Recombinant Human Serum Response Factor (SRF) Protein (His)

Name: Recombinant Human Serum Response Factor (SRF) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03372P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Serum Response Factor (SRF) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P11831
Target Symbol	SRF
Synonyms	c fos serum response element binding factor; c fos serum response element binding transcription factor; ELK3; ERP; MCM 1; MCM1; OTTHUMP00000039820; SAP2; Serum response factor; SRF; SRF serum response factor c fos serum response element binding transcription factor; SRF_HUMAN
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MLPTQAGAAAALGRGSALGGSLNRTPTGRPGGGGGTRGANGGRVPGNGAGLGPGRLEREAAAAAATTPAPTAGALYSGSEGDSESGEEEELGAERRGLKRSLSEMEIGMVVGGPEASAAATGGYGPVSGAVSGAKPGKKTRGRVKIKMEFIDNKLRRYTTFSKRKTGIMKKAYELSTLTGTQVLLLVASETGHVYTFATRKLQPMITSETGKALIQTCLNSPDSPPRSDPTTDQRMSATGFEETDLTYQVSESDSSGETKDTLKPAFTVTNLPGTTSTIQTAPSTSTTMQVSSGPSFPITNYLAPVSASVSPSAVSSANGTVLKSTGSGPVSSGGLMQLPTSFTLMPGGAVAQQVPVQAIQVHQAPQQASPSRDSSTDLTQTSSSGTVTLPATIMTSSVPTTVGGHMMYPSPHAVMYAPTSGLGDGSLTVLNAFSQAPSTMQVSHSQVQEPGGVPQVFLTASSGTVQIPVSAVQLHQMAVIGQQAGSSSNLTELQVVNLDTAHSTKSE
Expression Range	1-508aa
Protein Length	Full Length
Mol. Weight	53.6 kDa
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	HGNC: 11291 OMIM: 600589 KEGG: hsa:6722 STRING: 9606.ENSP00000265354 UniGene: PMID: 28900514 Findings indicate that miR-101-3p suppresses HOTAIR-induced proliferation and invasion through directly targeting SRF in gastric carcinoma cells. PMID: 28251884 promote GC metastasis by facilitating myofibroblast-cancer cell crosstalk PMID: 27323859 High SRF expression is associated with breast cancer. PMID: 26885614 Results identified SRF as one of the transcription factors responsible for docetaxel-resistant prostate cancer where docetaxel treatment increases its transcriptional activity. Its knockdown re-sensitizes resistant cells to docetaxel. PMID: 28249598 NANOG enabled reactivation of the ROCK and Transforming Growth Factor (TGF)-beta pathways-both of which were impaired in senescent cells-leading to ACTIN polymerization, MRTF-A translocation into the nucleus and serum response factor (SRF)-dependent myogenic gene expression. PMID: 27350449 HOTAIR is regulated by the RhoC-MRTF-A-SRF signaling pathway in breast cancer cells. PMID: 28069441 The findings of the work indicate a role for Galphaq and/or Galpha14 and in CCR2a/CCR2b-stimulated Rho A GTPase-mediated serum response factor activation. PMID: 26823487 Blood pressure-associated polymorphism controls ARHGAP42 expression via serum response factor DNA binding PMID: 28112683 Subset of cellular variants of myofibroma and myopericytoma showing a smooth muscle-like immunophenotype and harboring recurrent SRF-RELA gene fusions, which mimic sarcomas with myogenic differentiation. PMID: 28248815 We identified that SRF was a novel target gene for miR-22 by luciferase reporter assay and knockdown of SRF could cause endothelial dysfunction. PMID: 28161397 miR-181a/b is one of the factors involved in VSMC differentiation toward a synthetic phenotype through targeting at SR PMID: 27911586 miR-483-3p is upregulated in Endothelial progenitor cells (EPCs) from deep vein thrombosis patients, and it targets SRF to decrease EPCs migration and tube formation. PMID: 26801758 ADGRG2 constitutively activates RhoA-SRE pathways. PMID: 26321231 FLNA functions as a positive cellular transducer linking actin polymerization to MKL1-SRF activity, counteracting the known repressive complex of MKL1 and monomeric G-actin. PMID: 26554816 The SRF-IL6 axis is the critical mediator of YAP-induced stemness in mammary epithelial cells and breast cancer. PMID: 26671411 Data show that microRNA miR-320a is a key regulator of rtherogenesis, and down-regulating serum response factor (SRF). PMID: 25728840 These data support a central role of the SRF/MRTF pathway in the pathobiology of lung fibrosis. PMID: 25681733 STAT3 protein regulates vascular smooth muscle cell phenotypic switch by interaction with myocardin and SRF. PMID: 26100622 high levels of Myc engage Miz1 in repressive DNA binding complexes and suppress an SRF-dependent transcriptional program that supports survival of epithelial cells. PMID: 25896507 SRF regulates neutrophil migration, integrin activation, and trafficking. Disruption of the SRF pathway results in myelodysplasia and immune dysfunction. PMID: 25402621 Methylation changes of GFRA1, SRF, and ZNF382 may be a potential biomarker set for prediction of gastric carcinoma metastasis. PMID: 25009298 