Recombinant Human RhoGDI His Protein Summary
Description |
A recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 24-204 of Human RhoGDI Source: E.coli Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MSVNYKPPAQ KSIQEIQELD KDDESLRKYK EALLGRVAVS ADPNVPNVVV TGLTLVCSSA PGPLELDLTG DLESFKKQSF VLKEGVEYRI KISFRVNREI VSGMKYIQHT YRKGVKIDKT DYMVGSYGPR AEEYEFLTPV EEAPKGMLAR GSYSIKSRFT DDDKTDHLSW EWNLTIKKDW KD |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein |
Gene |
ARHGDIA |
Purity |
>95%, by SDS-PAGE |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
22.9 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
Buffer |
20 mM Tris-HCl buffer (pH 8.0), 1 mM DTT, 10% glycerol |
Preservative |
No Preservative |
Concentration |
1 mg/ml |
Purity |
>95%, by SDS-PAGE |
Alternate Names for Recombinant Human RhoGDI His Protein
Background
Rho GDP-dissociation inhibitor 1, also known ARHGDIA, belong to the RAS gene superfamily encoding small guanine nucleotide exchange (GTP/GDP) factors. Localized to the cytoplasm, ARHGDIA inhibits the dissociation of GDP from Rho proteins, thereby preventing GTP from binding to and subsequently activating Rho proteins. In humans ARHGDIA can be phosphorylated at Ser 101 by p21-activated kinase, an event that inhibits ARHGDIA activity and may result in positive feedback regulation of certain ARHGDIA target proteins. Recombinant human ARHGDIA protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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