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Human ELISA Kit · Neuroscience
Human Amyloid beta peptide 1-40,Aβ1-40 ELISA Kit
Sandwich quantitative immunoassay for amyloid beta peptide 1-40,Aβ1-40 in human cerebrospinal fluid (CSF) available in multiple catalog sizes:
Trial 24T 96T
Note: Please send inquiries regarding Trial 24T orders to support@diagnocine.com.
Detection Range
15.6-1,000 pg/ml
Sensitivity
7.8 pg/ml
Assay Time
3.5 hours
Sample Volume
50-100 μL
Product specifications
| Target name | amyloid beta peptide 1-40,Aβ1-40 |
| Uniprot No. | P05067 |
| Species | Homo sapiens (Human) |
| Sample types | cerebrospinal fluid (CSF) |
| Detection range | 15.6pg/ml-1000pg/ml |
| Sensitivity | 7.8pg/ml |
| Assay time | 3.5h |
| Sample loading volume | 50-100μL |
| Detection wavelength | 450 nm |
| Assay principle | Sandwich (Quantitative) |
| Data analysis | Standard curve + Curve Expert software |
| Research area | Neuroscience |
| Storage condition | 2-8°C (see protocol for full details) |
| Shipping condition | 4 °C |
| Shelf life | 6 months |
amyloid beta peptide 1-40,Aβ1-40 cerebrospinal fluid (CSF) Neuroscience Human ELISA
Lead Time
10 business days
Processing + 3-5 days shipping
Availability
In Stock : USA
Worldwide shipping available
Assay principle
Sample prep
Antibody capture
450 nm detection
Standard curve
Quantification
Antibody capture
450 nm detection
Standard curve
Quantification
In this sandwich ELISA, amyloid beta peptide 1-40,Aβ1-40 in the sample is captured between a pre-coated capture antibody and a detection antibody. Signal intensity is proportional to analyte concentration. Quantification uses a standard curve fitted with Curve Expert software, covering 15.6pg/ml-1000pg/ml with a minimum detectable dose of 7.8pg/ml.
For research use only (RUO). Not intended for diagnostic or therapeutic purposes. Validated in human cerebrospinal fluid (CSF) matrices only.
Alternative Names
amyloid beta peptide 1-40,Aβ1-40,amyloid β peptide 1-40
Function
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 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. By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons. 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.; Amyloid-beta 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. Amyloid-beta protein 42 is a more effective reductant than amyloid-beta protein 40. Amyloid-beta peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. APP42-beta 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).
Gene References into Functions
- A physical interaction between nicastrin (hNCT) and the gamma-secretase substrate amyloid beta-protein precursor (APPC100) confirmed the functionality of hNCT as a substrate recognizer. PMID: 28276527
- Our study provides new insights into the regulation of APP pre-mRNA processing, supports the role for nELAVLs as neuron-specific splicing regulators and reveals a novel function of AUF1 in alternative splicing. PMID: 28291226
- Besides, the promoting effect of Zn2+ on ABETA42 fast aggregation peaked at pH 6.8-7.8, which includes the pH values of the cerebrospinal fluid (pH 7.3) and hippocampus (pH 7.15-7.35). The findings demonstrate the significant effect of Zn2+ on ABETA aggregation and provide new insight into its mechanisms. PMID: 28378589
- Structural and biochemical differences between the Notch and the amyloid precursor protein transmembrane domains. PMID: 28439555
- Recombinant mutant KPI(R13I) domain of ABPP was ineffective in the inhibition of pro-thrombotic proteinases and did not inhibit the clotting of plasma in vitro. PMID: 28499154
- These results provide evidence for an emerging role of BAG-1M in the regulation of BACE1 expression and AD pathogenesis and that targeting the BAG-1M-NF-kappaB complex may provide a mechanism for inhibiting Abeta production and plaque formation. PMID: 28502705
- ethanol-induced eIF2alpha phosphorylation stimulates COX-2 expression and PGE2 production which induces the BACE1 expression and Abeta production via EP-2 receptor-dependent PKA/CREB pathway. PMID: 28668332
- The authors found that as already shown for oligomeric Abeta, also oligomeric Tau can bind to amyloid precursor protein (APP). Moreover, efficient intra-neuronal uptake of oligomeric Abeta and oligomeric Tau requires expression of APP. PMID: 28696204
- specific balance between the concentrations of monomeric and fibrillar alpha-synuclein determines the outcome of the Abeta42 aggregation reaction PMID: 28698377
- This study structurally characterized ABETA 40 and ABETA 42 monomers through pentamers which were converted from previously derived coarse-grained (DMD4B-HYDRA) simulations into all-atom conformations and subjected to explicit-solvent Molecular Dynamics. PMID: 28727426
- Study showed that the APP Osaka mutation has dual effects: it causes a loss-of-function of APP and gain-of-toxic-function of Abeta, though the latter seems to come out only after the former causes GABAergic depletion. Also present OSK-KI mice as a mouse model to replicate the hereditary form of recessive familial Alzheimer's disease. PMID: 28760161
- These results confirm the involvement of amyloid precursor protein (APP) in synaptogenesis and provide evidence to suggest that human APP overexpression specifically disturbs the structural and functional organization of active zone and results in altered Bruchpilot distribution and lowered probability of spontaneous neurotransmitter release. PMID: 28770114
- Authors measured cerebral morphological and neurochemical alterations using structural magnetic resonance imaging (MRI) and proton magnetic resonance spectroscopy ((1)H-MRS) in an AD model of APP/PS1 transgenic mice. PMID: 28797599
