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Polyclonal Antibody Gtpase Binding

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

Application Methods: Immunoprecipitation, Western Blotting

Background: OCRL1 is an inositol 5-phosphatase that selectively dephosphorylates the 5 position of the inositol ring. Its substrates include phosphatidylinositol 4,5-bisphosphate, inositol 1,4,5-trisphosphate, and inositol 1,3,4,5-tetrakisphosphate (1). Research studies indicate that mutations in OCRL1 are linked to Oculocerebrorenal syndrome or Lowe syndrome, an X-linked disorder distinguished by mental retardation and congenital cataracts, as well as Dent's disease (2,3). OCRL1 interacts with several endocytic proteins, including clathrin, AP-2, and RabGTPases (4-7). OCRL1 is localized to the Golgi complex, endosomes, and late stage clathrin-coated pits (6,8). OCRL1 controls early endosome function (8), regulating membrane traffic from endosomes to the Golgi. It is also involved in cytokinesis (9) and cilia assembly (10).

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

Application Methods: Western Blotting

Background: Tuberin is a product of the TSC2 tumor suppressor gene and an important regulator of cell proliferation and tumor development (1). Mutations in either TSC2 or the related TSC1 (hamartin) gene cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by development of multiple, widespread non-malignant tumors (2). Tuberin is directly phosphorylated at Thr1462 by Akt/PKB (3). Phosphorylation at Thr1462 and Tyr1571 regulates tuberin-hamartin complexes and tuberin activity (3-5). In addition, tuberin inhibits the mammalian target of rapamycin (mTOR), which promotes inhibition of p70 S6 kinase, activation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translation initiation), and eventual inhibition of translation (3,6,7).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Tuberin is a product of the TSC2 tumor suppressor gene and an important regulator of cell proliferation and tumor development (1). Mutations in either TSC2 or the related TSC1 (hamartin) gene cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by development of multiple, widespread non-malignant tumors (2). Tuberin is directly phosphorylated at Thr1462 by Akt/PKB (3). Phosphorylation at Thr1462 and Tyr1571 regulates tuberin-hamartin complexes and tuberin activity (3-5). In addition, tuberin inhibits the mammalian target of rapamycin (mTOR), which promotes inhibition of p70 S6 kinase, activation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translation initiation), and eventual inhibition of translation (3,6,7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Tuberin is a product of the TSC2 tumor suppressor gene and an important regulator of cell proliferation and tumor development (1). Mutations in either TSC2 or the related TSC1 (hamartin) gene cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by development of multiple, widespread non-malignant tumors (2). Tuberin is directly phosphorylated at Thr1462 by Akt/PKB (3). Phosphorylation at Thr1462 and Tyr1571 regulates tuberin-hamartin complexes and tuberin activity (3-5). In addition, tuberin inhibits the mammalian target of rapamycin (mTOR), which promotes inhibition of p70 S6 kinase, activation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translation initiation), and eventual inhibition of translation (3,6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Tuberin is a product of the TSC2 tumor suppressor gene and an important regulator of cell proliferation and tumor development (1). Mutations in either TSC2 or the related TSC1 (hamartin) gene cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by development of multiple, widespread non-malignant tumors (2). Tuberin is directly phosphorylated at Thr1462 by Akt/PKB (3). Phosphorylation at Thr1462 and Tyr1571 regulates tuberin-hamartin complexes and tuberin activity (3-5). In addition, tuberin inhibits the mammalian target of rapamycin (mTOR), which promotes inhibition of p70 S6 kinase, activation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translation initiation), and eventual inhibition of translation (3,6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Monkey, Mouse

