Cat: IPD-X25220

Recombinant Human ITGBL1 Protein (HEK293),His & Myc

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Analytical Data

  • Gene name

    ITGBL1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Osteoblast-specific cysteine-rich protein (Ten integrin EGF-like repeat domain-containing protein)

  • Species

    Human

  • Source

    HEK293

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O95965

  • Expression Region

    24-494aa

  • Molecular Weight

    56.5 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

ITGBL1, or Integrin Beta-Like Protein 1, is a member of the integrin family, which plays a crucial role in mediating cellular adhesion and communication within the extracellular matrix. Research into ITGBL1 has gained attention due to its potential involvement in various physiological and pathological processes, such as cell migration, differentiation, and tissue remodeling. Studies have indicated that ITGBL1 may be implicated in cancer progression, inflammation, and fibrosis, suggesting that it could serve as a biomarker for certain diseases or as a therapeutic target. The recombinant production of ITGBL1 protein allows for detailed analysis of its structure and function, facilitating the exploration of its role in cell signaling pathways and interactions with other proteins. Moreover, the ability to produce ITGBL1 in a laboratory setting opens avenues for developing novel therapeutic strategies and diagnostic tools. Understanding the mechanisms by which ITGBL1 influences cellular behavior could provide insights into its potential as a target for interventions in diseases where integrin signaling is dysregulated. Overall, ongoing research into ITGBL1 and its recombinant variants holds promise not only for advancing our knowledge of cellular dynamics but also for developing targeted treatments for conditions linked to integrin-mediated pathways.

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