추천 제품
생물학적 소스
rabbit
Quality Level
결합
unconjugated
항체 형태
affinity isolated antibody
항체 생산 유형
primary antibodies
클론
polyclonal
형태
buffered aqueous solution
분자량
antigen ~4 kDa
종 반응성
rat, human, mouse
포장
antibody small pack of 25 μL
기술
indirect ELISA: 0.2-0.4 μg/mL using β-amyloid peptide (22-35)
western blot: 0.25-0.5 μg/mL using β-amyloid peptide (1-40)
UniProt 수납 번호
배송 상태
dry ice
저장 온도
−20°C
타겟 번역 후 변형
unmodified
유전자 정보
human ... APP(351)
mouse ... App(11820)
rat ... App(54226)
일반 설명
Rabbit anti-β-amyloid (22-35) antibody specifically recognizes β-amyloid (22-35), β-amyloid (25-35), β-amyloid (1-40) and β-amyloid (1-42) and does not react with β-amyloid (32-35) and β-amyloid (35-25) by ELISA. The antibody detects β-amyloid (1-40) by immunoblotting (approx. 4kDa). Staining of the β-amyloid (1-40) band in immunoblotting is specifically inhibited by the immunizing peptide.
Cleavage of the amyloid precursor protein (APP) by γ-secretase produces the small fragment amyloid β (Aβ) peptide. Cleavage of APP occurs mostly at residue 40 but to a lesser extent residue 42. The amyloid β peptide contains a ~100 kDa soluble N-terminal fragment, and intracellular C-terminal fragments (CTFs) bearing the complete Aβ domain.
Proteolytic cleavage of the amyloid precursor protein (APP) produces the small fragment amyloid β peptide. Cleavage of APP occurs mostly at residue 40 but to a lesser extent residue 42. Aggregates of amyloid β peptide are found deposited in the brains of Alzheimer′s patients.
면역원
synthetic peptide corresponding to amino acids 22-35 of human β-amyloid (1-40) fragment, conjugated to KLH. This sequence corresponds to amino acids 693-706 of the human amyloid precursor protein APP, and is identical in mouse and rat APP.
애플리케이션
Rabbit anti-β-amyloid (22-35) antibody can be used for ELISA at a concentration of 0.2-0.4μg/mL using β-amyloid peptide (22-35). The product can also be used for western blot at 0.25-0.5μg/mL using β-amyloid peptide (1-40).
Anti-β-Amyloid (22-35) antibody produced in rabbit has been used in:
- western blot
- dot-blot assay
- indirect enzyme linked immunosorbent assay (ELISA)
생화학적/생리학적 작용
Secreted Aβ lead to synaptic and neuritic compromise and glial activation. Aggregates of amyloid β peptide are found deposited in the brains of Alzheimer′s patients. Aβ(25-35) and Aβ(22-35) fragments are highly toxic segments of β-amyloid peptides that promote inflammatory processes in astrocytes and fibrillary aggregation of Aβ, thus representing a promising therapeutic target for Alzheimer′s.
물리적 형태
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide and 1% bovine serum albumin.
면책조항
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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관련 제품
제품 번호
설명
가격
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
The Journal of neuroscience : the official journal of the Society for Neuroscience, 33(50), 19423-19433 (2013-12-18)
Tissue-specific overexpression of the human systemic amyloid precursor transthyretin (TTR) ameliorates Alzheimer's disease (AD) phenotypes in APP23 mice. TTR-β-amyloid (Aβ) complexes have been isolated from APP23 and some human AD brains. We now show that substoichiometric concentrations of TTR tetramers
Mechanisms of transthyretin inhibition of $\beta$-amyloid aggregation in vitro
The Journal of Neuroscience, 33(50), 19423-19433 (2013)
An Overview of APP Processing Enzymes and Products
Neuromolecular Medicine, 12, 1-1 (2010)
Mechanisms of Amyloid-beta Peptide Clearance: Potential Therapeutic Targets for Alzheimer's Disease
Biomolecules & Therapeutics, 20, 245-245 (2012)
eLife, 11 (2022-05-18)
Cleavage of membrane proteins in the lipid bilayer by intramembrane proteases is crucial for health and disease. Although different lipid environments can potently modulate their activity, how this is linked to their structural dynamics is unclear. Here, we show that
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