Recombinant Human Stratifin Protein

Name: Recombinant Human Stratifin Protein
Brand: Beta LifeScience
SKU: BL-2238NP
Availability: InStock

BL-2238NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Stratifin is produced by our E.coli expression system and the target gene encoding Met1-Ser248 is expressed.
Accession	P31947
Synonym	14-3-3 Protein Sigma; Epithelial Cell Marker Protein 1; Stratifin; SFN; HME1
Gene Background	Stratifin (SFN) belongs to the 14-3-3 family of proteins that act as important regulators of intracelluar signal transduction through their ability to bind specific motifs phosphorylated on serine or threonine. There are at least seven isoforms that have been identified in mammals (beta, gamma, epsilon, sigma, zeta, tau and eta). SFN can detected in many tissues, highly expressed in stratified squamous keratinizing epithelium. SFN is indicated as an epithelial cell marker and serves as a tumor suppressor whose expression can be down regulated by methylation. In addition, SFN plays a key role in maintaining the G2 checkpoint in cells and preventing mitotic death.
Molecular Mass	27.77 KDa
Apmol Mass	30 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 250mM NaCl, 1mM EDTA, 1mM DTT, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53.; p53-regulated inhibitor of G2/M progression.
Subcellular Location	Cytoplasm. Nucleus. Secreted. Note=May be secreted by a non-classical secretory pathway.
Protein Families	14-3-3 family
Database References	HGNC: 10773 OMIM: 601290 KEGG: hsa:2810 STRING: 9606.ENSP00000340989 UniGene: Hs.523718
Tissue Specificity	Present mainly in tissues enriched in stratified squamous keratinizing epithelium.

