Recombinant Human Mediator Of Rna Polymerase Ii Transcription Subunit 1 (MED1) Protein (His-SUMO)

Name: Recombinant Human Mediator Of Rna Polymerase Ii Transcription Subunit 1 (MED1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03792P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Mediator Of Rna Polymerase Ii Transcription Subunit 1 (MED1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q15648
Target Symbol	MED1
Synonyms	Activator-recruited cofactor 205 kDa component; ARC205; CRSP1; CRSP200; DRIP205; DRIP230; MED1; MED1_HUMAN; Mediator complex subunit 1; Mediator of RNA polymerase II transcription subunit 1; p53 regulatory protein RB18A; PBP; Peroxisome proliferator-activated receptor-binding protein; PPAR binding protein ; PPAR-binding protein; PPARBP ; PPARGBP; RB18A; Thyroid hormone receptor-associated protein complex 220 kDa component; Thyroid receptor-interacting protein 2; TR-interacting protein 2; Trap220; TRIP-2; TRIP2; Vitamin D receptor-interacting protein complex component DRIP205
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	FGEEYFDESSQSGDNDDFKGFASQALNTLGVPMLGGDNGETKFKGNNQADTVDFSIISVAGKALAPADLMEHHSGSQGPLLTTGDLGKEKTQKRVKEGNGTSNSTLSGPGLDSKPGKRSRTPSNDGKSKDKPPKRKKADTEGKSPSHSSSNRPF
Expression Range	878-1031aa
Protein Length	Partial
Mol. Weight	32.2kDa
Research Area	Epigenetics And Nuclear Signaling
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	Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells.
Subcellular Location	Nucleus. Note=A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3.
Protein Families	Mediator complex subunit 1 family
Database References	HGNC: 9234 OMIM: 604311 KEGG: hsa:5469 STRING: 9606.ENSP00000300651 UniGene: PMID: 29187405 maintenance of the cancer cell state is dependent on recruitment of Mediator and Cohesin through FOXA and master transcription factors PMID: 27739523 Data suggest that mediator complex subunit 1 (Med1/TRAP220) is a target for checkpoint kinase 2 (Chk2)-mediated phosphorylation and may play a role in cellular DNA damage responses by mediating proper induction of gene transcription upon DNA damage. PMID: 28430840 In a cohort of youth at risk for bipolar disorder, pathway analysis showed an enrichment of the glucocorticoid receptor (GR) pathway with the genes MED1, HSPA1L, GTF2A1 and TAF15, which might underlie the previously reported role of stress response in the risk for bipolar disorder in vulnerable populations. PMID: 28291257 modulation of ESR1-MED1 interactions by cAMP signaling plays a critical role in human decidualization. PMID: 26849466 Our data indicate that MED1 serves as a key mediator in ARv567es induced gene expression PMID: 25481872 Results show that miR-1 is downregulated in osteosarcoma cells but both of its targets Med1 and Med31 were overexpressed suggesting that MiR-1 plays an important role on the proliferation of osteosarcoma cells through regulation of Med1 and Med31. PMID: 24969180 MED1 is required for optimal PRDM16-induced Ucp1 expression PMID: 25644605 no association between SCZ and the SNPs of VDR, suggesting that VDR is not a major gene for SCZ in Chinese Han population. However, our data indicate a potential involvement of VDR SNPs in the susceptibility of risperidone-treated patients to MetS PMID: 24418047 hyperactivated ERK and/or AKT signaling pathways promoted MED1 overexpression in prostate cancer cells. PMID: 23538858 These results demonstrate a role for MED1 in mediating resistance to the pure anti-estrogen fulvestrant both in vitro and in vivo. PMID: 23936234 multiple modes of the GATA1-MED1 axis may help to fine-tune GATA1 function during GATA1-mediated homeostasis events. PMID: 24245781 Data concluded that those of VDR ff genotype may be regarded as "low responders" to vitamin D intake in terms of response of circulating 25(OH)D and certain inflammatory biomarkers. PMID: 23160722 MiR-205 is an epigenetically regulated tumor suppressor that targets MED1. PMID: 22869146 MED1 is recruited to the HER2 gene and required for its expression. PMID: 22964581 Med1 (also known as PBP/RB18A/TRAP220/DRIP205) is a component of the human TRAP/Mediator complex that plays an important role in the transcriptional control of various genes PMID: 22342682 functional communications between the MED1 subunit and the MED24-containing submodule that mediate estrogen receptor functions and growth of both normal mammary epithelial cells and breast carcinoma cells. PMID: 22331469 Studies indicate that the activation domain of p53 (p53AD) binds directly to the MED17 subunit of Mediator, whereas the p53 C-terminal domain (p53CTD) binds the