Recombinant Mouse Serum Response Factor (SRF) Protein (His-SUMO)

Name: Recombinant Mouse Serum Response Factor (SRF) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09495P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Serum Response Factor (SRF) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9JM73
Target Symbol	SRF
Synonyms	Srf; Serum response factor; SRF
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MLPSQAGAAAALGRGSALGGNLNRTPTGRPGGGGGTRGANGGRVPGNGAGLGQSRLEREAAAAAAPTAGALYSGSEGDSESGEEEELGAERRGLKRSLSEMELGVVVGGPEAAAAAAGGYGPVSGAVSGAKPGKKTRGRVKIKMEFIDNKLRRYTTFSKRKTGIMKKAYELSTLTGTQVLLLVASETGHVYTFATRKLQPMITSETGKALIQTCLNSPDSPPRSDPTTDQRMSATGFEEPDLTYQVSESDSSGETKDTLKPAFTVTNLPGTTSTIQTAPSTSTTMQVSSGPSFPITNYLAPVSASVSPSAVSSANGTVLKSTGSGPVSSGGLMQLPTSFTLMPGGAVAQQVPVQAIHVHQAPQQASPSRDSSTDLTQTSSSGTVTLPATIMTSSVPTTVGGHMMYPSPHAVMYAPTSGLADGSLTVLNAFSQAPSTMQVSHSQVQEPGGVPQVFLTAPSGTVQIPVSAVQLHQMAVIGQQAGSSSNLTELQVVNLDATHSTKSE
Expression Range	1-504aa
Protein Length	Full Length
Mol. Weight	67.2kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration. 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.
Subcellular Location	Nucleus.
Database References	KEGG: mmu:20807 STRING: 10090.ENSMUSP00000015749 UniGene: Mm.45044

