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Human Ras Protein Signal Transduction

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Interleukin-2 (IL-2) is a T cell stimulatory cytokine best known for inducing T cell proliferation and NK cell proliferation and activation (1,2). IL-2 also promotes peripheral development of regulatory T cells (Tregs) (3,4). Conversely, IL-2 is involved in the activation-induced cell death (AICD) that is observed post T cell expansion by increasing levels of Fas on CD4+ T cells (5). The effects of IL-2 are mediated through a trimeric receptor complex consisting of IL-2Rα, IL-2Rβ, and the common gamma chain, γc (1,2). IL-2Rα binds exclusively to IL-2 with low affinity and increases the binding affinity of the whole receptor complex including IL-2Rβ and γc subunits. IL-15 also binds to IL-2Rβ (1,2). γc is used by other cytokines including IL-4, IL-7, IL-9, IL-15, and IL-21 (1,2). Binding of IL-2 initiates signaling cascades involving Jak1, Jak3, Stat5, and the PI3K/Akt pathways (1,2).

$159
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to allophycocyanin (APC) and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Interleukin-2 (IL-2) is a T cell stimulatory cytokine best known for inducing T cell proliferation and NK cell proliferation and activation (1,2). IL-2 also promotes peripheral development of regulatory T cells (Tregs) (3,4). Conversely, IL-2 is involved in the activation-induced cell death (AICD) that is observed post T cell expansion by increasing levels of Fas on CD4+ T cells (5). The effects of IL-2 are mediated through a trimeric receptor complex consisting of IL-2Rα, IL-2Rβ, and the common gamma chain, γc (1,2). IL-2Rα binds exclusively to IL-2 with low affinity and increases the binding affinity of the whole receptor complex including IL-2Rβ and γc subunits. IL-15 also binds to IL-2Rβ (1,2). γc is used by other cytokines including IL-4, IL-7, IL-9, IL-15, and IL-21 (1,2). Binding of IL-2 initiates signaling cascades involving Jak1, Jak3, Stat5, and the PI3K/Akt pathways (1,2).

$129
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Interleukin-2 (IL-2) is a T cell stimulatory cytokine best known for inducing T cell proliferation and NK cell proliferation and activation (1,2). IL-2 also promotes peripheral development of regulatory T cells (Tregs) (3,4). Conversely, IL-2 is involved in the activation-induced cell death (AICD) that is observed post T cell expansion by increasing levels of Fas on CD4+ T cells (5). The effects of IL-2 are mediated through a trimeric receptor complex consisting of IL-2Rα, IL-2Rβ, and the common gamma chain, γc (1,2). IL-2Rα binds exclusively to IL-2 with low affinity and increases the binding affinity of the whole receptor complex including IL-2Rβ and γc subunits. IL-15 also binds to IL-2Rβ (1,2). γc is used by other cytokines including IL-4, IL-7, IL-9, IL-15, and IL-21 (1,2). Binding of IL-2 initiates signaling cascades involving Jak1, Jak3, Stat5, and the PI3K/Akt pathways (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ras association domain-containing protein 1 (RASSF1) is a member of the RASSF protein family (RASSF1-10), scaffold proteins whose members are unified by the presence of a Ras association (RA) domain that gives them structural similarity to Ras effector proteins (1). The RASSF1 gene is located in a genomic region exhibiting loss of heterozygosity in a more than 90% of small cell lung cancers, and up to 50% of non-small cell lung cancers (2), strongly implicating the RASSF1 gene as a tumor suppressor. Moreover, RASSF1 expression in tumor cells has been shown to be frequently suppressed by promoter hypermethylation, further suggesting a tumor suppressor function (3-5). Although multiple isoforms (RASSF1A-H) have been described, generated by alternative splicing and/or promoter usage, RASSF1A and RASSF1C appear to be the most widely expressed in normal tissues, with RASSF1A expression lost most frequently in tumor cells (6). Notably, RASSF1A has been identified as an effector protein in the Hippo signaling pathway, where it promotes association between MST1/2 and LATS1/2, leading to suppressive phosphorylation of the transcriptional co-activators YAP and TAZ (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: R-Ras, a member of the small GTPase family, is homologous to H-, K- and N-Ras, but does not activate MAP kinase pathways and is only weakly oncogenic (1). Instead, R-Ras is engaged in integrin activation (2). The effector loop and the carboxy-terminal proline-rich and prenylation sites of R-Ras are critical for integrin activation (3,4). Phosphorylation by EphB2 receptor tyrosine kinase and Src at Tyr66 of R-Ras suppresses integrin activity (5,6).

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

Application Methods: Western Blotting

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6).

