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IFIT1 Protein (AA 1-478) (Strep Tag)

This Recombinant IFIT1 protein is expressed in Cell-free protein synthesis (CFPS).
Catalog No. ABIN3093032
starts at
$20,480.57
Plus shipping costs $50.00, if applicable $20.00 dry ice
0.5 mg
Shipping to: United States
Delivery in 55 to 67 Business Days

Quick Overview for IFIT1 Protein (AA 1-478) (Strep Tag) (ABIN3093032)

Target

See all IFIT1 Proteins
IFIT1 (Interferon-Induced Protein with Tetratricopeptide Repeats 1 (IFIT1))

Protein Type

Recombinant

Origin

  • 5
  • 2
  • 1
Human

Source

  • 3
  • 1
  • 1
  • 1
  • 1
  • 1
Cell-free protein synthesis (CFPS)

Application

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

Purity

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

Grade

custom-made
  • Protein Characteristics

    AA 1-478

    Purification tag / Conjugate

    This IFIT1 protein is labelled with Strep Tag.

    Sequence

    MSTNGDDHQV KDSLEQLRCH FTWELSIDDD EMPDLENRVL DQIEFLDTKY SVGIHNLLAY VKHLKGQNEE ALKSLKEAEN LMQEEHDNQA NVRSLVTWGN FAWMYYHMGR LAEAQTYLDK VENICKKLSN PFRYRMECPE IDCEEGWALL KCGGKNYERA KACFEKVLEV DPENPESSAG YAISAYRLDG FKLATKNHKP FSLLPLRQAV RLNPDNGYIK VLLALKLQDE GQEAEGEKYI EEALANMSSQ TYVFRYAAKF YRRKGSVDKA LELLKKALQE TPTSVLLHHQ IGLCYKAQMI QIKEATKGQP RGQNREKLDK MIRSAIFHFE SAVEKKPTFE VAHLDLARMY IEAGNHRKAE ENFQKLLCMK PVVEETMQDI HFHYGRFQEF QKKSDVNAII HYLKAIKIEQ ASLTRDKSIN SLKKLVLRKL RRKALDLESL SLLGFVYKLE GNMNEALEYY ERALRLAADF ENSVRQGP
    Sequence without tag. The proposed Strep-Tag is based on experience with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If 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
    • State-of-the-art algorithm used for plasmid design (Gene synthesis).

    This protein is a predefined custom 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 predefined custom 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®).
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    Your project requires further customization? Contact us and discover our custom protein solutions

  • 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.
    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

    IFIT1 (Interferon-Induced Protein with Tetratricopeptide Repeats 1 (IFIT1))

    Alternative Name

    IFIT1

    Background

    Interferon-induced protein with tetratricopeptide repeats 1 (IFIT-1) (Interferon-induced 56 kDa protein) (IFI-56K) (P56),FUNCTION: Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Exhibits antiviral activity against several viruses including human papilloma and hepatitis C viruses. {ECO:0000269|PubMed:19008854, ECO:0000269|PubMed:19416887, ECO:0000269|PubMed:21976647, ECO:0000269|PubMed:23334420}.

    Molecular Weight

    55.4 kDa

    UniProt

    P09914

    Pathways

    Hepatitis C
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