MED1 subunit. PMID: 21326907 These results suggest that Mediator structural shifts induced by activator binding help stably orient pol II prior to transcription initiation within the human mediator-RNA polymerase II-TFIIF assembly. PMID: 22343046 Regulation of androgen receptor-dependent transcription by coactivator MED1 is mediated through a newly discovered noncanonical binding motif. PMID: 22102282 MED1 phosphorylation leads to ubiquitin-conjugating enzyme E2C (UBE2C) locus looping, UBE2C gene expression and cell growth in castration-resistant prostate cancer. PMID: 21556051 establish ARGLU1 as a new MED1-interacting protein required for estrogen-dependent gene transcription and breast cancer cell growth. PMID: 21454576 Vitamin D receptor rs2228570 polymorphism is associated with invasive ovarian carcinoma. PMID: 20473893 The core subunit MED1 facilitates VDR activity and regulating keratinocyte proliferation and differentiation PMID: 20520624 analysis of molecular mechanism of binding TRAP220 coactivator to Retinoid X Receptor alpha, activated by 9-cis retinoic acid PMID: 20398753 analysis of mediator in three different structural states: bound to the activator SREBP-1a, VP16, or an activator-free state PMID: 20534441 Results show that the cells of this aggressive form of breast cancer are genetically preprogrammed to depend on NR1D1 and PBP for the energy production necessary for survival. PMID: 20160030 regulates p53-dependent apoptosis PMID: 11840331 Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation PMID: 11912212 spermine significantly enhanced the interaction between HNF4alpha and full-length DRIP205 in an AF-2, NR-box-dependent manner. Spermine enhanced the interaction of DRIP205 with the VDR , but decreased the interaction of both HNF4alpha and VDR with GRIP1 PMID: 12089346 TFIID and human mediator coactivator (TRAP220) complexes assemble cooperatively on promoter DNA PMID: 12130544 there is a coregulatory role for subunits of this protein in androgen receptor-mediated gene expression PMID: 12218053 examination of regulation by cellular signaling pathways PMID: 12356758 extended LXXLL motif sequence determines the nuclear receptor binding specificity PMID: 12556447 DRIP205 has a role as a coactivator of FXR PMID: 15187081 DRIP205 coactivation of estrogen receptor alpha (ERalpha) involves multiple domains of both proteins PMID: 15471764 RB18A plays a central role to control p53wt and p53mut protein content and functions in cells through a loop of regulation, which involves MDM2 PMID: 15848166 MED1 exists predominantly in a TRAP/Mediator subpopulation enriched in RNA polymerase II and is required for ER-mediated transcription. PMID: 15989967 MED14 and MED1 are used by glucocorticoid receptor in a gene-specific manner, providing a mechanism for promoter selectivity by glucocorticoid receptor PMID: 16239257 ERK-mediated phosphorylation is a regulatory mechanism that controls TRAP220/Med1 expression levels and modulates its functional activity. PMID: 16314496 TRAP220/MED1 plays a novel coregulatory role in facilitating the recruitment of TRAP/Mediator to specific target genes involved in growth and cell cycle progression via GABP PMID: 16574658 Med1 depleted cells exhibited an exacerbated response to retinoids, both in terms transcriptional responses and of cellular differentiation. PMID: 16723356 Expression of TRAP220 mRNA and protein was shown to be decreased significantly in the temporal cortex of patients with epilepsy. PMID: 16934225 Both DRIP205 and SRC-3 are required for the keratinocyte differentiation PMID: 17223341 Recruitment of CBP and TRAP220 was diminished by the overexpression of a MED25 NR box deletion mutant, and by treatment with MED25 siRNA PMID: 17641689 phosphorylation of RXRalpha at serine 260 impaired the recruitment of DRIP205 and other coactivators to the VDR.RXRalpha complex PMID: 18003614 ERK-regulated site in Med1 protein is also essential for up-regulating interferon-induced transcription although not critical for binding to C/EBP-beta PMID: 18339625 ERK phosphorylation of MED1 is a regulatory mechanism that promotes MED1 association with Mediator and, as such, may facilitate a novel feed-forward action of nuclear hormones PMID: 18391015 Decreased MED1 transcript levels are observed in matched normal mucosa when compared with colorectal and ovarian cancers. PMID: 19127118 a decrease of RB18A/MED1 expression in human melanoma cells increases their tumorigenic phenotype. PMID: 19243021

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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.