Anti-RAC1 monoclonal antibody, clone 2B0C6D4

Name: Anti-RAC1 monoclonal antibody, clone 2B0C6D4
SKU: DCABH-5336
Rating: 5 (1 reviews)

Mouse anti-Human RAC1 monoclonal antibody for IHC-P, WB

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COA

SDS

Datasheet

Summary

Specifications

Clone

2B0C6D4

Species Reactivity

Mouse

Immunogen

Recombinant full length protein corresponding to Human Rac1 aa 1-192.Sequence: MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKP VNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPE VRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIG AVKYLECSALTQRGLKTVFDEAI

Conjugate

Unconjugated

Applications

Application Notes

WB: 1/1000 - 1/2000;

Target

Alternative Names

RAC1; ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1); ras-related C3 botulinum toxin substrate 1; p21 Rac1; Rac 1; TC 25; ras-like protein TC25; cell migration-inducing gene 5 protein; MIG5; Rac-1; TC-25; p21-Rac1;

Entrez Gene ID

5879

UniProt ID

A4D2P1

Product Background

Antigen Description

Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly.Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.

Pathway

Activation of Rac, organism-specific biosystem; Adaptive Immune System, organism-specific biosystem; Adherens junction, organism-specific biosystem; Adherens junction, conserved biosystem; Alpha6-Beta4 Integrin Signaling Pathway, organism-specific biosystem; Amyotrophic lateral sclerosis (ALS), organism-specific biosystem; Amyotrophic lateral sclerosis (ALS), conserved biosystem;

Citations

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References

Deletion of the Nucleotide Exchange Factor Vav3 Enhances Axonal Complexity and Synapse Formation but Tampers Activity of Hippocampal Neuronal Networks In Vitro

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

Authors: Wegrzyn, David; Wegrzyn, Christine; Tedford, Kerry; Fischer, Klaus-Dieter; Faissner, Andreas

Abstract

Vav proteins activate GTPases of the RhoA subfamily that regulate the cytoskeleton and are involved in adhesion, migration, differentiation, polarity and the cell cycle. While the importance of RhoA GTPases for neuronal morphology is undisputed, their regulation is less well understood. In this perspective, we studied the consequences of the deletion of Vav2, Vav3 and Vav2 and 3 (Vav2(-/-), Vav3(-/-), Vav2(-/-)/3(-/-)) for the development of embryonic hippocampal neurons in vitro. Using an indirect co-culture system of hippocampal neurons with primary wild-type (WT) cortical astrocytes, we analysed axonal and dendritic parameters, structural synapse numbers and the spontaneous network activity via immunocytochemistry and multielectrode array analysis (MEA). Here, we observed a higher process complexity in Vav3(-/-), but not in Vav2(-/-) neurons after three and five days in vitro (DIV). Furthermore, an enhanced synapse formation was observed in Vav3(-/-) after 14 days in culture. Remarkably, Vav2(-/-)/3(-/-) double knockout neurons did not display synergistic effects. Interestingly, these differences were transient and compensated after a cultivation period of 21 days. Network analysis revealed a diminished number of spontaneously occurring action potentials in Vav3(-/-) neurons after 21 DIV. Based on these results, it appears that Vav3 participates in key events of neuronal differentiation.

The supression of DOCK family members by their specific inhibitors induces the cell fusion of human trophoblastic cells

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Authors: Kiyokawa, Etsuko; Shoji, Hiroki; Daikoku, Takiko

Abstract

Purpose: Among the members of the DOCK family, DOCK1-5 function as guanine-nucleotide exchange factors for small GTPase Rac1, which regulates the actin cytoskeleton. It has been reported that in model organisms the Dock-Rac axis is required for myoblast fusion. We examined the role of DOCK1-5 in trophoblast fusion herein. Methods: We used a quantitative polymerase chain reaction (qPCR) to examine the mRNA expressions of DOCK1-5 and differentiation-related genes, i.e., fusogenic genes, in human trophoblastic cell lines, BeWo and JEG-3. We treated BeWo cells with TBOPP and C21 to inhibit DOCK1 and DOCK5. Cell dynamics and cell fusion were assessed by live imaging and immunostaining. The signaling pathways induced by DOCK1/5 inhibition were examined by western blotting. Results: DOCK1 and DOCK5 were expressed in BeWo cells. The inhibition of DOCK1 or DOCK5 did not prevent the cell fusion induced by forskolin (a common reagent for cell fusion); it induced cell fusion. DOCK1 inhibition induced cell death, as did forskolin. DOCK1 and DOCK5 inhibition for 24 and 48 h increased the expression of the genes ASCT2 and SYNCYTIN2, which code responsive proteins of trophoblast cell fusion, respectively. Conclusion: DOCK1 and DOCK5 inhibition participates in BeWo cell fusion, probably via pathways independent from forskolin-mediated pathways. (c) 2020 Elsevier Inc. All rights reserved.