ARG52226
anti-Amyloid Precursor Protein antibody
anti-Amyloid Precursor Protein antibody for Western blot and Rat
Neuroscience antibody
Overview
| Product Description | Rabbit Polyclonal antibody recognizes Amyloid Precursor Protein |
|---|---|
| Tested Reactivity | Rat |
| Predict Reactivity | Hu, Ms, Chk, Dog, NHuPrm |
| Tested Application | WB |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Target Name | Amyloid Precursor Protein |
| Antigen Species | Rat |
| Immunogen | KLH-conjugated synthetic peptide around the C-terminal region of Rat APP. |
| Conjugation | Un-conjugated |
| Alternate Names | CVAP; AAA; AICD-50; PN2; 50; Beta-APP42; AID; Gamma-CTF; S-APP-alpha; 57; AD1; PN-II; Beta-APP40; 42; 40; APPI; Alzheimer disease amyloid protein; Amyloid beta A4 protein; PreA4; ABETA; Amyloid intracellular domain 50; CTFgamma; Amyloid intracellular domain 57; 59; AICD-59; S-APP-beta; APP; AICD-57; Amyloid intracellular domain 59; ABPP; Protease nexin-II; Cerebral vascular amyloid peptide |
Application Instructions
| Application Suggestion |
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| Application Note | 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. * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. |
Properties
| Form | Liquid |
|---|---|
| Purification | Affinity Purified |
| Buffer | 10 mM HEPES (pH 7.5), 150 mM NaCl, 0.1 mg/ml BSA and 50% Glycerol |
| Stabilizer | 0.1 mg/ml BSA, 50% Glycerol |
| Storage Instruction | For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. |
| Note | For laboratory research only, not for drug, diagnostic or other use. |
Bioinformation
| Database Links | |
|---|---|
| Gene Symbol | APP |
| Gene Full Name | amyloid beta (A4) precursor protein |
| Background | 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). |
| Research Area | Neuroscience antibody |
| Calculated MW | 87 kDa. (79 - 120 kDa depending on glycosylation level) |
| PTM | 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-CTF(50), gamma-CTF(57) and gamma-CTF(59). Many other minor beta-amyloid peptides, beta-amyloid 1-X peptides, are found in cerebral spinal fluid (CSF) including the beta-amyloid 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 beta-amyloid 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 beta-amyloid peptides (beta-amyloid 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but not found on beta-amyloid 38, beta-amyloid 40 nor on beta-amyloid 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 beta-amyloid-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). Beta-amyloid peptides are degraded by IDE. |
