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Merck
모든 사진(3)

주요 문서

T9028

Sigma-Aldrich

Monoclonal Anti-Tubulin, Tyrosine antibody produced in mouse

clone TUB-1A2, ascites fluid

동의어(들):

Anti-CDCBM6, Anti-CSCSC1, Anti-M40, Anti-OK/SW-cl.56, Anti-TUBB1, Anti-TUBB5

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About This Item

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

생물학적 소스

mouse

Quality Level

결합

unconjugated

항체 형태

ascites fluid

항체 생산 유형

primary antibodies

클론

TUB-1A2, monoclonal

포함

15 mM sodium azide

종 반응성

human, plant, animal

기술

indirect immunofluorescence: 1:800 using cultured chicken fibroblasts
microarray: suitable
western blot: suitable

동형

IgG3

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

일반 설명

Monoclonal Anti-Tyrosine Tubulin (mouse IgG3 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Tubulin as a cylindrical filamentous structure and is present in almost all eukaryotic cells. Tubulin is a heterodimer which consists of α-tubulin and β-tubulin; both subunits have a molecular weight of 55 kDa and share considerable homology.
The intracellular cylindrical filamentous structure, microtubules is mainly made up of tubulin and is present in all eukaryotic cells. Monoclonal Anti-Tyrosine antibody can be used in immunocytochemical localization of tyrosinated α tubulin by indirect immunofluorescence labelling. Monoclonal Anti-Tyrosine antibody reacts specifically with tyrosine tubulin of bovine brain, African Green Monkey kidney cells (Vero), dog kidney (MDCK), marsupial kidney (Potoroo, PtK2), mouse pituitary tumour (AtT-20), yeast, and Xenopus.

특이성

The antibody reacts against tubulin′s C-terminal tyrosine in immunoblotting assays and may be used for localization of this epitope in cultured cells or tissue sections.

면역원

peptide containing the carboxy-terminal amino acids of α-tubulin

애플리케이션

Monoclonal Anti-Tyrosine Tubulin has been used in:
  • indirect immunofluorescent labelling
  • immunoblotting technique
  • immunocytochemical staining

생화학적/생리학적 작용

Tubulin acts as a major building block of microtubules. Tubulin tyrosinylation is involved in the assembly status of tubulin. A specific tubulinyl tyrosine carboxypeptidase removes the terminal tyrosine to yield an α-tubulin terminating in a glutamic acid residue while another enzyme modifies the α-tubulin by addition of tyrosine to the carboxy terminus to offer a potential cycle of tyrosine addition and loss.

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

12 - Non Combustible Liquids

WGK

WGK 1


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문서 라이브러리 방문

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Mayorova TD, et al.
Russian journal of developmental biology, 43(5), 271-285 (2012)
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Biophysical journal, 93(3), 886-894 (2007-05-15)
Inner-arm dynein-f of Chlamydomonas flagella is a heterodimeric dynein. We performed conventional in vitro motility assays showing that dynein-f translocates microtubules at the comparatively low velocity of approximately 1.2 microm/s. From the dependence of velocity upon the surface density of
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The evolutionary origin of gastrulation--defined as a morphogenetic event that leads to the establishment of germ layers--remains a vexing question. Central to this debate is the evolutionary relationship between the cell layers of sponges (poriferans) and eumetazoan germ layers. Despite
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PloS one, 6(9), e24152-e24152 (2011-09-21)
The TGF-β signaling pathway is a metazoan-specific intercellular signaling pathway known to be important in many developmental and cellular processes in a wide variety of animals. We investigated the complexity and possible functions of this pathway in a member of

문서

Microtubules of the eukaryotic cytoskeleton are composed of a heterodimer of α- and β-tubulin. In addition to α-and β-tubulin, several other tubulins have been identified, bringing the number of distinct tubulin classes to seven.

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