IL-17A Protein, Human

IL-17A is a homodimeric cytokine and plays a critical role in host defense mechanisms against many bacterial and fungal pathogens as well as allergic and autoimmune responses. IL-17A induces the production of antimicrobial peptides, cytokines, chemokines, and matrix metalloproteinases^[1][2]. IL-17A Protein, Human is a recombinant human IL-17A protein and is expressed in E. coli. It consists of 137 amino acids (I19-A155).

Interleukin-17A (IL-17A), also known as CTLA-8, belongs to the IL-17 cytokine family. IL-17A is expressed in memory Th17 cells and is a product of memory CD4⁺ T cells. IL-17A is also produced by a wide variety of immune cells, including CD8⁺ T cells, γδT cells, natural killer T (NKT) cells, monocytes, and neutrophils^[1][2][3].
The human IL-17A shares 63.23% amino acid sequence identity with mouse and 61.90% identity with rat.
IL-17A plays a critical role in host defense mechanisms against many bacterial and fungal pathogens as well as allergic and autoimmune responses. IL-17A induces the production of antimicrobial peptides (defensins and S100 proteins), cytokines (IL-6, G-CSF, and GM-CSF), chemokines (CXCL1, CXCL5, IL-8, CCL2, and CCL7), and matrix metalloproteinases (MMP1, MMP3, and MMP13). IL-17A is detrimental in viral infection through promoting neutrophilic inflammation. IL-17A is a homodimeric cytokine and shares similar biological activities with IL-17F. IL-17A binds to IL-17RA with high affinity, and IL-17RA is required for the biological activity of IL-17A. In tumorigenesis, IL-17A recruits myeloid derived suppressor cells (MDSCs) to dampen anti-tumor immunity. IL-17A also enhances tumor growth in vivo through the induction of IL-6^[1][2].
IL-17A can be used for the research of autoimmune diseases, infection and cancer^[1][4].

IL-17A (100 ng/mL; 24 h) inhibits the expression of thymic stromal lymphopoietin (TSLP) in human primary keratinocytes^[5].
IL-17A (0.1–100 ng/mL; 0-24 h) significantly potentiates TNF-α-induced IL-8 protein secretion and gene expression in a concentration- and time-dependent manner^[6].

1.Measured by its ability to induce IL-6 secretion by NIH-3T3 mouse embryonic fibroblast cells and the ED₅₀ is 1-7 ng/mL.
2.Measured by its ability to induce CXCL1/GRO alpha secretion in HT-29 human colon adenocarcinoma cells. The ED₅₀ for this effect is ≤3.340 ng/mL. Corresponding to a specific activity is ≥2.99 × 10⁵ U/mg.

• 
  Measured by its ability to induce IL-6 secretion by NIH‑3T3 mouse embryonic fibroblast cells.The ED₅₀ for this effect is 6.256 ng/mL, corresponding to a specific activity is 1.59×10⁵ U/mg.

Human

E. coli

Tag Free

Q16552 (G24-A155)

3605  [NCBI]

Full Length of Mature Protein

GITIPRNPGCPNSEDKNFPRTVMVNLNIHNRNTNTNPKRSSDYYNRSTSPWNLHRNEDPERYPSVIWEAKCRHLGCINADGNVDYHMNSVPIQQEILVLRREPPHCPNSFRLEKILVSVGCTCVTPIVHHVA

Approximately 16-17 kDa, based on SDS-PAGE under reducing conditions.

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

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.
2.Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCl, 200 mM NaCl, 500 mM arginine, pH 8.0.
3.Lyophilized from a 0.22 μm filtered solution of 4 mM HCl, pH 2.5.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

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).

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.

Room temperature in continental US; may vary elsewhere.

• [1]. Chen K, et al. Interluekin-17A (IL17A). Gene. 2017 May 30;614:8-14.  [Content Brief]

  [2]. Iwakura Y, et al. The roles of IL-17A in inflammatory immune responses and host defense against pathogens. Immunol Rev. 2008 Dec;226:57-79.  [Content Brief]

  [3]. Cua DJ, et al. Innate IL-17-producing cells: the sentinels of the immune system. Nat Rev Immunol. 2010 Jul;10(7):479-89.  [Content Brief]

  [4]. Wright JF, et al. The human IL-17F/IL-17A heterodimeric cytokine signals through the IL-17RA/IL-17RC receptor complex. J Immunol. 2008 Aug 15;181(4):2799-805.  [Content Brief]

  [5]. Kinoshita H, et al. Cytokine milieu modulates release of thymic stromal lymphopoietin from human keratinocytes stimulated with double-stranded RNA. J Allergy Clin Immunol. 2009 Jan;123(1):179-86.  [Content Brief]

  [6]. Henness S, et al. IL-17A acts via p38 MAPK to increase stability of TNF-alpha-induced IL-8 mRNA in human ASM. Am J Physiol Lung Cell Mol Physiol. 2006 Jun;290(6):L1283-90.  [Content Brief]