• Product name
    Anti-Amyloid Precursor Protein (phospho Y757) antibody
    See all Amyloid Precursor Protein primary antibodies
  • Description
    Rabbit polyclonal to Amyloid Precursor Protein (phospho Y757)
  • Host species
  • Specificity
    Rabbit polyclonal to APP (phospho Y757) ab19850 recognises various isoforms of APP in the phosphorylated state. ab19850 recognises both the mature (around 80 kDa) and immature (around 110 kDa) isoforms of APP. 10 named APP isoforms exist following alternative splicing, as well as a number of additional isoforms for which experimental confirmation may be lacking. Several C-terminal APP fragments around 50 kDa also exist and are well documented (Swiss Prot, Haverster EMBL databases).
  • Tested applications
    Suitable for: WB, IHC-FoFrmore details
  • Species reactivity
    Reacts with: Mouse
    Predicted to work with: Rat, Human
  • Immunogen

    Synthetic peptide within Human Amyloid Precursor Protein aa 750 to the C-terminus (C terminal) (phospho Y757) conjugated to Keyhole Limpet Haemocyanin (KLH). The exact sequence is proprietary.
    (Peptide available as ab20648)

  • Positive control
    • mouse brain
  • General notes

    Phosphorylation of APP at Tyr757 and 762 is important for MAPK8IP1, APBA1, shcA/shcC and DAB1 binding. Binding interactions regulated by phosphorylation determine the localisation and the function of APP. Therefore Amyloid Precursor Protein (phospho Y757) antibody will be a useful tool in tracing the processing, distribution and interaction of APP.


  • Form
  • Storage instructions
    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
  • Storage buffer
    Preservative: 0.02% Sodium Azide
    Constituents: 1% BSA, PBS, pH 7.4
  • Concentration information loading...
  • Purity
    Immunogen affinity purified
  • Primary antibody notes
    Phosphorylation of APP at Tyr757 and 762 is important for MAPK8IP1, APBA1, shcA/shcC and DAB1 binding. Binding interactions regulated by phosphorylation determine the localisation and the function of APP. Therefore Amyloid Precursor Protein (phospho Y757) antibody will be a useful tool in tracing the processing, distribution and interaction of APP.
  • Clonality
  • Isotype
  • Research areas


Our Abpromise guarantee covers the use of ab19850 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB Use a concentration of 0.5 - 1 µg/ml. Detects a band of approximately 55, 87, 110, 170 kDa (predicted molecular weight: 55, 87, 110 kDa).
IHC-FoFr 1/1000.


  • Function
    Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. 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. 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.
    Beta-amyloid 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. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 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).
  • Tissue specificity
    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.
  • Involvement in disease
    Alzheimer disease 1
    Cerebral amyloid angiopathy, APP-related
  • Sequence similarities
    Belongs to the APP family.
    Contains 1 BPTI/Kunitz inhibitor domain.
  • Domain
    The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells.
    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 NPXY site is also involved in clathrin-mediated endocytosis.
  • Post-translational
    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 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). Many other minor beta-amyloid peptides, beta-amyloid 1-X peptides, are found in cerebral spinal fluid (CSF) including the beta-amyloid 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 caspase-6, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of beta-amyloid peptides.
    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 beta-amyloid peptides (beta-amyloid 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but not found on beta-amyloid 38, beta-amyloid 40 nor on beta-amyloid 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. 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 beta-amyloid-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).
    Beta-amyloid peptides are degraded by IDE.
  • Cellular localization
    Membrane. Membrane, clathrin-coated pit. Cell surface protein that rapidly becomes internalized via clathrin-coated pits. 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. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. 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. 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.
  • Information by UniProt
  • Database links
  • Alternative names
    • A4 amyloid protein antibody
    • A4_HUMAN antibody
    • AAA antibody
    • ABETA antibody
    • ABPP antibody
    • AD1 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 beta (A4) precursor protein antibody
    • Amyloid beta A4 protein antibody
    • Amyloid beta protein antibody
    • Amyloid intracellular domain 50 antibody
    • Amyloid intracellular domain 57 antibody
    • Amyloid intracellular domain 59 antibody
    • Amyloid precursor protein antibody
    • APP antibody
    • APPI antibody
    • Beta amyloid peptide antibody
    • Beta-amyloid precursor protein antibody
    • Beta-APP40 antibody
    • Beta-APP42 antibody
    • C31 antibody
    • Cerebral vascular amyloid peptide antibody
    • CTFgamma antibody
    • CVAP antibody
    • Gamma-CTF(50) antibody
    • Gamma-CTF(57) antibody
    • Gamma-CTF(59) antibody
    • peptidase nexin II antibody
    • PN 2 antibody
    • PN II antibody
    • PN-II antibody
    • PN2 antibody
    • PreA4 antibody
    • Protease nexin II antibody
    • Protease nexin-II antibody
    • S-APP-alpha antibody
    • S-APP-beta antibody
    see all


