Cat: IPD-X27054

Recombinant Human HO-2/HMOX2 Protein,His

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Analytical Data

  • Gene name

    HO-2/HMOX2

  • 简介

    Through its catalytic activity, HO-2/HMOX2 protein promotes the oxidative cleavage of heme at the α-methylene bridge carbon, thereby releasing carbon monoxide (CO). This process simultaneously produces biliverdin IXalpha and releases the central heme iron chelate in the form of ferrous iron. HO-2/HMOX2 Protein, Human (His) is the recombinant human-derived HO-2/HMOX2 protein, expressed by E. coli , with C-6*His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HMOX2; HO-2; HO2; Heme Oxygenase 2

  • Species

    Human

  • Source

    E. coli

  • Tag

    C-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P30519-1

  • Expression Region

    S2-L291

  • AA Sequence

    SAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVL

  • Protein Length

    Cytoplasmic Domain

  • Molecular Weight

    31 & 35 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

HO-2 (heme oxygenase-2), also known as HMOX2, is an important enzyme that plays a critical role in heme metabolism, catalyzing the degradation of heme into biliverdin, carbon monoxide, and free iron. Unlike its isoform HO-1, which is inducible and often associated with stress responses, HO-2 is constitutively expressed in various tissues, particularly in the brain and heart, suggesting a fundamental role in maintaining cellular homeostasis and protecting against oxidative stress. Research on HO-2 has gained traction due to its potential implications in neuroprotection, cardiovascular health, and various pathological conditions, including neurodegenerative diseases and ischemic injuries. The study of recombinant HO-2 protein offers valuable insights into its enzymatic activity, regulatory mechanisms, and potential therapeutic applications. Recombinant expression systems enable detailed characterization of HO-2, including its interactions with heme and other cofactors, as well as the modulation of its activity by pharmacological agents. Investigating the structure-function relationship of HO-2 through recombinant protein studies can lead to the development of novel therapeutic strategies aimed at enhancing its protective effects or inhibiting its activity in pathological contexts. Overall, research on HO-2 recombinant protein not only contributes to our understanding of heme metabolism but also opens new avenues for targeting this enzyme in clinical applications.

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