Application Methods: Western Blotting

Background: Tuberin is a product of the TSC2 tumor suppressor gene and an important regulator of cell proliferation and tumor development (1). Mutations in either TSC2 or the related TSC1 (hamartin) gene cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by development of multiple, widespread non-malignant tumors (2). Tuberin is directly phosphorylated at Thr1462 by Akt/PKB (3). Phosphorylation at Thr1462 and Tyr1571 regulates tuberin-hamartin complexes and tuberin activity (3-5). In addition, tuberin inhibits the mammalian target of rapamycin (mTOR), which promotes inhibition of p70 S6 kinase, activation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translation initiation), and eventual inhibition of translation (3,6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Tuberin is a product of the TSC2 tumor suppressor gene and an important regulator of cell proliferation and tumor development (1). Mutations in either TSC2 or the related TSC1 (hamartin) gene cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by development of multiple, widespread non-malignant tumors (2). Tuberin is directly phosphorylated at Thr1462 by Akt/PKB (3). Phosphorylation at Thr1462 and Tyr1571 regulates tuberin-hamartin complexes and tuberin activity (3-5). In addition, tuberin inhibits the mammalian target of rapamycin (mTOR), which promotes inhibition of p70 S6 kinase, activation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translation initiation), and eventual inhibition of translation (3,6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: RanBP1 is a Ran binding protein that functions in nuclear trafficking for both nuclear import and export (1-3). Its protein sequence contains a Ran binding domain and a C-terminal nuclear export signal, which maintains its cytoplasmic localization (2,3). During nuclear export, RanBP1 forms a complex with RanGTP and CRM1/cargo, leading to dissociation of cargo from CRM1 (2,4). RanBP1 further stimulates RanGTP-RanGAP1 association to facilitate RanGTP hydrolysis and the generation of RanGDP to complete the final steps of nuclear export (5). During nuclear import, RanBP1 stabilizes the formation of a RanGDP-importin/NLS receptor-RanBP1 complex. This complex regulates the release of imported cargo into the nucleus (6,7). In addition to nuclear trafficking, RanBP1 also controls RanGTP distribution along mitotic microtubules, which localizes critical factors, such as cyclin B1 and HURP, to mitotic microtubles and regulates chromosome segregation (8,9). In vivo knock down or overexpression of RanBP1 has been shown to affect cellular ciliogenesis by regulating the local RanGTP concentation at the base of cilia (10).

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

Application Methods: Western Blotting

Background: The RalA binding protein 1 (RalBP1 or RLIP76) was originally identified as a GTP-RalA associated protein that acted as a downstream RalA effector in regulating Ral-Ras signaling (1). RalBP1 interacts with RalA and the endocytosis protein REPS2 (POB1) through its carboxy-terminal Ral binding domain. RalBP1 has an intrinsic GTPase activating function and interacts with Cdc42 through its centrally located Rho-GAP domain (1-3). A protein complex containing RalBP1/POB1/RalA regulates endocytosis of membrane receptors (4). RalBP1 also functions as a non-ABC transporter that catalyzes the ATP-dependent transport of numerous xenobiotics, including glutathione conjugates and some chemotherapeutic agents. RalBP1 transporter activity may play an important role in detoxification, drug resistance and the stress response (5-7). Increased expression of RalBP1 protein is associated with some forms of cancer and regression of cancer xenografts results from RalBP1 inhibition (8,9). Evidence to date suggests that RalBP1 may be a promising therapeutic target for cancer therapy.

