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Rabbit Anti-RhoA Polyclonal Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 4 - Rabbit Anti-RhoA Polyclonal Antibody AP52227
    Hela cells probed with RhoA/CPolyclonal Antibody, Unconjugated (AP52227) at 1:100 for 30 minutes followed by incubation with a conjugated secondary (PE Conjugated) (green) for 30 minutes compared to control cells (blue), secondary only (light blue) and isotype control (orange).
  • 1 - Rabbit Anti-RhoA Polyclonal Antibody AP52227
    L1 human colon carcinoma lysates L2 rat brain lysates probed with Anti RhoA Polyclonal Antibody, Unconjugated (AP52227) at 1:200 overnight at 4˚C. Followed by conjugation to secondary antibody at 1:3000 for 90 min at 37˚C. Predicted band 21kD. Observed band size:21kD.
  • 14 - Rabbit Anti-RhoA Polyclonal Antibody AP52227
    Formalin-fixed and paraffin embedded human skin labeled with Anti-RhoA Polyclonal Antibody (AP52227), Unconjugated 1:400 followed by conjugation to the secondary antibody and DAB staining
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IF, ICC, IHC-P
Primary Accession P61586
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Additional info
Gene ID 387
Other Names ARHA; ARH12; RHO12; RHOH12; Transforming protein RhoA; Rho cDNA clone 12; h12; RHOA
Dilution FC~~1:20~1:100
WB~~1:100~1:500
IHC-P~~1:100~1:500
Format0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glyce
StorageStore at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
Protein Information
Name RHOA
Synonyms ARH12, ARHA, RHO12
Function 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. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. 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 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. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. 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 (By similarity). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436,PubMed:19403695).
Cellular Location Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex. Midbody. Cell projection, lamellipodium. Note=Localized to cell-cell contacts in calcium-treated keratinocytes (By similarity). 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 a activated form and in a myosin- and actin-independent manner.
Research Areas

BACKGROUND

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. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. 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.

REFERENCES

Yeramian P.,et al.Nucleic Acids Res. 15:1869-1869(1987).
Fagan K.P.,et al.Exp. Eye Res. 59:235-237(1994).
Puhl H.L. III,et al.Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
Kalnine N.,et al.Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
Suzuki Y.,et al.Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.

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