APP/Protease nexin-II cDNA ORF Clone, Mouse, untagged

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APP/Protease nexin-II cDNA ORF Clone, Mouse, untagged: 产品信息

基因
种属
Mouse
NCBI 参考序列号
基因长度
2256 bp
序列特征
Identical with the Gene Bank Ref. ID sequence.
产品特征
Full length Clone DNA of Mouse amyloid beta (A4) precursor protein.
质粒
启动子
Enhanced CMV promoter
限制性酶切位点
HindIII + XbaI(6.1kb+2.26kb)
测序引物
T7( 5' TAATACGACTCACTATAGGG 3' ) BGH( 5' TAGAAGGCACAGTCGAGG 3' )
质控
The plasmid is confirmed by full-length sequencing.
筛选
细菌筛选抗性
Ampicillin
细胞筛选抗性
Hygromycin
应用
Stable or Transient mammalian expression
储存 & 运输
运输方式
Each tube contains lyophilized plasmid.
储存条件
The lyophilized plasmid can be stored at ambient temperature for three months.

APP/Protease nexin-II 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.**

APP/Protease nexin-II cDNA ORF Clone, Mouse, untagged: 验证图片

APP/Protease nexin-II cDNA ORF Clone, Mouse, untagged: 别称

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

APP/Protease nexin-II 背景信息

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.
全称
amyloid beta (A4) precursor protein
参考文献
  • 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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