Recombinant Human Syncytin-1 (ERVW-1) Protein (His)

Name: Recombinant Human Syncytin-1 (ERVW-1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06557P
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 Syncytin-1 (ERVW-1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9UQF0
Target Symbol	ERVW-1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	APPPCRCMTSSSPYQEFLWRMQRPGNIDAPSYRSLSKGTPTFTAHTHMPRNCYHSATLCMHANTHYWTGKMINPSCPGGLGVTVCWTYFTQTGMSDGGGVQDQAREKHVKEVISQLTRVHGTSSPYKGLDLSKLHETLRTHTRLVSLFNTTLTGLHEVSAQNPTNCWICLPLNFRPYVSIPVPEQWNNFSTEINTTSVLVGPLVSNLEITHTSNLTCVKFSNTTYTTNSQCIRWVTPPTQIVCLPSGIFFVCGTSAYRCLNGSSESMCFLSFLVPPMTIYTEQDLYSYVISKPRNKRVPILPFVIGAGVLGALGTGIGGITTSTQFYYKLSQELNGDMERVADSLVTLQDQLNSLAAVVLQNRRALDLLTAERGGTCLFLGEECCYYVNQSGIVTEKVKEIRDRIQRRAEELRNTGPWGLLSQ
Expression Range	21-443aa
Protein Length	Partial
Mol. Weight	53.1 kDa
Research Area	Cell Biology
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	This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. May induce fusion through binding of SLC1A4 and SLC1A5.; Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of membranes.
Subcellular Location	[Surface protein]: Cell membrane; Peripheral membrane protein.; [Transmembrane protein]: Cell membrane; Single-pass type I membrane protein.; [Syncytin-1]: Virion.
Protein Families	Gamma type-C retroviral envelope protein family, HERV class-I W env subfamily
Database References	HGNC: 13525 OMIM: 604659 KEGG: hsa:30816 STRING: 9606.ENSP00000419945
Tissue Specificity	Expressed at higher level in placental syncytiotrophoblast. Expressed at intermediate level in testis. Seems also to be found at low level in adrenal tissue, bone marrow, breast, colon, kidney, ovary, prostate, skin, spleen, thymus, thyroid, brain and tra