- Data show that amyloid precursor protein (APP) dimerization affects its interaction with LDL receptor related protein 1 (LRP1) and LDL-receptor related protein SorLA (SorLA), suggesting that APP dimerization modulates its interplay with sorting molecules and in turn its localization and processing. PMID: 28799085
- This study reports the transition dipole strengths and frequencies of the amyloid beta-sheet amide I mode for the aggregated proteins amyloid-beta1-40, calcitonin, alpha-synuclein, and glucagon. PMID: 28851219
- overall results and observations regarding human serum albumin, amyloid-beta, and metal ions advance our knowledge of how protein-protein interactions associated with amyloid-beta and metal ions could be linked to Alzheimer's disease pathogenesis PMID: 28930473
- RelA, RelB and c-Rel can be activated by Abeta1-40, all of which mediate pro-inflammatory cytokine transcription and retinal pigment epithelium damage. PMID: 29022897
- Data suggest that kinetics of degradation/proteolysis versus of aggregation of amyloid beta(1-40) and amyloid beta(1-42) at specific concentrations of amyloid beta, cathepsin B, and cystatin C can be modeled and predicted. PMID: 29046353
- This review highlights the existing link between oxidative stress and Alzheimer's disease, and the consequences towards the ABETA peptide and surrounding molecules in terms of oxidative damage. [review] PMID: 29080524
- Abeta fibrils start to accumulate predominantly within certain parts of the default mode network in preclinical Alzheimer's disease and already then affect brain connectivity. PMID: 29089479
- The results of study demonstrate that different degradation pathways play distinct roles in the removal of Abeta42 aggregates and in disease progression. These findings also suggest that pharmacologic treatments that are designed to stimulate cellular degradation pathways in patients with AD should be used with caution. PMID: 29127191
- Amyloid precursor protein (APP) binds the HIV-1 Gag polyprotein, retains it in lipid rafts and blocks HIV-1 virion production and spread. PMID: 29142315
- Enhancing mitochondrial proteostasis reduces amyloid-beta proteotoxicity PMID: 29211722
- This study applies methodologies on the initial stages of aggregation of a hexamer of Alzheimer's amyloid beta fragment 25-35 (ABETA 25-35) and finds that transitions within the hexameric aggregate are dominated by entropic barriers and speculates that especially the conformation entropy plays a major role in the formation of the fibril as a rate limiting factor. PMID: 29221375
- Data show that phospholipase D3 (PLD3) functions in endosomal protein sorting and plays an important role in regulating amyloid precursor protein (APP) processing. PMID: 29368044
- c-Abl is activated in AbetaOs exposed neurons and in Alzheimer's disease patient's brain, and the inhibition of activated c-Abl ameliorates cognitive deficits PMID: 29378302
- overexpression of APP may promote the onset of seborrhoeic keratosis and is a marker of skin ageing and UV damage. PMID: 29487944
- ABETA(1-42) doses >5 microM inhibited the growth of U87 cells compared with the 0 microM group after 24 and 48 h treatment. PMID: 29568933
- genetic manipulation of Sirt3 revealed that amyloid-beta increased levels of total tau acetylated tau through its modulation of Sirt3. PMID: 29574628
- findings show adverse effects of one-night sleep deprivation on brain ABB and expand on prior findings of higher Abeta accumulation with chronic less sleep. PMID: 29632177
- Amyloid fibrils of Abeta1-40 peptide can effectively initiate amyloid formation in different globular proteins and metabolites, converting native structures into beta-sheet rich assemblies. Structural and biophysical properties of the resultant protein fibrils display amyloid like characteristic features. PMID: 29723530
- This study presents nonequilibrium molecular dynamics data of the Amyloid beta (1-40) peptide, periodically driven by an oscillating electric field PMID: 29812922
- On the role of sidechain size and charge in the aggregation of Abeta42 with familial mutations. PMID: 29895690
- Gnetin C may thereby prevent Abeta toxicity by suppressing BACE1 and enhancing MMP-14, together with reducing both internalization and oligomerization of exogenous Abeta monomers. PMID: 29899186
- In vitro neuroprotective effects of naringenin nanoemulsion against beta-amyloid toxicity through the regulation of amyloidogenesis and tau phosphorylation. PMID: 30001606
- This study demonstrated that the APP21 transgenic rats develop age-dependent cognitive impairment and accelerated white matter inflammation. PMID: 30153843
++ 14 more research findings link this target to additional biology. Showing the 36 most recent — the full set appears on the complete datasheet.
Involvement in disease
Alzheimer disease 1 (AD1); Cerebral amyloid angiopathy, APP-related (CAA-APP)
Tissue Specificity
Expressed in the brain and in cerebrospinal fluid (at protein level). 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
Subcellular Location
Cell membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Perikaryon. Cell projection, growth cone. Membrane, clathrin-coated pit. Early endosome. Cytoplasmic vesicle.; [C83]: Endoplasmic reticulum. Golgi apparatus. Early endosome.; [C99]: Early endosome.; [Soluble APP-beta]: Secreted.; [Amyloid-beta protein 42]: Cell surface.; [Gamma-secretase C-terminal fragment 59]: Nucleus. Cytoplasm.
Protein Families
APP family
Database Links
Human Amyloid beta peptide 1-40,Aβ1-40 ELISA Kit | For research use only | Store 2-8°C | Diagnocine