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GBL Protein (AA 1-326) (Strep Tag)

This Recombinant GBL protein is expressed in Cell-free protein synthesis (CFPS).
Catalog No. ABIN3137146
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 GBL Protein (AA 1-326) (Strep Tag) (ABIN3137146)

Target

See all GBL Proteins
GBL (G protein beta subunit-like (GBL))

Protein Type

Recombinant

Origin

  • 4
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Mouse

Source

  • 5
  • 2
  • 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 1-326

    Purification tag / Conjugate

    This GBL protein is labelled with Strep Tag.

    Sequence

    MNTTPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEI TPDRSMIAAA GYQHIRMYDL NSNNPNPIIS YDGVSKNIAS VGFHEDGRWM YTGGEDCTAR IWDLRSRNLQ CQRIFQVNAP INCVCLHPNQ AELIVGDQSG AIHIWDLKTD HNEQLIPEPE SSITSAHIDP DASYMAAVNS AGNCYVWNLT GGIGDDVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA DQTCKIWRTS NFSLMTELSI KSSNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE TGEIKREYGG HQKAVVCLAF NDSVLG
    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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  • 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

    GBL (G protein beta subunit-like (GBL))

    Alternative Name

    Mlst8

    Background

    Target of rapamycin complex subunit LST8 (TORC subunit LST8) (G protein beta subunit-like) (Protein GbetaL) (Mammalian lethal with SEC13 protein 8) (mLST8),FUNCTION: Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals (PubMed:17141160). mTORC1 is activated in response to growth factors or amino acids (By similarity). In response to nutrients, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (By similarity). In the same time, it inhibits catabolic pathways by phosphorylating the autophagy initiation components ULK1 and ATG13, as well as transcription factor TFEB, a master regulators of lysosomal biogenesis and autophagy (By similarity). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (By similarity). Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity (By similarity). In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity (By similarity). mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive (By similarity). mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors (By similarity). mTORC2 promotes the serum-induced formation of stress-fibers or F-actin (By similarity). mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation (By similarity). mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422' (By similarity). mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657' (By similarity). {ECO:0000250|UniProtKB:Q9BVC4, ECO:0000269|PubMed:17141160}.

    Molecular Weight

    35.9 kDa

    UniProt

    Q9DCJ1

    Pathways

    PI3K-Akt Signaling, RTK Signaling, Fc-epsilon Receptor Signaling Pathway, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, Regulation of Actin Filament Polymerization, Autophagy, CXCR4-mediated Signaling Events, BCR Signaling, Warburg Effect
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