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- Table of Contents
Facts about Rho guanine nucleotide exchange factor 1.
Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12.
Human | |
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Gene Name: | ARHGEF1 |
Uniprot: | Q92888 |
Entrez: | 9138 |
Belongs to: |
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No superfamily |
115 kDa guanine nucleotide exchange factor; 115-kD protein; GEF1; LBCL2LSC; Lsc homolog; p115RhoGEF; P115-RHOGEF; Rho guanine nucleotide exchange factor (GEF) 1; rho guanine nucleotide exchange factor 1; SUB1.5
Mass (kDA):
102.435 kDA
Human | |
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Location: | 19q13.2 |
Sequence: | 19; NC_000019.10 (41883184..41907452) |
Ubiquitously expressed.
Cytoplasm. Membrane. Translocated to the membrane by activated GNA13 or LPA stimulation.
You might be new to the field of gene expression analysis and are wondering what the ARHGEF1 marker is. In this article, you'll be introduced to the principal antibodies and infographics used by Boster scientists. Flow cytometry is a highly effective method for studying the properties of cells and other biological specimens. There are numerous applications for flow cytometry within the fields of science and medicine.
We recently demonstrated that His primary antibodies can recognize human ARHGEF1 within a variety of tissues, including the lung, heart, and kidney. When stimulated with BK, the ARHGEF1 marker is required to activate hASMC Rhokinase. Furthermore, it is required for the activity of p65-dependent NF-kB in vivo. These data suggest that phosphorylation of ARHGEF1 by His primary antibodies is specific to cells that are p53 positive.
ARHGEF1 is essential for the contraction of the aortic arc, and its expression is elevated in ASMs after TGF-b treatment. Its role in regulating the contraction of ASMs is not evident. Its role in the regulation of ASM contraction will require further study. In the meantime this research provides an opportunity to develop antibodies against ASM. This research will aid in developing an effective and sensitive ASM contraction model.
The lymphocytes of ARHGEF1 deficient cells showed impairment in their mobility and extended trailing edges. Additionally, the ARHGEF1-deficient cells express lower levels of F-actin which is an important protein that plays a role in B cell function. Therefore, the recognition of ARHGEF1-deficient lymphocytes is essential to develop a more effective treatment for this condition. There are also several promising treatments that can be found to tackle these problems.
In order to use this antibody, you will need to lyse 2 to 5 million lymphocytes in a buffer containing 50 mM Tris pH7.4, 0.1% sodium deoxycholate, and 150 mM NaCl. Then, stain 30-50 mg of protein with several antibodies. Depending on your end-use you might want to dilute your ARHGEF1 antigen to a higher or lower concentration, or use lower concentration.
ARHGEF1 mutations cause decreased expression of the ARHGEF1 protein, which is essential for B cell differentiation. Patients who have mutations in ARHGEF1 have more B-cells that are transitional and an abnormally immunophenotype. A medial lymph node biopsy of patients suffering from ARHGEF1 deficiency shows mature myeloid cells, as well as a reduced percentage of plasma cells.
Transfection of ARHGEF1 from the human body into cells resulted in the addition of TGF-b and starvation. Transfection efficiency was high and reached a 90% knockdown rate. Western blot was used to knock down ARHGEF1 and fluorescence microscopy confirmed this. ARHGEF1 deficit in mice results in decreased F-actin polymerization. The mouse model is similar to characteristics of patients suffering from PAD.
The expression of ARHGEF1 protein has been linked to effects of TGF-b upon cofilin and RhoA/RhoKinase. In addition, we have demonstrated that ARHGEF1 is an important TGF-b target gene. We have also identified two compound heterozygous variants in ARHGEF1 by studying the results of two siblings. These mutations alter the function of the protein with annotation-dependent scores that total 41 for the Splice Acceptor variant.
We have created a series infographics for the Genetic Literacy Project to help you better know more about biotechnology, genetics and other areas. These graphic representations are designed to demonstrate how genetics can be utilized to benefit the people. We hope these infographics help you understand the world of genetics, biotechnology and the science behind it. Here are a few of our top examples:
PMID: 8810315 by Hart M.J., et al. Identification of a novel guanine nucleotide exchange factor for the rho GTPase.
PMID: 9135076 by Aasheim H.-C., et al. Characterization, expression and chromosomal localization of a human gene homologous to the mouse Lsc oncogene, with strongest expression in hematopoetic tissues.