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Unlike Rap1B, phosphorylation in the polybasic region of Rap1A (show RAP1A Proteins) does not detectably inhibit its prenylation or its binding to SmgGDS (show RAP1GDS1 Proteins)-607.
Data show that RAP1B expression was up-regulated in esophageal squamous cell carcinoma (ESCC) clinical samples and RAP1B interacted with DVL2 (show DVL2 Proteins) and activated Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling.
The protein expression of RAP1B and HIF-1 alpha (show HIF1A Proteins) contributed to gastric cancer malignant behavior and poor prognosis.
Cholera toxin and beta-adrenergic receptor activation phosphorylate Rap1B and inhibit its prenylation and membrane localization.
Glucocorticoids mediate induction of microRNA-708 to suppress ovarian cancer metastasis through targeting Rap1B.
Adenosine signaling reduces prenylation and plasma membrane localization of Rap1B, resulting in enhanced tumor cell scattering and invasiveness.
High concentrations of extracellular adenosine in the tumor microenvironment can chronically activate A2B (show ADORA2B Proteins) receptors to suppress Rap1B prenylation and signaling at the cell membrane, resulting in reduced cell-cell contact and promoting cell scattering.
TMZ as a standard chemotherapeutic agent for GBM inhibits the Rap1B expression and actin cytoskeleton remodeling to exert its cell killing by upregulating miR (show MLXIP Proteins)-181a/b/c/d subunits
Rap1b in both smooth muscle and endothelium plays a key role in maintaining blood pressure by controlling normal vascular tone.
findings show Rap1b expression decreased significantly in tubules of renal biopsies from patients with diabetic nephropathy (DN); findings indicate Rap1b ameliorates tubular injury and slows progression of DN by modulation of mitochondrial dysfunction via C/EBP-beta-PGC-1alpha signaling
These findings ascribe a new function to SLAT, and identify Rap1 as a target of SLAT function in TCR-mediated inside-out signaling.
Rap1 Is Essential for Mouse Development and Formation of Functional Vasculature
findings reveal key roles for the bidirectional synaptic expression of the Rap1b small GTPase (show RACGAP1 Proteins) and an associated local synaptic protein translation network in this process.
Rap1 deficiency impaired T-cell homeostasis.
Rap1b deficiency promoted the transcellular route of diapedesis through endothelial cell. Increased transcellular migration of Rap1b-deficient neutrophils in vitro was selectively mediated by enhanced PI3K-Akt (show AKT1 Proteins) activation and invadopodia-like protrusions.
Talin1 and Rap1 are critical for resorptive function, and their selective inhibition in mature osteoclasts retards pathological bone loss.
two different activation mechanisms of Rap1b as well as novel functions of Rap1b in platelet secretion and in integrin alpha(IIb)beta(3) outside-in signaling.
Rap1b-dependent VEGF (show VEGFA Proteins)-VEGFR2 (show KDR Proteins) activation is in part mediated via integrin alpha(v (show ITGAV Proteins))beta(3).
Upon activation, Rap1b colocalized with the scaffolding protein IQGAP1.
This gene encodes a member of the RAS-like small GTP-binding protein superfamily. Members of this family regulate multiple cellular processes including cell adhesion and growth and differentiation. This protein localizes to cellular membranes and has been shown to regulate integrin-mediated cell signaling. This protein also plays a role in regulating outside-in signaling in platelets. Alternate splicing results in multiple transcript variants. Pseudogenes of this gene are found on chromosomes 3, 5, 6 and 9.
RAP1B, member of RAS oncogene family
, ras-related protein Rap-1b
, GTP-binding protein smg p21B
, RAS-related protein RAP1B
, Ras family small GTP binding protein RAP1B
, small GTP binding protein
, RAS related protein 1b