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
12 - Non Combustible Liquids
wgk_germany
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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Izumi Dateyama et al.
Journal of cell science, 132(2) (2018-12-24)
The primary cilium, a solitary protrusion from most mammalian cells, functions as a cell sensor by receiving extracellular signals through receptors and channels accumulated in the organelle. Certain G-protein-coupled receptors (GPCRs) specifically localize to the membrane compartment of primary cilia.
Dong Hyun Kim et al.
Cell death & disease, 10(8), 570-570 (2019-07-31)
The initiation of centrosome duplication is regulated by the Plk4/STIL/hsSAS-6 axis; however, the involvement of other centrosomal proteins in this process remains unclear. In this study, we demonstrate that Cep131 physically interacts with Plk4 following phosphorylation of residues S21 and
Xavier Gaume et al.
Cell cycle (Georgetown, Tex.), 14(6), 902-919 (2015-01-16)
Nucleolin is a pleiotropic protein involved in a variety of cellular processes. Although multipolar spindle formation has been observed after nucleolin depletion, the roles of nucleolin in centrosome regulation and functions have not been addressed. Here we report using immunofluorescence
Tatsuo Miyamoto et al.
The EMBO journal, 39(12), e103499-e103499 (2020-05-06)
Primary cilia are antenna-like organelles on the surface of most mammalian cells that receive sonic hedgehog (Shh) signaling in embryogenesis and carcinogenesis. Cellular cholesterol functions as a direct activator of a seven-transmembrane oncoprotein called Smoothened (Smo) and thereby induces Smo
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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