Cat: PA1000-1985

Recombinant Human MMP13 Protein,His

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Analytical Data

  • Gene name

    MMP13

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MMP13;Collagenase 3

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P45452

  • Expression Region

    104-274aa

  • AA Sequence

    YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM LPDDDVQGIQSLYGPGDEDPN

  • Molecular Weight

    21 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

MMP13, also known as collagenase-3, is a member of the matrix metalloproteinase (MMP) family, which plays a critical role in the degradation of extracellular matrix components, particularly collagen. Its activity is particularly relevant in physiological processes such as tissue remodeling during development and wound healing, as well as in pathological conditions, including arthritis, cancer metastasis, and cardiovascular diseases. MMP13 is predominantly expressed in cartilage and is implicated in the pathological degradation of cartilage in osteoarthritis. The regulation of MMP13 activity is complex and involves various factors, including tissue inhibitors of metalloproteinases (TIMPs) and signaling pathways influenced by inflammatory cytokines. Due to its significant role in disease progression, MMP13 has emerged as a potential therapeutic target, making the study of its recombinant protein particularly important. The generation of recombinant MMP13 allows for detailed investigation of its biochemical properties, substrate specificity, and regulatory mechanisms, as well as the development of specific inhibitors that can potentially mitigate its overactivity in various disease states. Understanding the structure-function relationship of MMP13 and its role in disease pathways is crucial for the design of novel therapeutic strategies aimed at controlling its activity and mitigating the associated tissue damage. This line of research has important implications not only for understanding the mechanisms underlying degenerative diseases but also for the development of innovative treatments that can improve patient outcomes.

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