Product: APP Antibody
Catalog: AF6084
Description: Rabbit polyclonal antibody to APP
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Horse, Chicken, Xenopus
Mol.Wt.: 117kDa; 87kD(Calculated).
Uniprot: P05067
RRID: AB_2834853

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Product Info

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Pig(100%), Horse(100%), Chicken(100%), Xenopus(100%)
APP Antibody detects endogenous levels of total APP.
Cite Format: Affinity Biosciences Cat# AF6084, RRID:AB_2834853.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


A4_HUMAN; AAA; ABETA; ABPP; AD1; AICD-50; AICD-57; AICD-59; AID(50); AID(57); AID(59); Alzheimer disease amyloid protein; amyloid beta A4 protein; Amyloid intracellular domain 50; Amyloid intracellular domain 57; Amyloid intracellular domain 59; amyloid of aging and alzheimer disease; APP; APPI; beta-amyloid peptide; Beta-APP40; Beta-APP42; C31; Cerebral vascular amyloid peptide; CTFgamma; CVAP; Gamma-CTF(50); Gamma-CTF(57); Gamma-CTF(59); peptidase nexin-II; PN-II; PreA4; Protease nexin-II; S-APP-alpha; S-APP-beta;


P05067 A4_HUMAN:

Expressed in the brain and in cerebrospinal fluid (at protein level) (PubMed:2649245). 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. 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.

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.



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P05067 As Substrate

Site PTM Type Enzyme
K60 Ubiquitination
T107 O-Glycosylation
Y115 Phosphorylation
K178 Ubiquitination
S198 Phosphorylation
S206 Phosphorylation
T352 O-Glycosylation
T353 O-Glycosylation
K363 Ubiquitination
T366 O-Glycosylation
T367 O-Glycosylation
S370 O-Glycosylation
T371 O-Glycosylation
T381 O-Glycosylation
T381 Phosphorylation
K393 Ubiquitination
K429 Ubiquitination
S441 Phosphorylation
R468 Methylation
Y497 Phosphorylation
N542 N-Glycosylation
T600 O-Glycosylation
T633 O-Glycosylation
T651 O-Glycosylation
T652 O-Glycosylation
S656 O-Glycosylation
T659 O-Glycosylation
T663 O-Glycosylation
S667 O-Glycosylation
K670 Sumoylation
S679 Phosphorylation
S697 Phosphorylation
K724 Acetylation
K725 Acetylation
Y728 Phosphorylation
T729 Phosphorylation
S730 Phosphorylation
T743 Phosphorylation P53779 (MAPK10) , P45984 (MAPK9) , P06493 (CDK1) , P45983 (MAPK8)
K751 Ubiquitination
Y757 Phosphorylation P06241 (FYN) , P04629 (NTRK1) , P00519 (ABL1)
T761 Phosphorylation
Y762 Phosphorylation
K763 Ubiquitination

Research Backgrounds


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 (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). 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).


Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase and all terminating at Gln-686.

Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either CASP6, CASP8 or CASP9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides.

N-glycosylated. N- and O-glycosylated. O-glycosylation on Ser and Thr residues with core 1 or possibly core 8 glycans. Partial tyrosine glycosylation (Tyr-681) is found on some minor, short amyloid-beta peptides (amyloid-beta 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but not found on amyloid-beta protein 38, amyloid-beta protein 40 nor on amyloid-beta protein 42. Modification on a tyrosine is unusual and is more prevelant in AD patients. Glycans had Neu5AcHex(Neu5Ac)HexNAc-O-Tyr, Neu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr and O-AcNeu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr structures, where O-Ac is O-acetylation of Neu5Ac. Neu5AcNeu5Ac is most likely Neu5Ac 2,8Neu5Ac linked. O-glycosylations in the vicinity of the cleavage sites may influence the proteolytic processing. Appicans are L-APP isoforms with O-linked chondroitin sulfate.

Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. In dopaminergic (DA) neurons, phosphorylation on Thr-743 by LRKK2 promotes the production and the nuclear translocation of the APP intracellular domain (AICD) which induces DA neuron apoptosis. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin.

Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. In vitro, the APP-Cu(+) complex in the presence of hydrogen peroxide results in an increased production of amyloid-beta-containing peptides.

Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP).

Amyloid-beta peptides are degraded by IDE.

Sulfated on tyrosine residues.

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.
Note: Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles (PubMed:20580937). During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body (PubMed:10341243). Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions.


Cell surface.
Note: Associates with FPR2 at the cell surface and the complex is then rapidly internalized.

Nucleus. Cytoplasm.
Note: Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65) (PubMed:11544248). In dopaminergic neurons, the phosphorylated Thr-743 form is localized to the nucleus (By similarity).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
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 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. 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.

Subunit Structure:

Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and, NUMB and DAB1 (By similarity). Binding to DAB1 inhibits its serine phosphorylation (By similarity). Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons. Amyloid-beta associates with HADH2. Soluble APP binds, via its N-terminal head, to FBLN1. Interacts with CPEB1 and AGER (By similarity). Interacts with ANKS1B and TNFRSF21. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; dimerization is enhanced in the presence of Cu(2+) ions. Can form homodimers; this is promoted by heparin binding. Amyloid-beta protein 40 interacts with S100A9. CTF-alpha product of APP interacts with GSAP. Isoform APP695 interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides. The C99 fragment also interacts with SORL1. Isoform APP751 interacts with SORL1. Isoform APP770 interacts with SORL1. Interacts with PLD3. Interacts with VDAC1. Interacts with NSG1; could regulate APP processing (By similarity). Amyloid-beta protein 42 interacts with FPR2. Interacts with SYT7 (By similarity). Interacts (via transmembrane region) with PSEN1; the interaction is direct. Interacts with LRRK2. Interacts (via cytoplasmic domain) with KIF5B.


