ARL2BP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-163) and having a molecular mass of 20.9 kDa.
The ARL2BP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
MGSSHHHHHH SSGLVPRGSH MDALEGESFA LSFSSASDAE FDAVVGYLED IIMDDEFQLL QRNFMDKYYL EFEDTEENKL IYTPIFNEYI SLVEKYIEEQ LLQRIPEFNM AAFTTTLQHH KDEVAGDIFD MLLTFTDFLA FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK SSSLPASQNN LRH.
ARL2BP binds specifically to ARL2.GTP with high affinity but does not interact with ARL2.GDP, activated ARF, or RHO proteins . This specificity suggests that ARL2BP has a unique role distinct from other ARF proteins. The protein is considered the first ARL2-specific effector identified due to its interaction with ARL2.GTP and lack of ARL2 GTPase-activating protein activity .
Mutations in the ARL2BP gene have been associated with retinitis pigmentosa 66 (RP66), an autosomal recessive disorder that affects the retina and can lead to vision loss . This highlights the importance of ARL2BP in maintaining normal cellular functions and its potential implications in genetic disorders.
The human recombinant ARL2BP protein is often used in research to study its function and interactions. It is typically expressed in E. coli and purified for various experimental applications . The recombinant protein can be used in blocking assays, control experiments, and other biochemical studies to understand its role in cellular processes .