TMED9 Protein, Human (HEK293, Fc)

TMED9 is a key player in vesicle protein trafficking and plays an important role in the early secretory pathway, particularly in COPI vesicle-mediated retrograde transport. It promotes the recruitment of coat isoforms to the membrane, enhances ARFGAP2 activity, and ensures the specific retention of p24 complexes in cis-Golgi membranes, specifically affecting TMED2 and TMED10 localization. TMED9 Protein, Human (HEK293, Fc) is the recombinant human-derived TMED9 protein, expressed by HEK293 , with C-mFc labeled tag.

TMED9, a protein intricately involved in vesicular protein trafficking, predominantly operates within the early secretory pathway, particularly in COPI vesicle-mediated retrograde transport, facilitating coatomer recruitment to membranes. It enhances the coatomer-dependent activity of ARFGAP2 and plays a pivotal role in the specific retention of p24 complexes in cis-Golgi membranes, contributing notably to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. Beyond its involvement in retrograde transport, TMED9 is implicated in the organization of intracellular membranes, including the ER-Golgi intermediate compartment and the Golgi apparatus. It further participates in the ER localization of PTPN2 isoform PTPB. TMED9 exhibits a dynamic oligomeric state, existing as a monomer and homodimer in the endoplasmic reticulum, with a predominantly monomeric state in the endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi network. Oligomerization likely occurs with other members of the EMP24/GP25L family, such as TMED2, TMED7, and TMED10. Additionally, TMED9 engages in specific interactions with TMED5, COPG1, PTPN2, SPAST, and STX17, underscoring its multifaceted involvement in intracellular processes.

Human

HEK293

C-mFc

Q9BVK6/NP_059980.2 (L38-R202)

54732  [NCBI]

Partial

LYFHIGETEKKCFIEEIPDETMVIGNYRTQLYDKQREEYQPATPGLGMFVEVKDPEDKVILARQYGSEGRFTFTSHTPGEHQICLHSNSTKFSLFAGGMLRVHLDIQVGEHANDYAEIAAKDKLSELQLRVRQLVEQVEQIQKEQNYQRWREERFRQTSESTNQR

≥ 85%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.