GDI2 Protein, Human (P.pastoris, His)

GDI2 protein inhibits the exchange of GDP to GTP in Rab proteins and regulates intracellular membrane transport. GDI2 Protein, Human (P.pastoris, His) is the recombinant human-derived GDI2 protein, expressed by P. pastoris , with N-His labeled tag. The total length of GDI2 Protein, Human (P.pastoris, His) is 445 a.a., with molecular weight of ~52.7 kDa.

The GDI2 Protein acts as a GDP-dissociation inhibitor, preventing the exchange of GDP to GTP for most Rab proteins and thereby regulating intracellular membrane trafficking. By maintaining these small GTPases in their inactive GDP-bound form, GDI2 plays a crucial role in modulating cellular processes. It serves as a negative regulator of protein transport to the cilium and ciliogenesis by inhibiting RAB8A. GDI2 interacts with RHOH and the GDP-bound forms of various Rab proteins, including RAB3A, RAB3B, RAB3C, RAB5A, RAB5B, RAB5C, RAB8B, RAB10, RAB12, RAB35, and RAB43, with a lesser extent of binding to RAB3D. Furthermore, it interacts specifically with the GDP-bound inactive form of RAB8A, preventing its activation. The protein also interacts with DZIP1, negatively regulating the interaction between GDI2 and GDP-bound RAB8A. These interactions highlight the intricate regulatory role of GDI2 in governing membrane trafficking and cellular transport processes.

Human

P. pastoris

N-His

P50395 (1M-445D)

2665  [NCBI]

MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESASITPLEDLYKRFKIPGSPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVTEGSFVYKGGKIYKVPSTEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGIDPKKTTMRDVYKKFDLGQDVIDFTGHALALYRTDDYLDQPCYETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPIEEIIVQNGKVIGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRVICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETKEPEKEIRPALELLEPIEQKFVSISDLLVPKDLGTESQIFISRTYDATTHFETTCDDIKNIYKRMTGSEFDFEEMKRKKNDIYGED

Approximately 52.7 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.