MED6 Protein (AA 1-246) (Strep Tag)
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- Target See all MED6 Proteins
- MED6 (Mediator Complex Subunit 6 (MED6))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-246
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Origin
- Human
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Source
- Tobacco (Nicotiana tabacum)
- Purification tag / Conjugate
- This MED6 protein is labelled with Strep Tag.
- Application
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Sequence
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MAAVDIRDNL LGISWVDSSW IPILNSGSVL DYFSERSNPF YDRTCNNEVV KMQRLTLEHL NQMVGIEYIL LHAQEPILFI IRKQQRQSPA QVIPLADYYI IAGVIYQAPD LGSVINSRVL TAVHGIQSAF DEAMSYCRYH PSKGYWWHFK DHEEQDKVRP KAKRKEEPSS IFQRQRVDAL LLDLRQKFPP KFVQLKPGEK PVPVDQTKKE AEPIPETVKP EEKETTKNVQ QTVSAKGPPE KRMRLQ
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us. - Characteristics
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Key Benefits:
- Made in Germany - from design to production - by highly experienced protein experts.
- Protein expressed with ALiCE® and purified by multi-step, protein-specific process to ensure correct folding and modification.
- These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.
The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.
Expression System:- ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
- During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!
Concentration:- The concentration of our recombinant proteins is measured using the absorbance at 280nm.
- The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.
- We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.
- Purification
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Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):
- In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
- Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.
- Purity
- >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
- Endotoxin Level
- Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
- Top Product
- Discover our top product MED6 Protein
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- Application Notes
- In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.
- Comment
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ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein! - Restrictions
- For Research Use only
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- Format
- Liquid
- Buffer
- The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.
- Handling Advice
- Avoid repeated freeze-thaw cycles.
- Storage
- -80 °C
- Storage Comment
- Store at -80°C.
- Expiry Date
- Unlimited (if stored properly)
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- Target
- MED6 (Mediator Complex Subunit 6 (MED6))
- Alternative Name
- MED6 (MED6 Products)
- Synonyms
- NY-REN-28 Protein, wu:fa14c11 Protein, zgc:86933 Protein, 1500012F11Rik Protein, AU019660 Protein, AV213303 Protein, RNA polymerase transcriptional regulation mediator-like protein Protein, mediator complex subunit 6 Protein, hypothetical protein Protein, MED6 Protein, Med6 Protein, med6 Protein, CAALFM_C306170CA Protein
- Background
- Mediator of RNA polymerase II transcription subunit 6 (Activator-recruited cofactor 33 kDa component) (ARC33) (Mediator complex subunit 6) (hMed6) (Renal carcinoma antigen NY-REN-28),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. {ECO:0000269|PubMed:16595664}.
- Molecular Weight
- 28.4 kDa
- UniProt
- O75586
- Pathways
- Stem Cell Maintenance, Regulation of Lipid Metabolism by PPARalpha
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