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EIF3I Protein (AA 1-325) (Strep Tag)

Crystallography grade EIF3I Origin: Human Host: Tobacco (Nicotiana tabacum) Recombinant >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. ELISA, WB, SDS
Catalog No. ABIN3079378
  • Target See all EIF3I Proteins
    EIF3I (Eukaryotic Translation Initiation Factor 3, Subunit I (EIF3I))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 1-325
    Origin
    • 5
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    Human
    Source
    • 18
    • 2
    • 2
    • 1
    • 1
    Tobacco (Nicotiana tabacum)
    Purification tag / Conjugate
    This EIF3I protein is labelled with Strep Tag.
    Application
    ELISA, Western Blotting (WB), SDS-PAGE (SDS)
    Sequence
    MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY SSGGEDGYVR IHYFDPQYFE FEFEA
    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 EIF3I 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
    EIF3I (Eukaryotic Translation Initiation Factor 3, Subunit I (EIF3I))
    Alternative Name
    EIF3I (EIF3I Products)
    Synonyms
    EIF3S2 Protein, PRO2242 Protein, TRIP-1 Protein, TRIP1 Protein, eIF3-beta Protein, eIF3-p36 Protein, 36kDa Protein, D4Ertd632e Protein, Eif3s2 Protein, Trip1 Protein, eIF-3-beta Protein, eIF3 p36 Protein, eif3s2 Protein, hm:zehn0464 Protein, wu:fb62b08 Protein, zgc:56211 Protein, zgc:77823 Protein, CaO19.2967 Protein, eIF-3 39 kDa subunit homolog Protein, eIF3i Protein, eif3-beta Protein, eif3-p36 Protein, eif3i Protein, pro2242 Protein, trip-1 Protein, trip1 Protein, eukaryotic translation initiation factor 3 subunit I Protein, eukaryotic translation initiation factor 3, subunit I Protein, Eukaryotic Initiation Factor Protein, Eukaryotic translation initiation factor 3 subunit I Protein, translation initiation factor eIF3 subunit i Protein, eukaryotic translation initiation factor 3 subunit I L homeolog Protein, EIF3I Protein, Eif3i Protein, eif-3.I Protein, eIF3i Protein, eif3i Protein, TIF34 Protein, eif3i.L Protein
    Background
    Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36),FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03008, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
    Molecular Weight
    36.5 kDa
    UniProt
    Q13347
    Pathways
    Mitotic G1-G1/S Phases, DNA Replication, Ribonucleoprotein Complex Subunit Organization, Synthesis of DNA
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