Rabphilin-3AL (rabphilin-3A-like), also known as RPH3AL or NOC2, is a cytoplasmic Rab GTPase effector. It contains one FYVE-type zinc finger and one Rab-binding (RBD) domain, but unlike its related protein, rabphilin-3A, rabphilin-3AL does not contain any C2 domains. Rabphilin-3AL is expressed in a variety of tissues, with highest levels found in kidney, skeletal muscle, pancreas, liver, ovary, stomach, heart and thyroid. It is believed to play a role regulating calcium-dependent secretory vesicle exocytosis in endocrine and exocrine cells. Via its RBD domain, rabphilin-3AL is capable of binding Rab 27a and, through this interaction, rabphilin-3AL is recruited to dense-core vesicles. With lower affinity, rabphilin-3AL can also bind Rab 3 and Rab 8 with its RBD domain. Through an interaction with Rab 3, rabphilin-3AL can inhibit G-protein signaling in endocrine pancreas and positively regulate insulin secretion. Rabphilin-3AL knockout mice display accumulation of secretory granules and irregular shape in exocrine cells.

WB(1:100-1000), IHC-P(1:100-500), IF(IHC-P)(1:50-200)

Type: Primary
Antigen: RPH3AL
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Human, Mouse, Rat