SHARPIN Protein (AA 1-387) (Strep Tag)
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- Target Alle SHARPIN Produkte
- SHARPIN (SHANK-Associated RH Domain Interacting Protein (SHARPIN))
- Protein-Typ
- Recombinant
- Proteineigenschaft
- AA 1-387
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Spezies
- Human
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Quelle
- Tobacco (Nicotiana tabacum)
- Aufreinigungstag / Konjugat
- Dieses SHARPIN Protein ist gelabelt mit Strep Tag.
- Applikation
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Sequenz
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MAPPAGGAAA AASDLGSAAV LLAVHAAVRP LGAGPDAEAQ LRRLQLSADP ERPGRFRLEL LGAGPGAVNL EWPLESVSYT IRGPTQHELQ PPPGGPGTLS LHFLNPQEAQ RWAVLVRGAT VEGQNGSKSN SPPALGPEAC PVSLPSPPEA STLKGPPPEA DLPRSPGNLT EREELAGSLA RAIAGGDEKG AAQVAAVLAQ HRVALSVQLQ EACFPPGPIR LQVTLEDAAS AASAASSAHV ALQVHPHCTV AALQEQVFSE LGFPPAVQRW VIGRCLCVPE RSLASYGVRQ DGDPAFLYLL SAPREAPATG PSPQHPQKMD GELGRLFPPS LGLPPGPQPA ASSLPSPLQP SWSCPSCTFI NAPDRPGCEM CSTQRPCTWD PLAAAST
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
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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.
- Aufreinigung
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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.
- 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)
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- 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
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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! - Beschränkungen
- Nur für Forschungszwecke einsetzbar
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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.
- Handhabung
- Avoid repeated freeze-thaw cycles.
- Lagerung
- -80 °C
- Informationen zur Lagerung
- Store at -80°C.
- Haltbarkeit
- Unlimited (if stored properly)
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- Target
- SHARPIN (SHANK-Associated RH Domain Interacting Protein (SHARPIN))
- Andere Bezeichnung
- SHARPIN (SHARPIN Produkte)
- Synonyme
- 0610041B22Rik Protein, AW121341 Protein, RBCKL1 Protein, SIPL1 Protein, cpdm Protein, Conneck1 Protein, SHANK-associated RH domain interacting protein Protein, SHANK associated RH domain interactor Protein, SHANK-associated RH domain interactor Protein, Sharpin Protein, SHARPIN Protein
- Hintergrund
- Sharpin (Shank-associated RH domain-interacting protein) (Shank-interacting protein-like 1) (hSIPL1),FUNCTION: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:21455173, PubMed:21455180, PubMed:21455181). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed:21455173, PubMed:21455180, PubMed:21455181). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:21455173, PubMed:21455180, PubMed:21455181). LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (PubMed:21455173, PubMed:21455180, PubMed:21455181). The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed:28481331). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed:28481331). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:28481331). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed:23708998). {ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181, ECO:0000269|PubMed:23708998, ECO:0000269|PubMed:28481331}.
- Molekulargewicht
- 39.9 kDa
- UniProt
- Q9H0F6
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