Gene Functions References

Over-expressed and hypo-methylated SFN gene is associated with hepatocellular carcinoma. PMID: 27760737
Review/Meta-analysis: 14-3-3 sigma promoter methylation may be associated with the carcinogenesis of breast cancer and might represent a useful blood-based biomarker for the clinical diagnosis of breast cancer. PMID: 27999208
14-3-3sigma has a paracrine effect in educating stromal cells in tumor-associated microenvironment. PMID: 27175590
This data indicates that 14-3-3sigma contributes to P-gp overexpression through interaction with PXR with rifampin and paclitaxel treatment. PMID: 28077325
The impact of AKT1 on glucocorticoid receptor (GR)-induced transcriptional activity in cooperation with phospho-serine/threonine-binding protein 14-3-3, was examined. PMID: 27717743
Data showed that 14-3-3s contributed to ionizing radiation (IR) resistance possibly by regulating cell cycle progression and non-homologous end joining repair of IR-induced DNA double strand breaks via regulating the expression of Chk2 and PARP1. These findings suggest that 14-3-3s may be an upstream master regulator in chemo and radiation resistance and cancer cell survival. PMID: 28087741
Structural basis for the interaction of a human HSPB6 protein with the 14-3-3 universal signaling regulator has been reported. PMID: 28089448
Dual co-expression of human fetal Tau with PKA in Escherichia coli results in multisite Tau phosphorylation including also naturally occurring sites which were not previously considered in the context of 14-3-3 binding. Tau protein co-expressed with PKA displays tight functional interaction with 14-3-3 isoforms of a different type. PMID: 28575131
Data suggest that 14-3-3 sigma protein exhibits two individual secondary binding sites for peptide fragments of TAZ protein; these two pockets appear to be part of at least three physiologically relevant and structurally characterized 14-3-3 protein-protein interaction interfaces. PMID: 28681606
These results suggest that SFN facilitates lung tumor development and progression. SFN appears to be a novel oncogene with potential as a therapeutic target PMID: 26223682
SFN regulates cancer metabolic reprogramming. It opposes tumor-promoting metabolic programs by enhancing c-Myc poly-ubiquitination and degradation. SFN suppresses cancer glycolysis, glutaminolysis, and mitochondrial biogenesis. PMID: 26179207
Data show that overexpression of the 14-3-3sigma isoform resulted in a disruption of the tubulin cytoskeleton mediated by binding Tau protein. PMID: 26103986
K17 expression is accompanied by cytoplasmic expression of 14-3-3 sigma, indicative of their functional relationship in oral squamous cell carcinoma PMID: 25736868
SFN affects the water-holding capacity, barrier function and dermal matrix components in photoaging skin. An increase of SFN triggered by UVB irradiation may be one of the causes of alterations observed in photoaging skin. PMID: 25234834
Results suggest a role of Wig-1 as a survival factor that directs the p53 stress response toward cell cycle arrest rather than apoptosis through the regulation of FAS and 14-3-3sigma mRNA levels. PMID: 24469038
14-3-3sigma alone or combined with HSP70 are potential prognostic biomarkers for HCC PMID: 24923353
Decreased expression of immunoreactive 14-3-3sigma may be a predictor of poor prognosis in patients with uterine papillary serous carcinoma. PMID: 24201220
Cdc25B upregulation and 14-3-3sigma downregulation might promote development of bladder cancer and suggested a poor prognosis. PMID: 24234332
Studied differential protein expression of an anoikis-resistant CCA cell line culture, under attachment and nonattachment conditions. Data reveal 14-3-3sigma protein was intensely upregulated in detached CCA cells. PMID: 24030981
stratifin plays a role in regulating plakophilin-3 incorporation into the desmosomal plaque by forming a plakophilin-3 stratifin complex in the cytosol and thereby affecting desmosome dynamics in squamous epithelial cells. PMID: 24124604
this study identified the p53 regulated tumor suppressor 14-3-3sigma as a direct plakoglobin-p53 target gene. PMID: 23687381
14-3-3 sigma is expressed in ovarian granulosa cell tumors and steroid cell tumors, but it is not expressed in ovarian fibromas, thecomas, Sertoli cell tumors, endometrial stromal sarcomas, and sex-cord stromal tumors, unclassified PMID: 23370648
study concludes that LMP-1 may induce cell cycle arrest at G(2)/M progression via upregulation of 14-3-3sigma and Reprimo PMID: 23312294
Crystallographic determination of 14-3-3-sigma binding sites in the human peptidylarginine deiminase type VI. PMID: 22634725
Data suggest that down-regulation of 14-3-3 sigma plays a role in tumorigenesis in myometrium leading to leiomyoma; this mechanism may involve up-regulation of progesterone receptor and estrogen receptors. PMID: 22329840
Data define the subcellular localization and regulation of COP1 after DNA damage and provide a mechanistic explanation for the notion that 14-3-3sigma's impact on the inhibition of p53 E3 ligases is an important step for p53 stabilization after DNA damage. PMID: 20843328
14-3-3sigma expression is significantly associated with resistance to paclitaxel followed by 5-FU, epirubicin and cyclophosphamide, and this association is independent of other biological markers PMID: 22315133
Data show that SFN and SPARC form a complex thereby controlling the type I collagen synthesis and expression in fibroblasts. PMID: 22422640
down-regulation of 14-3-3sigma in the absence of CCDC6 demonstrated their direct association and supports the notion that CCDC6 contributes to cancer development, possibly through malignant pathways involving 14-3-3sigma PMID: 22399611
Multivariate analyses revealed that 14-3-3o expression was an independent prognostic parameter in gastric cancer. PMID: 21933426
14-3-3sigma-mediated molecular events that synergise with p53 may play important roles in the chemotherapy of breast cancer. PMID: 22192357
Epstein-Barr virus Rta-mediated transactivation of p21 and 14-3-3sigma arrests cells at the G1/S transition by reducing cyclin E/CDK2 activity. PMID: 21918011
role of hydrophobic residues at the dimeric interfac PMID: 21870863
data suggest that the CSN6-COP1 axis is involved in 14-3-3sigma degradation, and that deregulation of this axis will promote cell growth and tumorigenicity PMID: 21625211
Hypomethylation of the 14-3-3sigma promoter leads to increased expression in non-small cell lung cancer. PMID: 21755566
Data indicate that gene analysis revealed an up-regulation of all four 14-3-3 isoforms beta, eta, gamma, and sigma. PMID: 21416292
14-3-3sigma controls the in vivo epidermal proliferation-differentiation switch by reducing proliferative potential and forcing keratinocytes to exit the cell cycle, and that this effect associates with inhibition of the IGF-1 pathway. PMID: 21654836
found that metastatic ovarian tumors frequently overexpress 14-3-3 sigma PMID: 21249227
Transient down-regulation of 14-3-3 Sigma promotes maintenance of the p63-positive population without affecting normal differentiation. PMID: 21239874
14-3-3sigma protein likely contributes to the poor clinical outcome of human pancreatic cancers by causing resistance to radiation and anticancer drugs PMID: 21040574
14-3-3sigma has been cloned, purified and crystallized in complex with a phosphopeptide from the YAP 14-3-3-binding domain, which led to a crystal that diffracted to 1.15 A resolution. PMID: 20823509
up-regulation of 14-3-3 sigma protein is associated with scirrhous-type gastric carcinoma. PMID: 21115893
low expression of 14-3-3sigma appears to be a valuable marker for better survival in patient with undifferentiated nasopharyngeal carcinoma PMID: 20811675
14-3-3 sigma promoter hypermethylation can contribute to reducing or losing expression of this protein which plays an important role in the development of sporadic breast carcinomas & is involved in various types, grades, & lymphatic metastases. PMID: 19685192
The favorable OS for MF-CCA patients depends on the absence of clinical symptoms, negative lymph node metastasis, and curative hepatectomy. PMID: 20976731
downregulation of 14-3-3sigma protein was significantly associated with proliferation, invasion depth and lymph node metastasis of ESCC. Statistically significant correlations between expression of beta-catenin and 14-3-3sigma. PMID: 19664078
Indicate that stratifin could be a useful indicator for prognosis of esophageal squamous cell carcinoma, as well as a potential target for more effective therapy. PMID: 20108042
14-3-3 eta, beta, gamma and sigma isoforms were negatively expressed in meningioma PMID: 20388496
The relationship of 14-3-3-sigma with breast cancer metastasis and progression found in this study suggests a possible application of 14-3-3-sigma as a biomarker to screen for metastasis and treatment response. PMID: 20487521
The abnormal expression of 14-3-3 sigma and HSP27 is significantly associated with lymph node metastasis in colorectal cancer. PMID: 20336542

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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.

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