• Immunohistochemistry analysis of RhoA in paraffin-embedded human placenta using RhoA Rabbit polyclonal antibody (STJ115882) at dilution of 1:100 (40x lens). Perform microwave antigen retrieval with 10 mM Tris/EDTA buffer pH 9. 0 before commencing with immunohistochemistry staining protocol.
  • Western blot analysis of various lysates using RhoA Rabbit polyclonal antibody (STJ115882) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (STJS000856) at 1:10000 dilution. Lysates/proteins: 25 Mu g per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Enhanced Kit. Exposure time: 180s.

Anti-RHOA antibody (94-193) (STJ115882)

SKU:
STJ115882

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Host: Rabbit
Applications: WB/IHC/IP
Reactivity: Human/Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-RhoA (94-193) is suitable for use in Western Blot, Immunohistochemistry and Immunoprecipitation research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: PBS with 0.01% Thimerosal, 50% Glycerol, pH7.3.
Purification: Affinity purification
Dilution Range: WB 1:500-1:1000
IHC-P 1:50-1:200
IP 1:100-1:500
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: RHOA
Gene ID: 387
Uniprot ID: RHOA_HUMAN
Immunogen Region: 94-193
Immunogen: A synthetic peptide corresponding to a sequence within amino acids 94-193 of human RhoA (NP_001655.1).
Immunogen Sequence: NIPEKWTPEVKHFCPNVPII LVGNKKDLRNDEHTRRELAK MKQEPVKPEEGRDMANRIGA FGYMECSAKTKDGVREVFEM ATRAALQARRGKKKSGCLVL
Post Translational Modifications (Microbial infection) Substrate for botulinum ADP-ribosyltransferase. (Microbial infection) 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. (Microbial infection) 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. (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly. (Microbial infection) Glucosylated at Thr-37 by C.difficile toxins TcdA and TcdB in the colonic epithelium. Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption and cell death, resulting in the loss of colonic epithelial barrier function. (Microbial infection) Glycosylated (O-GlcNAcylated) at Thr-37 by C.novyi toxin TcdA. O-GlcNAcylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption. (Microbial infection) Stearoylated By S.flexneri N-epsilon-fatty acyltransferase IcsB, thereby disrupting the host actin cytoskeleton. Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling. Phosphorylation by SLK at Ser-188 in response to AGTR2 activation. Ubiquitinated by the BCR(KCTD13) and BCR(TNFAIP1) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and synaptic transmission in neurons. Ubiquitinated at Lys-135 in a FBXL19-mediated manner.leading to proteasomal degradation. Serotonylation of Gln-63 by TGM2 during activation and aggregation of platelets leads to constitutive activation of GTPase activity.
Function Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation.promotes KCNA2 endocytosis. Acts as an allosteric activator of guanine nucleotide exchange factor ECT2 by binding in its activated GTP-bound form to the PH domain of ECT2 which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the ECT2 catalytic center. May be an activator of PLCE1. In neurons, involved in the inhibition of the initial spine growth. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling. Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets. (Microbial infection) Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague.
Protein Name Transforming Protein Rhoa
Rho Cdna Clone 12
H12
Database Links Reactome: R-HSA-114604
Reactome: R-HSA-193634
Reactome: R-HSA-198203
Reactome: R-HSA-209563
Reactome: R-HSA-2173791
Reactome: R-HSA-392451
Reactome: R-HSA-3928662
Reactome: R-HSA-3928663
Reactome: R-HSA-4086400
Reactome: R-HSA-416482
Reactome: R-HSA-416550
Reactome: R-HSA-416572
Reactome: R-HSA-4420097
Reactome: R-HSA-5625740
Reactome: R-HSA-5625900
Reactome: R-HSA-5625970
Reactome: R-HSA-5627117
Reactome: R-HSA-5663220
Reactome: R-HSA-5666185
Reactome: R-HSA-5689896
Reactome: R-HSA-6785631
Reactome: R-HSA-6798695
Reactome: R-HSA-8849471
Reactome: R-HSA-8980692
Reactome: R-HSA-8985586
Reactome: R-HSA-9013106
Cellular Localisation Cell Membrane
Lipid-Anchor
Cytoplasmic Side
Cytoplasm
Cytoskeleton
Cleavage Furrow
Cell Cortex
Midbody
Cell Projection
Lamellipodium
Dendrite
Nucleus
Localized To Cell-Cell Contacts In Calcium-Treated Keratinocytes
Translocates To The Equatorial Region Before Furrow Formation In A Ect2-Dependent Manner
Localizes To The Equatorial Cell Cortex (At The Site Of The Presumptive Furrow) In Early Anaphase In An Activated Form And In A Myosin- And Actin-Independent Manner
Alternative Antibody Names Anti-Transforming Protein Rhoa antibody
Anti-Rho Cdna Clone 12 antibody
Anti-H12 antibody
Anti-RHOA antibody
Anti-ARH12 antibody
Anti-ARHA antibody
Anti-RHO12 antibody

Information sourced from Uniprot.org

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