Amyloid-β (phospho Thr743) rabbit pAb
ENT-A2011
Description
| REF | ENT-A2011 |
|---|---|
| Category | Antibody Polyclonal |
| Description | Amyloid-β (phospho Thr743) rabbit pAb |
| Source | Rabbit |
| Applications | WB;IHC;IF;ELISA |
| Reactivity | Human;Mouse;Rat |
| Reactivity | Human;Mouse;Rat |
| Dilution | Western Blot: 1/500 – 1/2000. Immunohistochemistry: 1/100 – 1/300. Immunofluorescence: 1/200 – 1/1000. ELISA: 1/10000. Not yet tested in other applications. |
| Immunogen | The antiserum was produced against synthesized peptide derived from human Amyloid beta A4 around the phosphorylation site of Thr743/668. AA range:711-760 |
| Storage Stability | -20°C/1 year |
| Clonality | Polyclonal |
| Isotype | IgG |
| Concentration | 1 mg/ml |
| Observed Band KD | 140kD |
| Human Gene ID | 351 |
| Human Swiss Prot Nº | P05067 |
| Subcellular Location | Cell membrane ; Single-pass type I membrane protein . Membrane ; Single-pass type I membrane protein . Perikaryon . Cell projection, growth cone . Membrane, clathrin-coated pit . Early endosome . Cytoplasmic vesicle . Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles (PubMed:20580937). 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 ves |
Other Name: APP; A4; AD1; Amyloid beta A4 protein; ABPP; APPI; APP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; PreA4; Protease nexin-II; PN-II
Background: This gene encodes 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. In addition, two of the peptides are antimicrobial peptides, having been shown to have bacteriocidal and antifungal activities. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene. [provided by RefSeq, Aug 2014],