RNF135 Protein (AA 1-432) (Strep Tag)

Produktnummer ABIN3087357

Produktdetails

Target: RNF135 (Ring Finger Protein 135 (RNF135))

Protein-Typ: Recombinant

Proteineigenschaft: AA 1-432

Spezies: Human

Quelle: Tobacco (Nicotiana tabacum)

Aufreinigungstag / Konjugat: Dieses RNF135 Protein ist gelabelt mit Strep Tag.

Applikation: ELISA, Western Blotting (WB), SDS-PAGE (SDS)

Sequenz: MAGLGLGSAV PVWLAEDDLG CIICQGLLDW PATLPCGHSF CRHCLEALWG ARDARRWACP TCRQGAAQQP HLRKNTLLQD LADKYRRAAR EIQAGSDPAH CPCPGSSSLS SAAARPRRRP ELQRVAVEKS ITEVAQELTE LVEHLVDIVR SLQNQRPLSE SGPDNELSIL GKAFSSGVDL SMASPKLVTS DTAAGKIRDI LHDLEEIQEK LQESVTWKEA PEAQMQGELL EAPSSSSCPL PDQSHPALRR ASRFAQWAIH PTFNLKSLSC SLEVSKDSRT VTVSHRPQPY RWSCERFSTS QVLCSQALSS GKHYWEVDTR NCSHWAVGVA SWEMSRDQVL GRTMDSCCVE WKGTSQLSAW HMVKETVLGS DRPGVVGIWL NLEEGKLAFY SVDNQEKLLY ECTISASSPL YPAFWLYGLH PGNYLIIKQV KV
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.

Produktmerkmale: 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.

Aufreinigung: Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):

1. 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.
2. 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.

Reinheit: >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin-Niveau: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Güteklasse: Crystallography grade

Anwendungsinformationen

Applikationshinweise: 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.

Kommentare:

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!

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.

Handhabung: Avoid repeated freeze-thaw cycles.

Lagerung: -80 °C

Informationen zur Lagerung: Store at -80°C.

Haltbarkeit: Unlimited (if stored properly)

Antigendetails

Target: RNF135 (Ring Finger Protein 135 (RNF135))

Andere Bezeichnung: RNF135 (RNF135 Produkte)

Synonyme: MMFD Protein, REUL Protein, Riplet Protein, 0610037N03Rik Protein, 2410006N06Rik Protein, LRRGT00184 Protein, ring finger protein 135 Protein, RNF135 Protein, Rnf135 Protein

Hintergrund: E3 ubiquitin-protein ligase RNF135 (EC 2.3.2.27) (RIG-I E3 ubiquitin ligase) (REUL) (RING finger protein 135) (RING finger protein leading to RIG-I activation) (Riplet) (RING-type E3 ubiquitin transferase RNF135),FUNCTION: E2-dependent E3 ubiquitin-protein ligase that functions as a RIGI coreceptor in the sensing of viral RNAs in cell cytoplasm and the activation of the antiviral innate immune response (PubMed:19017631, PubMed:19484123, PubMed:21147464, PubMed:23950712, PubMed:28469175, PubMed:31006531). Together with the UBE2D3, UBE2N and UB2V1 E2 ligases, catalyzes the 'Lys-63'-linked polyubiquitination of RIGI oligomerized on viral RNAs, an essential step in the activation of the RIG-I signaling pathway (PubMed:19017631, PubMed:21147464, PubMed:28469175, PubMed:31006531). Through a ubiquitin-independent parallel mechanism, which consists in bridging RIGI filaments forming on longer viral RNAs, further activates the RIG-I signaling pathway (PubMed:31006531). This second mechanism that synergizes with the ubiquitin-dependent one would thereby allow an RNA length-dependent regulation of the RIG-I signaling pathway (Probable). Associated with the E2 ligase UBE2N, also constitutively synthesizes unanchored 'Lys-63'-linked polyubiquitin chains that may also activate the RIG-I signaling pathway (PubMed:28469175, PubMed:31006531). {ECO:0000269|PubMed:19017631, ECO:0000269|PubMed:19484123, ECO:0000269|PubMed:21147464, ECO:0000269|PubMed:23950712, ECO:0000269|PubMed:28469175, ECO:0000269|PubMed:31006531, ECO:0000305|PubMed:31006531}.

Molekulargewicht: 47.9 kDa

UniProt: Q8IUD6