Product Details

Uniprot No.

Target Names

Alternative Names

A4 antibody; A4_HUMAN antibody; AAA antibody; ABETA antibody; ABPP antibody; AICD-50 antibody; AICD-57 antibody; AICD-59 antibody; AID(50) antibody; AID(57) antibody; AID(59) antibody; Alzheimer disease amyloid protein antibody; Amyloid intracellular domain 50 antibody; Amyloid intracellular domain 57 antibody; Amyloid intracellular domain 59 antibody; APP antibody; APPI antibody; Beta amyloid protein 42 antibody; Beta APP42 antibody; Beta-APP40 antibody; Beta-APP42 antibody; C31 antibody; Cerebral vascular amyloid peptide antibody; CVAP antibody; Gamma-CTF(50) antibody; Gamma-CTF(57) antibody; Gamma-CTF(59) antibody; PN-II antibody; PreA4 antibody; Protease nexin-II antibody; S-APP-alpha antibody; S-APP-beta antibody

Species Reactivity

Human

Immunogen

Recombinant Human APP protein

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

hIgG1

Clone No.

15A10

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4

Form

Liquid

Tested Applications

ELISA, IF, FC

Recommended Dilution

Application	Recommended Dilution
IF	1:50-1:200
FC	1:50-1:200

Protocols

ELISA Protocol
Immunofluorescence (IF) Protocol
Flow Cytometry (FC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Description

Amyloid precursor protein (APP) stands at the center of Alzheimer's disease research as the source of amyloid-beta peptides, the primary components of senile plaques characteristic of this neurodegenerative condition. Beyond its pathological significance, APP plays essential roles in neuronal development, synaptic plasticity, and cell adhesion, making it a critical target for investigators studying both normal brain function and disease mechanisms.

This recombinant monoclonal antibody against human APP, clone 15A10, offers the reproducibility and consistency that demanding research applications require. Produced using recombinant technology with a defined sequence, this antibody eliminates the lot-to-lot variability inherent in traditional hybridoma-derived reagents, ensuring your experimental results remain comparable across studies and over time. The human IgG1 isotype format and affinity chromatography purification deliver a high-quality reagent suitable for sensitive detection methods.

Validation studies demonstrate reliable performance in immunofluorescence and flow cytometry applications. Immunofluorescence staining has been successfully performed in both HeLa and A549 cell lines at dilutions of 1:30, revealing clear cellular localization when counter-stained with DAPI. Flow cytometry analysis of HeLa cells shows distinct positive signal separation from isotype control, confirming specific target recognition in fixed and permeabilized samples. These validated protocols provide researchers with flexible starting points for their own experimental optimization.

Whether you are investigating APP processing pathways, screening therapeutic candidates targeting amyloid production, or characterizing cellular models of neurodegeneration, this antibody provides a dependable tool for your neuroscience research. The unconjugated format allows compatibility with your preferred secondary detection systems across multiple experimental platforms.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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Target Background

