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Monoclonal Antibody Gtpase Binding

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, 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).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: Rab11 family proteins consist of closely related Rab11a, Rab11b, and Rab25. They are small GTPases thought to play an essential role in regulating endocytic membrane traffic (1,2). The GTP-bound active state Rab11 proteins interact with the Rab11 family interacting proteins (Rab11FIPs) via a conserved carboxy-terminal Rab11-binding domain (3,4). At least six members of the Rab11FIPs have been identified. Based on sequence homology and domain structures, Rab11FIP1, Rab11FIP2 and Rab11FIP5 are categorized as class I subfamily members, whereas Rab11FIP3 and Rab11FIP4 belong to the class II subfamily that bind Arf6 and Rab11 proteins (5-7). Research studies have implicated Rab11 family proteins and their interacting effectors in carcinogenesis (8,9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Ran GTPase activating protein 1 (RanGAP1) regulates GTP hydrolysis by Ran, which is required for the ability of Ran to regulate nucleocytoplasmic shuttling (1). A significant fraction of cellular RanGAP1 is covalently modified by SUMO-1, which is required for relocalization of RanGAP1from the cytoplasm to the nuclear pore complex and the mitotic spindle (2-5). Research studies demonstrate that RanGAP1 sumoylation is required for stable association of RanGAP1 with RanBP2. Together with the SUMO-conjugating enzyme UBC9/UBE2I, RanGAP1 and RanBP2 are part of a SUMO E3 ligase complex that is implicated in regulating nucleocytoplasmic protein trafficking (6-8). Phosphorylation of RanGAP1 occurs in a cell-cycle-dependent manner and may play a role in regulating RanGAP1 catalytic activity (9,10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, 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.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: TBC1 domain family member 7 (TBC1D7, TBC7) belongs to a family of TBC (Tre-2/Bub2/Cdc16) containing proteins that function as GTPase-activating proteins (GAPs) (1,2). TBC1D7 was initially identified as a novel binding protein within the TSC1-TSC2 complex, where it was thought to associate with TSC1 (3,4). Additional research indicates that TBC1D7 is a third subunit of the TSC1-TSC2 complex that possesses Rheb-GAP activity and signals upstream of mTORC1 (5). Knockdown of TBC1D7 limits the association between TSC1 and TSC2, resulting in reduced Rheb-GAP activity and increased mTORC1 signaling (5). Mutations in the corresponding TBC1D7 gene result in increased mTORC1 signaling, delayed autophagy, and are associated with intellectual disability (ID) and macrocrania (6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, 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).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Tuberin/TSC2 (D93F12) XP® Rabbit mAb #4308.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

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
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
Human

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
Human, 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
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: EPAC1 and EPAC2 (exchange proteins activated by cyclic AMP) are guanine nucleotide exchange factors (GEFs) that catalyze the exchange of GDP for GTP, activating Rap1 and Rap2 small GTPases. Rap activation by EPAC is cAMP-dependent and mediates cAMP signaling in part through protein kinase A (PKA) (reviewed in 1). EPAC signaling plays a significant role in a number of cellular processes including migration and focal adhesion formation (2), exocytosis (3), insulin signaling (4), axon growth and guidance (5) and neurotransmitter release (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The small GTPase Ran resides on both the cytosolic and nucleosolic sides of the nuclear pore complex (NPC) and regulates the import and export of various proteins to and from the nucleus. Like other small GTPases, Ran exists in either a GTP-bound or GDP-bound state. RanGTP that resides in the nucleus and promotes nuclear export, while cytosolic RanGDP promotes import. The gradient of RanGTP across the nuclear membrane allows for appropriate movement of cargo proteins across the NPC as well as maintenance of the mitotic spindle (1-3).Nuclear transport factor 2 (NTF2) regulates the subcellular distribution and function of Ran (4-5). The NTF2 homodimer facilitates the diffusion of RanGDP through NPCs via transient interactions with phenylalanine-glycine (FG) repeat domains on NPC proteins. NTF2 stabilizes the GDP-bound form of Ran until it is induced to dissociate by a nuclear factor in an ATP-dependent manor, thus allowing the guanine nucleotide exchange factor (GEF) RCC1 to mediate exchange of GDP for GTP on Ran (6-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: EPAC1 and EPAC2 (exchange proteins activated by cyclic AMP) are guanine nucleotide exchange factors (GEFs) that catalyze the exchange of GDP for GTP, activating Rap1 and Rap2 small GTPases. Rap activation by EPAC is cAMP-dependent and mediates cAMP signaling in part through protein kinase A (PKA) (reviewed in 1). EPAC signaling plays a significant role in a number of cellular processes including migration and focal adhesion formation (2), exocytosis (3), insulin signaling (4), axon growth and guidance (5) and neurotransmitter release (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: In Drosophila, lethal giant larvae (lgl), discs large (dlg), and scribble (scrib) act as tumor suppressor genes. Their loss of function in flies causes neoplastic overgrowth of larval brain tissue and imaginal epithelial cells hallmarked by disruption of the cytoskeletal network and cellular polarity (1,2). The human homolog of the Drosophila lgl protein, lethal giant larvae protein homolog 1(LLGL1), is a cytoskeletal protein implicated in regulating cellular organization, migration, and cell polarity (3). As in Drosophila, decreased expression of LLGL1 correlates with an increased incidence of cellular overgrowth and malignant transformation (4-6). In mammalian epithelial cells, LLGL1 redistributes from the cytoplasm to regions of cell-cell contact, allowing the establishment and maintainence of a polarized morphology (7). LLGL1 also plays a role in the formation of epithelial junctions via its direct interactions with PAR6 and aPKC, the latter of which has been shown to phosphorylate LLGL1 at Ser663, thus restricting its localization to the basolateral region of the cell (8). LLGL1 may also play an additional, unrealized role in cellular development and differentiation as indicated by the fact that Drosophila lgl has been implicated in controlling self-renewal and differentiation of progenitor cells (9). Recent studies in mice have suggested that a mammalian LLGL1 homolog that does not have tumor suppressor-like acitvity, LLGL2, is required for proper polarized invasion of trophoblasts and efficient branching morphogenesis during placental development (10).

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

Application Methods: Immunoprecipitation, 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).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated LRRK2 (D18E12) Rabbit mAb #13046.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Parkinson’s disease (PD), the second most common neurodegenerative disease after Alzheimer’s, is a progressive movement disorder characterized by rigidity, tremors, and postural instability. The pathological hallmarks of PD are progressive loss of dopaminergic neurons in the substantia nigra of the ventral midbrain and the presence of intracellular Lewy bodies (protein aggregates of α-synuclein, ubiquitin, and other components) in surviving neurons of the brain stem (1). Research studies have shown various genes and loci are genetically linked to PD including α-synuclein/PARK1 and 4, parkin/PARK2, UCH-L1/PARK5, PINK1/PARK6, DJ-1/PARK7, LRRK2/PARK8, synphilin-1, and NR4A2 (2).Leucine-rich repeat kinase 2 (LRRK2) contains amino-terminal leucine-rich repeats (LRR), a Ras-like small GTP binding protein-like (ROC) domain, an MLK protein kinase domain, and a carboxy-terminal WD40 repeat domain. Research studies have linked at least 20 LRRK2 mutations to PD, with the G2019S mutation being the most prevalent (3). The G2019S mutation causes increased LRRK2 kinase activity, which induces a progressive reduction in neurite length that leads to progressive neurite loss and decreased neuronal survival (4). Researchers are currently testing the MLK inhibitor CEP-1347 in PD clinical trials, indicating the potential value of LRRK2 as a therapeutic target for treatment of PD (5).