$299
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to PE-Cy7® and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Interleukin-2 (IL-2) is a T cell stimulatory cytokine best known for inducing T cell proliferation and NK cell proliferation and activation (1,2). IL-2 also promotes peripheral development of regulatory T cells (Tregs) (3,4). Conversely, IL-2 is involved in the activation-induced cell death (AICD) that is observed post T cell expansion by increasing levels of Fas on CD4+ T cells (5). The effects of IL-2 are mediated through a trimeric receptor complex consisting of IL-2Rα, IL-2Rβ, and the common gamma chain, γc (1,2). IL-2Rα binds exclusively to IL-2 with low affinity and increases the binding affinity of the whole receptor complex including IL-2Rβ and γc subunits. IL-15 also binds to IL-2Rβ (1,2). γc is used by other cytokines including IL-4, IL-7, IL-9, IL-15, and IL-21 (1,2). Binding of IL-2 initiates signaling cascades involving Jak1, Jak3, Stat5, and the PI3K/Akt pathways (1,2).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Pig, Rat, S. cerevisiae

Application Methods: Western Blotting

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6).

$759
30 rxns
1 Kit
The Active Ras Detection Kit provides all reagents necessary for measuring activation of Ras GTPase in the cell. GST-Raf1-RBD fusion protein is used to bind the activated form of GTP-bound Ras, which can then be immunoprecipitated with glutathione resin. Ras activation levels are then determined in western using a Ras mouse mAb.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The Ras superfamily of small GTP-binding proteins (G proteins) comprise a large class of proteins (over 150 members) that can be classified into at least five families based on their sequence and functional similarities: Ras, Rho, Rab, Arf, and Ran (1-3). These small G proteins have both GDP/GTP-binding and GTPase activities and function as binary switches in diverse cellular and developmental events that include cell cycle progression, cell survival, actin cytoskeletal organization, cell polarity and movement, and vesicular and nuclear transport (1). An upstream signal stimulates the dissociation of GDP from the GDP-bound form (inactive), which leads to the binding of GTP and formation of the GTP-bound form (active). The activated G protein then goes through a conformational change in its downstream effector-binding region, leading to the binding and regulation of downstream effectors. This activation can be switched off by the intrinsic GTPase activity, which hydrolyzes GTP to GDP and releases the downstream effectors. These intrinsic guanine nucleotide exchange and GTP hydrolysis activities of Ras superfamily proteins are also regulated by guanine nucleotide exchange factors (GEFs) that promote formation of the active GTP-bound form and GTPase activating proteins (GAPs) that return the GTPase to its GDP-bound inactive form (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey

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

Background: Mitofusins are mitochondrial transmembrane GTPases that function to regulate mitochondrial fusion, a process that occurs in concert with mitochondrial division and is necessary for the maintenance of structural and genetic mitochondrial integrity (1,2). Two mitofusins have been described in mammals, mitofusin-1 and -2, which share 60% amino acid identity and appear to function coordinately to regulate mitochondrial fusion (3). Mitochondrial fusion is widely recognized as important for normal cell growth and development (4), and may have evolved as a mechanism to offset the deleterious effects of mtDNA mutations (3). Null mutations in either mitofusin are embryonic lethal in mice, whereas conditional knockout studies have shown that combined deletion of mitofusin-1 and mitofusin-2 in skeletal muscle results in severe mitochondrial dysfunction (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Fructose-1,6-bisphosphatase 1 (FBP1 or FBPase 1), a rate limiting enzyme in gluconeogenesis, catalyzes the conversion of fructose-1,6-bisphosphate to fructose-6-phosphate (1). Inhibition of FBP1 expression in basal-like breast cancer (BLBC) cells leads to metabolic reprogramming, including enhanced glycolysis, which leads to increased glucose uptake, biosynthesis of macromolecules, and activation of PKM2 (1). This metabolic reprogramming endows tumor cells with cancer stem cell (CSC)-like properties, thereby increasing their tumorigenicity (1). Depletion of FBP1 was also reported in more than 600 clear cell renal cell carcinoma (ccRCC) tumors, suggesting that FBP1 may inhibit ccRCC tumor progression (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Small GTPases act as molecular switches, regulating processes such as cell migration, adhesion, proliferation and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of bound GDP for GTP, and inhibited by GTPase activating proteins (GAPs), which catalyze the hydrolysis of GTP to GDP. RASAL2 was initially identified as a GAP for the small GTPase, Ras, and later shown to interact with the Rho-GEF ECT2, and to regulate Rho activity in human astrocytoma cells (1).Researchers have implicated RASAL2 as a suppressor of migration and metastasis in human cancer (2), and have shown that RASAL2 downregulation promotes epithelial-mesenchymal transition and metastasis in ovarian cancer (3) and lung cancer (4). Conversely, other research studies show that RASAL2 can be oncogenic in triple negative breast cancer through activation of Rac1 signaling (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: DHCR24/Seladin-1 was identified as a molecular basis for desmosterolosis (1). It encodes for 24-dehydrocholesterol reductase (3β-hydroxysterol Δ-24-reductase). This enzyme reduces desmosterol in cholesterol biosynthesis (1). Recessive mutations in this gene in desmosterolosis patients lead to a defective enzyme resulting in increased levels of desmosterol (1). DHCR24/Seladin-1 is induced upon oxidative stress and was found to mediate Ras-induced senescence resulting from increased reactive oxygen species (2). Studies further indicate that the level of DHCR24/Seladin-1 is induced in the acute response and reduced in the chronic response to oxidative stress in a cholesterol dependent manner (3). Moreover, overexpression of DHCR24/Seladin-1 bearing two mutations that abolish its reductase acitivity causes the cells to lose protection from oxidative stress (3). These findings thus link the reductase activity of DHCR24/Seladin-1 to its protective role in oxidative stress. This enzyme has also been demonstrated to be a hydrogen peroxide scavenger (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Lymphocyte activation occurs in part through activation of the Ras signaling pathway following lymphocyte receptor stimulation. The RasGRP family of guanine nucleotide exchange factors (GEFs) catalyzes the exchange of GDP for GTP on Ras family small GTPases, promoting their active GTP-bound form. Diacylglycerol (DAG) or phorbol ester binding to RasGRP family members causes their translocation to the cell membrane and stimulates their activity (1,2). While T-Cells express RasGRP1, B-cells express both RasGRP1 and RasGRP3. RasGRP3 is important in linking B-cell receptor (BCR) activation to Ras signaling (3). In response to BCR stimulation, RasGRP3 is phosphorylated at Thr133 by PKC. This phosphorylation event further activates RasGRP3 in response to DAG, which stimulates PKC activity (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: RalA and RalB are members of the Ras family of small GTPases and are highly homologous in protein sequence. The functions of RalA and RalB are distinct yet overlapping. By binding to various effector proteins, RalA and RalB serve as important GTP sensors for exocytosis and membrane trafficking (1-3). RalA is required for Ras-related tumorigenesis (4) and RalB is important for tumor survival (5). In addition to tumor formation, Ral proteins also play a role in cancer cell migration and metastatic tumor invasion (6,7).

