Cat: IPD-X26537

Recombinant Human S100A9 Protein,His

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Analytical Data

  • Gene name

    S100A9

  • 简介

    The S100A9 protein is a calcium and zinc binder that plays a critical regulatory role in inflammation and immune responses. Its diverse functions include induction of neutrophil chemotaxis, adhesion, enhanced bactericidal activity through SYK, PI3K/AKT and ERK1/2 activation, and promotion of phagocytosis. S100A9 Protein, Human (His) is the recombinant human-derived S100A9 protein, expressed by E. coli , with N-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured by its ability to induce CXCL1/KC secretion by C3H/10T1/2 mouse embryonic fibroblast cells.The ED50 for this effect is ≤4.506 μg/mL, corresponding to a specific activity is ≥221.93 units/mg. Measured by its ability to induce CXCL1/KC secretion by C3H10T1/2 mouse embryonic fibroblast cells.The ED50 for this effect is 4.506 μg/mL, corresponding to a specific activity is 221.93 units/mg.

  • Alternative Names

    Protein S100-A9; Calgranulin-B; Calprotectin L1H subunit; Leukocyte L1 complex heavy chain; MRP-14; CAGB; CFAG

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-6*His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P06702

  • Expression Region

    T2-P114

  • Protein Length

    Partial

  • Molecular Weight

    15-16 kDa as determined by reducing SDS-PAGE; 30-32 kDa as determined by non-reducing SDS-PAGE.

  • 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

Heme oxygenase-1 (HO-1) is an enzyme that plays a pivotal role in the catabolism of heme, leading to the production of biliverdin, carbon monoxide, and free iron. It is a key player in various physiological processes, including oxidative stress response, apoptosis, and inflammation, making it a crucial target for therapeutic interventions in various diseases. Research has increasingly focused on the upregulation of HO-1 as a cytoprotective mechanism, particularly in conditions such as ischemia-reperfusion injury, neurodegenerative disorders, and cardiovascular diseases. The enzyme's expression is often induced by various stressors and cytokines, highlighting its role as a regulatory protein in cellular defense mechanisms. Investigations into recombinant HO-1 protein have allowed scientists to explore its functional properties, potential therapeutic applications, and the molecular pathways involved in its action. Given its antioxidant and anti-inflammatory properties, recombinant HO-1 is being studied for its potential in the treatment of diseases characterized by oxidative stress and inflammation. Furthermore, understanding the regulatory mechanisms of HO-1 expression and activity may lead to novel strategies for enhancing its protective effects in clinical settings. Thus, the study of HO-1, particularly in its recombinant form, holds significant promise for the development of innovative therapeutic approaches aimed at mitigating tissue damage and improving outcomes in various pathological conditions.

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