SNAP23 Protein, Human (His, Strep)

SNAP23 Protein is an essential part of the receptor for membrane fusion machinery, regulating vesicle docking and fusion. It forms homotetramers and heterotetramers with STX4 and VAMP3. It interacts with SNAPIN, SYN4, STX1A, and STX12, as well as multiple syntaxins and synaptobrevins/VAMPs. Additionally, it interacts with ZDHHC13 and ZDHHC17. SNAP23 Protein, Human (His, Strep) is the recombinant human-derived SNAP23 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of SNAP23 Protein, Human (His, Strep) is 211 a.a., .

SNAP23, a pivotal player in cellular membrane dynamics, takes on the crucial role of an essential component within the high-affinity receptor for the general membrane fusion machinery, orchestrating the intricate dance of transport vesicle docking and fusion. Forming homotetramers via its coiled-coil domain, SNAP23 doesn't just stand alone; it engages in heterotetrameric formations, partnering with STX4 and VAMP3. Moreover, it collaborates within complexes, binding with VAMP8 and STX1A, as well as with VAMP8 and STX4 in the pancreas. This versatile protein interacts concurrently with SNAPIN and SYN4, and forms tight bonds with multiple syntaxins and synaptobrevins/VAMPs. Among its molecular associates, SNAP23 engages with STX1A, STX12, ZDHHC13, and ZDHHC17, highlighting its intricate participation in various cellular processes.

Human

E. coli

N-Strep;N-6*His

O00161 (M1-S211)

8773

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

<1 EU/μg, determined by LAL method.