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Phospho-APP-Y757 Antibody Blocking PeptideSynthetic peptide
| Country | United States
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| Catalog # | Size | Availability | Price | |
| BP3027a | 0.1 mg 400 ul | In Stock | $ 45.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
- Citiations : 0
- Reviews
- Protocols
- Backgrounds
Phospho-APP-Y757 Antibody Blocking Peptide - Product info | |
| Primary Accession | P05067 |
| Clone Names | 4101212 |
| Calculated MW | 86943 Da |
Phospho-APP-Y757 Antibody Blocking Peptide - Additional info | |
| Gene ID 351 | |
| Target/Specificity The synthetic peptide sequence used to generate the antibody AP3027a was selected from the region of human Phospho-APP-Y757. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. | |
| Format The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml. | |
| Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. | |
| Precautions This product is for research use only. Not for use in diagnostic or therapeutic procedures. | |
Phospho-APP-Y757 Antibody Blocking Peptide - Protein Information | |
| Name APP | |
| Synonyms A4, AD1 | |
| 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 Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity) N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) | |
| Cellular 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 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 | |
| Tissue Location 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 | |
Phospho-APP-Y757 Antibody Blocking Peptide - Related products
AP3025a: Phospho-APP-S198 Antibody
AP3026a: Phospho-APP-S730 Antibody
AP3027a: Phospho-APP-Y757 Antibody
AP6306a: APP Antibody (N-term)
AP6306b: APP Antibody (C-term)
AP6306c: APP Antibody (C-term D672)
BP3025a: Phospho-APP-S198 Antibody Blocking Peptide
BP3026a: Phospho-APP-S730 Antibody Blocking Peptide
BP3027a: Phospho-APP-Y757 Antibody Blocking Peptide
BP6306a: APP Antibody (N-term) Blocking Peptide
BP6306b: APP Antibody (C-term) Blocking Peptide
BP6306c: APP Antibody (C-term D672) Blocking Peptide
BP9053a: APP-pY756 Antibody Blocking Peptide
Phospho-APP-Y757 Antibody Blocking Peptide - Research Areas
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BACKGROUND
APP is a cell surface receptor and transmembrane 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).
REFERENCES
Blomqvist, M.E., et al., Neurobiol. Aging 26(6):795-802 (2005). Yoon, I.S., et al., J. Biol. Chem. 280(20):20140-20147 (2005). Chen, M., et al., Biochem. Biophys. Res. Commun. 330(3):714-721 (2005). Yamamoto, M., et al., Am. J. Pathol. 166(5):1475-1485 (2005). Moir, R.D., et al., J. Biol. Chem. 280(17):17458-17463 (2005).
