyloid-beta peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Amyloid-beta protein 42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also binds GPC1 in lipid rafts. ; 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).功能2:
/文献:
/研究领域:
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文献和实验Designing Animal Models of Alzheimer’s Disease with Amyloid Precursor Protein (APP)Transgenes
Amyloid precursor protein (APP) and Alzheimer’s disease are irrevocably linked, as APP is cleaved to form the Aβ peptides that are the major components of amyloid plaques. One of the most resilient hypotheses about the cause of AD centers
Lentivirus-Expressed siRNA Vectors Against Alzheimer Disease
Amyloid precursor protein (APP) has been implicated in the pathogenesis of Alzheimer disease, and the accumulation of APP products ultimately leads to the familiar histopathological and clinical manifestations associated with this most common
Introduction to Alzheimer’s Disease
and neurofibrillary tangles came to be known as Alzheimer’s disease (AD), a term that was later broadened to include senile forms of dementia with similar neuropathological findings. It was Divry (3 ) who first demonstrated the presence of amyloid at the center
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