SRF promotes gastric cancer metastasis and the epithelial to mesenchymal transition through miR-199a-5p-mediated downregulation of E-cadherin. PMID: 25080937 Studied a new therapeutic alternative in the treatment of multiresistant lung adenocarcinoma via siRNA-specific transfection of six crucial molecules involved in lung carcinogenesis: SFR, E2F1, Survivin, HIF1, HIF2 and STAT3. PMID: 24627437 These results suggest that SRF is critical for HCC to acquire a mesenchymal phenotype, which leads to resistance against a sorafenib-mediated apoptotic effect. PMID: 24173109 Dilated cardiomyopathy-associated FHOD3 variant impairs the ability to induce activation of transcription factor serum response factor. PMID: 24088304 results demonstrate that serum response factor (SRF) nuclear expression in castration-resistant prostate cancer bone metastases is associated with survival with patients with shortest survival showing high SRF nuclear expression and patients with longest survival having low SRF nuclear expression PMID: 24249383 Androgen-responsive SRF target genes affect CaP cell behavior. PMID: 23576568 The RhoA signaling axis, a well known upstream stimulator of SRF action that harbors drugable targets, conveyed androgen-responsiveness to SRF. PMID: 23469924 Transfection of the NSCLC cell lines with specific siRNAs against SRF, E2F1 and survivin resulted in a very considerable reduction of the intracellular mRNA concentration. PMID: 23152437 Itk enhances Galpha13 mediated activation of serum response factor (SRF) transcriptional activity dependent on its ability to interact with Galpha13, but its kinase activity is not required to enhance SRF activity. PMID: 23454662 Substitution of any of the TFBS from our particular search of MEF2, CREB and SRF significantly decreased the number of identified clusters PMID: 23382855 High expression of serum response factor is associated with gastric carcinoma. PMID: 23134219 Upon neuronal injury via facial nerve transection, constitutively active SRF enhances motorneuron survival. PMID: 22537405 Dysfunction or loss of the SRF-activating mitogen-associated kinase pathway under stress conditions in transgenic mice may be part of Parkinson's disease etiology. PMID: 22356487 Lmod1 is a new SMC-restricted SRF/MYOCD target gene. PMID: 22157009 Downregulation of the activity of the MRTF-SRF axis and the expression of muscle-specific microRNAs, particularly miR-1, may contribute to COPD-associated skeletal muscle dysfunction. PMID: 21998125 overexpression of serum response factor in hepatocellular carcinoma may play an important role in tumor cell migration and invasion through upregulation of matrix metalloproteinase-2 and matrix metalloproteinase-9 PMID: 21842128 RTVP-1 plays a role in the effect of serum response factor on glioma cell migration PMID: 21777672 Data show that serum response factor (SRF) is one of miR-483-5p target genes. PMID: 21893058 SRF is able to gain nuclear entry through an auxiliary, nuclear localization sequence-independent mechanism PMID: 21131446 These data define serum response factor as a host cell transcription factor that regulates immediate early gene expression in Toxoplasma-infected cells. PMID: 21479245 Serum response factor up-regulation, combined with the presence of co-morbidities, increase the risk of recurrent gastric ulcer bleeding. PMID: 21410985 SRF pathway alterations are linked to insulin resistance, may contribute to type 2 diabetes pathogenesis, and could represent therapeutic targets PMID: 21393865 Data show that the ancestor sequence of SRF- and MEF2-type MADS domains is more similar to MEF2-type MADS domains than to SRF-type MADS domains. PMID: 20724380 Overexpression of SRF in hepatocellular carcinoma (HCC) cells modulates the Wnt/beta-catenin pathway, and this plays an important role in HCC progression. PMID: 20811705 Data reveal that serum response factor is a novel interferon (IFN)gamma-regulated gene and further elucidate the molecular pathway between IFNgamma, IFNgamma-regulated genes, and SRF and its target genes. PMID: 20685657 two transcription factors, SRF and TFAP2, as well as an intronic element encompassing EGR3-like sequence, that work together to regulate expression of the FXN gene PMID: 20808827 SRF depletion affects the expansion of the high and low differentiation grade HCC cells HepG2 and JHH6 PMID: 20144681 Data show that serum response factor is an essential regulator of primary human vascular smooth muscle cell proliferation and senescence. PMID: 20096952

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.