MABT29
Anti-Ninein Antibody, clone 79-160-7
clone 79-160-7, from mouse
Synonym(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
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
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biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
79-160-7, monoclonal
species reactivity
human
technique(s)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... NIN(51199)
General description
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.
Immunogen
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).
Immunoprecipitation Analysis: The antibody has been shown to immunoprecipitate Ninein in L929 cells. (Delgehyr, 2005).
Quality
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.
Western Blot Analysis: 1 µg/mL of the antibody detected Ninein in 10 µg of Hek293 cell lysate.
Target description
~ 250 kDa observed MW. An unidentified nonspecific band appears at ~ 50 kDa
Physical form
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.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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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