
Phospho-Amyloid Beta A4 (Thr743/668) Rabbit Polyclonal Antibody#abs130712
Dear customers, kindly note that the price mentioned above is just for your reference. To obtain the detailed price, we kindly request you to contact our seller, Vecent. Data Examples Western blot analysis of Amyloid beta A4 phosphorylation expression in HeLa whole cell lysates,The lane on the...
Description
Catalog-specification | Delivery time | USD price |
abs130712-50ug | 1-2 Weeks | 201 |
abs130712-100ug | 1-2 Weeks | 301 |
Dear customers, kindly note that the price mentioned above is just for your reference. To obtain the detailed price, we kindly request you to contact our seller, Vecent.
Overview | |
Description | The cell surface receptor, known as APP, plays a crucial role in various neural processes such as neurite growth, neuronal adhesion, and axonogenesis. It undergoes cleavage by secretases, resulting in the formation of multiple peptides. Interestingly, some of these peptides have the ability to bind to the acetyltransferase complex Fe65/TIP60, which subsequently triggers transcriptional activation. This intricate molecular mechanism influences crucial events within the nervous system, ultimately contributing to its proper development and function. |
Other names | The following are various abbreviations and terms related to a protein called Amyloid beta A4 (A4) associated with Alzheimer's disease and aging: 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. |
Source | Rabbit |
Specificity | The antibody against Phospho-Amyloid beta A4 (Thr743/668) is designed to specifically recognize Amyloid beta A4 protein only when phosphorylated at Threonine 743/668. This antibody can detect endogenous levels of the protein in biological samples. By targeting this specific phosphorylation site, the antibody provides a more precise and reliable tool for studying the function of Amyloid beta A4 in various cellular processes. |
| Reactivity | Human;Mouse;Rat |
Predictive reaction species | Chicken;Xenopus;Horse;Pig; |
| Antigen | Amyloid β A4 |
Application | : |
| Immunogen | A highly comparable substance can be produced by rearranging the information provided in the original text. The substance is a synthetic peptide that originates from human Amyloid beta A4, specifically focusing on the phosphorylation site of Threonine 743/668. |
Properties | |
| MW | 140kDa |
| Concentration | 1mg/ml |
Purification | The affinity-purified antibody was obtained from purified rabbit serum through sequential chromatography on affinity columns specific for phospho- and non-phospho-peptides. It is important to note that the generated content should be significantly different from the original text and not follow the ChapGPT-based conversation method. |
Clonality | Polyclonal Antibody |
| Stability & Storage | To preserve the quality of the product, it is recommended to store it at a temperature of -20 °C for a duration of one year. It is important to avoid subjecting the product to repeated freeze and thaw cycles. |
Storage buffer | The provided information is regarding Rabbit IgG, which is stored in phosphate-buffered saline at a pH of 7.4. The solution contains 150mM NaCl, 0.02% sodium azide, and 50% glycerol. It is recommended to store it at a temperature of -20 °C. The stability of this substance is guaranteed for a period of 12 months from the date of receipt. |
Target | |
Background | 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 Cu2+-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 Cu2+ ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. |
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. |
| Posttranslational modification | 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). 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 caspase-6, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta 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 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. 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. |
Celluar localization | Cytoskeleton;Cytosol;Endoplasmic reticulum;Endosome;Extracellular region or secreted;Golgi apparatus;Nucleus;Plasma Membrane; |
| UniPort | P05067 |
Data Examples

Western blot analysis of Amyloid beta A4 phosphorylation expression in HeLa whole cell lysates,The lane on the left is treated with the antigen-specific peptide.
This product is for research use only, not for use in diagnostic prodecures or in human.
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