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Merck
모든 사진(3)

문서

M1570

Sigma-Aldrich

Anti-Myosin (Skeletal, Fast) antibody, Mouse monoclonal

enhanced validation

clone MY-32, purified from hybridoma cell culture

동의어(들):

Monoclonal Anti-Myosin (Skeletal, Fast) antibody produced in mouse

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.41

생물학적 소스

mouse

Quality Level

결합

unconjugated

항체 형태

purified immunoglobulin

항체 생산 유형

primary antibodies

클론

MY-32, monoclonal

형태

buffered aqueous solution

종 반응성

rat, chicken, rabbit, mouse, human, bovine, guinea pig, feline

포장

antibody small pack of 25 μL

향상된 검증

independent
Learn more about Antibody Enhanced Validation

농도

~1.0 mg/mL

기술

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 10-20 μg/mL using porcine tongue
microarray: suitable
western blot: 0.5-1.0 μg/mL using total extract of rabbit skeletal muscle

동형

IgG1

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

유사한 제품을 찾으십니까? 방문 제품 비교 안내

일반 설명

Localizes an epitope on the myosin heavy chain. Stains the fast (type II) and neonatal isomyosin molecules found in skeletal muscle, but does not stain cardiac muscle, smooth muscle or non-muscle myosin in cultured cells. Does react with human rhabdomyosarcomas.

면역원

rabbit muscle myosin.

애플리케이션

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
The level of mysosin (fast) in serum samples from sportsmen with past injury was determined by western blot using monoclonal mouse anti-myosin (skeletal/fast) as the primary antibody at a dilution of 1:90000.

물리적 형태

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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 1


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.

이 제품을 이미 가지고 계십니까?

문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

Yanlin Wang et al.
Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology, 40(6), 1255-1265 (2019-03-21)
Myotonic dystrophy type 1 (DM1) is caused by CTG nucleotide repeat expansions in the 3'-untranslated region (3'-UTR) of the dystrophia myotonica protein kinase (DMPK) gene. The expanded CTG repeats encode toxic CUG RNAs that cause disease, largely through RNA gain-of-function.
Charlotte Capitanchik et al.
Nucleus (Austin, Tex.), 9(1), 410-430 (2018-06-19)
Laminopathies yield tissue-specific pathologies, yet arise from mutation of ubiquitously-expressed genes. A little investigated hypothesis to explain this is that the mutated proteins or their partners have tissue-specific splice variants. To test this, we analyzed RNA-Seq datasets, finding novel isoforms
Alan P Tenney et al.
Cell reports, 29(2), 437-452 (2019-10-10)
The somatotopic motor-neuron projections onto their cognate target muscles are essential for coordinated movement, but how that occurs for facial motor circuits, which have critical roles in respiratory and interactive behaviors, is poorly understood. We report extensive molecular heterogeneity in
Emranul Huq et al.
American journal of physical anthropology, 166(1), 95-106 (2018-01-11)
We hypothesized that the vertical leaper Galago senegalensis will have epaxial extensor muscles with a fast fiber phenotype to facilitate rapid spinal extension during leaping in comparison to the slow-moving quadruped Nycticebus coucang. To test this, we determined the percentage
Danielle Buck et al.
The Journal of general physiology, 143(2), 215-230 (2014-01-29)
Titin is a molecular spring that determines the passive stiffness of muscle cells. Changes in titin's stiffness occur in various myopathies, but whether these are a cause or an effect of the disease is unknown. We studied a novel mouse

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