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Polyclonal Antibody Immunofluorescence Immunocytochemistry Mitosis

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The cohesin complex consists of a heterodimer between SMC1 (SMC1A or B) and SMC3, bound by additional RAD21 and STAG proteins (STAG1, 2, or 3) (1,2). These proteins form a ring-like structure that mediates the cohesion of two sister chromatids after DNA replication in S phase (1,2). RAD21 and STAG2 are phosphorylated by Polo-like kinase (PLK) during prophase, which leads to the dissociation of cohesin complexes from the chromosome arms; however, cohesin remains bound to centromeres until anaphase (3,4). RAD21 is cleaved by separin/ESPL1 in anaphase, which leads to dissociation of the remaining cohesin from centromeres, enabling sister chromatids to segregate during mitosis (5). RAD21 is also cleaved by caspase-3 and caspase-7 during apoptosis, resulting in a 64 kDa carboxy-terminal cleavage product that translocates to the cytoplasm and may help to trigger apoptosis (6,7). In addition to mediating cohesion of sister chromatids, the cohesin complex plays important roles in gene regulation and DNA repair, as SMC1 and SMC3 are both phosphorylated by ATM and ATR kinases upon DNA damage (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Western Blotting

Background: INCENP (inner centromere protein antigens 135 kDa, 155 kDa) is a chromosomal passenger protein crucial for multiple events that mediate chromosome separation during mitosis (1). At prophase INCENP is associated with chromatin whereas during prometaphase and metaphase it translocates to the inner centromere (1). Depletion of INCENP results in aberrant chromosome alignment at the metaphase plate, incomplete chromosome separation, and disruption of proper spindle formation and cytokinesis (2). INCENP is part of the chromosomal passenger complex that also contains Aurora B, borealin and survivin (2). Aurora B and INCENP are mutually dependent on each other for proper localization (3), and in Drosophila cells and C.elegans embryos that lack INCENP or survivin, Aurora B cannot organize the kinetochores and the midbody (4,5). Phosphorylation on INCENP by CDK1 on Thr59 and Thr388 leads to the association of INCENP with Plk1, another important regulator of mitotic entry and exit (6). Interaction of INCENP with Plk1 is necessary for recruitment of Plk1 to the kinetochores, and the metaphase to anaphase transition (6). Interactions have also been reported between INCENP and heterochromatin protein 1α (HP1) (7) and β-tubulin (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Western Blotting

Background: INCENP (inner centromere protein antigens 135 kDa, 155 kDa) is a chromosomal passenger protein crucial for multiple events that mediate chromosome separation during mitosis (1). At prophase INCENP is associated with chromatin whereas during prometaphase and metaphase it translocates to the inner centromere (1). Depletion of INCENP results in aberrant chromosome alignment at the metaphase plate, incomplete chromosome separation, and disruption of proper spindle formation and cytokinesis (2). INCENP is part of the chromosomal passenger complex that also contains Aurora B, borealin and survivin (2). Aurora B and INCENP are mutually dependent on each other for proper localization (3), and in Drosophila cells and C.elegans embryos that lack INCENP or survivin, Aurora B cannot organize the kinetochores and the midbody (4,5). Phosphorylation on INCENP by CDK1 on Thr59 and Thr388 leads to the association of INCENP with Plk1, another important regulator of mitotic entry and exit (6). Interaction of INCENP with Plk1 is necessary for recruitment of Plk1 to the kinetochores, and the metaphase to anaphase transition (6). Interactions have also been reported between INCENP and heterochromatin protein 1α (HP1) (7) and β-tubulin (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: RCC2/TD-60 is a member of the RCC1 (regulator of chromosome condensation 1) family of guanine nucleotide exchange factors. RCC2/TD-60 is associated with the chromosome passenger complex (CPC), which also consists of aurora B kinase, borealin, INCENP (inner centromere protein) and survivin. The CPC acts at various stages of mitosis, interacts with microtubules and is required for proper chromosome segregation and cytokinesis. Regulation of aurora B kinase is key in the regulation of the CPC (reviewed in 1,2). In late mitosis, RCC2/TD-60 is required for spindle assembly and recruitment of survivin and aurora B (3). RCC2/TD-60 is also required for aurora B activation in vitro and localization of the CPC to centromeres (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The nuclear mitotic apparatus protein (NuMA) is a coiled coil protein involved in the formation and maintenance of the mitotic spindle. NuMA plays a role in chromatin organization during interphase, which influences mammary epithelial differentiation (1,2). During apoptosis, carboxy-terminal cleavage of NuMA may amplify signaling in the cell death pathway (2). NuMA is phosphorylated at numerous sites, with phosphorylation at Ser395 occurring in an ATM/ATR-dependent manner in response to DNA damage (3,4).Phosphorylation at Thr2055 by CDK1 is required for spindle pole association of NuMA at the onset of mitosis. Dephosphorylation by PPP2CA leads to enhancement of NuMA at the cell cortex in anaphase and proper cell-cycle progression (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The Ras family small GTPase Ran is involved in nuclear envelope formation, assembly of the mitotic spindle, and nuclear transport (1,2). Like other small GTPases, Ran is active in its GTP-bound form and inactive in its GDP-bound form. Nuclear RanGTP concentration is maintained through nuclear localization of guanine nucleotide exchange factor (GEF) activity, which catalyzes the exchange of bound GDP for GTP. Regulator of chromatin condensation 1 (RCC1) is the only known RanGEF (3). RCC1 is dynamically chromatin-bound throughout the cell cycle, and this localization is required for mitosis to proceed normally (4,5). Appropriate association of RCC1 with chromatin is regulated through amino-terminal phosphorylation (5,6) and methylation (7). RCC1 regulation of RanGTP levels in response to histone modifications regulates nuclear import during apoptosis (8). In mitosis RCC1 is phosphorylated at Ser11, possibly by cyclin B/cdc2 (9-11). This phosphorylation may play a role in RCC1 interaction with chromatin and RCC1 RanGEF activity (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin)

