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Rat Rac Protein Signal Transduction

Also showing Rat Regulation of Rac Protein Signal Transduction

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Epidermal growth factor receptor pathway substrate 8 (Eps8) is an adaptor protein and can be phosphorylated by several receptor tyrosine kinases including EGFR and Src (1,2). Eps8 is composed of an N-terminal PTB domain, followed by an SH3 domain and a C-terminal effector domain. Eps8 controls actin-based motility by capping the barbed end of actin and bundling actin subunits through its C-terminal effector domain (3,4). The C-terminal α hexlical structure of Eps8 interacts directly with actin to exert these capping and bundling functions (5). The actin capping activity requires the release of Eps8 autoinhibitory binding through SH3 domain interaction with an adaptor molecule, such as Abi-1 (6). This SH3 domain of Eps8 also binds to RN-tre to regulate the down stream Rab5-mediated endocytosis pathway (6). Eps8 functions by binding several receptor tyrosine kinases, such as EGFR or FGFR, to enhance receptor mediated mitogenic Rac signaling and Rab5 endocytosis (6,7). The effector region of Eps8 is necessary for this process. By association with Abi-1 and forming the Eps8/Abi-1/Sos-1 complex, Eps8 couples initial growth factor stimulation to actin motility and the Rac activation pathway (8,9). Eps8 has been shown to be important in the cellular function of filopodial protrusions, cell migration, microvilli formation, and focal adhesion (10-13). Research studies have demonstrated that through its involvement in actin related cellular functions, Eps8 plays a role in cancer cell growth, survival, motility, and invasiveness (14-18).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated OGT (D1D8Q) Rabbit mAb #24083.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: O-GlcNAcylation is a post-translational modification where β-D-N-acetylglucosamine (GlcNAc) is covalently linked to cytoplasmic and nuclear proteins at serine or threonine residues (1,2). This modification is important in many cellular processes including metabolism, cell growth and morphogenesis, apoptosis, and transcription (2,3), and research studies have implicated this modification in cancer (1). The reversible protein modification by O-GlcNAc, which has been suggested to be a nutrient and stress sensor, is catalyzed by two highly conserved enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) (4).

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

Application Methods: Western Blotting

Background: ADP-ribosylation factor (Arf) proteins are low molecular weight GTP binding proteins that belong to the Ras GTPase superfamily (1). Arf proteins are grouped into three distinct classes based on amino acid sequence and structural similarity, with Arf6 as the single class III protein to date. Arf6 is localized mainly to the plasma membrane and endosomes (1,2). This small GTPase interacts with PIP5K, PLD and Rac1, proteins important in lipid metabolism and actin regulation. Arf6 function depends upon its cycling between GDP- and GTP-bound states, which is regulated by associated GAP and GEF factors (3,4). Plasma membrane-associated Arf6 appears to play several functions during the many steps of membrane trafficking, including regulating membrane receptor internalization in both clathrin-dependent and independent pathways, endosomal recycling, and proximal actin reorganization and remodeling (5,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: O-GlcNAcylation is a post-translational modification where β-D-N-acetylglucosamine (GlcNAc) is covalently linked to cytoplasmic and nuclear proteins at serine or threonine residues (1,2). This modification is important in many cellular processes including metabolism, cell growth and morphogenesis, apoptosis, and transcription (2,3), and research studies have implicated this modification in cancer (1). The reversible protein modification by O-GlcNAc, which has been suggested to be a nutrient and stress sensor, is catalyzed by two highly conserved enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: ADP-ribosylation factor (Arf) proteins are low molecular weight GTP binding proteins that belong to the Ras GTPase superfamily (1). Arf proteins are grouped into three distinct classes based on amino acid sequence and structural similarity, with Arf6 as the single class III protein to date. Arf6 is localized mainly to the plasma membrane and endosomes (1,2). This small GTPase interacts with PIP5K, PLD and Rac1, proteins important in lipid metabolism and actin regulation. Arf6 function depends upon its cycling between GDP- and GTP-bound states, which is regulated by associated GAP and GEF factors (3,4). Plasma membrane-associated Arf6 appears to play several functions during the many steps of membrane trafficking, including regulating membrane receptor internalization in both clathrin-dependent and independent pathways, endosomal recycling, and proximal actin reorganization and remodeling (5,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Neurofibromin is a Ras-specific GTPase activating protein (RasGAP), down-regulating Ras signaling (1). Studies have shown, that mutations in NF1 inhibit its activity, resulting in benign tumors such as neurofibromas, which may form along nerves throughout the body resulting in neurofibromatosis type 1 (NF1) (2). NF1 is one of the most common autosomal dominant diseases however it remains unclear how mutation of NF1 may lead to other features of NF1 (3). In addition, NF1 mutations occur in 5-10% of human sporadic malignancies such as glioblastomas, lung adenocarcinomas, melanomas, breast and ovarian cancers, and acute myeloid leukemias. Mutations in NF1 can cause resistance to therapies including chemotherapy and radiation therapy (3).