  • Lane 1 : Amyloid Precursor Protein (non modified) C-terminal antibody
    Lane 2 : Anti-Amyloid Precursor Protein (phospho Y757) antibody (ab19850) at 0.5 µg/ml

    All lanes : mouse dentate gyrus lysate

    All lanes : Rabbit IgG 2nd ab at 1/25000 dilution

    Predicted band size: 55, 87, 110 kDa
    Observed band size: 110,55,87 kDa
    why is the actual band size different from the predicted?
    Additional bands at: 170 kDa (possible isoform)

    Rabbit polyclonal to APP (phospho Y757) ab19850 recognises various isoforms of APP in the phosphorylated state including the mature (around 80 kDa) and immature (around 110 kDa) APP isoforms. ab19850 also detects several C-terminal fragments around 50 kDa which are well documented in public databases (e.g Swiss Prot, EMBL). The band around 170 kDa could not be assigned to APP, but is possibly an isoform of APP.

  • Anti-Amyloid Precursor Protein (phospho Y757) antibody (ab19850) at 1/1000 dilution + Mouse Hippocampus whole cell lysate

    Goat anti-rabbit IgG HRP

    Developed using the ECL technique.

    Performed under reducing conditions.

    Predicted band size: 55, 87, 110 kDa
    Observed band size: 130,50,95 kDa why is the actual band size different from the predicted?
    Additional bands at: 170 kDa, 190 kDa (possible non-specific binding). We are unsure as to the identity of these extra bands.

    Exposure time: 1 minute

    This image is courtesy of an Abreview submitted by Florian Plattner on 7 December 2005.

    See Abreview

  • ab19850 at 1/1000 staining mouse brain tissue sections by IHC (Formalin/PFA fixed sections). The tissue was paraformaldehyde fixed and a heat mediated antigen retrieval step in a Na Citrate buffer was performed. The tissue was permeabilized and incubated with ab19850 for 18 hours. A biotinylated goat anti-rabbit IgG was used as the secondary. The sections were counterstained with Congo red. The image shows Congo red positive plaque core surrounded by phospho-APP positive neurites in AD model mouse.

    See Abreview


ab19850 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

1-6 of 6 Abreviews or Q&A


In the file attached are the answers to your questionnaire. We try to understand what is wrong and we try different approaches but no result match.

I hope to hear news in brief.

) Abcam product code ab19850

2) Abcam order reference number or product batch number

3) Description of the problem: phospho APP band do not match the holoAPP band
4) Sample preparation:
Type of sample (whole cell lysates, fraction, recombinant protein…): wholr cell lysates for cortical primary neuronal cultures;
Lysis buffer : RIPA Buffer
Protease inhibitors: yes
Phosphatase inhibitors: NaF, NaOrt
Reducing agent: No
Boiling for ≥5 min? yes (5min)
Protein loaded ug/lane or cells/lane: 50ug
Positive control
Negative control