Background: The maintenance of glucose homeostasis is an essential physiological process that is regulated by hormones. An elevation in blood glucose levels during feeding stimulates insulin release from pancreatic β cells through a glucose sensing pathway (1). Insulin is synthesized as a precursor molecule, proinsulin, which is processed prior to secretion. A- and B-peptides are joined together by a disulfide bond to form insulin, while the central portion of the precursor molecule is cleaved and released as the C-peptide. Insulin stimulates glucose uptake from blood into skeletal muscle and adipose tissue. Insulin deficiency leads to type 1 diabetes mellitus (2).

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat, S. cerevisiae

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Clathrin-coated vesicles provide for the intracellular transport of cargo proteins following endocytosis and during multiple vesicle trafficking pathways. Vesicles form at specialized areas of the cell membrane where clathrin and associated proteins form clathrin-coated pits. Invagination of these cell membrane-associated pits internalizes proteins and forms an intracellular clathrin-coated vesicle (1,2). Clathrin is the most abundant protein in these vesicles and is present as a basic assembly unit called a triskelion. Each clathrin triskelion is composed of three clathrin heavy chains and three clathrin light chains. Clathrin heavy chain proteins are composed of several functional domains, including a carboxy-terminal region that permits interaction with other heavy chain proteins within a triskelion, and a globular amino-terminal region that associates with other vesicle proteins (2). Adaptor proteins, such as AP2, epsin and EPS15, are responsible for the recruitment of vesicle proteins to sites of pit formation and the assembly of the clathrin-coated vesicle. Following vesicle invagination, the GTPase dynamin constricts the neck of the nascent vesicle to complete formation of the free, cytosolic vesicle (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Echinoderm microtubule-associated protein-like 4 (EML4) is a 120 kDa microtubule-associated WD-repeat protein of the echinoderm microtubule-associated protein family (1). The expression of EML4 is necessary for correct intracellular microtubule network formation (2). EML4 protein expression is upregulated during mitosis and downregulated during the remaining cell cycle (1). During mitosis, EML4 is heavily phosphorylated and is associated with the mitotic spindle (2). The amino-terminal segment of EML4 is essential for microtubule association and function.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Ribosomal protein S3 (rpS3) is a component of the 40S ribosomal subunit and is involved in translation. HSP90 interacts with both the amino-terminus and carboxy-terminus of rpS3, preventing its ubiquitination and degradation and thereby retaining the integrity of the ribosome (1). rpS3 has also been shown to function as an endonuclease during DNA damage repair (2,3). Furthermore, overexpression of rpS3 sensitizes lymphocytic cells to cytokine-induced apoptosis, indicating a third role for rpS3 during apoptosis (4). The functions of rpS3 during DNA damage repair and apoptosis have been mapped to two distinct domains (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Nonmuscle myosin is an actin-based motor protein essential to cell motility, cell division, migration, adhesion, and polarity. The holoenzyme consists of two identical heavy chains and two sets of light chains. The light chains (MLCs) regulate myosin II activity and stability. The heavy chains (NMHCs) are encoded by three genes, MYH9, MYH10, and MYH14, which generate three different nonmuscle myosin II isoforms, IIa, IIb, and IIc, respectively (reviewed in 1). While all three isoforms perform the same enzymatic tasks, binding to and contracting actin filaments coupled to ATP hydrolysis, their cellular functions do not appear to be redundant and they have different subcellular distributions (2-5). The carboxy-terminal tail domain of myosin II is important in isoform-specific subcellular localization (6). Research studies have shown that phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin)

Background: Glucose homeostasis is regulated by hormones. Elevation of blood glucose levels during feeding stimulates insulin release from pancreatic β-cells through a glucose sensing pathway (1). Proinsulin, the insulin precursor molecule, is processed prior to its secretion. Insulin is composed of A-peptide and B-peptide which are joined by a disulfide bond. The center one-third of the molecule is cleaved and released as C-peptide, which has a longer half-life than insulin (2).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: CD2AP is a scaffolding protein that is thought to link membrane proteins to the cytoskeleton (1-3). It plays a role in formation of tight junctions in specialized cell types such as the slit diaphragm in the kidney glomerulus (4). CD2AP is also involved in the immunological synapse between CD2 expressing T cells and antigen presenting cells (5). It has been shown that interaction between CD2AP and other cytoskeletal proteins may regulate the endocytosis of EGFR (3).