Cat: IPD-X40275

Recombinant Escherichia phage lambda gam Protein ,His & Myc

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Analytical Data

  • Gene name

    gam

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    gamma

  • Species

    Escherichia phage lambda

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P03702

  • Expression Region

    1-138aa

  • Molecular Weight

    23.8 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

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Protein Description

GAM (Glycoaminoglycan-binding protein) is a significant subject of research due to its multifaceted role in cell signaling, tissue regeneration, and disease progression. Understanding the structure and function of GAMs has important implications in various fields including developmental biology, immunology, and cancer research. These proteins are known to bind glycosaminoglycans, which are essential components of the extracellular matrix and play crucial roles in cellular interactions and signaling pathways. The dysregulation of GAMs has been linked to several pathological conditions, such as cancer metastasis and inflammatory diseases, making them attractive targets for therapeutic intervention. Recent advancements in biophysical and molecular biology techniques have allowed researchers to elucidate the complex mechanisms underlying GAM functions and their interactions with other biomolecules. This growing body of research aims to harness the potential of GAMs in regenerative medicine and targeted drug delivery, paving the way for innovative treatments that leverage their unique properties. As the scientific community continues to explore GAMs, they offer promising avenues for understanding fundamental biological processes and developing novel therapeutic strategies.

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