Recombinant Human CXCL9/MIG Protein, CF Summary
Product Specifications
Thr23-Thr125
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
11106-MG
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with mouse CXCR3. The ED50 for this effect is 0.020‑0.300 µg/mL.
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2 μg/lane of Recombinant Human CXCL9/MIG Protein (Catalog # 11106-MG) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 12-17 kDa.
Reconstitution Calculator
Background: CXCL9/MIG
CXCL9, a member of the alpha subfamily of chemokines that lack the ELR domain, was initially identified as a lymphokine-activated gene in mouse macrophages. Human CXCL9 was subsequently cloned using mouse MIG cDNA as a probe. The CXCL9 gene is induced in macrophages and in primary glial cells of the central nervous system specifically in response to IFN-gamma. CXCL9 has been shown to be a chemoattractant for activated T‑lymphocytes and TIL but not for neutrophils or monocytes. The human CXCL9 cDNA encodes a 125 amino acid residue precursor protein with a 22 amino acid residue signal peptide that is cleaved to yield a 103 amino acid residue mature protein. CXCL9 has an extended carboxy‑terminus containing greater than 50% basic amino acid residues and is larger than most other chemokines. The carboxy‑terminal residues of CXCL9 are prone to proteolytic cleavage resulting in size heterogeneity of natural and recombinant CXCL9. CXCL9 with large carboxy‑terminal deletions have been shown to have diminished activity in the calcium flux assay. MIG also functions in vivo as a potent chemoattractant for tumor-infiltrating lymphocytes and activates peripheral blood lymphocytes, as well as NK cells and TH1 lymphocytes. Therefore, MIG could be a potential candidate for antiangiogenic and immunomodulation therapy for tumor disease. A chemokine receptor (CXCR3) specific for CXCL9 and IP-10 has been cloned and shown to be highly expressed in IL-2-activated T‑lymphocytes.
- Loetscher, M. et al. (1996) J. Exp. Med. 184:963.
- Liao, F. et al. (1995) J. Exp. Med. 182:1301.
- Vanguri, P. (1995) J. Neuroimmunol. 56:35.
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