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Hamster Mitosis

Also showing Hamster Regulation of Mitosis

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The initiation of DNA replication in mammalian cells is a highly coordinated process that ensures duplication of the genome only once per cell division cycle. Origins of replication are dispersed throughout the genome, and their activities are regulated via the sequential binding of pre-replication and replication factors. The origin recognition complex (ORC) is thought to be bound to chromatin throughout the cell cycle (1,2). The pre-replication complex (Pre-RC) forms in late mitosis/early G1 phase beginning with the binding of CDT1 and cdc6 to the origin, which allows binding of the heterohexameric MCM2-7 complex. The MCM complex is thought to be the replicative helicase, and formation of the pre-RC is referred to as chromatin licensing. Subsequent initiation of DNA replication requires the activation of the S-phase promoting kinases cdk2 and cdc7. Cdc7, which is active only in complex with its regulatory subunit dbf4, phosphorylates MCM proteins bound to chromatin and allows binding of the replication factor cdc45 and DNA polymerase (3,4).Replication licensing is controlled in part by the degradation of cdc6 in quiescent cells. Phosphorylation of cdc6 by cdk2 prevents its degradation, allowing pre-replication complexes to form (5). Cdc6 has recently been shown to play an important role in the intra-S-phase p21 Waf1/Cip1-dependent DNA damage response (6,7). Both cdc6 and CDT1 are degraded by the ubiquitin proteasome pathway in response to DNA damage associated with re-replication (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey

Application Methods: Western Blotting

Background: The entry of eukaryotic cells into mitosis is regulated by cdc2 kinase activation, a process controlled at several steps including cyclin binding and phosphorylation of cdc2 at Thr161 (1). However, the critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of cdc2 at Thr14 and Tyr15 (2). Phosphorylation at Thr14 and Tyr15, resulting in inhibition of cdc2, can be carried out by Wee1 and Myt1 protein kinases (3,4). The cdc25 phosphatase may be responsible for removal of phosphates at Thr14 and Tyr15 and subsequent activation of cdc2 (1,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The entry of eukaryotic cells into mitosis is regulated by cdc2 kinase activation, a process controlled at several steps including cyclin binding and phosphorylation of cdc2 at Thr161 (1). However, the critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of cdc2 at Thr14 and Tyr15 (2). Phosphorylation at Thr14 and Tyr15, resulting in inhibition of cdc2, can be carried out by Wee1 and Myt1 protein kinases (3,4). The cdc25 phosphatase may be responsible for removal of phosphates at Thr14 and Tyr15 and subsequent activation of cdc2 (1,5).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Dog, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Protein phosphatase 1 (PP1) is a ubiquitous eukaryotic protein serine/threonine phosphatase involved in the regulation of various cell functions. Substrate specificity is determined by the binding of a regulatory subunit to the PP1 catalytic subunit (PP1c). It is estimated that over fifty different regulatory subunits exist (1).The myosin phosphatase holoenzyme is composed of three subunits: PP1c, a targeting/regulatory subunit (MYPT/myosin-binding subunit of myosin phosphatase), and a 20 kDa subunit of unknown function (M20). MYPT binding to PP1cδ alters the conformation of the catalytic cleft and increases enzyme activity and specificity (2). Two MYPT isoforms that are 61% identical have been described. MYPT1 is widely expressed, while MYPT2 expression appears to be exclusive to heart and brain (3). Related family members include MBS85, MYPT3, and TIMAP (4).Myosin phosphatase regulates the interaction of actin and myosin in response to signaling through the small GTPase Rho. Rho activity inhibits myosin phosphatase via Rho-associated kinase (ROCK). Phosphorylation of MYPT1 at Thr696 and Thr853 results in phosphatase inhibition and cytoskeletal reorganization (5,6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Protein phosphatase 1 (PP1) is a ubiquitous eukaryotic protein serine/threonine phosphatase involved in the regulation of various cell functions. Substrate specificity is determined by the binding of a regulatory subunit to the PP1 catalytic subunit (PP1c). It is estimated that over fifty different regulatory subunits exist (1).The myosin phosphatase holoenzyme is composed of three subunits: PP1c, a targeting/regulatory subunit (MYPT/myosin-binding subunit of myosin phosphatase), and a 20 kDa subunit of unknown function (M20). MYPT binding to PP1cδ alters the conformation of the catalytic cleft and increases enzyme activity and specificity (2). Two MYPT isoforms that are 61% identical have been described. MYPT1 is widely expressed, while MYPT2 expression appears to be exclusive to heart and brain (3). Related family members include MBS85, MYPT3, and TIMAP (4).Myosin phosphatase regulates the interaction of actin and myosin in response to signaling through the small GTPase Rho. Rho activity inhibits myosin phosphatase via Rho-associated kinase (ROCK). Phosphorylation of MYPT1 at Thr696 and Thr853 results in phosphatase inhibition and cytoskeletal reorganization (5,6).

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

Application Methods: Western Blotting

Background: Ran is a small GTPase of the Ras family that plays a central role in the spacial and temperal organization of eukaryotic cells. During interphase, Ran-GDP localizes to the cytoplasm and Ran-GTP to the nucleus. This polarized localization of Ran ensures its role in nuclear transport (1). During mitosis, Ran-GTP is chromatin associated, where it promotes spindle assembly and nuclear envolope formation (1,2). In S phase, Ran-GTP associates with and inhibits MCM helicase, ensuring precise chromosomal DNA duplication during the cell cycle (3).

