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anti-Human RAB8A Antibodies:
anti-Mouse (Murine) RAB8A Antibodies:
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Dog (Canine) Monoclonal RAB8A Primary Antibody for IF, IP - ABIN968211
Bahadoran, Aberdam, Mantoux, Buscà, Bille, Yalman, de Saint-Basile, Casaroli-Marano, Ortonne, Ballotti: Rab27a: A key to melanosome transport in human melanocytes. in The Journal of cell biology 2001
Show all 5 Pubmed References
Dog (Canine) Monoclonal RAB8A Primary Antibody for IF, IP - ABIN968210
Chavrier, Vingron, Sander, Simons, Zerial: Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line. in Molecular and cellular biology 1991
Show all 5 Pubmed References
Human Polyclonal RAB8A Primary Antibody for FACS, IHC (p) - ABIN1881723
Kato, Sekine, Oh, Kim, Umezawa, Abe, Yokoyama-Kobayashi, Aoki: Construction of a human full-length cDNA bank. in Gene 1995
Show all 2 Pubmed References
Cow (Bovine) Polyclonal RAB8A Primary Antibody for ELISA, WB - ABIN2476294
Vacca, Bazellières, Nouar, Harada, Massey-Harroche, Le Bivic: Drebrin E depletion in human intestinal epithelial cells mimics Rab8a loss of function. in Human molecular genetics 2014
Human Polyclonal RAB8A Primary Antibody for ELISA, WB - ABIN408690
Yoshimura, Egerer, Fuchs, Haas, Barr: Functional dissection of Rab GTPases involved in primary cilium formation. in The Journal of cell biology 2007
GRAF1 (show ARHGAP26 Antibodies)-mediated removal of Rab8 from the cell surface restricts its activity during protrusion formation, thereby facilitating dynamic adjustment of the polarity axis.
the TNPO1 (show TNPO1 Antibodies)-Rab8-ciliary targeting signals complex mediates selective entry into and retention of cargos within cilia.
Ectopic expression of an N-terminal-truncated ARHGEF10 (show ARHGEF10 Antibodies) mutant led to the generation of large vesicle-like structures containing both Rab6 (show RAB6A Antibodies) and Rab8.
report the design of a bioavailable StRIP3 analogue that harbors two hydrophobic cross-links and exhibits increased binding affinity, combined with robust cellular uptake and extremely high proteolytic stability. Localization experiments reveal that this double-stapled peptide and its target protein Rab8a accumulate in the same cellular compartments
knockdown of another Parkinson's disease (PD) gene, LRRK2 (show LRRK2 Antibodies), which phosphorylates Rab8a, similarly impairs retromer trafficking, secretory autophagy and Golgi-derived vesicle secretion, thus demonstrating converging roles of two PD genes TMEM230 and LRRK2 (show LRRK2 Antibodies) on Rab8a function, and suggesting that retromer and secretory dysfunction play an important role in PD pathogenesis.
Rab8 can induce Rac1- and Tiam1 (show TIAM1 Antibodies)-dependent cortical actin polymerization and focal adhesion disassembly through the proteases MT1-MMP (show MMP14 Antibodies) and calpain, and Rho-GTPase (show RACGAP1 Antibodies)-dependent mechanisms
Data demonstrate that EHBP1L1 links Rab8 and the Bin1 (show BIN1 Antibodies)-dynamin (show DNM1 Antibodies) complex, which generates membrane curvature and excises the vesicle at the endocytic recycling compartment for apical transport.
Further exploration of the NINL (show NINL Antibodies)-associated interactome identifies MICAL3 (show MICAL3 Antibodies), a protein known to interact with Rab8 and to play an important role in vesicle docking and fusion.
The small GTPase (show RACGAP1 Antibodies) Rab8 interacts with VAMP-3 (show VAMP3 Antibodies) to regulate the delivery of recycling T-cell receptors to the immune synapse.
the role of Rabin8 (show RAB3IP Antibodies) (a mammalian ortholog of Sec2p) with Rab8-nucleotide-exchange factor activity in autophagy in mammalian cells, was examined.
Cc2d2a (show CC2D2A Antibodies), localized at the photoreceptor connecting cilium/transition zone, facilitates protein transport through a role in Rab8-dependent vesicle trafficking and fusion.
Data show that elipsa (show TRAF3IP1 Antibodies) encodes a coiled-coil polypeptide that localizes to cilia, and that it interacts genetically with Rabaptin5, a well-studied regulator of endocytosis, which in turn interacts with Rab8, a small GTPase (show RACGAP1 Antibodies), known to localize to cilia.
The small GTPase (show RACGAP1 Antibodies) Rab8a regulates lipid uptake and storage in skeletal muscle.
Rab8a and Rab11a (show RAB11A Antibodies) Are Dispensable for Rhodopsin (show RHO Antibodies) Transport in Mouse Photoreceptors
With CRISPR/Cas9-mediated gene editing to stably knock out and recover Rab8a in macrophage cell lines, this study matches Akt (show AKT1 Antibodies) signaling profiles with cytokine outputs, confirming that Rab8a is a novel regulator of the Akt (show AKT1 Antibodies)/mammalian target of rapamycin (mTOR (show FRAP1 Antibodies)) pathway downstream of multiple Toll (show TLR4 Antibodies)-like Receptors.
these results indicate an indispensable role for Rab8A in insulin (show INS Antibodies)-regulated GLUT4 (show SLC2A4 Antibodies) trafficking in C2C12 cells.
Results highlight a novel role of Rab8, downstream of IFT20, in the pathway that regulates T cell receptor (TCR) recycling, through recruiting VAMP-3 and promoting the fusion with the synaptic membrane of endosomes carrying TCR cargoes.
Rab8a thus controls Wnt (show WNT2 Antibodies) delivery in producing cells and is crucial for Paneth cell maturation.
Rab8a acts as an activator of Fsp27 (show CIDEC Antibodies)-mediated LD fusion and growth.
Simultaneous loss of Rab8a and Rab8b (show RAB8B Antibodies) has little effect on ciliogenesis, whereas additional loss of Rab10 (show RAB10 Antibodies) greatly affects ciliogenesis.
The protein encoded by this gene is a member of the RAS superfamily which are small GTP/GDP-binding proteins with an average size of 200 amino acids. The RAS-related proteins of the RAB/YPT family may play a role in the transport of proteins from the endoplasmic reticulum to the Golgi and the plasma membrane. This protein shares 97%, 96%, and 51% similarity with the dog RAB8, mouse MEL, and mouse YPT1 proteins, respectively and contains the 4 GTP/GDP-binding sites that are present in all the RAS proteins. The putative effector-binding site of this protein is similar to that of the RAB/YPT proteins. However, this protein contains a C-terminal CAAX motif that is characteristic of many RAS superfamily members but which is not found in YPT1 and the majority of RAB proteins. Although this gene was isolated as a transforming gene from a melanoma cell line, no linkage between MEL and malignant melanoma has been demonstrable. This oncogene is located 800 kb distal to MY09B on chromosome 19p13.1.
, hematopoietic SH2 domain containing
, ras-related protein Rab-8A
, RAB8A, member RAS oncogene family
, member RAS oncogene family
, Ras-related protein Rab-8A
, mel transforming oncogene (RAB8 homolog)
, mel transforming oncogene (derived from cell line NK14)
, mel transforming oncogene (derived from cell line NK14)- RAB8 homolog
, oncogene c-mel
, ras-associated protein RAB8
, RAB8, member RAS oncogene family
, cell line NK14 derived transforming oncogene