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RAB1A encodes a member of the Ras superfamily of GTPases. Additionally we are shipping RAB1A Antibodies (43) and RAB1A Proteins (14) and many more products for this protein.
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Rab1 is regulated by the host in a similar fashion, and that the innate immunity kinase TAK1 (show MAP3K7 ELISA Kits) and Legionella effectors compete to regulate Rab1 by switch II modifications during infection.
Rab1A may be involved in the pathogenesis of human lung cancer in an mTOR (show FRAP1 ELISA Kits)- and MAPK (show MAPK1 ELISA Kits)-independent manner.
In clinical samples, the expression of Rab1A or DHX33 was reversely correlated with miR (show MLXIP ELISA Kits)-634. Re-expression of Rab1A or DHX33 abrogated the miR (show MLXIP ELISA Kits)-634-mediated inhibition of cell proliferation and migration. Collectively, our data suggest a tumor suppressor role of miR (show MLXIP ELISA Kits)-634 in hepatocellular carcinoma.
New Rab1 binding sites have been discovered using an ensemble of clustering methods.
Leucine-rich repeat kinase 2 (LRRK2) can interact with several Rab proteins, and such ractions may serve to recruit LRRK2 to distinct subcellular organelles to phosphorylate select substrate proteins involved in membrane trafficking events.
As a Rab1a effector, C9orf72 controls initiation of autophagy by regulating the Rab1a-dependent trafficking of the ULK1 (show ULK1 ELISA Kits) autophagy initiation complex to the phagophore.
our data indicate that miR (show MLXIP ELISA Kits)-1202 suppresses proliferation and induces endoplasmic reticulum stress and apoptosis through targeting and inhibiting Rab1A in glioma cells. These results suggest miR (show MLXIP ELISA Kits)-1202 as a potential therapeutic target for the treatment of glioma patients.
Upregulation of RAB1A is associated with triple-negative breast cancer.
For RAB1A, a high accuracy for the discrimination of human hepatocellular carcinoma and nontumorous liver tissue was observed.
The ability of Rab1 to regulate WHAMM and the Arp2/3 complex represents a distinct strategy for membrane remodeling in which a Rab G-protein recruits the actin nucleation machinery but dampens its activity.
The authors demonstrate in zebrafish that nf1 (show NF1 ELISA Kits) loss leads to aberrant activation of RAS signaling in MYCN (show MYCN ELISA Kits)-induced neuroblastomas that arise in these precursors, and that the GTPase-activating protein (GAP)-related domain (GRD) is sufficient to suppress the acceleration of neuroblastoma in nf1 (show NF1 ELISA Kits)-deficient fish, but not the hypertrophy of sympathoadrenal cells in nf1 (show NF1 ELISA Kits) mutant embryos.
Ras activity levels control the repopulation and expansion of adult melanocyte precursors after tissue loss, enabling the recovery of patterned melanocyte stripes during zebrafish appendage regeneration.
Drosophila Tempura, a novel protein prenyltransferase alpha subunit, regulates notch signaling via Rab1 and Rab11.
Results suggest a novel function for Rab1a in the regulation of cell migration through controlling integrin beta1 recycling and localization to lipid rafts via a specific downstream effector pathway.
clear effect of subcutaneous zoledronic acid administration in vivo on the prenylation of Rab1A, Rab5B (show RAB5B ELISA Kits), Rab7A (show RAB7A ELISA Kits) and Rab14 (show RAB14 ELISA Kits) in mouse peritoneal macrophages, confirming that systemic treatment with bisphosphonate drug can inhibit prenylation in myeloid cells in vivo outside the skeleton.
Rab1A regulates anterograde melanosome transport by recruiting kinesin-1 to melanosomes through interaction with SKIP
These data indicate that AMPylation of Rab1 is an effective strategy to maintain this GTPase (show RACGAP1 ELISA Kits) on the Legionella-containing vacuole membrane.
Rab1A is the first crucial component of the anterograde melanosome transport machinery to be identified in mammalian skin melanocytes.
Acute expression of Rab1 and Rab3d DN constructs partially alleviated this negative feedback mechanism and resulted in impaired ER to Golgi trafficking of procollagen.
Legionella pneumophila SidD catalyzed AMP release from Rab1, generating de-AMPylated Rab1 accessible for inactivation by LepB; identified SidD as missing link connecting processes of early Rab1 accumulation and subsequent removal during infection
Rab1 and Rab6 GTPases may play a role in modulating the function of retina by mediating the transport of nascent proteins along the early secretary pathway, particularly in the process of the light adaptation.
Data show Trs130 (mTrs130) is a component of an analogous TRAPP complex that this complex is enriched on COPI (Coat Protein (show GOLPH3 ELISA Kits) I (show ANXA2 ELISA Kits))-coated vesicles it specifically activates Rab1.
elevated expression of Rab1 protected against alpha-Synuclein-induced dopaminergic neuron loss in animal models of Parkinson Disease
This gene encodes a member of the Ras superfamily of GTPases. Members of the gene family cycle between inactive GDP-bound and active GTP-bound forms. This small GTPase controls vesicle traffic from the endoplasmic reticulum to the Golgi apparatus. Multiple alternatively spliced transcript variants have been identified for this gene which encode different protein isoforms.
GTP binding protein Rab1a
, RAB1, member RAS oncogene family
, Rab GTPase YPT1 homolog
, YPT1-related protein
, ras-related protein Rab-1A
, RAB1A, member RAS oncogene family
, RAB1B, member RAS oncogene family
, Rab-protein 1
, dendritic arbor reduction 6
, rab1A protein
, hypothetical protein
, RNase 5
, ribonuclease 5
, ras-related YPT1 protein