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| | ANTI-ASPARTYL PROTEASE 2 Basic information |
| Product Name: | ANTI-ASPARTYL PROTEASE 2 | | Synonyms: | POLYCLONAL ANTIBODY TO BACE1;Anti-BACE 1, C-Terminus (485-501) antibody produced in rabbit;Anti-BACE 1, N-Terminus (46-62) antibody produced in rabbit;ANTI-BACE 1 (EE-17);ANTI-ASPARTYL PROTEASE 2;ANTI-BETA-SECRETASE 1;ANTI-BACE 1 (LK-16);Anti-β-Site APP Cleaving Enzyme | | CAS: | | | MF: | | | MW: | 0 | | EINECS: | | | Product Categories: | | | Mol File: | Mol File | ![ANTI-ASPARTYL PROTEASE 2 Structure]() |
| | ANTI-ASPARTYL PROTEASE 2 Chemical Properties |
| storage temp. | -20°C | | form | buffered aqueous solution | | biological source | rabbit |
| WGK Germany | - | | Storage Class | 10 - Combustible liquids |
| | ANTI-ASPARTYL PROTEASE 2 Usage And Synthesis |
| Uses | Anti-BACE 1, N-Terminus (46-62) antibody produced in rabbit has been used in western blotting. | | General Description | The membrane-associated aspartic protease BACE-1 (β-site APP cleaving enzyme, Asp2 or memapsin 2) has been identified as β-secretase. BACE-1 constitutes the predominant β-secretase activity in human brain tissue. It is highly expressed in neurons, the major site of Aβ generation. BACE-1 is localized within the Golgi and endosomal compartments, among the several intracellular sites where Aβ is thought to be produced. BACE-1 is initially an inactive proenzyme and localized in endoplasmic reticulum. | | Biochem/physiol Actions | Overexpression of β-site APP cleaving enzyme, Asp2 or memapsin 2 (BACE-1) leads to increased β-secretase activity while displaying appropriate cleavage site specificity for APP. The N-glycosylation and phosphorylation of BACE-1 within its C-terminal domain regulated its intracellular trafficking. |
| | ANTI-ASPARTYL PROTEASE 2 Preparation Products And Raw materials |
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