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- Table of Contents
Facts about Serum response factor.
The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. Required for cardiac differentiation and maturation.
Human | |
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Gene Name: | SRF |
Uniprot: | P11831 |
Entrez: | 6722 |
Belongs to: |
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No superfamily |
MCM1; serum response factor (c-fos serum response element-binding transcriptionfactor); serum response factor
Mass (kDA):
51.593 kDA
Human | |
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Location: | 6p21.1 |
Sequence: | 6; NC_000006.12 (43171269..43181506) |
Nucleus.
In this article, you will learn about Boster Bio's Anti-Serum Response Factor/SRF Marker, its applications, specificity, and validation. Read on for some of the most important points to consider when purchasing this product. There are several benefits to SRF markers that make them a valuable investment for any research lab. However, you should consider the limitations of these markers before making the decision to purchase them.
The serum response factor, also known as SRF, is a protein that stimulates cell proliferation and differentiation. It belongs to the MADS box superfamily of transcription factors. It binds to the serum response element in the promoter region of target genes and regulates the activity of many immediate-early genes. It participates in a number of processes including cell proliferation, apoptosis, cell differentiation, and cell cycle regulation. The protein also participates in the regulation of the cell cycle and the activation of the kinase pathway, as it controls the activity of several downstream factors.
Recent studies have implicated SRF as a potential oncogenic factor, making it a promising target for cancer therapy. In particular, two groups have linked SRF with Helicobacter pylori, a bacterial pathogen that colonizes human gastric mucosa, causing chronic gastritis, peptic ulcers, and gastric adenocarcinoma. Both groups have linked SRF to certain types of cancer, with the type one strain carrying a cag pathogenicity island and conferring greater virulence.
Mericskay and colleagues confirmed SRF's role in smooth muscle function by creating an inducible mouse model of CIPO. These mice showed symptoms of cachexia, while autopsy revealed impaired GI motility and severe dilation of the gastrointestinal tract. This finding has important implications for the diagnosis and treatment of a range of diseases resulting from defects in GI contractile function. The work suggests that SRF could play a critical role in the prevention of various diseases, from common to rare, life-threatening conditions.
The SRF marker is a protein with two DNA-binding domains. It also has a 90-amino acid transcriptional activation domain. The protein's biophysical structures were elucidated through X-ray crystal analysis. The protein contains two alpha-I helices on top of a major groove in DNA. It contains two beta-sheets separated by a beta-loop that allows dimerization of monomers.
Because SRF has such a broad role in cellular activities, its studies have been extensive. Due to its widespread expression in mesoderm-derived tissues, more than 1,000 studies have been published on SRF. In the past two decades, SRF has attracted much attention in the digestive system, and recent discoveries in this area have been largely aimed at advancing the field of human gastrointestinal medicine. This article will provide an update on several areas of digestive research.
The serum response factor (SRF) is a transcription factor and molecular sequence that mediates the transient response of many cellular genes to growth and development stimulation. It is an essential component for cardiac differentiation. It is a 67-kDa protein with molecular fragments and is involved in the expression of several cellular genes. Its role is crucial for cardiac development, and identifying the underlying mechanisms is essential.
In addition to targeting genes, SRF is involved in EMT and migration in NRK-52E cells. Western blot analysis shows the induction of SRF mRNA and decreased expression of E-cadherin. Transwell chamber migration assays reveal arrowheads and migrated cells. A transwell chamber migration assay demonstrates that SRF induces EMT. The numbers of migrated cells were also determined using a transwell chamber migration assay.
Further studies will focus on the role of SRF in regulating the development of axons. Using axon-specific inhibitor of GSK-3, SRF will affect axon growth. Further experiments will explore whether SRF inhibits the function of GSK-3 in regulating axon growth. These findings will improve the understanding of the mechanisms involved in the progression of nephropathy.
In vitro studies are also important for SRF-MRTF. However, in vivo staining of the genes involved in the complexes is needed to establish their functional roles. While the bulk RNAseq data shows that SRF-MRTF complexes are involved in samples from the craniofacial and incadrodontic regions, it is difficult to assess the compensation between the two complexes without in vivo expression patterns.
The SRF gene contains a regulatory domain. The gene's N-terminal extension is a binding site for cofactors. The beta loop competes with a transcription factor called MRTF-A. The second alpha helix contains an interaction site with YAP. YAP is also indirectly bound to SRF through the MRTF-A and TEAD transcription factors. Therefore, this marker is highly specific for lung cancer.
The SRF gene is expressed in all cells, including adult cardiac myocytes. The SRF 153(A3) gene is induced in adult cardiomyocytes to enter the mitotic cell cycle. SRF153(A3) is also known to induce stem cell factors and regulate cardiomyocyte dedifferentiation and cell cycle reentry. When paired with YAP5SA mRNA, SRF153(A3) induces alpha-EDU incorporation in 35% of cardiomyocytes. Furthermore, the SRF marker promotes the expression of the origin of replication genes.
The SRF gene is highly conserved across the human genome. In addition to the SRF gene, SRF53(A3) binds a sarcomeric cardiac actin promoter. In addition, SRF's interaction with the NKX2-5 protein and GATA4 promoter increases SRF's transcription. Its C-actin binding activity is facilitated by ETS factors.
The SRF gene is essential for smooth muscle differentiation in both cardiac and smooth muscle. The SRF gene activates myocardin's promyogenic activity. However, association with SRF enhances its activity and provides a molecular basis for cooperativity among CArG boxes that are essential for smooth muscle gene activation. This research demonstrates the importance of the SRF gene. The study was performed on 10T1/2 cells cultured in DMEM with 10% FBS. The transfection was performed using Lipofectamine 2000. The plasmid was 0.5 mg.
Although SRF is an important marker for prostate cancer, research has shown that the SRF gene may also represent a potential therapeutic target. It may be useful in the stratification of treatment options for men with advanced prostate cancer. Further studies should be performed on SRF to assess its role as a potential therapeutic target. So, it is vital to note that the SRF gene is highly conserved and may also play an important role in the treatment of advanced prostate cancer.
The Availability of the SRF Marker is important for a number of reasons, including its role in neuronal growth. It is also a major effector of NGF signaling and a key mediator of NGF-dependent target innervation of sensory neurons. Whether or not this marker is relevant for a given condition is largely unknown, but it may help in understanding the mechanisms underlying human neurogenesis.
Although there are no studies in humans, it is likely that it plays an important role in nervous system development. In vitro studies of SRF have shown that it contributes to the transcription and signaling of growth factors in neural tissue. A recent study in mice revealed that the SRF gene is required for early mesodermal differentiation, but the SRF-/ mice die in utero at E6.5. The availability of SRF conditional mutant mouse lines has greatly facilitated the study of SRF's in-vivo functions.
The SRF protein is essential for the differentiation of different cell types. Its target genes are dependent on the cell type and belong to different functional categories, such as cell-type-specific genes and developmental processes. Srf prefers open or active regions and can interact with multiple signals to control gene activity. A number of diseases are associated with a defective activity of Srf. It may also contribute to the repression of cell-type-specific genes in disease samples from human subjects.
PMID: 3203386 by Norman C., et al. Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element.
PMID: 8375385 by Janknecht R., et al. C-terminal phosphorylation of the serum-response factor.