Anti-Beta Amyloid Antibody
|Applications||ELISA, IF, IHC, WB|
|Product Name||Anti-Beta Amyloid Antibody|
|Storage & Handling||Store at -20°C for one year, at 4°C for one month. We suggest the antibody be aliquotted into small vials and stored frozen at -20°C upon receiving. Avoid repeated freezing and thawing.|
|Description||Anti-Beta Amyloid Antibody tested for ELISA, IF, IHC, WB in Human; Mouse.|
|Cite This Product||Anti-Beta Amyloid Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # A00081-2)|
|Contents/Buffer||0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2|
|Immunogen||This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to the amino terminus (aa 1-14) of human beta amyloid conjugated to KLH using maleimide.|
Assay Dilutions Overview
Western Blot, 1:1, 000-1:5000
IF Microscopy: 1:50-1:200
ELISA : 1:10,000 - 1:30,000
Images And Assay Conditions
Beta Amyloid was detected in immunohistochemical frozen sections of TG APP23 mouse brain cortex tissues using rabbit anti-Beta Amyloid affinity purified polyclonal antibody (Catalog # A00081-2) at 1:200. Carl Hobbs, King`s College London, United Kingdom.
Beta Amyloid was detected in paraffin-embedded sections of human heart tissues using rabbit anti-Beta Amyloid affinity purified polyclonal antibody (Catalog # A00081-2) at 5 µg/ml. The immunohistochemical section was developed using SABC method (Catalog #
Western blot analysis of Beta Amyloid expression in HEK293 whole cell lysates (lane 1), mouse brain whole cell lysates (lane 2) and A-172 whole cell lysates (lane 3). Beta Amyloid at 40 kDa was detected using rabbit anti-Beta Amyloid affinity purified pol
ELISA results of purified Rabbit anti-Beta Amyloid Antibody tested against BSA-conjugated peptide of immunizing peptide. Each well was coated in duplicate with 0.1 µg of conjugate. The starting dilution of antibody was 5 µg/ml and the X-axis represents th
Western blot analysis of Beta Amyloid expression in mouse brain extract (lane 1) and mouse spinal chord (lane 2). A 40-50 kDa band consistent with a higher MW precursor form of beta amyloid was detected using rabbit anti-Beta Amyloid affinity purified pol
Western blot analysis of Beta Amyloid expression in HEK293 whole cell lysates (lane 1), HeLa Lysate whole cell lysates (lane 2), MCF-7 cell lysates (lane 3), Jurkat cell lysates (lane 4), A431 cell lysates (lane 5), LNCaP cell lysates (lane 6), A-172 cell
Protein Target Info (Source: Uniprot.org)
|Protein Name||Amyloid beta A4 protein|
|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. .|
|Alternative Names||Amyloid beta A4 protein;ABPP;APPI;APP;Alzheimer disease amyloid protein;Cerebral vascular amyloid peptide;CVAP;PreA4;Protease nexin-II;PN-II;N-APP;Soluble APP-alpha;S-APP-alpha;Soluble APP-beta;S-APP-beta;C99;Beta-amyloid protein 42;Beta-APP42;Beta-amyloid protein 40;Beta-APP40;C83;P3(42);P3(40);C80;Gamma-secretase C-terminal fragment 59;Amyloid intracellular domain 59;AICD-59;AID(59);Gamma-CTF(59);Gamma-secretase C-terminal fragment 57;Amyloid intracellular domain 57;AICD-57;AID(57);Gamma-CTF(57);Gamma-secretase C-terminal fragment 50;Amyloid intracellular domain 50;AICD-50;AID(50);Gamma-CTF(50);C31;APP;A4, AD1;|
|Subcellular Localization||Membrane; Single-pass type I membrane protein. 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.|
|Molecular Weight||86943 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein 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. .|
|Research Areas||Human, Mouse
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