Cat: IPD-X29544

Recombinant Rat LOX Protein,His

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Analytical Data

  • Gene name

    LOX

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Lysyl oxidase

  • Species

    Rat

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P16636

  • Expression Region

    163-411aa

  • Molecular Weight

    33 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.

Quality inspection process

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Protein Description

LOX (Lysyl oxidase) is a copper-dependent enzyme that plays a crucial role in the cross-linking of collagen and elastin, thereby influencing the structural integrity and mechanical properties of extracellular matrix (ECM) in various tissues. Its function is pivotal in processes such as tissue remodeling, wound healing, and fibrosis. Dysregulation of LOX activity has been implicated in various pathological conditions, including cancer progression, cardiovascular diseases, and fibrotic disorders. Consequently, LOX has emerged as a potential therapeutic target. Research endeavors have focused on the molecular mechanisms regulating LOX expression and activity, as well as its role in disease progression. Recombinant LOX proteins have been developed to facilitate studies on enzyme kinetics, substrate specificity, and interactions with ECM components. Moreover, these recombinant proteins are utilized in the development of biomaterials and tissue engineering applications, aiming to harness LOX's ability to enhance ECM stability and promote tissue regeneration. Overall, the investigation of LOX and its recombinant forms provides valuable insights into its biological functions and therapeutic potentials in addressing various health challenges.

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