추천 제품
생물학적 소스
rabbit
결합
unconjugated
항체 형태
whole antiserum
항체 생산 유형
primary antibodies
클론
polyclonal
포함
15 mM sodium azide
종 반응성
chicken
기술
indirect immunofluorescence: 1:500 using cultured chicken fibroblasts
western blot: suitable using cultured cells and chicken gizzard extract
배송 상태
dry ice
저장 온도
−20°C
타겟 번역 후 변형
unmodified
유전자 정보
chicken ... ACTN2(396263) , ACTN4(396024)
일반 설명
α-Actinin is a 100kDa actin-binding protein that is found in muscle as well as non-muscle cells. Rabbit anti-α-actinin antibody stains α-actinin in cell cultures using indirect immunofluorescence. The antibody reacts best with cultured chicken fibroblasts, however, adequate labeling may also be obtained with cells of other species. In an immunoblot assay, the antiserum specifically stains the α-actinin band.
α-Actinin is a member of the spectrin superfamily. It consists of an antiparallel homodimer, with an N-terminal actin-binding domain (ABD), a central domain of four spectrin-like repeats (SRs), and a C-terminal calmodulin-like domain (CAMD) with two pairs of EF-hand motifs (EFs). α-Actinin exists in four isoforms: α-actinin 1, α-actinin 2, α-actinin 3 and α-actinin 4. In smooth muscles, α-actinin is present in dense bodies and plaques whereas, in normal skeletal muscles, it is associated with Z-discs that define muscle sarcomere.
특이성
Anti-α-Actinin specifically stains α-actinin in cell cultures using indirect immunfluorescent labeling techniques. The antibody reacts best with cultured chicken fibroblasts, however adequate labeling may also be obtained with cells of other species.
면역원
α-actinin from chicken gizzard
애플리케이션
Anti-Actinin antibody was used to detect actinin in human mesangial cells. Cells were first grown on glass cover slips, fixed in cold methanol and permeabilized with 3.5% paraformaldehyde/0.1% Tween-20 for 5 min at room temperature.
Rabbit anti-α-actinin antibody has been used for:
- co-immunoprecipitation studies
- immunoblotting studies
- immunofluorescence
생화학적/생리학적 작용
α-Actinin is an actin-crosslinking Z-disk protein. It plays a vital role in linking the cytoskeleton to different transmembrane proteins in a variety of junctions. α-Actinin modulates receptor activities and serves as a cytoskeleton scaffold for diverse signaling pathways. It is implicated in muscle contraction.
물리적 형태
Supplied as a liquid with 0.1% sodium azide as a preservative.
저장 및 안정성
For continuous use, store at 2-8 °C for up to one month. For extended storage, the solution may be frozen in working aliquots. Repeated freezing and thawing is not recommended. Storage in "frost-free" freezers not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.
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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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
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
B Sjöblom et al.
Cellular and molecular life sciences : CMLS, 65(17), 2688-2701 (2008-05-20)
Alpha-actinin is a cytoskeletal actin-binding protein and a member of the spectrin superfamily, which comprises spectrin, dystrophin and their homologues and isoforms. It forms an anti-parallel rod-shaped dimer with one actin-binding domain at each end of the rod and bundles
L J Swatzell et al.
Plant & cell physiology, 40(2), 173-183 (1999-04-15)
Integrins are a large family of integral membrane proteins that function in signal transduction in animal systems. These proteins are conserved in vertebrates, invertebrates, and fungi. Evidence from previous research suggests that integrin-like proteins may be present in plants as
Peter Nagy et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(38), 16524-16529 (2010-09-04)
Ligand-driven dimerizations of ErbB receptor subunits fulfill a fundamental role in their activation. We have used the number and brightness analysis technique to investigate the existence of preformed ligand-independent dimers and clusters and to characterize the initial steps in the
Ana Virel et al.
Molecular biology and evolution, 21(6), 1024-1031 (2004-03-12)
The N-terminal actin-binding domain of alpha-actinin is connected to the C-terminal EF-hands by a rod domain. Because of its ability to form dimers, alpha-actinin can cross-link actin filaments in muscle cells as well as in nonmuscle cells. In the prototypic
Amanda W Smith et al.
Acta biomaterialia, 8(1), 31-40 (2011-09-17)
Poly(ethylene glycol) (PEG) microspheres were assembled around HL-1 cardiomyocytes to produce highly porous modular scaffolds. In this study we took advantage of the immiscibility of PEG and dextran to improve upon our previously described modular scaffold fabrication methods. Phase separating
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