GSP1, Recombinant, Saccharomyces cerevisiae, aa2-219, His-Tag (GTP-binding Nuclear Protein GSP1/CNR1)

Cat# 373539-20ug

Size : 20ug

Brand : US Biological

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373539 GSP1, Recombinant, Saccharomyces cerevisiae, aa2-219, His-Tag (GTP-binding Nuclear Protein GSP1/CNR1)

Clone Type
Polyclonal
Swiss Prot
P32835
Grade
Purified
Shipping Temp
Blue Ice
Storage Temp
-20°C

GTP-binding protein involved in nucleoCytoplasmic domain transport. Required for the import of protein into the nucleus and also for RNA export. Essential for cell viability. By analogy with Ras, Ran may be activated when GTP is exchanged for bound GDP by RCC1 and inactivated when GTP is hydrolyzed by Ran upon activation by RanGAP1.||Source:|Recombinant protein corresponding to aa2-219 from saccharomyces cerevisiae GSP1, fused to His-Tag at N-terminal, expressed in Yeast.||Molecular Weight: |~26.7kD||Amino Acid Sequence:|SAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGEIKFDVWDTAGQEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIVLCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVASPALAPPEVQVDEQLMQQYQQEMEQATALPLPDEDDADL||Storage and Stability:|May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months after receipt at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Applications
Source: Recombinant, Yeast|Purity: ≥90% (SDS-PAGE)|Concentration: As Reported |Form: Supplied as a liquid in Tris, 50% glycerol.||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Form
Supplied as a liquid in Tris, 50% glycerol.
Purity
≥90% (SDS-PAGE)
References
1. "Regulation of RNA processing and transport by a nuclear guanine nucleotide release protein and members of the Ras superfamily." Kadowaki T., Goldfarb D., Spitz L.M., Tartakoff A.M., Ohno M.EMBO J. 12:2929-2937(1993).