Ral GDS Rap-binding domain (Ral GDS RBD) (Agarose)

Catalog No : USB-R1035-50
771.29€
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Product name Ral GDS Rap-binding domain (Ral GDS RBD) (Agarose)
Catalog No USB-R1035-50
Supplier’s Catalog No R1035-50
Supplier US Biologicals
Source antigen E. coli
Reactivity
Cross reactivity
Applications
Molecular weight
Storage -20°C
Other names
Grade Affinity Purified
Purity ~90%. Purified by glutathione-agarose chromatography.
Form Supplied as a liquid in glutathione-agarose slurry, TBS, 50% glycerol.
Reactivity life 12 months
Note For reserch purpose only
Description A GST-tagged fusion protein, corresponding to amino acids 788–884 of human Ral GDS-Rap binding domain (RBD), expressed in E. coli. Provided bound to glutathione-agarose. Specifically binds to and precipitates GTP-Rap1 (Mr 22kD), not GDP-Rap1 from cell lysates. Recommended for use with cells that have high levels of Rap1 expression (e.g., platelets). Applications: Suitable for use in Affinity Precipitation Assay, Affinity Precipitation and Immunoblot Analysis. Other applications not tested. Affinity Precipitation Assay: 30ug (~47ul of slurry) precipitated GTP-Rap1 from HEK293 lysates under the conditions described in the affinity precipitation protocol. The precipitated GTP-Rap1 was detected by Western Blot analysis using 2ug/ml of polyclonal anti-Rap1. The antibody detected two additional unknown proteins of Mr ~62 and 88kD. Affinity Precipitation and Western Blot Analysis: Samples were treated as described for affinity precipitation assay: HEK293 lysate in TLB preincubated with GDP prior to precipitation with Ral GDS-RBD; HEK293 lysate in TLB preincubated with GTPgS prior to precipitation with Ral GDS-RBD. Optimal dilutions to be determined by the researcher. 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.