Beta-amyloid 39/Beta-APP39 Recombinant Protein | APP recombinant protein

Beta-amyloid 39/Beta-APP39 Protein, Human, Recombinant (aa 672-710, His & GST Tag)

Cat. Num. AAA8120444

• Gene Names: APP; AAA; AD1; PN2; ABPP; APPI; CVAP; ABETA; PN-II; CTFgamma
• Purity: >85% as determined by SDS-PAGE
• Synonyms: Beta-amyloid 39/Beta-APP39; Beta-amyloid 39/Beta-APP39 Protein; Human; Recombinant (aa 672-710; His & GST Tag); Human Beta-amyloid 39/Beta-APP39 Protein (aa 672-710; AAA Protein; ABETA Protein; ABPP Protein; AD1 Protein; APPI Protein; CTFgamma Protein; CVAP Protein; PN-II Protein; PN2 Protein; amyloid beta (A4) precursor protein; APP recombinant protein

• Host: E Coli
• Purity/Purification: >85% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile 50mM Tris, 100mM NaCl, 20% glycerol, 0.05% Tween 20, pH9.5. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of C
• Sequence: Asp672-Val710

• Species: Human
• Predicted N Terminal: Met
• Tag: N-GST & His
• Protein Construction: A DNA sequence encoding the amino acids (Asp672-Val710) of human Amyloid beta A4 protein (APP770)(P05067-1), corresponding to the Beta-amyloid protein 39, was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

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Related Product Information for APP recombinant protein

Background: 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 beta- and gamma-secretase to produce the amyloid-beta-protein (Abeta, 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, alpha-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Abeta 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.

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.

NCBI and Uniprot Product Information

• NCBI GI #: 4502167
• NCBI GeneID: 351
• NCBI Accession #: NP_000475.1
• NCBI GenBank Nucleotide #: NM_000484.3
• UniProt Accession #: P05067; P09000; P78438; Q13764; Q13778; Q13793; Q16011; B2R5V1; B4DII8; D3DSD1; D3DSD2; D3DSD3
• Molecular Weight: 86,943 Da
• NCBI Official Full Name: amyloid beta A4 protein isoform a
• NCBI Official Synonym Full Names: amyloid beta (A4) precursor protein
• NCBI Official Symbol: APP
• NCBI Official Synonym Symbols: AAA; AD1; PN2; ABPP; APPI; CVAP; ABETA; PN-II; CTFgamma
• NCBI Protein Information: amyloid beta A4 protein; preA4; protease nexin-II; peptidase nexin-II; beta-amyloid peptide; alzheimer disease amyloid protein; cerebral vascular amyloid peptide
• UniProt Protein Name: Amyloid beta A4 protein
• Protein Family: Amyloid beta A4 protein
• UniProt Gene Name: APP
• UniProt Synonym Gene Names: A4; AD1; APP; CVAP; PN-II; S-APP-alpha; S-APP-beta; AICD-59; AID(59); AICD-57; AID(57); AICD-50; AID(50)
• UniProt Entry Name: A4_HUMAN

NCBI Description

This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

APP: a cell surface receptor that influences neurite growth, neuronal adhesion and axonogenesis. Cleaved by secretases to form a number of peptides, some of which bind to the acetyltransferase complex Fe65/TIP60 to promote transcriptional activation. The Abeta peptide is released from the cell, its extracellular deposition and accumulation form the main components of amyloid plaques in Alzheimer's disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis. Can promote transcription activation through binding to Fe65-Tip60 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. 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. Induces a RAGE-dependent pathway that activates 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. Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, JIP1, SHC1 and, NUMB and DAB1. Binding to DAB1 inhibits its serine phosphorylation. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Amyloid beta-42 binds nAChRA7 in hippocampal neurons. Beta-amyloid associates with HADH2. Soluble APP binds, via its N-terminal head, to FBLN1. Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex- opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra- striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. 10 isoforms of the human protein are produced by alternative splicing. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non- neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Belongs to the APP family.

Protein type: Cell surface; Receptor, misc.; Transcription factor; Membrane protein, integral; Apoptosis

Chromosomal Location of Human Ortholog: 21q21.3

Cellular Component: Golgi apparatus; extracellular space; cell surface; intracellular membrane-bound organelle; integral to plasma membrane; extracellular region; integral to membrane; dendritic spine; coated pit; intercellular junction; cytosol; ER to Golgi transport vesicle; lipid raft; ciliary rootlet; nuclear envelope lumen; perinuclear region of cytoplasm; axon; apical part of cell; cytoplasm; plasma membrane; synapse; spindle midzone; dendritic shaft; neuromuscular junction; endosome; receptor complex

Molecular Function: serine-type endopeptidase inhibitor activity; heparin binding; identical protein binding; protein binding; protease activator activity; enzyme binding; DNA binding; transition metal ion binding; PTB domain binding; acetylcholine receptor binding; receptor binding

Biological Process: extracellular matrix organization and biogenesis; adult locomotory behavior; locomotory behavior; mRNA polyadenylation; positive regulation of mitotic cell cycle; protein amino acid phosphorylation; regulation of translation; platelet degranulation; synaptic growth at neuromuscular junction; forebrain development; dendrite development; visual learning; collateral sprouting in the absence of injury; neuromuscular process controlling balance; cell adhesion; neurite development; cholesterol metabolic process; platelet activation; Notch signaling pathway; cellular copper ion homeostasis; regulation of epidermal growth factor receptor activity; axon cargo transport; mating behavior; regulation of multicellular organism growth; endocytosis; axon midline choice point recognition; smooth endoplasmic reticulum calcium ion homeostasis; neuron apoptosis; negative regulation of neuron differentiation; axonogenesis; suckling behavior; ionotropic glutamate receptor signaling pathway; regulation of synapse structure and activity; regulation of protein binding; innate immune response; positive regulation of transcription from RNA polymerase II promoter; response to oxidative stress; blood coagulation; neuron remodeling

Disease: Alzheimer Disease