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

Application Methods: Immunofluorescence (Immunocytochemistry), 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
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Dynamin is a family of large GTPases that has been implicated in the formation of vesicles of both the endocytotic and secretory processes (1). Dynamin plays an important role in the internalization of cell surface receptors, a process that attenuates the response to extracellular signals. It has been illustrated that dynamin interacts with signaling proteins such as Src, PLCγ, PKC and G-proteins. PKC and Src phosphorylate dynamin, and its phosphorylation may regulate the endocytosis of cell surface receptors (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: CaMKII is an important member of the calcium/calmodulin-activated protein kinase family, functioning in neural synaptic stimulation and T cell receptor signaling (1,2). CaMKII has catalytic and regulatory domains. Ca2+/calmodulin binding to the CaMKII regulatory domain relieves autoinhibition and activates the kinase (3). The activated CaMKII further autophosphorylates at Thr286 to render the kinase constitutively active (3). The threonine phosphorylation state of CaMKII can be regulated through PP1/PKA. PP1 (protein phosphatase 1) dephosphorylates phospho-CaMKII at Thr286. PKA (protein kinase A) prevents phospho-CaMKII (Thr286) dephosphorylation through an inhibitory effect on PP1 (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: CaMKII is an important member of the calcium/calmodulin-activated protein kinase family, functioning in neural synaptic stimulation and T cell receptor signaling (1,2). CaMKII has catalytic and regulatory domains. Ca2+/calmodulin binding to the CaMKII regulatory domain relieves autoinhibition and activates the kinase (3). The activated CaMKII further autophosphorylates at Thr286 to render the kinase constitutively active (3). The threonine phosphorylation state of CaMKII can be regulated through PP1/PKA. PP1 (protein phosphatase 1) dephosphorylates phospho-CaMKII at Thr286. PKA (protein kinase A) prevents phospho-CaMKII (Thr286) dephosphorylation through an inhibitory effect on PP1 (4).

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

Application Methods: Western Blotting

Background: CaMKII is an important member of the calcium/calmodulin-activated protein kinase family, functioning in neural synaptic stimulation and T cell receptor signaling (1,2). CaMKII has catalytic and regulatory domains. Ca2+/calmodulin binding to the CaMKII regulatory domain relieves autoinhibition and activates the kinase (3). The activated CaMKII further autophosphorylates at Thr286 to render the kinase constitutively active (3). The threonine phosphorylation state of CaMKII can be regulated through PP1/PKA. PP1 (protein phosphatase 1) dephosphorylates phospho-CaMKII at Thr286. PKA (protein kinase A) prevents phospho-CaMKII (Thr286) dephosphorylation through an inhibitory effect on PP1 (4).

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

Application Methods: Western Blotting

Background: CaMKII is an important member of the calcium/calmodulin-activated protein kinase family, functioning in neural synaptic stimulation and T cell receptor signaling (1,2). CaMKII has catalytic and regulatory domains. Ca2+/calmodulin binding to the CaMKII regulatory domain relieves autoinhibition and activates the kinase (3). The activated CaMKII further autophosphorylates at Thr286 to render the kinase constitutively active (3). The threonine phosphorylation state of CaMKII can be regulated through PP1/PKA. PP1 (protein phosphatase 1) dephosphorylates phospho-CaMKII at Thr286. PKA (protein kinase A) prevents phospho-CaMKII (Thr286) dephosphorylation through an inhibitory effect on PP1 (4).