RNF111 Protein (AA 1-989) (Strep Tag)
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- Antigène Voir toutes RNF111 Protéines
- RNF111 (Ring Finger Protein 111 (RNF111))
- Type de proteíne
- Recombinant
- Attributs du protein
- AA 1-989
- Origine
- Souris
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Source
- Tobacco (Nicotiana tabacum)
- Purification/Conjugué
- Cette RNF111 protéine est marqué à la Strep Tag.
- Application
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Séquence
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MSQWTPEFNE LYTLKVAMKS GTPDAPTTQE SLKAVLLHPQ PLGATKSFPA EVEMINSKVG NEFSHLCDDS QKQEKDMTGN QQEQEKSGVV RKKRKSQQAG PSYVQNCVKE NQEILGRRQQ LETPSDEDND SSLSECLSSP SSSLHFGGSD TVTSDEDKEV SVRHTQPVLS AKSRSHSARS HKWPRTEADP VPSLLMKRPC FHGSALRRVT CRKRLVKSSS SQRTQKQKER MLVQRKKREA LAQRKYALLS SSSSSSENDL SSDSSSSSST DGEEDLCASA SENPSNPAAP SGSIDEDVVV IEASFTPQVT ANEEINVTST DSEVEIVTVG ESYRSRSTLG HSRSHWSQGS SSHTGRPQES RNRSRISTVI QPLRQNAAEV VDLTVDEDEP TIVPTTSARM DSQTTSASIN NSNPSTSEQA SDTTSTVASS QPSTVSETEA TLTSNSATGS SVGDDVRRTA SSAVPESGPP AMPRLPSCCP QHSPCGGTSQ SHHALAHPHS SCFQQHGHHF QHHHHHHHTP HPAVPVSPSF SDPACPVERP QVQAPCGANS SSGSSYHDQQ ALPVDLSNSA LRTHGSGGFH GASAFDPCCP VTSSRAAVFG HQAAAAPTQP LSIDGYGSSM VAQPQPQPPP QPSLSSCRHY MPPPYASLTR PLHHQASACH HSHGNAPPQT QPPPQVDYVI PHPVHAFHSQ ISSHAASHPV APPPPTHLGS TAAPIPQHLP PAHQPISHHI PAPAPSAQRL HPHEVMQRME VQRRRMMQHP TRAHERPPPH PHRMHPNYGH GHHIHVPQTM SSHPRQAPER TAWELGIEAG VTAATYTPGA LHPHLAHYHA PPRLHHLQLG ALPLMVPDMA GYPHIRYISS GLDGASFRGP FRGNFEELIH LEERLGNVNR GASQGTIERC TYPHKYKKVT TDWFSQRKLH CKQDGEEGTE EDTEEKCTIC LSILEEGEDV RRLPCMHLFH QVCVDQWLIT NKKCPICRVD IEAQLPSES
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. - Attributs du produit
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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.
- Pureté
- ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
- niveau d'endotoxine
- Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
- Top Product
- Discover our top product RNF111 Protéine
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- Indications d'application
- 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.
- Commentaires
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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.
- Conseil sur la manipulation
- Avoid repeated freeze-thaw cycles.
- Stock
- -80 °C
- Stockage commentaire
- Store at -80°C.
- Date de péremption
- Unlimited (if stored properly)
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- Antigène
- RNF111 (Ring Finger Protein 111 (RNF111))
- Autre désignation
- Rnf111 (RNF111 Produits)
- Synonymes
- ARK Protein, Arkadia Protein, RNF111 Protein, rnf111 Protein, ark Protein, MGC81253 Protein, MGC146379 Protein, ring finger protein 111 Protein, ring finger 111 Protein, RNF111 Protein, Rnf111 Protein, rnf111-b Protein, rnf111 Protein
- Sujet
- E3 ubiquitin-protein ligase Arkadia (EC 2.3.2.27) (RING finger protein 111) (RING-type E3 ubiquitin transferase Arkadia),FUNCTION: E3 ubiquitin-protein ligase required for mesoderm patterning during embryonic development (PubMed:11298452). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP (PubMed:14657019). Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP (PubMed:14657019). In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL (By similarity). Associates with UBE2D2 as an E2 enzyme (By similarity). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (PubMed:23530056). Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (By similarity). Mediates ubiquitination and degradation of sumoylated PML (PubMed:23530056). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (PubMed:23530056). {ECO:0000250|UniProtKB:Q6ZNA4, ECO:0000269|PubMed:11298452, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:17341133, ECO:0000269|PubMed:23530056}.
- Poids moléculaire
- 107.9 kDa
- UniProt
- Q99ML9
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