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RNF31 Protein (AA 1-1066) (Strep Tag)

Crystallography grade RNF31 Origin: Mouse Host: Tobacco (Nicotiana tabacum) Recombinant ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. ELISA, SDS, WB
Catalog No. ABIN3136901
  • Target See all RNF31 Proteins
    RNF31 (Ring Finger Protein 31 (RNF31))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 1-1066
    Origin
    Mouse
    Source
    • 1
    Tobacco (Nicotiana tabacum)
    Purification tag / Conjugate
    This RNF31 protein is labelled with Strep Tag.
    Application
    ELISA, SDS-PAGE (SDS), Western Blotting (WB)
    Sequence
    MPGDEERGFL AAREELASAL RWDSAQVFPL EQLMPLLATS LPPAARYLQL DAGRLVRCNA HGEPRNYLNT LSTALNILEK YGRNLLSPQR PRYWRSVKFN NPVFRSTVDA VQGGRDVLRL YGYTEERPDG LSFPEGQEEP DEYQVAVVTL EVLLLRTELS LLLQNTHPRQ NALDQLLRES VEDGMLQLSE FHPLLREIVP GPRPSAQGST PGPCFLCGSA PGTLHCPACN QVSCPACDIL FHGHPSRAHH LRQALPGSHQ TASLSSSLPA SSQPRPPSSS LALGDSSLSS PDPANACLPW HCLTCATLNE PWAVFCAVCS QPKGCKVPGI EGSHGTGGLE PEPARDQWAC QSCTFENEAA AVLCAICERP RLAQPPSLVV DSHDAGVCQQ SLKQEDPLLT AAQPQVWYCD HCTFCNSGPV WVCAMCNRTR DPIPTQPALQ SYPSSLEKGR PKPGSSQHLG SSLPASCGDP EKQRQDKMRK EGLQLVSMIQ EGETAGASPE EVFSALQYSG TEVPLQWLRS ELSYVLEMVA ELAGQQDPEL GAFSCQEARK AWLDRHGNLD EAVEECVRAR RRKVHELQSL GFGPKEGSLQ ALFQHGGDVA RALTELQRQR LEPFHQRLWD RDPEPTPCWD GLDRQSLVRR LLAVYTLPSW GRAELALALL QETPRNYELL DVVEAVRHSQ DRAFLRRLLA QECAVCGWAL PRNRMQALIS CECTICPECF RQHFTIALKE KHITDMVCPA CGRPDLTDDA QLLSYFSTLD IQLRESLDPD AYALFHKKLT EAVLMRDPKF LWCAQCSFGF IYEREQLEAT CPQCHQTFCV RCKRQWEEQH RGRSCEDFQN WKRTNDPEYQ AQGLAMYLQE NGIDCPKCKF SYALARGGCM HFHCTQCRHQ FCSGCYNAFY AKNKCPDPNC KVKKSLHGHH PRDCLFYLRD WTAARLQKLL QDNNVMFNTE PPAGTRAVPG GGCRVMEQKE VHSGFRDEAC GKETPPGYAG LCQAHYKEYL VSLINAHSLD PATLYEVEEL ETATIRYLHL APQPADGEDL PAYQARLLQK LREEVPLGQS IARRRK
    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 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
    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.
    Purity
    ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
    Endotoxin Level
    Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
    Grade
    Crystallography grade
    Top Product
    Discover our top product RNF31 Protein
  • 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
  • Format
    Liquid
    Buffer
    The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.
    Handling Advice
    Avoid repeated freeze-thaw cycles.
    Storage
    -80 °C
    Storage Comment
    Store at -80°C.
    Expiry Date
    Unlimited (if stored properly)
  • Target
    RNF31 (Ring Finger Protein 31 (RNF31))
    Alternative Name
    Rnf31 (RNF31 Products)
    Synonyms
    RNF31 Protein, HOIP Protein, ZIBRA Protein, AL033293 Protein, BC031509 Protein, Flj10111 Protein, Paul Protein, mFLJ00217 Protein, ring finger protein 31 Protein, RNF31 Protein, rnf31 Protein, Rnf31 Protein
    Background
    E3 ubiquitin-protein ligase RNF31 (EC 2.3.2.31) (HOIL-1-interacting protein) (HOIP) (Putative Ariadne-like ubiquitin ligase) (PAUL) (RING finger protein 31) (RING-type E3 ubiquitin transferase RNF31),FUNCTION: E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:28701375). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (By similarity). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:28701375). 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 (By similarity). 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 (By similarity). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (By similarity). Recruited to the surface of bacteria by RNF213, which initiates the bacterial ubiquitin coat (By similarity). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (By similarity). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (By similarity). RNF31 is required for linear ubiquitination of BCL10, thereby promoting TCR-induced NF-kappa-B activation (By similarity). Binds polyubiquitin of different linkage types (By similarity). {ECO:0000250|UniProtKB:Q96EP0, ECO:0000269|PubMed:28701375}.
    Molecular Weight
    119.3 kDa
    UniProt
    Q924T7
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