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Amyloid beta (A4) Precursor Protein (APP) antibody
|Synonyms||APP, APP-like, APPL, Abeta, BcDNA:GH04413, EG:65F1.5, DmelCG7727, CG7727, AAA, AD1, PN2, ABPP, APPI, CVAP, ABETA, CTFgamma, aaa, ad1, pn2, abpp, appi, cvap, abeta, MGC88882, ctfgamma|
Alternatives Immunohistochemistry (IHC), Western Blotting (WB)
|10 references available|
|Quantity||500 µg (Variants)|
|Price||454.67 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 7 to 8 Business Days|
|Alternative name||Amyloid beta A4 protein (Alzheimer disease amyloid A4 protein homolog, ABPP, APP)|
|Immunogen||A synthetic peptide from human Amyloid beta A4 protein (Alzheimer disease amyloid A4 protein homolog, ABPP, APP) conjugated to an immunogenic carrier protein was used as the immunogen. The immunogen is homologous in many species including rat, mouse, monkey, zebra fish, chicken and xenopus.|
|Description||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). DEVELOPMENTAL STAGE: From 6 days to 7 months, levels of KPI-containing isoforms increase in the brain cortex and hippocampus. Levels of L-APP increase in all brian regions during the same period, but levels are low compared to non-L-APP isoforms. 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.|
|Specificity||Appears to be specific for APP.|
|Application Notes||IHC, WB. A working concentration of 10-50 µg/ml is recommended. The optimal concentration should be determined by the end user. Not yet tested in other applications.|
|Storage||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.|
|Restrictions||For Research Use only|
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).
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).
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).
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).
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).
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).
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).
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).
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).
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).