Recombinant Human MEP50) Protein

Name: Recombinant Human MEP50) Protein
Brand: Beta LifeScience
SKU: BL-1245SG
Availability: InStock

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

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Product Overview

Tag	GST
Host Species	Human
Accession	BC001679
Synonym	WDR77, HKMT1069, MGC2722, Nbla10071, RP11-552M11.3
Background	Methylosome protein 50 (MEP50) is a component of methylosome that contains the methyltransferase JBP1 (PRMT5) and the pICln protein. The methylosome functions to modify specific arginines to dimethylarginines in the arginine- and glycine-rich domains of several spliceosomal Sm proteins. Within the methylosome, MEP50 binds protein substrates and activates the oncogenic protein arginine methyl transferase 5 (PRMT5).
Description	Full-length recombinant human MEP50 (WDR77) protein was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	Full Length
Molecular Weight	68 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human MEP50) Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage.
Subcellular Location	Nucleus. Cytoplasm.
Database References	HGNC: 29652 OMIM: 611734 KEGG: hsa:79084 STRING: 9606.ENSP00000235090 UniGene: PMID: 29518110 Data indicate that ZNF326 is an interaction partner and substrate of the PRMT5/WDR77 complex. PMID: 28977470 In an in vitro assay of vascular smooth muscle cells, circRNA WDR77 silencing significantly inhibited cell proliferation and migration. Bioinformatics methods revealed that miR-124 and fibroblast growth factor 2 (FGF-2) were downstream targets of circRNA WDR77. PMID: 29042195 SFN treatment of tumors results in reduced MEP50 level and H4R3me2s formation, confirming that that SFN impacts this complex in vivo. These studies suggest that the PRMT5/MEP50 is required for tumor growth and that reduced expression of this complex is a part of the mechanism of SFN suppression of tumor formation. PMID: 28854561 Results provide evidence that PRMT5 and p44 regulate gene expression of growth and anti-growth factors to promote lung tumorigenesis. PMID: 27480244 TSC22D2 protein might be a member of the PRMT5 complex via direct binding of WDR77. PMID: 27337956 MEP50 genes reduces gene expression through histone arginine methylation in keratinocytes. PMID: 26763441 MEP50 can transform cells independent of AR and ER. PMID: 25277535 Data indicate that MEP50 WD repeat protein is essential for methylation of histones H4 and H2A by PRMT5 arginine methyltransferase. PMID: 25713080 These findings characterize PKG as a novel regulator of AR-mediated transcription by enhancing AR cofactor p44/WDR77's function. PMID: 23755100 Data indicate a transcription complex androgen receptor (AR)-p44-Smad1, and confirmed for physical interaction by co-immunoprecipitaion. PMID: 23734213 These studies suggest a novel mechanism by which proliferation and differentiation of prostate epithelial cells are controlled by WDR77's location in the cell. PMID: 23145110 structure of the surprising hetero-octameric complex reveals the close interaction between the seven-bladed beta-propeller MEP50 and the N-terminal domain of PRMT5, and delineates the structural elements of substrate recognition. PMID: 23071334 p44 plays a role in mediating the effects of hormones during ovarian tumorigenesis. PMID: 22022581 These results provide a basis for understanding subcellular transport of p44/WDR77 during prostate development and tumorigenesis. PMID: 21789256 expression and function of p44 in breast cancer; expression of p44 shows strong cytoplasmic expression in morphologically normal terminal ductal lobular units, while nuclear p44 is observed in both ductal carcinoma in situ and invasive carcinoma PMID: 19840198 Here, we describe a novel component of the methylosome, a 50-kilodalton WD repeat protein termed methylosome protein 50 (MEP50). PMID: 11756452 SUZ12 might have a role in transcriptional regulation through physical interaction with MEP50 that can be an adaptor between PRMT5 and its substrate H2A PMID: 16712789 Forced nuclear localization of p44 inhibited prostate cancer cell growth by G1 cell-cycle arrest. PMID: 17032745 results suggest distinct functions of the nuclear and the p44/protein arginine methyltransferase 5 complexes in the developing fetal testis and in the oncogenesis of testicular tumors. PMID: 17437848 nuclear p44 and cytoplasmic p44 have distinct and opposing functions in the regulation of prostate cancer cell proliferation PMID: 18356297

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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.