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NAT10 Protein (AA 1-1025) (Strep Tag)

Crystallography grade NAT10 Origine: Humain Hôte: Tobacco (Nicotiana tabacum) Recombinant >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. ELISA, WB, SDS
N° du produit ABIN3094030
  • Antigène Voir toutes NAT10 Protéines
    NAT10 (N-Acetyltransferase 10 (GCN5-Related) (NAT10))
    Type de proteíne
    Recombinant
    Attributs du protein
    AA 1-1025
    Origine
    • 3
    • 1
    Humain
    Source
    • 2
    • 1
    • 1
    Tobacco (Nicotiana tabacum)
    Purification/Conjugué
    Cette NAT10 protéine est marqué à la Strep Tag.
    Application
    ELISA, Western Blotting (WB), SDS-PAGE (SDS)
    Séquence
    MHRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK ARPSVLWCYK KELGFSSHRK KRMRQLQKKI KNGTLNIKQD DPFELFIAAT NIRYCYYNET HKILGNTFGM CVLQDFEALT PNLLARTVET VEGGGLVVIL LRTMNSLKQL YTVTMDVHSR YRTEAHQDVV GRFNERFILS LASCKKCLVI DDQLNILPIS SHVATMEALP PQTPDESLGP SDLELRELKE SLQDTQPVGV LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIIQSLNPE FNKAVIRVNV FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS LLGPYLVFMA STINGYEGTG RSLSLKLIQQ LRQQSAQSQV STTAENKTTT TARLASARTL YEVSLQESIR YAPGDAVEKW LNDLLCLDCL NITRIVSGCP LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN SPNDLQMLSD APAHHLFCLL PPVPPTQNAL PEVLAVIQVC LEGEISRQSI LNSLSRGKKA SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM YYEGRFPCLE EKVLETPQEI HTVSSEAVSL LEEVITPRKD LPPLLLKLNE RPAERLDYLG VSYGLTPRLL KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK TLTDEDEADQ GGWLAAFWKD FRRRFLALLS YQFSTFSPSL ALNIIQNRNM GKPAQPALSR EELEALFLPY DLKRLEMYSR NMVDYHLIMD MIPAISRIYF LNQLGDLALS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR KVVKLFNEVQ EKAIEEQMVA AKDVVMEPTM KTLSDDLDEA AKEFQEKHKK EVGKLKSMDL SEYIIRGDDE EWNEVLNKAG PNASIISLKS DKKRKLEAKQ EPKQSKKLKN RETKNKKDMK LKRKK
    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 NAT10 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
    NAT10 (N-Acetyltransferase 10 (GCN5-Related) (NAT10))
    Autre désignation
    NAT10 (NAT10 Produits)
    Synonymes
    ALP Protein, NET43 Protein, AI429152 Protein, zgc:66119 Protein, DDBDRAFT_0190093 Protein, DDBDRAFT_0234062 Protein, DDB_0190093 Protein, DDB_0234062 Protein, RGD1306717 Protein, N-acetyltransferase 10 Protein, N-acetyltransferase 10 (GCN5-related) Protein, ribosome biogenesis ATPase (predicted) Protein, hypothetical protein Protein, N-acetyltransferase 10 (GCN5-related) L homeolog Protein, NAT10 Protein, Nat10 Protein, nat10 Protein, CC1G_12871 Protein, MCYG_05927 Protein, PITG_19671 Protein, MGYG_06040 Protein, SPAC20G8.09c Protein, nat10.L Protein
    Sujet
    RNA cytidine acetyltransferase (EC 2.3.1.-) (18S rRNA cytosine acetyltransferase) (N-acetyltransferase 10) (N-acetyltransferase-like protein) (hALP),FUNCTION: RNA cytidine acetyltransferase that catalyzes the formation of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed:25411247, PubMed:25653167, PubMed:30449621, PubMed:35679869). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed:30449621, PubMed:35679869). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed:30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed:25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25411247, PubMed:25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed:30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed:14592445, PubMed:18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed:31722219). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000250|UniProtKB:P53914, ECO:0000269|PubMed:14592445, ECO:0000269|PubMed:17631499, ECO:0000269|PubMed:18082603, ECO:0000269|PubMed:19303003, ECO:0000269|PubMed:25411247, ECO:0000269|PubMed:25653167, ECO:0000269|PubMed:26882543, ECO:0000269|PubMed:27993683, ECO:0000269|PubMed:30165671, ECO:0000269|PubMed:30449621, ECO:0000269|PubMed:31722219, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:35679869}.
    Poids moléculaire
    115.7 kDa
    UniProt
    Q9H0A0
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