Anti-SNURPORTIN1/SNUPN Antilichaam Picoband® 31.0550 Vervoeging

Snurportin1 is a protein that in humans is encoded by the SNUPN gene. The nuclear import of the spliceosomal snRNPs U1, U2, U4 and U5, is dependent on the presence of a complex nuclear localization signal. The latter is composed of the 5'-2,2,7-terminal trimethylguanosine (m3G) cap structure of the U snRNA and the Sm core domain. The protein encoded by this gene interacts specifically with m3G-cap and functions as an snRNP-specific nuclear import receptor. Alternatively spliced transcript variants encoding the same protein have been identified for this gene.

Protein Hook homolog 3; h-hook3; Hhk3; HOOK3

SNUPN

10073

O95149

Human, Mouse, Rat

No cross-reactivity with other proteins.

E.coli-derived human SNURPORTIN1/SNUPN recombinant protein (Position: M1-N360) .

Highly expressed in chromaffin cells of the adrenal medulla (at protein level) . Detected in peripheral sympathetic ganglia (at protein level) . Found in some paracrine cells in stomach and duodenum (at protein level) .

Flow Cytometry

Golgi Proteins, Protein Trafficking, Signal Transduction, Vesicle Transport

Immunogen affinity purified.

Liquid

Probably serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking. Component of the FTS/Hook/FHIP complex (FHF complex) . The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex) . May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex. Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) .

1. Dong, X., Biswas, A., Suel, K. E., Jackson, L. K., Martinez, R., Gu, H., Chook, Y. M. Structural basis for leucine-rich nuclear export signal recognition by CRM1. Nature 458: 1136-1141, 2009. Note: Erratum: Nature 461: 550 only, 2009. 2. Huber, J., Cronshagen, U., Kadokura, M., Marshallsay, C., Wada, T., Sekine, M., Luhrmann, R. Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure. EMBO J. 17: 4114-4126, 1998. 3. Monecke, T., Guttler, T., Neumann, P., Dickmanns, A., Gorlich, D., Ficner, R. Crystal structure of the nuclear export receptor CRM1 in complex with snurportin 1 and RanGTP. Science 324: 1087-1091, 2009.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

49229 MW

6

Hook microtubule tethering protein 3

Cytoskeleton. Golgi apparatus.

Chromaffin granule amine transporter

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.