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Data suggest that Rab35, interacting with TBC1D10A, functions in vascular endothelial cells as a negative regulator of histamine-evoked, Ca2+-dependent Weibel-Palade body exocytosis, most likely acting through the downstream effectors ACAP2 and Arf6. (Rab35 = rab GTP-binding protein 53; TBC1D10A = TBC1 domain family member 10A; ACAP2 = centaurin beta2; Arf6 = ADP-ribosylation factor 6)
EPI64, a candidate GAP that is specific for Rab27.
Data suggest that EPI64A and B, which are ubiquitously expressed members of the EPI64 subfamily, inactivate Ras and certain Rabs at the periphery of cells.
EPI64 regulates membrane trafficking both by stabilizing Arf6-GTP and by inhibiting the recycling of membrane through the tubular endosome by decreasing Rab8a-GTP levels.
analysis of recycling of the Ca2+-activated K+ channel, KCa2.3, is dependent upon RME-1, Rab35/EPI64C, and an N-terminal domain
EPI64 is a GTPase-activating protein specific for Rab27A
These data reveal that microvilli have distinct cytoskeletal subdomains and that EPI64 regulates microvillar structure.
EPI64C and Rab35 regulate a recycling pathway in T cells and contribute to immunological synapse formation, most likely by participating in TCR transport to the immunological synapse
Acts as GTPase-activating protein for RAB27A (By similarity).
EBP50-PDX interactor of 64 kDa
, EBP50-PDZ interactor of 64 kD
, TBC1 domain family member 10A