Gene Functions References

The results demonstrate an unexpected function of Srf via a mechanism by which extracellular stimuli actively destabilize cell identity and suggest Srf involvement in a wide range of diseases. PMID: 29643333
Forebrain-specific serum response factor deletion decreased acute stress-mediated immediate early gene induction. PMID: 27914009
this study uncovered an SRF contribution to several processes of epileptogenesis in the pilocarpine model. PMID: 28716058
these data indicate that Emerin, a conserved nuclear lamina protein, couples extracellular matrix mechanics and SRF-Mkl1-dependent transcription. PMID: 28576971
findings reveal for the first time that SM22 is expressed in the nucleus in addition to the cytoplasm of VSMCs to regulate the transcription of Nik and its downstream proinflammatory NF-kB signal pathways as a modulator of SRF during vascular inflammation PMID: 29284006
Cigarette smoke is one of the major causes for COPD pathogenesis, inducing COPD-associated skeletal muscle atrophy which is closely related to decreasing SRF nucleic translocation, and down-regulation of SRF target genes involved in muscle growth and nutrition. PMID: 28260872
Synergy between TAZ and SRF in regulating smooth muscle gene activation was observed in primary aortic vascular smooth muscle cells. This novel signalling pathway links TGFbeta signalling to induction of smooth muscle genes through a mechanism involving regulation of TAZ and SRF proteins. PMID: 28342289
Modifications at most transcription start sites are dependent on the TCF family of ERKregulated SRF cofactors. PMID: 28286024
Blood pressure-associated polymorphism controls ARHGAP42 expression via serum response factor DNA binding PMID: 28112683
regulates smooth muscle contractility via myotonic dystrophy protein kinases and L-type calcium channels PMID: 28152551
knockdown of MKL1 induces a significant increase in the transcriptional activity of PPARgamma target genes and MKL1 interacts with PPARg, suggesting that SRF and MKL1 independently inhibit brown adipogenesis and that MKL1 exerts its effect mainly by modulating PPARgamma activity PMID: 28125644
Our results elucidate the specific role of the transcription factors CREB, SRF, and MEF2 in the depression and potentiation components of ODP in vivo, therefore better informing future attempts to find therapeutic targets for diseases where activity-dependent plasticity is disrupted. PMID: 28607167
The actin cytoskeleton regulatory pathway, MAPK and dilated cardiomyopathy signaling pathways, as well as CFL1 and ITGB6 genes, may be regulated by Srf to serve important roles in the progression of corneal disease. PMID: 27922676
The inducible and conditional deletion of SRF in the adult mouse hippocampus increases the epileptic phenotype in the kainic acid model of epilepsy. There was a robust decrease in activity-induced gene transcription in SRF knockout mice. SRF target genes are associated with synaptic plasticity and epilepsy. PMID: 25636686
the controlled and timely activation of SRF is essential for the coordinated growth of neuronal processes. PMID: 26638868
Increased serum response factor activity provokes podocytes' epithelial-mesenchymal transition and dysfunction in diabetic nephropathy. PMID: 26408645
A role for SRF in the transcriptional regulation of DUSP5 PMID: 26691724
Exploration of the molecular causes of enhanced cardiac hypertrophy revealed significant activation of beta-catenin/GSK-3beta signaling, whereas MAPK and MKL1/serum-response factor pathways were inhibited. PMID: 26719331
these findings reveal a key role of the SRF/CTGF/miR-133a axis in the regulation of cardiac fibrosis PMID: 26440278
Study uncovered important roles of neurons and neuronally expressed SRF in multiple sclerosis associated de- and remyelination PMID: 25639799
These data support a central role of the SRF/MRTF pathway in the pathobiology of lung fibrosis. PMID: 25681733
the actin, myocardin-related transcription factors and serum response factor (actin-Mrtf-Srf) pathway is specifically downregulated in the muscle atrophy that is induced through disuse in mice. PMID: 25344251
These results identify SRF and its MRTF cofactors as major transcriptional regulators of endothelial cell junctional stability, guaranteeing physiological functions of the cerebral microvasculature. PMID: 26221020
Silencing Malat1 inhibits myocyte differentiation and decreases Srf at RNA and protein levels. Srf silencing decreases Malat1 expression. Malat1 contains an miR-133 functional target site, and the interplay between Malat1 and Srf is miR-133 dependent. PMID: 25868726
SRF cooperated with MEF2 to sustain the expression of LMOD3 and other components of the contractile apparatus, thereby establishing a regulatory circuit to maintain skeletal muscle function. PMID: 25774500
results indicate that Foxf2 signaling in smooth muscle cells is essential for intestinal development and serum response factor signaling PMID: 25631042
Identified a set of direct SRF target genes acting in posterior nascent mesoderm which are enriched for transcripts associated with migratory function. We further show that cell migration is impaired in Srf mutant embryos. PMID: 25020278
SRF-VP16iHep murine hepatocellular carcinoma reveal convergent Ras/MAPK and Rho/actin signaling as a highly oncogenic driver mechanism for hepatocarcinogenesis PMID: 25266280
leading to a PDGF-responsive SRF-driven transcriptional program in the midface PMID: 25453829
Increased SRF negatively affects transcription of SRF gene targets. PMID: 24550211
Data show that the binding of WIP to actin controls the actin dynamics MRTFA-SRF-Focal adhesion assembly signaling cascade. PMID: 24797074
MKL1/2 and ELK4 co-regulate distinct serum response factor (SRF) transcription programs in macrophages. PMID: 24758171
Data indicate that despite normal neutrophil numbers, neutrophil function is severely impaired in serum response factor (SRF) knockout (KO) neutrophils. PMID: 24574460
SRF-dependent miR-210 expression may operate as a novel silencer of the Shh signaling pathway. PMID: 23818299
Our findings reveal a novel phosphorylation and activation of SRF by GSK-3 that is critical for SRF-dependent axon growth in mammalian central neurons. PMID: 24623780
Serum response factor indirectly regulates type I interferon-signaling in macrophages. PMID: 23705899
Data indicate that interferon regulatory factor 8 (IRF8) inhibited smooth muscle cells (SMCs) marker gene expression through regulating serum response factor (SRF) transactivation in a myocardin-dependent manner. PMID: 24248596
sustained Akt1-induced alphaSMA synthesis markedly decreased upon RNA silencing of SRF and myocardin. PMID: 24106278
Overexpression of transcription factors MYOCD and SRF alone or in conjunction with Mesp1 and SMARCD3 enhanced the basal but necessary cardio-inducing effect of the previously reported GATA4, TBX5, and MEF2C. PMID: 23704920
Foxf1 also directly binds to serum response factor (SRF) and myocardin-related transcription factors (MRTFs). PMID: 23946491
these results strongly support a role for -mediated alternative splicing in the regulation of contractile gene expression, achieved in part through modulating the activity of SRF, a key cardiac transcription factor. PMID: 23437181
Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics PMID: 23644458
SRF is selectively required for endothelial filopodia formation and cell contractility during sprouting angiogenesis, but seems dispensable for vascular remodeling PMID: 23674601
angiogenic homeostasis is ensured by differential stage-specific functions of SRF target gene products in the developing versus the mature retinal vasculature PMID: 23563308
Serum response factor controls transcriptional network regulating epidermal function and hair follicle morphogenesis. PMID: 23151848
Activated mDia promoted rapid and reversible nuclear actin network assembly, subsequent MAL nuclear accumulation, and SRF activity. PMID: 23558171
SRF-related decreases in vasomotor tone and cell-matrix attachment increase arterial elasticity in large arteries. PMID: 23426017
Data suggest that in mouse liver SRF is regulated via dramatic diurnal changes of actin dynamics, leading to the rhythmic translocation of the SRF coactivator Myocardin-related transcription factor-B (MRTF-B) into the nucleus. PMID: 23374345
SRF has a major part to play in the control of local blood flow via its central role in pressure-induced myogenic tone in resistance arteries. PMID: 23264443
SRF plays a key role in the modulation of cardiac fibrosis through repression of cardiomyocyte CTGF expression in a paracrine fashion. PMID: 22563064

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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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