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: In multicellular organisms, intercellular junctions play essential roles in tissue integrity and maintenance of cell polarity. Tight junctions (TJs) form a continuous barrier to fluids across the epithelium and endothelium (reviewed in 1). Adherens junctions (AJs) are dynamic structures that form cell-cell contacts linking cells into a continuous sheet (reviewed in 2). The actin filament-binding protein, Afadin, binds to nectin forming a connection to the actin cytoskeleton (3). AJs are formed when nectin assembles cadherin at the cell-cell adhesion site and these junctions are then involved in the formation and maintenance of TJs (4,5). Afadin has two splice variants: l-afadin, which is ubiquitously expressed, and s-afadin, which is expressed predominantly in neural tissue. s-Afadin is a shorter form lacking one of the three proline-rich regions found in l-afadin, as well as the carboxyl-terminal F-actin binding region (6). Human s-afadin is identical to AF-6, the ALL-1 fusion partner involved in acute myeloid leukemias (7). Recent work has also shown that afadin is involved in controlling the directionality of cell movement when it is localized at the leading edge of moving cells (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Mig6 was identified as a gene which is induced when quiescent fibroblasts are treated by mitogens (1). During cell cycle progression, Mig6 expression levels are also regulated (1). Mig6 mRNA levels were found to increase upon stimulation by chronic stresses including diabetic nephropathy (2). Overexpression of this gene leads to the activation of stress-activated protein kinases (SAPKs)/c-Jun amino-terminal kinases (JNKs) (2). Furthermore, Mig6 was found to interact with epidermal growth factor receptor (EGFR) when stimulated by epidermal growth factor (EGF) (3). Deletion of the Mig6 gene in mice results in hyperactivation of EGFR and signaling through the mitogen-activated protein kinase (MAPK) pathway, causing overproliferation and abnormal differentiation of epidermal keratinocytes in these animals. Inhibition of endogenous EGFR signaling by Iressa abolished skin defects observed in Mig6(-/-) mice, indicating that Mig6 is a specfic negative regulator of EGFR signaling (4). Furthermore, expression of Mig6 was significantly lower in skin, breast, pancreatic and ovarian cancers, suggesting a role of Mig6 as a tumor suppressor (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Formins are a family of large multidomain actin nucleation/polymerization proteins characterized by their catalytic FH2 domains. The mammalian diaphanous-related formin (mDia/diap) subfamily, including mDia1/diap1, mDia2/diap3 and mDia3/diap2, are effectors of Rho family small GTPases. In response to Rho, mDia/diap proteins are involved in the regulation of multiple cell functions including cytoskeletal dynamics, migration, adhesion, polarity and cell shape (reviewed in 1,2).mDia1/diap1 is activated by GTP-bound Rho, leading to Rho-associated kinase (ROCK)-dependent stress fiber formation (3,4). Rho activation of mDia1 has also been shown to regulate serum response factor (SRF)-dependent transcription (5), and has been implicated in human cancer phenotypes such as ras-mediated transformation, metastasis and invasion (reviewed in 6).mDia3/diap2, activated by the Rho family small GTPase cdc42, regulates the attachment of microtubules to the kinetochore during mitosis in mammalian cells (7).Rho-dependent activation of mDia2/diap3 is important in assembly of the contractile ring during cytokinesis (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The expansion of hexanucleotide GGGGCC repeats in the C9orf72 gene causes chromosome 9p-linked neurodegenerative diseases amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) (1,2). The specific mechanism by which of these repeats contributes to disease etiology is currently an active area of investigation (3). Several gain of function mechanisms have been proposed. These mechanisms include toxicity from C9orf72 RNA containing the hexanucleotide repeats (4) and toxicity generated from dipeptide repeat proteins produced by repeat-associated non-ATG translation (5). In addition to gain of function mechanisms, the genetic hexanucleotide repeat expansions may cause a loss of function of the C9orf72 protein. C9orf72 contains a predicted DENN (differentially expressed in normal and neoplastic cells) domain that typically functions as guanine exchange factors for Rab GTPases, proteins that play key regulatory roles in membrane trafficking (6). Consistent with C9orf72 normally functioning in membrane trafficking, biochemical and genetic studies revealed that C9orf72 forms a protein complex with Sim-Magenis chromosome region 8 (SMCR8) and WD repeat-containing protein 41 (WDR41) to regulate the autophagy-lysosomal pathway (7), suggesting that C9orf72-dependent alterations in the autophagy-lysosomal pathway might contribute to ALS/FTD pathology.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Rab7 and Rab9 are members of the Ras superfamily of small Rab GTPases (1). Both proteins are located in late endosomes, but exert different functions. Rab7 associates with the RIPL effector protein to control membrane trafficking from early to late endosome and to lysosomes (2,3). Rab7 also helps to regulate growth receptor endocytic trafficking and degradation (3,4), and maturation of phagosome and autophagic vacuoles (4-6). Rab9 interacts with its effector proteins p40 and TIP47 (7,8) to promote the MPR (mannose 6-phosphate receptor)-associated lysosomal enzyme transport between late endosomes and the trans Golgi network (9,10).

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

Application Methods: Western Blotting

Background: IQGAPs are scaffolding proteins involved in mediating cytoskeletal function. They contain multiple protein interaction domains and bind to a growing number of molecules including actin, myosin light chain, calmodulin, E-cadherin, and β-catenin (reviewed in 1). Through their GAP-related domains, they bind the small GTPases Rac1 and cdc42. IQGAPs lack GAP activity, however, and regulate small GTPases by stabilizing their GTP-bound (active) forms (2,3). Research studies have shown that the function and distribution of the IQGAP proteins widely vary. IQGAP1 is ubiquitously expressed and has been found to interact with APC (4) and the CLIP170 complex (5) in response to small GTPases, promoting cell polarization and migration. Additional research studies have suggested that IQGAP1 could play a part in the invasiveness of some cancers (6-8). IQGAP2, which is about 60% identical to IQGAP1, is expressed primarily in liver (3), but lower levels have been detected in the prostate, kidney, thyroid, stomach, and testis (9,10). Research studies have shown that IQGAP2 displays tumor suppressor properties (11). Less is known about the function of IQGAP3, but this protein is present in the lung, brain, small intestine, and testis (9) and is only expressed in proliferating cells (12), suggesting a role in cell growth and division.

