Datasheet

Biological Description

Specificity	Anti-Rho A Mouse Antibody [G4B13] detects endogenous levels of total Rho A protein.
Background	RhoA is a member of the Rho family of small GTPases that functions as a molecular switch to regulate cytoskeletal dynamics, cell shape, motility, and adhesion. RhoA encompasses a conserved GTPase domain that cycles between an inactive GDP-bound and an active GTP-bound state, controlling its interaction with downstream effectors. RhoA’s functions primarily involve activating Rho-associated kinases (ROCK1 and ROCK2), which phosphorylate substrates like myosin light chain (MLC) to promote actomyosin contractility, stress fiber formation, and focal adhesion assembly critical for cell migration and morphogenesis. Regulation of RhoA activity is mediated by guanine nucleotide exchange factors (GEFs) that facilitate GDP-GTP exchange to activate RhoA, GTPase-activating proteins (GAPs) that enhance GTP hydrolysis to inactivate it, and guanine nucleotide dissociation inhibitors (GDIs) that sequester inactive RhoA in the cytosol. Post-translational modifications such as phosphorylation at sites including Ser188 by protein kinase A or ERK and oxidation of cysteine residues modulate RhoA’s activity and localization, influencing processes like tumorigenesis, neurite outgrowth, and vascular function. RhoA also participates in redox-regulated signaling by controlling the production of reactive oxygen species (ROS), which in turn can regulate RhoA activity through feedback mechanisms. RhoA inhibition has been linked to enhanced neurite extension in neuronal cells, while aberrant RhoA activation contributes cancer and cardiovascular diseases.

Specificity

Anti-Rho A Mouse Antibody [G4B13] detects endogenous levels of total Rho A protein.

Background

RhoA is a member of the Rho family of small GTPases that functions as a molecular switch to regulate cytoskeletal dynamics, cell shape, motility, and adhesion. RhoA encompasses a conserved GTPase domain that cycles between an inactive GDP-bound and an active GTP-bound state, controlling its interaction with downstream effectors. RhoA’s functions primarily involve activating Rho-associated kinases (ROCK1 and ROCK2), which phosphorylate substrates like myosin light chain (MLC) to promote actomyosin contractility, stress fiber formation, and focal adhesion assembly critical for cell migration and morphogenesis. Regulation of RhoA activity is mediated by guanine nucleotide exchange factors (GEFs) that facilitate GDP-GTP exchange to activate RhoA, GTPase-activating proteins (GAPs) that enhance GTP hydrolysis to inactivate it, and guanine nucleotide dissociation inhibitors (GDIs) that sequester inactive RhoA in the cytosol. Post-translational modifications such as phosphorylation at sites including Ser188 by protein kinase A or ERK and oxidation of cysteine residues modulate RhoA’s activity and localization, influencing processes like tumorigenesis, neurite outgrowth, and vascular function. RhoA also participates in redox-regulated signaling by controlling the production of reactive oxygen species (ROS), which in turn can regulate RhoA activity through feedback mechanisms. RhoA inhibition has been linked to enhanced neurite extension in neuronal cells, while aberrant RhoA activation contributes cancer and cardiovascular diseases.

Usage Information

Application

WB, IP, IHC, IF , FCM

Dilution

WB	IHC	IF	FCM
1:100-1:1000	1:50-1:500	1:50-1:500	1 µg per 1 x 10⁶ cells

Reactivity

Mouse, Rat, Human

Source

Mouse

MW

24 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/33126816/
https://pubmed.ncbi.nlm.nih.gov/28300846/

Anti-Rho A Mouse Antibody [G4B13]

Biological Description

Usage Information

References

Application Data