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

Application Methods: Western Blotting

Background: Reptin/RuvBL2 and Pontin/RuvBL1 are closely related members of the AAA+ (ATPase associated with diverse cellular activities) superfamily of proteins, and are putatively homologous to bacterial RuvB proteins that drive branch migration of Holliday junctions (1). Reptin and Pontin function together as essential components of chromatin remodeling and modification complexes, such as INO80, TIP60, SRCAP, and Uri1, which play key roles in regulating gene transcription (1,2). In their capacity as essential transcriptional co-regulators, Reptin and Pontin have both been implicated in oncogenic transformations, including those driven by c-Myc, β-catenin, and E1A (2-7).

$303
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Cofilin and actin-depolymerization factor (ADF) are members of a family of essential conserved small actin-binding proteins that play pivotal roles in cytokinesis, endocytosis, embryonic development, stress response, and tissue regeneration (1). In response to stimuli, cofilin promotes the regeneration of actin filaments by severing preexisting filaments (2). The severing activity of cofilin is inhibited by LIMK or TESK phosphorylation at Ser3 of cofilin (3-5). Phosphorylation at Ser3 also regulates cofilin translocation from the nucleus to the cytoplasm (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Cofilin is a conserved actin-severing protein required for processes that rely on actin dynamics, including cytokinesis and cell motility (reviewed in 1). Regulation of actin dynamics requires the controlled cycling between the phosphorylated and unphosphorylated forms of cofilin (2). The severing activity of cofilin is inhibited by LIMK or TESK phosphorylation at the conserved amino-terminal Ser3 of cofilin (3,4). Slingshot (SSH) phosphatase, for which there have been three mammalian isoforms identified, dephosphorylates cofilin in vivo (5). Chronophin (CIN, PDXP) is a haloacid dehalogenase phosphatase that also dephosphorylates cofilin. Alteration of CIN activity through overexpression of either the wildtype or phosphatase-inactive mutant CIN interferes with actin dynamics, cell morphology and cytokinesis (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Wiskott-Aldrich syndrome proteins (WASPs) mediate actin dynamics by activating the Arp2/3 actin nucleation complex in response to activated Rho family GTPases. In mammals, five WASP family members have been described. Hematopoietic WASP and ubiquitously expressed N-WASP are autoinhibited in unstimulated cells. Upon stimulation they are activated by cdc42, which relieves the autoinhibition in conjunction with phosphatidyl inositol 4,5-bisphosphate. Three WAVE (Wasf, SCAR) family proteins are similar in sequence to WASP and N-WASP but lack the WASP/N-WASP autoinhibition domains and are indirectly activated by Rac (reviewed in 1). Both WASP and WAVE functions appear to be essential, as knockout of either N-WASP or Scar-2 in mice results in cardiac and neuronal defects and embryonic lethality (2,3). Loss of WASP results in immune system defects and fewer immune cells (4). WAVE-2 (WASF2) is widely distributed, while WAVE-1 and WAVE-3 are strongly expressed in brain (5). WAVE-3 may act as a tumor suppressor in neuroblastoma, a childhood disease of the sympathetic nervous system (6). Increased expression of WAVE-3 is seen in breast cancer, and studies in breast adenocarcinoma cells indicate that WAVE-3 regulates breast cancer progression, invasion and metastasis through the p38 mitogen-activated protein kinase (MAPK) pathway (7,8).

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

Application Methods: Western Blotting

Background: Rho family small GTPases regulate processes such as cell migration, adhesion, proliferation, and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of GDP for GTP. GEF-H1 is a Rho GEF that localizes to microtubules and regulates Rho activity in response to microtubule destabilization (1). Loss of interaction between GEF-H1 and microtubules leads to activation of Rho (2). Phosphorylation of GEF-H1 at Ser886 (Ser885 in mouse), a site located in the 14-3-3 binding motif, has been implicated in recruitment of 14-3-3 and GEF-H1 to microtubules (3), and in the regulation of RhoA activity in response to mitotic kinases during cytokinesis (4).GEF-H1 has also been shown to localize to tight junctions and modulate polarized cell permeability (5,6). GEF-H1 is inactivated by binding to cingulin at epithelial tight junctions, inactivating RhoA and leading to G1/S arrest (6).

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

Application Methods: Western Blotting

Background: BIRC6/BRUCE/APOLLON is a member of the inhibitor of apoptosis protein (IAP) family. BIRC6 is a huge 530 kDa membrane-associated protein with a single survivin-like baculoviral IAP repeat (BIR) domain at the amino terminus, and a ubiquitin-conjugating enzyme domain at the carboxy terminus (1-3). Several research studies support the notion that BIRC6 functions as a dual regulator of cell death and cell division (4-6), and BIRC6 is the only essential BIR-containing protein in mammalian cell growth and development (4,7). Research studies have documented the overexpression of BIRC6 in colon cancer stem cells and in other cancer cell lines (8,9). BIRC6 inhibits apoptosis by either 1) binding to and inhibiting caspases (10) or 2) ubiquitinating the IAP antagonist SMAC and the apoptosis initiator caspase 9, thereby targeting these proteins for proteasomal degradation (4,5). BIRC6 itself is regulated by ubiquitination and proteasomal degradation upon stimulation of apoptosis (7,11).