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Ras activity is regulated by GAP (GTPase activating proteins) and GEFs (guanine nucleotide exchange factors). Ras-GRF1 (also known as CDC25Mm) is neuronal RasGEF and is regulated by heterotrimeric G proteins and calcium influx (1,2). Binding to calmodulin and phosphorylation stimulate Ras-GRF1 activity (1,2). Multiple PKA phosphorylation sites on Ras-GRF have been identified. Phosphorylation on the two major sites, Ser54 and Ser822, inhibits Ras-GRF activity (3). Carbachol (a muscarinic agonist)-induced phosphorylation on Ser916 is essential but not sufficient for maximal Ras-GRF activity (4). It has been reported that Ras-GRF1 also shows GEF activity toward Rac after phosphorylation by the tyrosine kinase Src (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Ras activity is regulated by GAP (GTPase activating proteins) and GEFs (guanine nucleotide exchange factors). Ras-GRF1 (also known as CDC25Mm) is neuronal RasGEF and is regulated by heterotrimeric G proteins and calcium influx (1,2). Binding to calmodulin and phosphorylation stimulate Ras-GRF1 activity (1,2). Multiple PKA phosphorylation sites on Ras-GRF have been identified. Phosphorylation on the two major sites, Ser54 and Ser822, inhibits Ras-GRF activity (3). Carbachol (a muscarinic agonist)-induced phosphorylation on Ser916 is essential but not sufficient for maximal Ras-GRF activity (4). It has been reported that Ras-GRF1 also shows GEF activity toward Rac after phosphorylation by the tyrosine kinase Src (5).

$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, Mouse, Rat

Application Methods: Western Blotting

Background: Filamins are a family of dimeric actin binding proteins that function as structural components of cell adhesion sites. They also serve as a scaffold for subcellular targeting of signaling molecules (1). The actin binding domain (α-actinin domain) located at the amino terminus is followed by as many as 24 tandem repeats of about 96 residues and the dimerization domain is located at the carboxy terminus. In addition to actin filaments, filamins associate with other structural and signaling molecules such as β-integrins, Rho/Rac/Cdc42, PKC and the insulin receptor, primarily through the carboxy-terminal dimerization domain (1-3). Filamin A, the most abundant, and filamin B are widely expressed isoforms, while filamin C is predominantly expressed in muscle (1). Filamin A is phosphorylated by PAK1 at Ser2152, which is required for PAK1-mediated actin cytoskeleton reorganization (4).

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

Application Methods: Western Blotting

Background: Rap1 and Rap2 belong to the Ras subfamily of small GTPases and are activated by a wide variety of stimuli through integrins, receptor tyrosine kinases (RTKs), G-protein coupled receptors (GPCR), death domain associated receptors (DD-R) and ion channels (1,2). Like other small GTPases, Rap activity is stimulated by guanine nucleotide exchange factors (GEF) and inactivated by GTPase activating proteins (GAP). A wide variety of Rap GEFs have been identified: C3G connects Rap1 with RTKs through adaptor proteins such as Crk, Epacs (or cAMP-GEFs) transmit signals from cAMP, and CD-GEFs (or CalDAG-GEFs) convey signals from either or both Ca2+ and DAG (1). Rap1 primarily regulates multiple integrin-dependent processes such as morphogenesis, cell-cell adhesion, hematopoiesis, leukocyte migration and tumor invasion (1,2). Rap1 may also regulate proliferation, differentiation and survival through downstream effectors including B-Raf, PI3K, RalGEF and phospholipases (PLCs) (1-4). Rap1 and Rap2 are not fuctionally redundant as they perform overlapping but distinct functions (5). Recent research indicates that Rap2 regulates Dsh subcellular localization and is required for Wnt signaling in early development (6).