SHARPIN Protein (AA 1-387) (His tag)
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- Target See all SHARPIN products
- SHARPIN (SHANK-Associated RH Domain Interacting Protein (SHARPIN))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-387
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Origin
- Human
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Source
- HEK-293 Cells
- Purification tag / Conjugate
- This SHARPIN protein is labelled with His tag.
- Purpose
- Made-to-order recombinant SHARPIN Protein expressed in mammalian cells.
- Sequence
- 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 Purification-Tag is based on experiences 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.
- Specificity
- If you are looking for a specific domain and are interested in a partial protein or a different isoform, please contact us regarding an individual offer.
- Characteristics
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Key Benefits:
- Made to order protein - from design to production - by highly experienced protein experts.
- Protein expressed in mammalian cells and purified in one-step affinity chromatography
- The optimized expression system ensures reliability for intracellular, secreted and transmembrane proteins.
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
If you are not interested in a full length protein, please contact us for individual protein fragments.
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. - Purity
- > 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
- Grade
- custom-made
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- Application Notes
- We expect the protein to work for functional studies. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Buffer
- The buffer composition is at the discretion of the manufacturer.
- Handling Advice
- Avoid repeated freeze-thaw cycles.
- Storage
- -80 °C
- Storage Comment
- Store at -80°C.
- Expiry Date
- 12 months
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- Target
- SHARPIN (SHANK-Associated RH Domain Interacting Protein (SHARPIN))
- Alternative Name
- SHARPIN (SHARPIN Products)
- Background
- 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}.
- Molecular Weight
- 39.9 kDa
- UniProt
- Q9H0F6
- AlphaFold
- Q9H0F6
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