Rabbit NuMA Polyclonal Antibody | anti-NuMA antibody

Phospho-NuMA (Ser169) Antibody

Cat. Num. AAA9610752

• Gene Names: NUMA1; NUMA; NMP-22
• Reactivity: Human, Mouse; Predicted: Pig, Bovine, Horse, Sheep, Dog
• Applications: Western Blot, ELISA
• Purity: Purified rabbit serum by affinity purification via sequential chromatography on phospho- and non-phospho-peptide affinity columns.
• Synonyms: NuMA; Polyclonal Antibody; Phospho-NuMA (Ser169) Antibody; Centrophilin stabilizes mitotic spindle in mitotic cells; NMP 22; Nuclear matrix protein 22; Nuclear mitotic apparatus protein 1; Nuclear mitotic apparatus protein; NUMA 1; NUMA; NuMA protein; NUMA1; NUMA1_HUMAN; SP H antigen; SP-H antigen; Structural nuclear protein; anti-NuMA antibody

• Host: Rabbit
• Reactivity: Human, Mouse; Predicted: Pig, Bovine, Horse, Sheep, Dog
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: Phospho-NuMA (Ser169) Antibody detects endogenous levels of NuMA only when phosphorylated at Ser169.
• Purity/Purification: Purified rabbit serum by affinity purification via sequential chromatography on phospho- and non-phospho-peptide affinity columns.
• Form/Format: Liquid; Phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Concentration: 1mg/ml (varies by lot)
• Sequence Length: 2115

• Applicable Applications for anti-NuMA antibody: Western Blot (WB), Peptide ELISA (EIA)
• Application Notes: WB: 1:500-1:2000; ELISA (Peptide): 1:20000-1:40000
• Immunogen: A synthesized peptide derived from human NuMA around the phosphorylation site of Ser169.
• Subcellular Location: Nucleus; Cytoskeleton; Plasma Membrane; Cytosol; Cytoskeleton; Cytosol; Cytoskeleton
• Preparation and Storage: Store at -20 degree C. Stable for 12 months from date of receipt.

Western Blot (WB)

(Western blot analysis of Phospho-NuMA (Ser169) in lysates of K562?, using Phospho-NuMA (Ser169) Antibody.)

Related Product Information for anti-NuMA antibody

Description: Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:7769006, PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:12445386, PubMed:11956313). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:23027904, PubMed:22327364, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24996901, PubMed:24371089). Binds also to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24996901, PubMed:24371089). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity).

Post Translational Modifications: Phosphorylation and dephosphorylation on Thr-2055 regulates the extent of cortical NUMA1 and the dynein-dynactin complex localization during mitotic metaphase and anaphase (PubMed:23921553). In metaphase, phosphorylation on Thr-2055 occurs in a kinase CDK1-dependent manner; this phosphorylation maintains low levels of cortical dynein-dynactin complex at metaphase, and hence proper spindle positioning (PubMed:7769006, PubMed:23921553, PubMed:24371089). In anaphase, dephosphorylated on Thr-2055 by phosphatase PPP2CA; this dephosphorylation stimulates its membrane association and with the dynein-dynactin complex its enrichment at the cell cortex, and hence robust spindle elongation (PubMed:23921553, PubMed:24371089). Probably also phosphorylated on Thr-2015 and Ser-2087 by CDK1; these phosphorylations may regulate its cell cortex recruitment during metaphase and anaphase (PubMed:23870127). Phosphorylated on Thr-1047, Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization (PubMed:22327364). ADP-ribosylated by TNKS at the onset of mitosis; ADP-ribosylation is not required for its localization to spindle poles (PubMed:16076287). O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status (PubMed:20068230). Ubiquitinated with 'Lys-63'-linked polyubiquitin chains. Deubiquitination by the BRISC complex is important for the incorporation of NUMA1 into mitotic spindle poles and normal spindle pole function, probably by modulating interactions between NUMA1, dynein-dynactin complex and importin-beta.

