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Amyloid beta (A4) Precursor Protein (APP) (AA 400-450) antibody

Details for Product No. ABIN350070, Supplier: Login to see
Antigen
  • APP
  • APP-like
  • APPL
  • Abeta
  • BcDNA:GH04413
  • CG7727
  • Dmel\\CG7727
  • EG:65F1.5
  • appl
  • aaa
  • abeta
  • abpp
  • ad1
  • appi
  • ctfgamma
  • cvap
  • pn2
  • AAA
  • ABETA
  • ABPP
  • AD1
  • APPI
  • CTFgamma
  • CVAP
  • PN-II
  • PN2
  • Abpp
  • Adap
  • Ag
  • Cvap
  • E030013M08Rik
  • betaApp
  • app
  • wu:fj34d10
  • wu:fk65e12
  • zgc:85740
Alternatives
anti-Human Amyloid beta (A4) Precursor Protein antibody for Enzyme Immunoassay
Epitope
AA 400-450
122
109
52
35
25
20
19
17
17
15
15
14
14
14
13
11
10
8
8
8
6
6
6
5
5
5
5
5
5
5
5
5
4
4
4
4
4
3
3
3
3
3
3
3
3
3
3
3
2
2
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human, Rat (Rattus), Mouse (Murine)
823
307
276
41
11
9
8
8
6
3
2
2
1
1
1
1
Host
Rabbit
579
223
50
3
2
Clonality
Polyclonal
Conjugate
Un-conjugated
48
37
35
17
13
13
13
13
13
13
13
13
12
11
11
2
2
1
Application
Immunohistochemistry (IHC), Western Blotting (WB)
563
316
230
150
147
75
57
33
29
20
15
10
9
8
6
3
2
2
2
2
1
Supplier
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Immunogen A synthetic peptide from aa region 400-450 of human APP conjugated to blue carrier protein was used as the antigen. The peptide is homologous in rat and mouse.
Specificity Specific for APP.
Purification Whole serum
Alternative Name APP (APP Antibody Abstract)
Background This gene encodes a cell surface receptor andtransmembrane 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.
Subcellular location: Membrane, Single-pass type I membrane protein. Membrane, clathrin-coated pit. Note: 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 Fe65. Beta-APP42 associates withFPRL1 at the cell surface and the complex is then rapidly internalized (By similarity). 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.
Tissue specificity: In the brain, non-L-APP isoforms are expressed in neurons, isoform APP695 being the predominant form. In astrocytes and microglial cells, almost 50% is L-isoform (appican). Also known as: Alzheimer disease amyloid A4 protein homolog, ABPP, APP, Amyloidogenic glycoprotein, AG, Amyloid beta A4 protein, amyloid beta (A4) precursor protein, AAA, AD1, PN2, ABPP, APPI, CVAP, ABETA, CTF gamma, Peptidase nexin-II, Alzheimer disease.
Research Area Signaling
Pathways Caspase Cascade in Apoptosis, EGFR Signaling Pathway
Application Notes A dilution of 1 : 300 to 1 : 2000 is recommended.
The optimal dilution should be determined by the end user.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
Expiry Date 12 months
Background publications Gu, Misonou, Sato et al.: "Distinct intramembrane cleavage of the beta-amyloid precursor protein family resembling gamma-secretase-like cleavage of Notch." in: The Journal of biological chemistry, Vol. 276, Issue 38, pp. 35235-8, 2001 (PubMed).

Tsuchida, Shioi, Yamada et al.: "Appican, the proteoglycan form of the amyloid precursor protein, contains chondroitin sulfate E in the repeating disaccharide region and 4-O-sulfated galactose in the linkage region." in: The Journal of biological chemistry, Vol. 276, Issue 40, pp. 37155-60, 2001 (PubMed).

Iijima, Ando, Takeda et al.: "Neuron-specific phosphorylation of Alzheimer's beta-amyloid precursor protein by cyclin-dependent kinase 5." in: Journal of neurochemistry, Vol. 75, Issue 3, pp. 1085-91, 2000 (PubMed).

Sandbrink, Moenning, Masters et al.: "Expression of the APP gene family in brain cells, brain development and aging." in: Gerontology, Vol. 43, Issue 1-2, pp. 119-31, 1997 (PubMed).

Sandbrink, Masters, Beyreuther: "APP gene family. Alternative splicing generates functionally related isoforms." in: Annals of the New York Academy of Sciences, Vol. 777, pp. 281-7, 1996 (PubMed).

Shioi, Pangalos, Ripellino et al.: "The Alzheimer amyloid precursor proteoglycan (appican) is present in brain and is produced by astrocytes but not by neurons in primary neural cultures." in: The Journal of biological chemistry, Vol. 270, Issue 20, pp. 11839-44, 1995 (PubMed).

Schubert, Schroeder, LaCorbiere et al.: "Amyloid beta protein precursor is possibly a heparan sulfate proteoglycan core protein." in: Science (New York, N.Y.), Vol. 241, Issue 4862, pp. 223-6, 1988 (PubMed).

Shivers, Hilbich, Multhaup et al.: "Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact." in: The EMBO journal, Vol. 7, Issue 5, pp. 1365-70, 1988 (PubMed).

Kang, Mueller-Hill: "The sequence of the two extra exons in rat preA4." in: Nucleic acids research, Vol. 17, Issue 5, pp. 2130, 1989 (PubMed).

Potempska, Styles, Mehta et al.: "Purification and tissue level of the beta-amyloid peptide precursor of rat brain." in: The Journal of biological chemistry, Vol. 266, Issue 13, pp. 8464-9, 1991 (PubMed).