Key features and details
- Expression system: Escherichia coli
- Purity: > 85% SDS-PAGE
- Active: Yes
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE, Functional Studies
Product nameRecombinant human RhoA protein (Active)
See all RhoA proteins and peptides
The specific activity of RhoA was 10.9 nmol/min/mg in GPTase-Glo assay.
Purity> 85 % SDS-PAGE.
Expression systemEscherichia coli
Protein lengthFull length protein
SequenceMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDG KQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWT PEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANR IGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGC
Molecular weight informationSDS-PAGE molecular weight: ~ 23kDa.
Amino acids1 to 190
TagsHis tag N-Terminus
Additional sequence informationGenBank: NM_001664. Full-length mature protein lacking the signal peptide.
Our Abpromise guarantee covers the use of ab268932 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
Preservative: 1.02% Imidazole
Constituents: 0.82% Sodium phosphate, 1.74% Sodium chloride, 0.002% PMSF, 0.004% DTT, 25% Glycerol (glycerin, glycerine)
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Aplysia ras related homolog 12
FunctionRegulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP.
Sequence similaritiesBelongs to the small GTPase superfamily. Rho family.
DomainThe basic-rich region is essential for yopT recognition and cleavage.
modificationsSubstrate for botulinum ADP-ribosyltransferase.
Cleaved by yopT protease when the cell is infected by some Yersinia pathogens. This removes the lipid attachment, and leads to its displacement from plasma membrane and to subsequent cytoskeleton cleavage.
AMPylation at Tyr-34 and Thr-37 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo.
Ubiquitinated by the BCR(BACURD1) and BCR(BACURD2) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration.
Cellular localizationCell membrane. Cytoplasm > cytoskeleton.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab268932 has not yet been referenced specifically in any publications.