IL-36 gamma/IL-1F9 Protein, Human

Customer Review

Based on 1 Customer Validation

IL-36 gamma (IL-1F9), a subform of IL-36 family, belongs to IL-1 superfamily. IL-36 gamma mediates inflammatory response. L-36 beta binds to IL-36R and recruits the co-receptor IL-1RacP, and thereby activating NF-κB and MAPK signaling pathways, but the activation requires N-terminal cleavage by neutrophil granule-derived proteases. IL-36 gamma/IL-1F9 Protein, Human is a recombinant human IL-36 gamma without any tag, which is produced in E. coli.

For research use only. We do not sell to patients.
  • Species: Human
  • Source: E. coli
  • Storage:
    Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
  • Biological Activity
  • Technical Parameters
  • Product Properties
  • Documentation
  • References
  • Help & FAQs

Biological Activity

Description

IL-36 gamma (IL-1F9), a subform of IL-36 family, belongs to IL-1 superfamily. IL-36 gamma mediates inflammatory response. L-36 beta binds to IL-36R and recruits the co-receptor IL-1RacP, and thereby activating NF-κB and MAPK signaling pathways, but the activation requires N-terminal cleavage by neutrophil granule-derived proteases[1][2]. IL-36 gamma/IL-1F9 Protein, Human is a recombinant human IL-36 gamma without any tag, which is produced in E. coli.

Background

IL-36 gamma (IL-1F9), a subform of IL-36 family, belongs to IL-1 superfamily. IL-36 gamma is expressed in peripheral blood lymphocytes, keratinocytes, bronchial epithelial cells and THP-1 cells[3].
The sequence of amino acids in IL-36 gamma differs in different species. Human IL-36 gamma shares <55% aa sequence identity with mouse.
IL-36 gamma has β-trefoil structure. L-36 gamma binds to IL-36R and recruits the co-receptor IL-1RAcP. So that heterodimeric signaling complex brings Toll/IL-1R (TIR) domains of the 2 receptor chains in close proximity, and thereby activating NF-κB and MAPK signaling pathways[1]. But the activation requires N-terminal cleavage at Val1518 by neutrophil granule-derived proteases, such as cathepsin G, elastase and proteinase-3[1][2]. IL-36 gamma is associated with chronic inflammation and cancers. IL-36 gamma is up-regulated in skin psoriatic lesions, inaganglionic and ganglionic areas of the colon in patients with Hirschsprung's disease, and inflamed mucosa of patients with inflammatory bowel disease (IBD)[1][4].
IL-36 gamma is a pro-inflammatory factor. IL-36 gamma mediates inflammatory response through the activation of NF-κB and MAPK signaling pathway[2].

In Vitro

IL-36 gamma (human, 50 ng/mL for 4 h or 100 ng/mL for 24 h) promotes the expression of pro-inflammatory cytokines and antibacterial peptides in NHOKs (oral keratinocytes)[5].
IL-36 gamma (human, 0.1 ng/mL, 3 days) promotes colony formation, migration and invasion of AGS cells[6].

Verified Bioactivity

The ability to induce IL-8 secretion in A431 human epithelial carcinoma cells has an ED50 value of 5-20 ng/mL.

MCE Validation Data

  • Purity - SDS-PAGE

    Purity - SDS-PAGE

    ≥ 95%, as determined by reducing SDS-PAGE.

  • Bioactivity - Cell-Based Assay

    Bioactivity - Cell-Based Assay

    The ability to induce IL-8 secretion in A431 human epithelial carcinoma cells has an ED50 value of 15.07 ng/mL.

Technical Parameters

  • Species Human
  • Source E. coli
  • Tag Tag Free
  • Accession
  • Gene ID
  • Protein Length

    Full Length of Isoform-1

  • Synonyms

    IL36G; Interleukin 1-Related Protein 2; Prev. IL1F9; Interleukin-36 Gamma; IL-1RP2; IL1RP2; IL-1F9; Interleukin 1 Family, Member 9; IL-1H1; IL-1 Related Protein 2; IL1H1; IL-1-Related Protein 2; IL1E; IL-1-Epsilon; Interleukin-1 Homolog 1; IL-1 Epsilon; I

  • AA Sequence

    SMCKPITGTINDLNQQVWTLQGQNLVAVPRSDSVTPVTVAVITCKYPEALEQGRGDPIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDLYGQPEPVKPFLFYRAKTGRTSTLESVAFPDWFIASSKRDQPIILTSELGKSYNTAFELNIND

  • Predicted Molecular Mass

    17 kDa

  • Molecular Weight

    Approximately 14-16 kDa, based on SDS-PAGE under reducing conditions.

  • Purity

    ≥ 95%, as determined by reducing SDS-PAGE.

Product Properties

Appearance

Lyophilized powder

Formulation

Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 100 mM NaCl, 0.1 mM EDTA, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Storage & Stability

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Room temperature in continental US; may vary elsewhere.

References

Calculators

Reconstitution Calculator

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

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=
Mass (in vial) Mass (in vial)
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Desired Reconstitution Concentration Desired Reconstitution Concentration
Dilution Calculator

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

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The Specific Activity Calculator Equation
  • Specific Activity (Unit/mg)
  • Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) Specific Activity (Unit/mg)
Unit/mg
= 106 ÷
Biological Activity (ED50) Biological Activity (ED50)
106 ÷
ng/mL
MOQ
Minimum order quantity
100 mg

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