The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1.

The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells.

The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization.

The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis.

The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers.

The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2.

Belongs to the APP family.

Research Fields

· Human Diseases > Neurodegenerative diseases > Alzheimer's disease.

· Organismal Systems > Nervous system > Serotonergic synapse.


1). Tetrahydroxy stilbene glycoside ameliorates Alzheimer's disease in APP/PS1 mice via glutathione peroxidase related ferroptosis. International Immunopharmacology (PubMed: 34333354) [IF=5.6]

Application: IF/ICC    Species: Mouse    Sample: brain

Fig. 8. TSG regulates the ferroptosis in various glial cells in APP/PS1 and WT mouse brains. Western blotting assay was performed to detect the expression of related proteins. (A) The protein expression levels of GPX4, GPX1, FTH1, xCT, CD98, DMT1, ACSL4, NCOA4, Ferritin Light Chain and Ferritin Heavy Chain were assessed. The levels were normalized to β-actin. (B) GPX4, GFAP and DAPI fluorescence staining co-localization of WT, APP/PS1 and TSG 60 mg/kg group. (C) GPX4, Iba1 and DAPI fluorescence staining co-localization of WT, APP/PS1 and TSG 60 mg/kg group. P# < 0.05, P## < 0.01, P### < 0.001 vs WT group. P* < 0.05, P** < 0.01, P*** < 0.001 vs APP/PS1 group. 2×, 100 × magnification, scare bar: 500 and 100 μm, n = 5/group.

2). Cerebroprotein hydrolysate attenuates neurodegenerative changes in Alzheimer’s mice model via ferroptosis pathway. Frontiers in Pharmacology [IF=5.6]

3). Carnitine palmitoyltransferase 1 (CPT1) alleviates oxidative stress and apoptosis of hippocampal neuron in response to beta-Amyloid peptide fragment Aβ25-35. Bioengineered (PubMed: 34424821) [IF=4.9]

Application: WB    Species: Mice    Sample: Aβ25-35-induced HT22 cells

Figure 5. CPT1C overexpression decreased the deposition of AD marker proteins in Aβ25-35-induced HT22 cells. Following transfection of Ov-CPT1C or Ov-NC for 24 h, HT22 cells were treated with Aβ25–35 for another 24 h (a) The mRNA expressions of App, p-Tau and Bace-1 were evaluated using RT-qPCR. (b) The protein expressions of App, p-Tau and Bace-1 were evaluated using western blot. ***P < 0.001 vs. Control group, ###P < 0.001 vs Aβ25-35 + Ov-NC.

4). LongShengZhi Capsule attenuates Alzheimer-like pathology in APP/PS1 double transgenic mice by reducing neuronal oxidative stress and inflammation. Frontiers in Aging Neuroscience (PubMed: 33328962) [IF=4.8]

5). Long-Term Administration of Triterpenoids From Ganoderma lucidum Mitigates Age-Associated Brain Physiological Decline via Regulating Sphingolipid Metabolism and Enhancing Autophagy in Mice. Frontiers in Aging Neuroscience (PubMed: 34025387) [IF=4.8]

Application: WB    Species: mouse    Sample: brain

FIGURE 9 | Ameliorate effects of Ganodenic acid A by regulating sphingolipid metabolism in 3 × Tg-AD mice. (A) Experimental procedure in 3 × Tg-AD mice;(B) The AD biomarkers of p-Tau, Aβ, APOE, TREM2, CD33, the inflammatory cytokines of TNF-α and NF-κB p65 and the autophagy level of LC3A/B were measured in brain tissues

6). Polarization of Microglia to the M2 Phenotype in a Peroxisome Proliferator-Activated Receptor Gamma–Dependent Manner Attenuates Axonal Injury Induced by Traumatic Brain Injury in Mice. Journal of Neurotrauma (PubMed: 29649924) [IF=4.2]

Application: IHC    Species: mouse    Sample: cerebral cortex

Fig. 2:| Immunohistochemical staining for beta-amyloid precursor protein (β-APP) in cerebral cortex after TBI in mice (A). Scale bar = 20 μm. Immunoreactivity for β-APP determined by average optical density (AOD), was attenuated by rosiglitazone and enhanced by GW992 (B). * p < 0.05, ** p < 0.01.

7). Regular Exercise Enhances Cognitive Function and Intracephalic GLUT Expression in Alzheimer\'s Disease Model Mice. JOURNAL OF ALZHEIMERS DISEASE (PubMed: 31561359) [IF=4.0]

Application: WB    Species: mouse    Sample: brain

Fig. 1. The expression A and P-Tau. Representative immunoblots of A and P-Tau in the cortex (A-C) and hippocampus (D-F) in each group. Protein immunoreactivity was normalized to -actin. Individual data are presented as the mean ± S.E.M. from four individual mice in each group.

8). GPNMB mitigates Alzheimer's disease and enhances autophagy via suppressing the mTOR signal. NEUROSCIENCE LETTERS (PubMed: 34695452) [IF=2.5]

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