Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
The protein encoded by RASA1 is located in the cytoplasm and is part of the GAP1 family of GTPase-activating proteins. Additionally we are shipping RASA1 Kits (14) and RASA1 Proteins (4) and many more products for this protein.
Showing 10 out of 102 products:
Human Monoclonal RASA1 Primary Antibody for WB - ABIN395417
Hemerly, Bastos, Cerutti: Identification of several novel non-p.R132 IDH1 variants in thyroid carcinomas. in European journal of endocrinology / European Federation of Endocrine Societies 2010
Show all 5 references for ABIN395417
Human Polyclonal RASA1 Primary Antibody for EIA, WB - ABIN954457
Wiemels, Kang, Chang, Zheng, Kouyoumji, Zhang, Smith, Scelo, Metayer, Buffler, Wiencke: Backtracking RAS mutations in high hyperdiploid childhood acute lymphoblastic leukemia. in Blood cells, molecules & diseases 2010
Show all 5 references for ABIN954457
Human Polyclonal RASA1 Primary Antibody for WB - ABIN656874
Oinuma, Ito, Katoh, Negishi: Semaphorin 4D/Plexin-B1 stimulates PTEN activity through R-Ras GTPase-activating protein activity, inducing growth cone collapse in hippocampal neurons. in The Journal of biological chemistry 2010
Cow (Bovine) Monoclonal RASA1 Primary Antibody for ICC, IF - ABIN266005
Muto, Yi, Harrison, Dávalos, Fancher, Ziegler, Feigel, Kondo, Nishibe, Sessa, Dardik: Eph-B4 prevents venous adaptive remodeling in the adult arterial environment. in The Journal of experimental medicine 2011
Data show that patients with low level of Ras GTPase-activating protein 1 (RASA1) expression correlated with a significantly poorer survival compared to those with high level of RASA1 expression.
Results show that oncogenic KRAS can activate Rho through miR-31-mediated regulation of RASA1 indicating miR-31 acts as a KRAS effector to modulate invasion and migration in pancreatic cancer.
PTP1B (show PTPN1 Antibodies) dephosphorylates PITX1 (show PITX1 Antibodies) to weaken its protein stability and the transcriptional activity for p120RasGAP gene expression
Data suggest that, in response to netrin-1 (show NTN1 Antibodies)/netrin receptor (DCC (show DCC Antibodies)) signaling, p120RasGAP is recruited to growth cones and supports axon outgrowth; p120RasGAP Src (show SRC Antibodies) homology 2 domains exhibit scaffolding properties sufficient to support axon outgrowth.
Maternal and fetal capillary malformation-arteriovenous malformation due to a novel RASA1 mutation presenting with prenatal non-immune hydrops fetalis have been found.
This is the second largest study on isolated, non-syndromic Port-wine stain; data suggest that GNAQ (show GNAQ Antibodies) is the main genetic determinant in this condition. Moreover, isolated port-wine stains are distinct from capillary malformations seen in RASA1 disorders.
Data showed that hypoxia regulated the expression of miR (show MLXIP Antibodies)-182 and RASA1 to promote HCC (show FAM126A Antibodies) angiogenesis.
p120RasGAP shields Akt (show AKT1 Antibodies) from deactivating phosphatases in FGF1 (show FGF1 Antibodies) signaling, but loses this ability once cleaved by caspase-3 (show CASP3 Antibodies).
Capillary malformation-arteriovenous malformation syndrome (CM-AVM) is an autosomal dominant disorder caused by RASA1 mutations.
Multifocal, small, round-to-oval, pinkish-to-red cutaneous capillary malformations are seen in more than 90% of people with RASA1 mutations.
The data suggest that nitrosylation of H-Ras (show HRAS Antibodies) rearranges the adsorptive potential and intrinsic GTPase (show RACGAP1 Antibodies) activity of H-Ras (show HRAS Antibodies) through modification of C-terminal cysteines of molecule.
Double-deficient RASA1-neurofibromin 1 (show NF1 Antibodies) mice developed T cell acute lymphoblastic leukemia/lymphoma, which originated at an early point in T cell development and was dependent on activating mutations in the Notch1 (show NOTCH1 Antibodies) gene.
Rasa1 may have a role in pathogenesis of capillary malformation-arteriovenous malformation in a mouse model
Regulation of Rasa1 translation by miR (show MLXIP Antibodies)-132 was seen in severed axons, demonstrating local function within the axon.
RASA1 mutation is responsible for the aberrant lymphatic architecture and functional abnormalities, as visualized in the PKWS subject and in the animal model.
MicroRNA-31 activates the RAS pathway and functions as an oncogenic MicroRNA by repressing RAS p21 (show D4S234E Antibodies) GTPase activating protein 1 (RASA1)
14-3-3 (show YWHAQ Antibodies) negatively regulates the RGC downstream of the PI3-kinase (show PIK3CA Antibodies)/Akt (show AKT1 Antibodies) signaling pathway
Caspase-3 (show CASP3 Antibodies) is a stress intensity sensor that controls cell fate by either initiating a RasGAP cleavage-dependent cell resistance program or a cell suicide response mediated by akt (show AKT1 Antibodies).
Data reveal a role for RASA1 as a physiological negative regulator of lymphatic endothelial cell growth that maintains the lymphatic vasculature in a quiescent functional state through its ability to inhibit Ras signal transduction.
Ca2 (show CA2 Antibodies)+-dependent monomer and dimer formation switches CAPRI (show RASA4 Antibodies) Protein between Ras GTPase-activating protein (GAP) and RapGAP (show RAP1GAP Antibodies) activities
statins inhibit GGPP biosynthesis in the mevalonate pathway, and then inhibit signal transduction in the Ras/ERK (show EPHB2 Antibodies) and Ras/Akt (show AKT1 Antibodies) pathways, thereby inhibiting bFGF (show FGF2 Antibodies), HGF (show HGF Antibodies), TGF-beta (show TGFB1 Antibodies) expression
The protein encoded by this gene is located in the cytoplasm and is part of the GAP1 family of GTPase-activating proteins. The gene product stimulates the GTPase activity of normal RAS p21 but not its oncogenic counterpart. Acting as a suppressor of RAS function, the protein enhances the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, thereby allowing control of cellular proliferation and differentiation. Mutations leading to changes in the binding sites of either protein are associated with basal cell carcinomas. Mutations also have been associated with hereditary capillary malformations (CM) with or without arteriovenous malformations (AVM) and Parkes Weber syndrome. Alternative splicing results in two isoforms where the shorter isoform, lacking the N-terminal hydrophobic region but retaining the same activity, appears to be abundantly expressed in placental but not adult tissues.
, Ras GTPase-activating protein
, vacuolar peduncule
, vacuolar pedunculi
, ras GTPase-activating protein 1
, triphosphatase-activating protein
, GTPase-activating protein
, RAS p21 protein activator (GTPase activating protein RAS p21)
, RAS p21 protein activator 1