| Product Name | RND1, 1-200aa, Human |
|---|---|
| Description | RND1, also known as Rho 6, is Rho-related GTPases form a distinct branch of the Rho family, since they differ from other Rho proteins in size, charge, and biochemical properties. It appears to be constitutively in the activated GTP-bound form and acts as negative regulators of actin assembly and of cell adhesion. It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors. Recombinant human RND1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. |
| Synonyms | Rho-related GTP-binding protein Rho6, ARHS, FLJ42294, RHO6, RHO |
| Host | E. coli |
| Molecular Weight | 21.7 kDa (184aa) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MKERRAPQPV VARCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY TACLETEEQR VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETV DSALKKWRTE ILDYCPSTRV LLIGCKTDLR TDLSTLMELS HQKQAPISYE QGCAIAKQLG AEIYLEGSAF TSEKSIHSIF RTASMLCLNK PSPLPQKSPV |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 0.4M Urea, 5% glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Nobes C.D. et al. (1998) J. Cell Biol. 141: 187-197. Garrett M.D. et al. (1989) J. Biol. Chem. 264: 10-13. |
| Background | RND1, also known as Rho 6, is Rho-related GTPases form a distinct branch of the Rho family, since they differ from other Rho proteins in size, charge, and biochemical properties. It appears to be constitutively in the activated GTP-bound form and acts as negative regulators of actin assembly and of cell adhesion. It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors. Recombinant human RND1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. |
| Supplier | ARP |
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