抗体

Anti-Amyloid Precursor Protein

MBS502005

0.1毫升

345美元

多克隆

兔

未共轭

抗体

Anti-Amyloid Precursor Protein

Amyloid Precursor Protein

amyloid beta A4 protein; Amyloid beta A4 protein; amyloid beta A4 protein; AG; ABPP; amyloid A4; amyloidogenic glycoprotein; alzheimer disease amyloid A4 protein homolog; amyloid beta (A4) precursor protein; ABPP; APP; Alzheimer disease amyloid A4 protein homolog; Amyloidogenic glycoprotein; AGCleaved into the following 14 chains:N-APPSoluble APP-alpha; S-APP-alphaSoluble APP-beta; S-APP-betaC99Beta-amyloid protein 42; Alternative name(s):; Beta-APP42Beta-amyloid protein 40; Alternative name(s):; Beta-APP40C83P3(42)P3(40)C80Gamma-secretase C-terminal fragment 59; Alternative name(s):; Gamma-CTF(59)Gamma-secretase C-terminal fragment 57; Alternative name(s):; Gamma-CTF(57)Gamma-secretase C-terminal fragment 50; Alternative name(s):; Gamma-CTF(50)

淀粉样蛋白前体

App; App; Abeta; APP; AG; S-APP-alpha; S-APP-beta

A4_RAT

多克隆

兔

大鼠

770

Specific for ~115k APP protein. Immunolabeling of the APP protein band is completely blocked by preadsorption of the antibody with the peptide used as antigen.

Affinity Purified (Prepared from rabbit serum by affinity purification on a column made with the C-terminal peptide used as antigen.)

100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.

Store at -20 degree C; stable for at least one year.

免疫印迹(免疫印迹)

Quality Control: Western blots performed on each lot. WB: 1:1000

Antigen: Peptide corresponding to amino acid residues from the C-terminal region of rat APP. Immunogen Information: Synthetic peptide corresponding to amino acid residues from the C-terminal region conjugated to KLH. Immunogen Species: Rat

Reactivity Assumed Based on 100% Sequence Homology: Canine, chicken, human, mouse and non-human primate. Species Reactivity Note: The antibody has been directly tested for reactivity in rat tissue. It is anticipated that the antibody will also work with canine, chicken, human, mouse and non-human primate tissues based on the fact that these species have 100% homology with the amino acid sequence used as antigen. Biological Significance: A large body of evidence has implicated the amyloid precursor protein (APP) in the pathogenesis of Alzheimer's disease (AD) (Kamenetz et al., 2003). The phosphorylation of APP at Thr668 is thought to play a critical role in generation of the soluble APP (beta) and beta-amyloid peptide (abeta) which are the major components of senile plaques in patient brains inflicted with AD (Liu et al., 2003; Ando et al., 2001).

亲和纯化兔多克隆抗体

Ando K, Iijima KI, Elliott JI, Kirino Y, Suzuki T (2001) Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid. J Biol Chem 276:40353-40361. Kamenetz F, Tomita T, Hsieh H, Seabrook G, Borchelt D, Iwatsubo T, Sisodia S, Malinow R (2003) APP processing and synaptic function. Neuron 37:925-937. Liu F, Su Y, Li B, Zhou Y, Ryder J, Gonzalez-DeWhitt P, May PC, Ni B (2003) Regulation of amyloid precursor protein (APP) phosphorylation and processing by p35/cdk5 and p25/cdk5. FEBS Lett 547:193-196.

27436861

NP_062161.1

NM_019288.2

P08592

115

Activated TLR4 Signalling Pathway (936709); Advanced Glycosylation Endproduct Receptor Signaling Pathway (936728); Alzheimer's Disease Pathway (83489); Alzheimer's Disease Pathway (509); Amyloids Pathway (936191); Class A/1 (Rhodopsin-like Receptors) Pathway (936109); Cytosolic Sensors Of Pathogen-associated DNA Pathway (936738); DEx/H-box Helicases Activate Type I IFN And Inflammatory Cytokines Production Pathway (936746); Delta-Notch Signaling Pathway (198480); Disease Pathway (936186)

activates voltage dependent calcium channels; may induce neuronal apoptosis [RGD, Feb 2006]

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 . By similarity. Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb . By similarity. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 . By similarity. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV . By similarity. 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 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 . By similarity.Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicits inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also bind GPC1 in lipid rafts . By similarity.Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain.The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis . By similarity.N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) . By similarity. Subunit structure: Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and NUMB and DAB1 . By similarity. Binding to DAB1 inhibits its serine phosphorylation . By similarity. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) . By similarity and DDB1. In vitro, it binds MAPT via the MT-binding domains . By similarity. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner . By similarity. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons . By similarity. Beta-amyloid associates with HADH2 . By similarity. Interacts with CPEB1, ANKS1B, TNFRSF21 and AGER . By similarity. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; this is promoted by heparin binding . By similarity. Beta-amyloid protein 40 interacts with S100A9 . By similarity. CTF-alpha product of APP interacts with GSAP . By similarity. Interacts with SORL1 . By similarity. Ref.10 Ref.11. 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-CTF59 peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Associates with GPC1 in perinuclear compartments . By similarity. Beta-APP42 associates with FPRL1 at the cell surface and the complex is then rapidly internalized . By similarity. APP sorts to the basolateral surface in epithelial cells . By similarity. During neuronal differentiation, the Thr-742 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Ref.19. 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) Ref.8 Ref.9. 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 brain regions during the same period, but levels are low compared to non-L-APP isoforms. Induction: Phosphorylation of mature, glycosylated APP occurs 48-72 hours after treatment of neuronal cells with nerve growth factor which correlates with the timing of neurite outgrowth. Ref.19. Domain: The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells.The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The NPXY site is also involved in clathrin-mediated endocytosis. Post-translational 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 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF50, gamma-CTF57 and gamma-CTF59 . By similarity.Proteolytically cleaved by caspases during neuronal apoptosis . By similarity. Cleavage at Asp-739 by either caspase-3, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of beta-amyloid peptides . By similarity.N-glycosylated. Ref.21O-glycosylated. O-linkage of chondroitin sulfate to the L-APP isoforms produces the APP proteoglycan core proteins, the appicans. The chondroitin sulfate chain of appicans contains 4-O-sulfated galactose in the linkage region and chondroitin sulfate E in the repeated disaccharide region. Ref.21Phosphorylation 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. 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. Ref.17 Ref.18 Ref.19 Ref.20Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond . By similarity.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) . By similarity.Beta-amyloid peptides are degraded by IDE . By similarity. Miscellaneous: Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between beta-amyloid molecules resulting in beta-amyloid-metal aggregates. Rat and mouse beta-amyloid peptides have an arginine residue substituted for the bridging histidine residue and are thus less capable of forming amyloid aggregates. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding . By similarity. Sequence similarities: Belongs to the APP family.Contains 1 BPTI/Kunitz inhibitor domain. Mass spectrometry: Molecular mass is 5911.3 Da from positions 721 - 770. Determined by MALDI. Ref.6Molecular mass is 6024.4 Da from positions 720 - 770. Determined by MALDI. Ref.6

0.1毫升

345美元