
Thermo Fisher Scientific Amyloid Precursor Protein Monoclonal Antibody (mAbP2-1)
Amyloid Precursor Protein을 검출하는 Thermo Fisher Scientific의 단클론 항체로, 인간 및 비인간 영장류 시료에 반응합니다. WB, ICC/IF, ELISA, IP 등 다양한 응용에 적합하며, native APP에 특이적입니다. 1 mg/mL 농도의 액상 형태로 제공되며, -80°C에서 보관합니다.
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- OMA103132
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- pk
카탈로그
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Applications and Tested Dilutions
| Application | Tested Dilution | Publications |
|---|---|---|
| Western Blot (WB) | 5 µg/mL | View 3 publications |
| Immunocytochemistry (ICC/IF) | 1:200 | View 1 publication |
| ELISA | 10 µg/mL | View 6 publications |
| Immunoprecipitation (IP) | 25 µg/mL* | View 1 publication |
Product Specifications
| Specification | Description |
|---|---|
| Species Reactivity | Human, Non-human primate |
| Published Species | Human, Mouse |
| Host / Isotype | Mouse / IgG1 |
| Class | Monoclonal |
| Type | Antibody |
| Clone | mAbP2-1 |
| Immunogen | Native, secreted form of APP |
| Conjugate | Unconjugated |
| Form | Liquid |
| Concentration | 1.0 mg/mL |
| Purification | Protein G |
| Storage Buffer | PBS, pH 7.4 |
| Contains | No preservative |
| Storage Conditions | -80°C, Avoid Freeze/Thaw Cycles |
| Shipping Conditions | Dry ice |
| RRID | AB_325526 |
Product Specific Information
OMA1-03132 detects amyloid precursor protein (APP) from human and monkey tissues.
This antibody is specific for native, non-denatured protein, and does not cross-react with mouse or rat APP, nor other APP homologs.
OMA1-03132 has been successfully used in Western blot (non-reducing conditions), immunocytochemistry, immunoprecipitation, and ELISA procedures.
It is not suitable for IHC on paraffin-embedded tissues and does not recognize APP if samples are boiled in Laemmli buffer containing reducing agents (DTT or β-ME).
Can be used in immunoprecipitation utilizing 25 µg/mL of OMA1-03132 linked sepharose.
The antigen is the native, secreted form of human APP, and the recognized epitope maps to residues 104–118 of APP.
Target Information
Amyloid beta peptide (Abeta/Beta-amyloid) is the major constituent of amyloid plaques found in the brains of individuals with Alzheimer’s disease.
Abeta peptide (40–43 amino acids) is generated from beta-amyloid precursor protein (beta APP) through sequential cleavage by beta-secretase (BACE) and gamma-secretase.
Gamma-secretase, a multi-subunit complex including presenilin-1 and -2, cleaves the carboxyl-terminal domain of beta APP, releasing amyloid beta peptide.
Nicastrin, a transmembrane glycoprotein associated with presenilins, binds to the carboxyl-terminus of beta APP and modulates Abeta production.
Abeta forms extracellular filamentous protein deposits in amyloid cores, neuritic plaques, and neurofibrillary tangles.
Abnormal beta amyloid deposits are characteristic of Alzheimer’s disease and also found in Lewy body dementia, Down’s syndrome, Dutch-type amyloidosis, cerebral amyloid angiopathy, and the Guam Parkinson-Dementia complex.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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