Subunit Structure: Homodimer (PubMed:10075938). Also forms multiarm oligomers by association of C-terminal tail domains, oligomers may further assemble to form a hexagonal nuclear lattice-like network (PubMed:10075938). Associates with the dynein-dynactin complex; this association promotes the transport and accumulation of NUMA1 at the mitotic spindle poles that is inhibited by the BRISC complex in a PLK1-dependent manner (PubMed:10811826, PubMed:17172455, PubMed:23027904, PubMed:22327364, PubMed:26195665). Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (PubMed:26766442). Interacts (via C-terminus) with microtubules (MTs); this interaction is direct and promotes both MT bundle formation and stability in a dynein-dynactin complex- and CDK1-independent manner (PubMed:12445386, PubMed:11956313, PubMed:26765568). Interacts with EPB41 and EPB41L2; these interactions are negatively regulated by CDK1 during metaphase and are important for anaphase-specific localization of NUMA1 in symmetrically dividing cells (PubMed:23870127, PubMed:24996901). Interacts (via C-terminus) with GPSM2 (via TPR repeats); this interaction is direct, prevented by competitive binding of INSC, is inhibited in a PLK1-dependent manner, blocks the association of NUMA1 with MTs and inhibits NUMA1-induced MT bundle formation, prevents the association of NUMA1 with SPAG5, induces mitotic spindle pole localization of GPSM2, both metaphase cell cortex localization of NUMA1 and mitotic spindle organization (PubMed:11781568, PubMed:12445386, PubMed:22327364, PubMed:24109598, PubMed:27462074, PubMed:21816348). Does not interact with GPSM2 during anaphase (PubMed:23870127). Interacts (via C-terminus) with the nuclear importin alpha/importin beta receptor; this interaction is inhibited by RanGTP (PubMed:11163243). Interacts (via C-terminus) with KPNB1; this interaction is inhibited by RanGTP and the BRISC complex (PubMed:11229403, PubMed:26195665). Interacts with ABRAXAS2 and the BRISC complex; these interactions regulate mitotic spindle assembly (PubMed:26195665). Interacts (via N-terminal end of the coiled-coil domain) with RAE1; this interaction promotes mitotic spindle formation (PubMed:17172455). Interacts (via C-terminus) with SPAG5 (via C-terminus); this interaction promotes the recruitment of SPAG5 to the MTs at spindle poles in a dynein-dynactin-dependent manner and regulates mitotic spindle organization and proper chromosome alignment during mitosis (PubMed:27462074). Interacts with TNKS; this interaction occurs at the onset of mitosis (PubMed:12080061, PubMed:16076287). Interacts with TNKS2 (PubMed:12080061). Interacts with tubulin (PubMed:11956313).

Similarity: The C-terminal tubulin-binding domain mediates direct binding to microtubules, independently of dynein-dynactin complex, and induces their bundling and stabilization (PubMed:11956313). The 4.1-binding domain is necessary for its cortical stability and spindle orientation (PubMed:24109598).

NCBI and Uniprot Product Information

• NCBI GI #: 71361682
• NCBI GeneID: 4926
• NCBI Accession #: NP_006176.2
• NCBI GenBank Nucleotide #: NP_006176.2
• UniProt Accession #: Q14980
• Molecular Weight: Observed: 240KD; Predicted: 239 kDa
• NCBI Official Full Name: nuclear mitotic apparatus protein 1 isoform 1
• NCBI Official Synonym Full Names: nuclear mitotic apparatus protein 1
• NCBI Official Symbol: NUMA1
• NCBI Official Synonym Symbols: NUMA; NMP-22
• NCBI Protein Information: nuclear mitotic apparatus protein 1
• UniProt Protein Name: Nuclear mitotic apparatus protein 1
• Protein Family: Nucleomorphin
• UniProt Gene Name: NUMA1
• UniProt Synonym Gene Names: NUMA; NuMA protein
• UniProt Entry Name: NUMA1_HUMAN

NCBI Description

This gene encodes a large protein that forms a structural component of the nuclear matrix. The encoded protein interacts with microtubules and plays a role in the formation and organization of the mitotic spindle during cell division. Chromosomal translocation of this gene with the RARA (retinoic acid receptor, alpha) gene on chromosome 17 have been detected in patients with acute promyelocytic leukemia. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2013]

Uniprot Description

NuMA-1: a coiled-coil nuclear protein that is required to establish and maintain mammalian spindle poles. Dissociates from condensing chromosomes during early prophase, before the complete disintegration of the nuclear lamina. As mitosis progresses it reassociates with telophase chromosomes very early during nuclear reformation, before substantial accumulation of lamins on chromosomal surfaces is evident. Two human splice-variant isoforms have been described.

Protein type: Cell cycle regulation; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 11q13

Cellular Component: spindle pole; nuclear matrix; dendrite; chromosome; cytosol; nucleoplasm; Golgi membrane; cell soma; apical part of cell; spindle microtubule; cytoplasm; spindle; nucleus

Molecular Function: protein binding; microtubule binding; structural molecule activity

Biological Process: mitosis; meiotic cell cycle; establishment of mitotic spindle orientation; cell division; mitotic cell cycle; G2/M transition of mitotic cell cycle; nuclear organization and biogenesis

Disease: Acute Promyelocytic Leukemia