Recombinant Human CXCL9 (MIG) (carrier-free)

Pricing & Availability
Other Names
Monokine induced by interferon gamma (MIG), Small inducible cytokine, subfamily B, member 9 (SCYB9)
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Human_CXCL9_RECOM_BA_091916
Baf3-mCXCR3 transfectants chemoattracted by human CXCL9.
  • Human_CXCL9_RECOM_BA_091916
    Baf3-mCXCR3 transfectants chemoattracted by human CXCL9.
Cat # Size Price Quantity Avail. Save
578102 10 µg 125 CHF
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578104 25 µg 225 CHF
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578106 100 µg 595 CHF
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578108 500 µg 2'400 CHF
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Description

CXCL9 is an inflammatory chemokine initially identified by differential screening of a cDNA library from lymphokine-activated macrophages. CXCL9 is a CXC chemokine and member of the non-ELR (lacking a Glu-Leu-Arg motif in the N-terminal region) CXC chemokine family. CXCL9 shares the CXCR3 receptor with CXCL10 and CXCL11, and these ligands differ in their receptor-binding and -activating properties; CXCL11 is more potent than CXCL10, and CXCL10 is more potent than CXCL9. An alternative spliced variant, CXCR3B, has been described for CXCR3. CXCR3B mediates the angiostatic effect of CXCR3 ligands and is the receptor for PF4 (CXCL4). CXCR3B has been detected in human neoplastic tissues. CXCL9 plays a key role in leukocyte trafficking, acting on activated CD4+ Th1 cells, CD8+ T cells, IL-2 activated T lymphocytes, and NK cells. Also, CXCL9 (as well as CXCL10 and CXCL11) induces angiostatic effects in human microvacular endothelial cells. In addition, CXCL9 enhances T lymphocyte function in alloimmune response; CXCL9 induces T cells proliferation and cytokine production in an experimental model of cardiac allograft vasculopathy. CXCL9 is induced by cytokines, particularly IFNγ during infection, injury, or immunoinflammatory responses, and it can be inactivated by CD26/dipeptidil peptidase IV after truncation by this protease. Amino-terminal truncation of CXCL9 by CD26 impairs lymphocyte chemotaxis, but the antiangiogenic activity is not affected.  In rheumatoid arthritis, CXCL9 is synergistically stimulated by TNFα or IL-1a and IFNγ.

Product Details
Technical Data Sheet (pdf)

Product Details

Reactivity
Human
Source
Human CXCL9, amino acids Thr23 - Thr125 (Accession # NM_002416.1) was expressed in E. coli.
Molecular Mass
The 103 amino acid recombinant protein has a predicted molecular mass of approximately 11.7 kD. The DTT-reduced protein migrates at approximately 15 kD, and the non-reduced protein migrates at approximately 18 kD by SDS-PAGE. The N-terminal amino acid is Threonine.
Purity
>98%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in PBS.
Endotoxin Level
Less than 0.01 ng per µg cytokine 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 one month, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored from -20°C to -70°C. Stock solutions can also be prepared at 50-100 µg/mL in sterile buffer (PBS, HPBS, DPBS, or EBSS) containing carrier protein such as 0.2-1% BSA or HSA and stored in working aliquots at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
Activity
Bioactivity was measured by its property to chemoattract Baf3-mCXCR3 transfectants in a dose dependent manner. ED50 = 0.4 — 0.8 µg/ml.
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 validated 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.

Antigen Details

Structure
Chemokine
Distribution
CXCL9 is secreted by monocytes, macrophages, APC, eosinophils, endothelial cells, and B cells. Also, CXCL9 is secreted by fibroblasts in inflammatory conditions.
Function
CXCL9 plays a key role in leukocyte trafficking, acting on activated CD4+ Th1 cells, CD8+ T cells, IL-2 activated T lymphocytes, and NK cells. Also, CXCL9 (as well as CXCL10 and CXCL11) induces angiostatic effects in human microvacular endothelial cells.
Ligand/Receptor
CXCR3A, CXCR3B
Cell Type
Hematopoietic stem and progenitors
Biology Area
Cell Biology, Immunology, Signal Transduction, Stem Cells
Molecular Family
Cytokines/Chemokines
Antigen References

1. Loetscher M, et al. 1996. J. Exp. Med. 184:963.
2. Lambeir AM, et al. 2001. J. Biol. Chem. 276:29839.
3. Lasagni L, et al. 2003. J. Exp. Med. 197:1537.
4. Whiting D, et al. 2004. J. Immunol. 172:7417.
5. Proost P, et al. 2004. J. Leuko. Biol. 75:777.
6. Gorbachev AV, et al. 2007. J. Immunol. 178: 2278.
7. Rosenblum JM, et al. 2010. J. Immunol. 184:3450.
8. Crawford MA, et al. 2010. PLoS Pathog. 6:e1001199.

Gene ID
4283 View all products for this Gene ID
UniProt
View information about CXCL9 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.

Go To Top Version: 3    Revision Date: 09.19.2016

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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