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

Application Methods: Western Blotting

Background: KSR1 (kinase supressor of Ras) was identified from a genetic screen in Drosophila and C. elegans as a component of the Ras signaling pathway (1). KSR1 has a putative carboxy-terminal kinase domain that lacks a key Lys residue for phospho-group transfer. Although reports indicate that ceramide and EGF activate KSR1 (2,3), other evidence demonstrates that KSR1 regulates Raf in a kinase-independent manner (4,5). It is now widely accepted that KSR1 functions as a scaffold that binds MEK1/2 and 14-3-3 protein constitutively and binds ERK1/2 in a Ras activation-dependent manner (1,5,6). HSP70/HSP90 and p50 Cdc37 associate with the KSR1 complex to ensure its stability (5). Multiple phosphorylation sites have been identified: Ser297 and Ser392 mediate 14-3-3 binding, and putative MAPK phosphorylation sites include Thr260, Thr274 and Ser443 (6). C-TAK1 (Cdc25C-associated kinase 1) binds and phosphorylates KSR1 at Ser392 in quiescent cells (7). In response to stimuli, Ser392 is dephosphorylated by PP2A, which leads to ERK1/2 association and allows the KSR1 complex to translocate from cytosol to membrane, where the MAPK pathway is activated (8). IMP, a Ras-responsive E3 ubiquitin ligase, is also involved in interaction with KSR1 and may regulate its localization and stability (9). Very high expression levels of KSR1 inhibit MAPK signaling, whereas physiological levels promote MAPK signaling, indicating that the scaffold protein can turn signaling "on" or "off" depending on the scaffold concentration (10).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: While overcoming the G1/S checkpoint to commence DNA replication requires cyclin E, and traversing the G2/M checkpoint to initiate mitosis requires cyclin B to be present, cyclin A seems to be required for both S-phase and M-phase (1). A number of studies have described the ability of over-expressed cyclin A to accellerate the G1 to S transition causing DNA replication, and cyclin A antisense DNA can prevent DNA replication (2-4). Cyclin A availability is apparently the rate-limiting step for entry into mitosis, and cyclin A is required for completion of prophase (5). At late prophase, cyclin A may no longer be necessary as cdc2/cyclinB1 becomes active (5).

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

Application Methods: Western Blotting

Background: RalA and RalB are members of the Ras family of small GTPases and are highly homologous in protein sequence. The functions of RalA and RalB are distinct yet overlapping. By binding to various effector proteins, RalA and RalB serve as important GTP sensors for exocytosis and membrane trafficking (1-3). RalA is required for Ras-related tumorigenesis (4) and RalB is important for tumor survival (5). In addition to tumor formation, Ral proteins also play a role in cancer cell migration and metastatic tumor invasion (6,7).