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Key Documents

MABT29

Sigma-Aldrich

Anti-Ninein Antibody, clone 79-160-7

clone 79-160-7, from mouse

Synonyme(s) :

ninein (GSK3B interacting protein), Glycogen synthase kinase 3 beta-interacting protein, ninein centrosomal protein, GSK3B-interacting protein

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About This Item

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

Source biologique

mouse

Niveau de qualité

Forme d'anticorps

purified antibody

Type de produit anticorps

primary antibodies

Clone

79-160-7, monoclonal

Espèces réactives

human

Technique(s)

immunoprecipitation (IP): suitable
western blot: suitable

Isotype

IgG2aκ

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... NIN(51199)

Description générale

Ninein is a coiled-coil, centrosomal protein that is a necessary component in microtubule minus-end anchorage and positioning, and may have a role as a maturation factor for centrosomes. It may also be involved in microtubule nucleation. More recent studies have identified ninein as a crucial component in the formation of blood vessels. Expression of ninein is ubiquitous, but significantly higher levels have been observed in skeletal muscle and heart tissue. There have been 8 isoforms characterized due to alternative splicing.

Immunogène

Recombinant protein corresponding to human Ninein.

Application

Anti-Ninein Antibody, clone 79-160-7 is an antibody against Ninein for use in WB & IP.
Immunocytochemistry Analysis: 1:500 dilution of the antibody has been shown to detect Ninein in HeLa and A431 cells.

Immunoprecipitation Analysis: The antibody has been shown to immunoprecipitate Ninein in L929 cells. (Delgehyr, 2005).

Qualité

Evaluated by Western Blot in Hek293 cell lysate.

Western Blot Analysis: 1 µg/mL of the antibody detected Ninein in 10 µg of Hek293 cell lysate.

Description de la cible

~ 250 kDa observed MW. An unidentified nonspecific band appears at ~ 50 kDa

Forme physique

Format: Purified
Purified mouse monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine, pH 7.4, 150 mM NaCl with 0.05% sodium azide.

Autres remarques

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

David K Moss et al.
Journal of cell science, 120(Pt 17), 3064-3074 (2007-08-19)
Cell-to-cell contact and polarisation of epithelial cells involve a major reorganisation of the microtubules and centrosomal components. The radial microtubule organisation is lost and an apico-basal array develops that is no longer anchored at the centrosome. This involves not only
Nathalie Delgehyr et al.
Journal of cell science, 118(Pt 8), 1565-1575 (2005-03-24)
The centrosome organizes microtubules by controlling nucleation and anchoring processes. In mammalian cells, subdistal appendages of the mother centriole are major microtubule-anchoring structures of the centrosome. It is not known how newly nucleated microtubules are anchored to these appendages. We
Ninein leads the way in vessel sprouting.
Bautch, Victoria L
Arteriosclerosis, Thrombosis, and Vascular Biology, 28, 2094-2095 (2008)
Susanne Graser et al.
The Journal of cell biology, 179(2), 321-330 (2007-10-24)
Primary cilia (PC) function as microtubule-based sensory antennae projecting from the surface of many eukaryotic cells. They play important roles in mechano- and chemosensory perception and their dysfunction is implicated in developmental disorders and severe diseases. The basal body that
Aamir Ali et al.
Nature communications, 14(1), 289-289 (2023-01-27)
Organization of microtubule arrays requires spatio-temporal regulation of the microtubule nucleator γ-tubulin ring complex (γTuRC) at microtubule organizing centers (MTOCs). MTOC-localized adapter proteins are thought to recruit and activate γTuRC, but the molecular underpinnings remain obscure. Here we show that

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