5) Percentage of gel
Type of membrane: nitrocelulose
Protein transfer verified
Blocking agent and concentration: BSA 5%
Blocking time: 4h
Blocking temperature: 20oC
6) Primary antibody (If more than one was used, describe in “additional notes”) :
Concentration or dilution: 1:1000
Diluent buffer: TBS-T 1x
Incubation time: 4h + ON + 1h
Incubation temperature: 20oC

7) Secondary antibody:
Reacts against: Rabbit
Concentration or dilution: 1:5000
Diluent buffer : TBS-t1x 3% Milk
Incubation time: 2h
Incubation temperature: 20oc
Fluorochrome or enzyme conjugate: horseradish peroxidase
8) Washing after primary and secondary antibodies:
Buffer: TBS-T 1x
Number of washes: 3, 10min

9) Detection method: chemioluminescence – Ilumminata Crescendo, Millipore
10) How many times have you run this staining? Several
Do you obtain the same results every time? yes
What steps have you altered to try and optimize the use of this antibody?

Read More

Thank you for taking time to complete our questionnaire. I am sorry to hear that this antibody is not providing satisfactory results.

The details provided will enable us to investigate this case and will provide us with vital information for monitoring product quality.

Having reviewed this case, I would like to offer some suggestions to help optimize the results from ab19850 Anti-Amyloid Precursor Protein (phospho Y757) antibody . I would also appreciate if you can confirm some further details:

1. It is not quite clear if you see nothing at all, or rather a wrong band size. Could you please clarify this by sending an image

2. Most of our antibodies are tested and optimized to work under reducing conditions, and we usually state on our datasheet if the gel should be run under non-reducing conditions. I would therefore suggest to add a reducing agent like beta- mercapthoethanol or DTT into your sample buffer. Otherwise it may be that the antibody may not be able to detect its target.

3.In order to prevent a masking of your target, please do not block longer than one hour.

4. I am not sure if I understood how you incubated the primary antibody; 4h + ON + 1h: Does this mean you performed three independent experiments? Do you incubate over night as well at 20C?

5. I would suggest to stick with one blocking agent, in your case BSA for both antibodies incubations. Mixing them usually increases the background.

I am looking forward hearing from you with the requested details.

Read More


Thank you for contacting us.

I am sorry to hear you are experiencing difficulties with one of our products. We take product complaints very seriously, and investigate every product that we feel may not be performing correctly. Our policy is that we are happy to offer a refund, credit note or free of charge replacement when a product is not working in a successfully tested applications or species (and the product has been purchased in the last 180 days).

However, from our records I could see that you have ordered this antibody last year in November, and this is unfortunately far out of our guarantee range.

Nonetheless, I am more than happy to have a look at your protocol to see if we can help you otherwise.

I am attaching our questionnaire so that we can gather further information regarding the samples tested and the protocol used. Once we receive the completed questionnaire, we will look at the protocol and see if there are any suggestions we can make that may improve the results.
I look forward to receiving your reply.

Read More


Thank you for contacting us.

The possible explanation for thedifference in molecular weightcould bedue to the difference in glycosylaiton of the protein. You may check publications to know more about this difference.

I hope this information is helpful to you. Please do not hesitate to contact us if you need any more advice or information.

Read More


The sequence is present in all isoforms except the second one:Isoform APP305 as 306-770aa is missing. Altogether 10 isoforms (http://www.uniprot.org/uniprot/P05067)

Read More
Abcam guarantees this product to work in the species/application used in this Abreview.
Immunohistochemistry (PFA perfusion fixed frozen sections)
Mouse Tissue sections (brain)
Antigen retrieval step
Heat mediated - Buffer/Enzyme Used: Na Citrate sol. pH=6.0 for 30 min
Yes - Triton 100X

Dr. Inga Kadisha

Verified customer

Submitted Jun 01 2007

Abcam guarantees this product to work in the species/application used in this Abreview.
Western blot
Mouse Tissue lysate - whole (Hippocampus)
Blocking step
BSA as blocking agent for 1 hour(s) and 0 minute(s) · Concentration: 3%

Mr. Florian Plattner

Verified customer

Submitted Dec 07 2005


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