SHARPIN Protein (AA 1-380) (Strep Tag)

Catalog No. ABIN3136796

Product Details

Target: SHARPIN (SHANK-Associated RH Domain Interacting Protein (SHARPIN))

Protein Type: Recombinant

Protein Characteristics: AA 1-380

Origin: Mouse

Source: Cell-free protein synthesis (CFPS)

Purification tag / Conjugate: This SHARPIN protein is labelled with Strep Tag.

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

Brand: AliCE®

Sequence: MSPPAGGAAV AADPASPVVL LAVHAAVRPL GAGQDAEAQP RKLQLIADPE RPGRFRLGLL GTEPGAVSLE WPLEAICYTV RGPNQHELQP PPGGPGTFSV HFLDPEEAQQ WAALVRDATA EGQNGSGSPA PAPAPAMCPI SPPCSSMAQI PKATQPEVDL PQSSGNFKKE ELATRLSQAI AGGDEKAAAQ VAAVLAQHHV ALNVQLMEAW FPPGPIRLQV TVEDATSVLS SSSSAHVSLK IHPHCSIAAL QDQVFSEFGF PPAVQRWVIG RCLCMPERSL ASYGVSQDGD PAFLYLLSAP REVSGQSLQN SKMDRKLGLF PQSLGLPHDL QPSSSSLPSP SQPGWSCPSC TFINASNRPG CEMCSTQRPC AWDPLAAAST
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.

Characteristics: Key Benefits:

• Made in Germany - from design to production - by highly experienced protein experts.
• Protein expressed with ALiCE® and purified in one-step affinity chromatography
• 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 try to ensure that you receive soluble 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 against its specific reference buffer.
• We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

Purification: One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (AliCE®).

Purity: > 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).

Grade: custom-made

Application Details

Application Notes: 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.

Comment:

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

Handling

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer.
Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: 12 months

Target Details

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) (mSIPL1),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:17538631, 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:17538631, PubMed:21455173, PubMed:21455180, PubMed:21455181). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:17538631, 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. 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. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (By similarity). {ECO:0000250|UniProtKB:Q9H0F6, ECO:0000269|PubMed:17538631, ECO:0000269|PubMed:21455173, ECO:0000269|PubMed:21455180, ECO:0000269|PubMed:21455181}.

Molecular Weight: 39.9 kDa

UniProt: Q91WA6