MUL1 Protein (AA 1-352) (Strep Tag)
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- Antigène Voir toutes MUL1 Protéines
- MUL1 (Mitochondrial E3 Ubiquitin Protein Ligase 1 (MUL1))
- Type de proteíne
- Recombinant
- Attributs du protein
- AA 1-352
- Origine
- Souris
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Source
- Tobacco (Nicotiana tabacum)
- Purification/Conjugué
- Cette MUL1 protéine est marqué à la Strep Tag.
- Application
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Séquence
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MESGSRPSLG QVILLGTSSM VTAVLYSIYR QKAQVAQELK GAKKIHLGED LKGILSEAPG KCVPYAVIEG AVRSVKETLN SQFVENCKGV IQRLSLQEHK MVWNRTTHLW NDYSKIIHQR TNTVPFDLVP HEDGVAVSVR VLKPLDSVDL GLETVYEKFH PSVQSFTDAI GHYISGERPK GIQETEEMLK VGATLTGIGE LVLDNNAVRL QPPKQGMQYY LSSQDFDSLL HRQESSVRLW KILVLVFGFA TCATLFFILR KQYLHRQERL RQQQLQEEFL EHEAQLLSQA SPEDRESLKS ACVVCLSNFK SCVFLECGHV CSCRQCYLAL PEPKRCPICR REITRVIPLY NS
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 MUL1 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
- MUL1 (Mitochondrial E3 Ubiquitin Protein Ligase 1 (MUL1))
- Autre désignation
- Mul1 (MUL1 Produits)
- Synonymes
- C1orf166 Protein, GIDE Protein, MAPL Protein, MULAN Protein, RNF218 Protein, RP11-401M16.2 Protein, mul1 Protein, zgc:92166 Protein, 0610009K11Rik Protein, AV000801 Protein, Gide Protein, RGD1309944 Protein, im:7146383 Protein, zgc:165594 Protein, mitochondrial E3 ubiquitin protein ligase 1 Protein, mitochondrial E3 ubiquitin protein ligase 1 L homeolog Protein, mitochondrial E3 ubiquitin protein ligase 1a Protein, mitochondrial ubiquitin ligase activator of NFKB 1 Protein, mitochondrial E3 ubiquitin protein ligase 1b Protein, MUL1 Protein, mul1.L Protein, mul1a Protein, Mul1 Protein, mul1b Protein
- Sujet
- Mitochondrial ubiquitin ligase activator of NFKB 1 (EC 2.3.2.27) (E3 ubiquitin-protein ligase MUL1) (Growth inhibition and death E3 ligase) (Protein Hades) (RING-type E3 ubiquitin transferase NFKB 1),FUNCTION: Exhibits weak E3 ubiquitin-protein ligase activity (By similarity). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity). Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteasomal degradation (By similarity). Mediates polyubiquitination of cytoplasmic TP53 at 'Lys-27' which targets TP53 for proteasomal degradation, thus reducing TP53 levels in the cytoplasm and mitochondrion (By similarity). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (By similarity). Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization (By similarity). Likely to promote mitochondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway (PubMed:24898855). May also be involved in the sumoylation of the membrane fission protein DNM1L (By similarity). Inhibits cell growth (By similarity). When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (By similarity). Involved in the modulation of innate immune defense against viruses by inhibiting RIGI-dependent antiviral response (By similarity). Can mediate RIGI sumoylation and disrupt its polyubiquitination (By similarity). {ECO:0000250|UniProtKB:Q969V5, ECO:0000269|PubMed:24898855}.
- Poids moléculaire
- 39.8 kDa
- UniProt
- Q8VCM5
- Pathways
- Positive Regulation of Endopeptidase Activity
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