Recombinant Human IL-17A (carrier-free)

Pricing & Availability
Other Names
Interleukin-17A, Cytotoxic T-lymphocyte-associated antigen 8, cytotoxic T-lymphocyte-associated serine esterase 8, CTLA-8, IL-17
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Product Citations
publications
rh_IL-17A_BA_121508.jpg
Induction of IL-6 in human dermal fibroblast by IL-17A.
  • rh_IL-17A_BA_121508.jpg
    Induction of IL-6 in human dermal fibroblast by IL-17A.
Cat # Size Price Quantity Avail. Save
570502 10 µg $125
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570504 25 µg $195
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570506 100 µg $550
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570508 500 µg $1,600
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Description

IL-17A was initially identified from a subtracted cDNA library between closely related murine lymphoid cells and called CTLA-8, and share 58% homology with an open reading frame of the T-lymphotropic Herpesvirus Samirii virus (viral IL-17) (5). IL-17A belongs to a family of cytokines, which has five members; designated IL-17A-F. IL-17 is expressed by a unique lineage of CD4 T cells (Th17) that develop in response to IL-23, in particular under conditions in which Th1 and Th2 development are suppressed. IL-17A shares the greatest homology (55%) with IL-17F. Both IL-17A and IL-17F are produced by Th17 cells. IL-17A and IL-17F can either exist as IL-17A homodimers and IL-17F homodimers or as IL-17A-IL-17F heterodimers (6). IL-17 is a key mediator of autoimmune disorders, including rheumatoid arthritis, psoriasis, inflammatory bowel disease, and asthma, and plays a role in host defense (7).

Product Details
Technical data sheet

Product Details

Source
Human IL-17A, amino acids Ile20-Ala155 (Accession # NM_002190) was expressed in E. coli.
Molecular Mass
The 137 amino acid N-terminal methionylated recombinant protein has a predicted molecular mass of 15,666 Da. This protein exists as a disulfide-linked homodimer. The DTT-reduced protein migrates at approximately 16kDa by SDS-PAGE. The non-reduced protein migrates as a homodimer, at approximately 28kDa by SDS-PAGE.
Purity
Purity is >98%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in 10mM NaH2PO4, 300mM NaCl, pH 7.2.
Endotoxin Level
Endotoxin level is <0.1 EU/µg (<0.01ng/µg) protein as determined by the LAL method.
Concentration
10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial (please contact technical support for concentration, or use our Lookup tool if you have a lot number.)
Please note, new lots of the 100 µg size will be lot-specific and may differ from previous lots that had a fixed concentration.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
Activity
The ED50 is 2 - 4 ng/ml, corresponding to a specific activity 5 - 2.5 x 105 units/mg, as determined by a dose dependent stimulation of normal human dermal fibroblasts production of IL-6.
Application

Bioassay

Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Product Citations
  1. Luo J, et al. 2019. Mediators Inflamm. 2019:9050965. PubMed

Antigen Details

Structure
Cytokine
Distribution

IL-17A is largely produced by activated memory T lymphocytes, CD4+ T helper cells (Th17), neutrophils, CD8(+), NK, and gamma-delta T cells (3).

Function
IL-17A is a potent regulator of granulopoiesis and neutrophil recruitment under normal and inflammatory conditions. Organ overexpression of IL-17A increases circulating neutrophil numbers and recruitment into the organs by induction of CXCL2, IL-1β, and G-CSF. Il-17A induces CXCL1, CXCL2, CXCL5, and CXCL8 in human epithelial cells. IL-17A also cooperates with TLR ligands, IL-1 beta, and TNF alpha to enhance inflammatory reactions and stimulate production of beta-defensins and other antimicrobial peptides (1, 2).
Interaction
IL-17AR is expressed in epithelial cells, fibroblasts, B and T lymphocytes, myelomonocytic cells, marrow stromal cells, synovial endothelial cells and chondrocytes from arthritic patients express IL-17R (4).
Ligand/Receptor
IL-17A signals through a heteromeric receptor composed of IL-17RA and IL-17RC.
Biology Area
Cell Biology, Immunology, Neuroinflammation, Neuroscience
Molecular Family
Cytokines/Chemokines
Antigen References

1. Yu J, et al. Front Biosci 13:170-177 2008.
2. Toy D, et al. J. Immunol. 177:36-39 2006.
3. Benghiat FS, et al. Transplant Rev 23:11-18 2009.
4. Honorati MC, et al. Rheumatology 40:522-527 2001.
5. Rouvier E, et al. J. Immunol. 150:5445-5456 1993.
6. Liang SC, et al. J. Immunol. 179:7791-7799 2007.
7. Ouyang W, et al. Immunity 28:454-467 2008.

Gene ID
3605 View all products for this Gene ID
UniProt
View information about IL-17A on UniProt.org

Related FAQs

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

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For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

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Toll-Free Phone: 1-877-Bio-Legend (246-5343) Phone: (858) 768-5800 Fax: (877) 455-9587

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