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AGO1 Protein (AA 1-857) (Strep Tag)

Crystallography grade EIF2C1 Origine: Souris Hôte: Tobacco (Nicotiana tabacum) Recombinant ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. WB, ELISA, SDS
N° du produit ABIN3136505
  • Antigène Voir toutes AGO1 (EIF2C1) Protéines
    AGO1 (EIF2C1) (Eukaryotic Translation Initiation Factor 2C, 1 (EIF2C1))
    Type de proteíne
    Recombinant
    Attributs du protein
    AA 1-857
    Origine
    Souris
    Source
    • 2
    • 2
    • 1
    • 1
    Tobacco (Nicotiana tabacum)
    Purification/Conjugué
    Cette AGO1 protéine est marqué à la Strep Tag.
    Application
    Western Blotting (WB), ELISA, SDS-PAGE (SDS)
    Séquence
    MEAGPSGAAA GAYLPPLQQV FQAPRRPGIG TVGKPIKLLA NYFEVDIPKI DVYHYEVDIK PDKCPRRVNR EVVEYMVQHF KPQIFGDRKP VYDGKKNIYT VTALPIGNER VDFEVTIPGE GKDRIFKVSI KWLAIVSWRM LHEALVSGQI PVPLESVQAL DVAMRHLASM RYTPVGRSFF SPPEGYYHPL GGGREVWFGF HQSVRPAMWK MMLNIDVSAT AFYKAQPVIE FMCEVLDIRN IDEQPKPLTD SQRVRFTKEI KGLKVEVTHC GQMKRKYRVC NVTRRPASHQ TFPLQLESGQ TVECTVAQYF KQKYNLQLKY PHLPCLQVGQ EQKHTYLPLE VCNIVAGQRC IKKLTDNQTS TMIKATARSA PDRQEEISRL MKNASYNLDP YIQEFGIKVK DDMTEVTGRV LPAPILQYGG RNRAIATPNQ GVWDMRGKQF YNGIEIKVWA IACFAPQKQC REEVLKNFTD QLRKISKDAG MPIQGQPCFC KYAQGADSVE PMFRHLKNTY SGLQLIIVIL PGKTPVYAEV KRVGDTLLGM ATQCVQVKNV VKTSPQTLSN LCLKINVKLG GINNILVPHQ RSAVFQQPVI FLGADVTHPP AGDGKKPSIT AVVGSMDAHP SRYCATVRVQ RPRQEIIEDL SYMVRELLIQ FYKSTRFKPT RIIFYRDGVP EGQLPQILHY ELLAIRDACI KLEKDYQPGI TYIVVQKRHH TRLFCADKNE RIGKSGNIPA GTTVDTNITH PFEFDFYLCS HAGIQGTSRP SHYYVLWDDN RFTADELQIL TYQLCHTYVR CTRSVSIPAP AYYARLVAFR ARYHLVDKEH DSGEGSHISG QSNGRDPQAL AKAVQVHQDT LRTMYFA
    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.
    Attributs du produit
    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.
    Pureté
    ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
    niveau d'endotoxine
    Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
    Classe de qualité
    Crystallography grade
    Top Product
    Discover our top product EIF2C1 Protéine
  • Indications d'application
    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.
    Commentaires

    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.
    Conseil sur la manipulation
    Avoid repeated freeze-thaw cycles.
    Stock
    -80 °C
    Stockage commentaire
    Store at -80°C.
    Date de péremption
    Unlimited (if stored properly)
  • Antigène
    AGO1 (EIF2C1) (Eukaryotic Translation Initiation Factor 2C, 1 (EIF2C1))
    Autre désignation
    Ago1 (EIF2C1 Produits)
    Synonymes
    Ago Protein, Ago-1 Protein, Ago1 Protein, CG6671 Protein, Dm Ago1 Protein, Dmel\\CG6671 Protein, MRE20 Protein, ago1 Protein, ago1-1 Protein, anon-WO0257455.29 Protein, dAGO1 Protein, dAgo1 Protein, l(2)04845 Protein, l(2)4845 Protein, l(2)k00208 Protein, l(2)k08121 Protein, GB12654 Protein, dsim_GLEANR_9718 Protein, DsimGD25729 Protein, GD25729 Protein, EIF2C1 Protein, EIF2C Protein, GERP95 Protein, Q99 Protein, Eif2c1 Protein, ARGONAUTE 1 Protein, T1N15.2 Protein, T1N15_2 Protein, Argonaute-1 Protein, protein argonaute-2 Protein, argonaute 1 Protein, Argonaute 1 Protein, protein argonaute-1 Protein, argonaute 1, RISC catalytic component Protein, argonaute RISC catalytic subunit 1 Protein, Stabilizer of iron transporter SufD / Polynucleotidyl transferase Protein, AGO1 Protein, LOC552062 Protein, ago1 Protein, LOC659936 Protein, Dsim\AGO1 Protein, Ago1 Protein, LOC100386910 Protein, LOC100482671 Protein, LOC475337 Protein
    Sujet
    Protein argonaute-1 (Argonaute1) (mAgo1) (Argonaute RISC catalytic component 1) (Eukaryotic translation initiation factor 2C 1) (eIF-2C 1) (eIF2C 1) (Piwi/argonaute family protein meIF2C1),FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. May also be required for transcriptional gene silencing (TGS) of promoter regions which are complementary to bound short antigene RNAs (agRNAs). {ECO:0000269|PubMed:19174539}.
    Poids moléculaire
    97.2 kDa
    UniProt
    Q8CJG1
    Pathways
    Fc-epsilon Receptor Signaling Pathway, Regulatory RNA Pathways, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, Hormone Transport, Regulation of Actin Filament Polymerization, Stem Cell Maintenance, Ribonucleoprotein Complex Subunit Organization
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