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

genetic manipulation of Sirt3 revealed that amyloid-beta increased levels of total tau acetylated tau through its modulation of Sirt3. PMID: 29574628
brain. In the present study, two familial Ab42 mutations, namely A2V (harmful) and A2T (protective) have been analyzed and compared with the wild-type (WT) by performing all-atom molecular dynamics (MD) simulations in the absence and presence of curcumin, a well-known inhibitor of Abeta plaque formation. Mutant A2V was found to exhibit highest stability followed by WT and mutant A2T in the absence of curcumin PMID: 28054501
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
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
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
Western diet (WD) dramatically increases ABETA levels and generates pyroglutamate-ABETA deposits. PMID: 28039031
This study demonstrated that the APP21 transgenic rats develop age-dependent cognitive impairment and accelerated white matter inflammation. PMID: 30153843
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
In vitro neuroprotective effects of naringenin nanoemulsion against beta-amyloid toxicity through the regulation of amyloidogenesis and tau phosphorylation. PMID: 30001606
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
This data demonstrates a specific function of APP or its metabolites is involved in the changes that occur during high fat diet-induced obesity. PMID: 28262782
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
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
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
overexpression of APP may promote the onset of seborrhoeic keratosis and is a marker of skin ageing and UV damage. PMID: 29487944
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
Structural and biochemical differences between the Notch and the amyloid precursor protein transmembrane domains. PMID: 28439555
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
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
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
On the role of sidechain size and charge in the aggregation of Abeta42 with familial mutations. PMID: 29895690
The mechanism involved in the interaction of HSP60-Ass conjugate with HLA-DR-DRB allele considering the fact that Ass (1-42) is highly immunogenic in human and interactions evoked highly robust T-cell response through MHC class II binding predictions. PMID: 27106586
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
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
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
This study presents nonequilibrium molecular dynamics data of the Amyloid beta (1-40) peptide, periodically driven by an oscillating electric field PMID: 29812922
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
electrostatic interactions in the center of the Abeta peptide sequence play a crucial role in the three-dimensional fold of the fibrils, and by inference, fibril-induced neuronal toxicity and AD pathogenesis PMID: 27414264
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
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
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
specific balance between the concentrations of monomeric and fibrillar alpha-synuclein determines the outcome of the Abeta42 aggregation reaction PMID: 28698377
Nuclear HSP70 leads to enhancement of vaccinia H1-related phosphatase (VHR) activity via protein-protein interaction rather than its molecular chaperone activity, thereby suppressing excessive ERK activation. Downregulation of either VRK3 or HSP70 rendered cells vulnerable to glutamate-induced apoptosis. PMID: 27941812
The Network analyses identified APP expression in temporal cortex in patient with late-onset Alzheimer's disease. PMID: 28242297
alpha-synuclein (Parkinson) and Abeta peptide (Alzheimer) no longer form Ca(2+)-permeable pores in presence of drugs that target either cholesterol or ganglioside or both membrane lipids. PMID: 27352802
APP processing is regulated throughout differentiation of cortical neurons and that amyloidogenic APP processing, as reflected by Abeta1-40/42, is associated with mature neuronal phenotypes. PMID: 27383650
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
while Reelin expression is enhanced in the Alzheimer's brain, the interaction of Reelin with Abeta hinders its biological activity PMID: 27531658
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
Enhancing mitochondrial proteostasis reduces amyloid-beta proteotoxicity PMID: 29211722
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
results suggest that co-oligomers are a common form of aggregate when Abeta isoforms are present in solution and may potentially play a significant role in Alzheimer's disease. PMID: 27346247
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
different Ramachandran angle values could possibly be traced to the unique conformational folding avenues sampled by the Abeta42 peptide owing to the presence of its two extra residues. PMID: 27808259
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
Shape complementarity between close-packed residues plays a critical role in the amyloid aggregation process. This study probes such "steric zipper" interactions in amyloid-beta (ABETA 40), whose aggregation is linked to Alzheimer's disease, by replacing natural residues by their stereoisomers. Stereoisomers can cause complex site dependent changes in amyloid properties. PMID: 28140589
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
These results suggest that APPsw transgenic zebrafish well simulate the pathological characters of Alzheimer's disease and can be used as an economic Alzheimer's disease transgenic model. PMID: 27978793
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
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

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Involvement in disease

Alzheimer disease 1 (AD1); Cerebral amyloid angiopathy, APP-related (CAA-APP)

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

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

Database Links

HGNC: 620

OMIM: 104300

KEGG: hsa:351

STRING: 9606.ENSP00000284981

UniGene: Hs.434980

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Code	CSB-RA001950MA3HU
Size	US$210
	Order now
Image	Immunofluorescence staining of Hela cell with CSB-RA001950MA3HU at 1:30, counter-stained with DAPI. The cells were fixed in 4% formaldehyde and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4C. The secondary antibody was FITC-conjugated AffiniPure Goat Anti-Human IgG(H+L). Immunofluorescence staining of A549 cell with CSB-RA001950MA3HU at 1:30, counter-stained with DAPI. The cells were fixed in 4% formaldehyde and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4C. The secondary antibody was FITC-conjugated AffiniPure Goat Anti-Human IgG(H+L). Overlay Peak curve showing hela cells stained with CSB-RA001950MA3HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/110⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated Goat Anti-human IgG(H+L) at 1:200 dilution for 35min at 4℃.Control antibody (green line) was human IgG (1ug/110⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.
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APP Recombinant Monoclonal Antibody

Product Details

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Target Background