Amyloid Precursor Protein cDNA ORF Clone, Mouse, C-DDK (Flag®) tag

Cat: MG50402-CF
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Amyloid Precursor Protein cDNA ORF Clone, Mouse, C-DDK (Flag®) tag 基本信息
基因
种属
Mouse
NCBI 参考序列号
参考序列ORF长度
2088 bp
序列描述
Identical with the Gene Bank Ref. ID sequence except for the point mutations: 6 G>A, 498 C>T not causing the amino acid variation.
描述
Full length Clone DNA of Mouse amyloid beta (A4) precursor protein with C terminal Flag tag.
质粒
启动子
Enhanced CMV promoter
载体
pCMV3-C-FLAG
限制性酶切位点
HindIII + XbaI (6kb + 2.13kb)
标签序列
FLAG Tag Sequence: GATTACAAGGATGACGACGATAAG
测序引物
T7( 5' TAATACGACTCACTATAGGG 3' )
BGH( 5' TAGAAGGCACAGTCGAGG 3' )
质控
The plasmid is confirmed by full-length sequencing.
筛选
抗生素(大肠杆菌)
Kanamycin
抗生素(哺乳动物细胞)
Hygromycin
应用
Stable or Transient mammalian expression
储存 & 运输
运输
Each tube contains lyophilized plasmid.
储存
The lyophilized plasmid can be stored at ambient temperature for three months.
Amyloid Precursor Protein cDNA ORF 核苷酸序列及氨基酸序列信息

**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**

Amyloid Precursor Protein cDNA ORF Clone, Mouse, C-DDK (Flag®) tag Validated Images
Cynomolgus CD19/B4/CVID3 Gene Plasmid Map 5619
Mouse Amyloid beta A4 protein Gene Expression validated Image 14176
The plasmid was transfected into 293H adherent cells with Sinofection reagent (Cat# STF01). After 48 h, Immunofluorescence staining of cells. Cells were fixed with 4% PFA, permeabilzed with 0.3% Triton X-100 in PBS, blocked with 10% serum, and incubated with Mouse anti-Flag Tag monoclonal antibody (CST#8146S) at 37℃ 1 hour. Then cells were stained with Goat Anti-mouse IgG secondary antibody. The fluorescent signal is detected by fluorescence microscope. Each expression experiment has negative control.
Amyloid Precursor Protein cDNA ORF Clone, Mouse, C-DDK (Flag®) tag Alternative Names
Abeta cDNA ORF Clone, Mouse;Abpp cDNA ORF Clone, Mouse;Adap cDNA ORF Clone, Mouse;Ag cDNA ORF Clone, Mouse;betaApp cDNA ORF Clone, Mouse;Cvap cDNA ORF Clone, Mouse;E030013M08Rik cDNA ORF Clone, Mouse
Amyloid Precursor Protein Background Information

Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.

Full Name
amyloid beta (A4) precursor protein
References
  • Grimm MO, et al. (2007) Amyloid beta as a regulator of lipid homeostasis. Trends Mol Med. 13(8): 337-44.
  • Smith EE, et al. (2009) Beta-amyloid, blood vessels, and brain function. Stroke. 40(7): 2601-6.
  • Gouras GK, et al. (2010) Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease. Acta Neuropathol. 119(5): 523-41.
  • Palop JJ, et al. (2010) Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks. Nat Neurosci. 13(7): 812-8.
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