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Sigma-Aldrich

Anti-phospho-Ser/Thr-Pro MPM-2 Antibody, Cy5 conjugate

Upstate®, from mouse

Synonyme(s) :

Anti-MPM-2 Cy5 Antibody, Cy5 Anti-MPM-2, Phospho-Ser/Thr-Pro Detection

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

CY5 conjugate

Forme d'anticorps

purified antibody

Type de produit anticorps

primary antibodies

Clone

monoclonal

Espèces réactives

vertebrates

Fabricant/nom de marque

Upstate®

Technique(s)

immunocytochemistry: suitable
immunofluorescence: suitable
western blot: suitable

Isotype

IgG1

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

phosphorylation (pSer/pThr)

Description générale

This antibody recognizes a variety of proteins that are phosphorylated during mitosis.
Progression of cells from interphase to mitosis involves alterations in cell structures and activities. The transition from G2 to M phase is induced by M phase-promoting factor, or MPF. In M phase, many proteins are phosphorylated directly by MPF or indirectly by kinases activated by MPF. These M-phase phosphoproteins (MPPs, or MPHOSPHs) permit disassembly of interphase structures and generation of M-phase enzymatic activities and structures. Also, known as Forkhead-related protein FKHL16 or Hepatocyte nuclear factor 3 forkhead homolog 11.

Spécificité

Recognizes a phosphorylated epitope (phospho-[Ser/Thr]Pro) found in phosphoproteins such as MAP2, HSP70, cdc25, and DNA topoisomerase IIα, most of which are phosphorylated at the onset of mitosis. The number of phosphoproteins recognized by MPM-2 varies from species to species and with the cell type.

Immunogène

Mitotic human HeLa cell lysate

Application

Anti-phospho-Ser/Thr-Pro Antibody, MPM-2, Cy5 conjugate is a Mouse Monoclonal Antibody for detection of phospho-Ser/Thr-Pro also known as Mitotic protein #2 & has been tested in IF, WB, ICC.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Cell Cycle, DNA Replication & Repair

Qualité

Routinely evaluated by immunoblot on colcemid-treated HeLa cell lysates.

Forme physique

100μg Cy5-conjugated mouse IgG1 in 200μl of PBS containing 1% BSA, 0.05% Tween®-20, 0.05% sodium azide.
Protein G Purified

Stockage et stabilité

1 year at 4°C from date of shipment

Remarque sur l'analyse

Control
Colcemid-treated HeLa cell lysates

Informations légales

TWEEN is a registered trademark of Croda International PLC
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Thomas Blasi et al.
Nature communications, 7, 10256-10256 (2016-01-08)
Imaging flow cytometry combines the high-throughput capabilities of conventional flow cytometry with single-cell imaging. Here we demonstrate label-free prediction of DNA content and quantification of the mitotic cell cycle phases by applying supervised machine learning to morphological features extracted from
Pavlína Víšková et al.
Nature communications, 15(1), 1992-1992 (2024-03-06)
I-Motifs (iM) are non-canonical DNA structures potentially forming in the accessible, single-stranded, cytosine-rich genomic regions with regulatory roles. Chromatin, protein interactions, and intracellular properties seem to govern iM formation at sites with i-motif formation propensity (iMFPS) in human cells, yet
Rebecca J Harris et al.
Nature communications, 14(1), 7243-7243 (2023-11-10)
Histone modifications influence the recruitment of reader proteins to chromosomes to regulate events including transcription and cell division. The idea of a histone code, where combinations of modifications specify unique downstream functions, is widely accepted and can be demonstrated in
Hisayo Nishida-Fukuda et al.
PloS one, 16(4), e0249912-e0249912 (2021-04-15)
HASPIN is a serine/threonine kinase that regulates mitosis by phosphorylating histone H3 at threonine 3. The expression levels of HASPIN in various cancers are associated with tumor malignancy and poor survival, suggesting that HASPIN inhibition may suppress cancer growth. As
Nicola Brownlow et al.
Nature communications, 5, 5685-5685 (2014-12-09)
Exit from mitosis is controlled by silencing of the spindle assembly checkpoint (SAC). It is important that preceding exit, all sister chromatid pairs are correctly bioriented, and that residual catenation is resolved, permitting complete sister chromatid separation in the ensuing

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