Human AGFG1 protein (Recombinant) (N-His) (STJP008202)

SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
STJP008202
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General Information

Short DescriptionRecombinant-Human AGFG1-N-His protein was developed from e.coli for the region N-His. For use in research applications.
ApplicationsELISA/Immunogen/SDS-PAGE/WB
HostE.coli
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

Dilution RangeReconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
FormulationLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Storage InstructionUse a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt.

Target Information

Gene SymbolAGFG1
Gene ID3267
Uniprot IDAGFG1_HUMAN
ImmunogenHomo sapiens (Human)
Immunogen RegionMet1-Thr151

Additional Info

Post Translational Modifications O-glycosylated.
Function Required for vesicle docking or fusion during acrosome biogenesis. May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication.
Protein Name Arf-Gap Domain And Fg Repeat-Containing Protein 1
Hiv-1 Rev-Binding Protein
Nucleoporin-Like Protein Rip
Rev-Interacting Protein
Rev/Rex Activation Domain-Binding Protein
Database Links Reactome: R-HSA-8856825
Reactome: R-HSA-8856828
Cellular Localisation Nucleus
Cytoplasmic Vesicle
Alternative Protein Names Arf-Gap Domain And Fg Repeat-Containing Protein 1 protein
Hiv-1 Rev-Binding Protein protein
Nucleoporin-Like Protein Rip protein
Rev-Interacting Protein protein
Rev/Rex Activation Domain-Binding Protein protein
AGFG1 protein
HRB protein
RAB protein
RIP protein

Information sourced from Uniprot.org

Citations

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