Gene Functions References

These data revealed that human endogenous retrovirus W env might contribute to increase nitric oxide production and microglial migration ability in neuropsychological disorders by regulating the expression of inducible nitric oxide synthase. PMID: 28656540
CD47 seems to mediate fusion mostly through broad contact surfaces between the partners' cell membrane while syncytin-1 mediate fusion through phagocytic-cup like structure. PMID: 27714815
HERV-W was expressed in demyelinated lesions from multiple sclerosis brains, which were all positive for this endogenous pathogenic protein. Pronounced HERV-W immunoreactivity in active multiple sclerosis lesions was intimately associated with areas of active demyelination throughout the successive stages of lesion evolution in multiple sclerosis brains. PMID: 27456869
ERVWE1, ERVFRDE1 and ERV3 transcription was down-regulated in hydatidiform moles and gestational trophoblastic neoplasia. PMID: 26992684
Study found no associations between embroynal ERVW-1 polymorphisms and preeclampsia. PMID: 27546366
Identification of the two CpG dinucleotides around transcription start site as key epigenetic elements has provided valuable information for further studies on the epigenetic regulation of syncytin-1 in pancreatic cancer cells PMID: 26230721
Positive associations were observed between HERV-w methylation and dietary intakes of beta-carotene and carotenoids in a population of obese subjects. PMID: 25340371
Syncytin-1 and ASCT-2 is localized at the acrosomal region and equatorial segment of the spermatozoa. PMID: 24687878
Data show that Multiple Sclerosis-Associated Retrovirus (MSRV) is predominantly expressed over ERWVE1 in astrocyte-derived U-87 glioblastoma cell line. PMID: 24814867
The effect of ETS1 on syncytialization of trophoblasts likely results, at least in part, from inhibition of syncytin expression. PMID: 25651508
These results indicated that aberrant hypermethylation is involved in downregulation of syncytin-1, and epigenetic alterations may play a significant role in the development of preeclampsia PMID: 23888950
Exosomes from cultured primary villous cytotrophoblasts and sera of pregnant women have syncytin-1 on their surfaces. It acts on cellular binding and uptake of exosomes. PMID: 24812088
Increased trophoblast apoptosis and altered expression levels of syncytin-1, calpain 1, and AIF is observed in preeclamptic placentas. PMID: 24413738
Syncytin-1 overexpression may be an indicator of urothelial cell carcinoma risk. PMID: 24013223
Insertionally polymorphic HERV-K113 and HERV-K115 are not associated with HIV infections. PMID: 24204983
Influenza A virus infection transactivated ERVWE1 by increasing the transcription of GCM1. PMID: 24478419
Overexpression of HERV-W envelope gene elevated the levels of SK3 channel in neuroblastoma cells. PMID: 23727510
Syncytin-1 knockdown significantly inhibited BeWo cell growth and DNA synthesis and Syncytin-1 could promote the G1/S transition through p15 and CDK4. PMID: 23333240
In discordant monozygotic twins, HERVWE1 expression is higher in smaller fetuses and lower in larger counterparts. Methylation of the HERVWE1 gene promoter region may participate in gene regulation. PMID: 23290063
This study linked decreased Syncytin-1 expression to an epigenetic hypermethylation of the entire promoter of ERVW-1. PMID: 23457515
HERV-W env transcription was found to be elevated in bipolar disorder and schizophrenia subjects compared to controls. Molecular sequence characteristics may represent distinct features of the genome of patients with bipolar disorder and schizophrenia. PMID: 23212585
Corticotropin-releasing hormone did not influence the differentiation of isolated trophoblasts into functional syncytium as determined by beta-hCG secretion, albeit inducing syncytin-1 expression. PMID: 22971074
Data suggest that sorting of syncytin-1 into placental exosomes represents mechanism allowing syncytin-1 to reach and interact with target cells of maternal immune system to execute its immune-modulatory roles during pregnancy. PMID: 22999499
proposed that Syncytin-1 is regulated by PPARgamma/RXRalpha signaling during placentogenesis to drive multinuclear syncytiotrophoblast layer formation and maintenance. PMID: 22573555
The role of syncytin-1 and Pb1 in cell-cell fusion was studied using lentiviral vectors that express short hairpin RNAs for stable knockdown of both genes. PMID: 22573740
The findings suggested that syncytin 1 is shed from the placenta into the maternal circulation in association with placental microvesicles, and modulates immune cell activation and the responses of immune cells to lipopolysaccharide stimulation. PMID: 22348442
Data show that beta-catenin/BCL9-Like (BCL9L)/T-cell factor 4 (TCF4) signalling directly targets the GCM1/syncytin pathway and thereby regulates the fusion of human choriocarcinoma cells. PMID: 22109522
results further highlighted the existence of a correlation between the extent of the decrease in the expression levels of both syncytins 1 and 2 fusogenic proteins and the degree of severity of preeclampsia symptoms PMID: 21493955
HERV-W env triggers brain-derived neurotrophic factor (BDNF) production in human U251 glioma cells. PMID: 20100784
Analysis of non-spliced ERVWE1 mRNAs and env mRNAs detected efficient splicing of endogenously expressed RNAs in trophoblastic but not in non-placental cells. PMID: 21771862
CD9 increases GCM1 expression via the cAMP/PKA signaling pathway, resulting in the increase in ERVWE1 expression. PMID: 19692500
HERV-W syncytin expression apparently does not play role in endometriosis. However, it may possibly influence development of endometriosis because of increased expression in normal endometrium in endometriosis patients. PMID: 19903052
contributor to normal placental architecture, especially in the fusion processes of cytotrophoblasts to syncytiotrophoblasts. the gene expression of syncytin may be altered in cases with placental dysfunction such as preeclampsia or HELLP syndrome. PMID: 11854637
mRNA abundance for syncytin showed stimulation by forskolin in BeWo cells PMID: 12175968
syncytin-mediated trophoblastic fusion in human cells is regulated by GCMa PMID: 12397062
Syncytin gene activation is highest in term placenta PMID: 12620933
Hypoxia alters expression and function of syncytin and its receptor during trophoblast cell fusion of human placental BeWo cells: implications for impaired trophoblast syncytialisation in pre-eclampsia. PMID: 12757936
Syncytin gene expression is down-regulated by hypoxia, which strengthens the hypothesis that syncytin is reduced in disturbed pregnancies in the course of placental hypoxia. PMID: 14520239
syncytin promoter is located in the 5' long terminal repeat (LTR) of the HERV-W gene and that binding sites for CBF and Oct in the proximal promoter are critical for transcriptional regulation of the gene in trophoblast cells. PMID: 14613893
relative L1 and HERV-W expression levels are elevated in representative samples of malignant vs. non-malignant ovarian tissues PMID: 15109395
Cytoplasmic domain of syncytin is not essential for syncytin-mediated fusion but may play regulatory role. Intramolecular interaction between two heptad repeat regions (HRA and B) is involved in fusion process. PMID: 15269105
Syncytin's proinflammatory properties in the nervous system demonstrate a novel role for an endogenous retrovirus protein, which may be a target for therapeutic intervention. PMID: 15452578
The 146-bp region of the 5'-flanking region (nt-294/-148) of the human syncytin gene acts as a placenta-specific enhancer. PMID: 15888734
GCMa-driven syncytin expression is the key mechanism for syncytiotrophoblast formation PMID: 16004993
Syncytin transcripts were found in first-trimester trophoblast cells with both villous and extravillous phenotypes and also in the JAR and JEG-3 choriocarcinoma cell lines. PMID: 16760410
evaluation of the interaction of the HERV-W envelope with the hASCT2 receptor; a region consisting of the N-terminal 124 amino acids of the mature glycoprotein surface subunit was determined as the minimal receptor-binding domain PMID: 16820059
Syncytin is expressed by human cancer cells and is involved in cancer-endothelial cell fusions PMID: 16871371
Median viral RNA levels for syncytin-1 were higher in brains of MS patients relative to non-MS patients and median syncytin-1 DNA levels in MS brains were higher than non-MS brain tissue. PMID: 17209768
Transcripts from the HERV-W element on chromosome 7q21.2 encoding syncytin and from the SOD1 gene were detected at elevated levels in biopsies from the most affected muscles from MND patients compared to biopsies from control individuals. PMID: 17453631
present evidence in support of the direct role for syncytin-A in mouse trophoblast stem cell fusion and differentiation involved in placental dev. PMID: 17762178

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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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