Recombinant Mouse CCL21/6Ckine Protein Summary
Details of Functionality |
Measured by its ability to chemoattract 5-10 day cultured human peripheral blood lymphocytes (PBL). The ED50 for this effect is 50-200 ng/mL. Measured by its ability to chemoattract BaF3 mouse pro‑B cells transfected with human CCR7. The ED50 for this effect is 3-15 ng/mL. |
Source |
E. coli-derived mouse CCL21/6Ckine protein Ser24-Gly133 |
Accession # |
|
N-terminal Sequence |
Ser24 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Ccl21a |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
12 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
16-17 kDa, reducing conditions |
Publications |
Read Publications using 457-6C in the following applications:
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Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein. |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse CCL21/6Ckine Protein
Background
CCL21, also known as 6Ckine, TCA-4, SLC, Exodus-2, and A21, is a 12 kDa homeostatic chemokine that plays an important role in adaptive immune responses and inflammation (1). Unlike other CC chemokines, mouse CCL21 has a 36 amino acid (aa) C-terminal extension which mediates its attachment to carbohydrate structures and extracellular matrix components (2, 3). Mature mouse CCL21 shares 71% and 84% aa sequence identity with human and rat CCL21, respectively (4‑6). In mouse, three genes encode CCL21, with B and C forms being identical and the A form carrying serine at aa 65 instead of leucine. Both human and mouse CCL21 signal through the chemokine receptor CCR7, while mouse CCL21 additionally can signal through CXCR3 (7). CCL21 is constitutively presented on initial lymphatic vessels, high endothelial venules (HEV), and lymph node dendritic cells (DC) (8‑10). Immobilized CCL21 promotes the docking of DC to lymphatic vessels and the retention of T cells by lymph node DC, resulting in T cell priming for activation (8, 9). DC interaction with the anchored chemokine can induce CCL21 cleavage and release of an 8 kDa fragment that lacks the C‑terminal extension (10). During chronic inflammation or tissue damage, CCL21 is up‑regulated on local vascular endothelial cells, macrophages, T cells, and neurons (11‑14). In these settings, it promotes fibrosis, inflammatory cytokine production, and neuropathic pain (12‑14). The soluble chemokine is elevated in rheumatoid arthritis synovial fluid and in the serum of coronary artery disease patients (11, 13). CCL21 has been shown to exert either angiogenic or angiostatic effects (11, 15, 16). These effects, in combination with the ability of CCL21 to attract immune suppressor cells (Treg and MDSC) to a tumor site can have positive or negative effects on tumor progression (16, 17).
- Forster, R. et al. (2008) Nat. Rev. Immunol. 8:362.
- Yang, B.G. et al. (2007) J. Immunol. 179:4376.
- Rey-Gallardo, A. et al. (2010) Glycobiology 20:1139.
- Tanabe, S. et al. (1997) J. Immunol. 159:5671.
- Hromas, R. et al. (1997) J. Immunol. 159:2554.
- Hedrick, J.A. and A. Zlotnik (1997) J. Immunol. 159:1589.
- Jenh, C. et al. (1999) J. Immunol. 162:3765.
- Tal, O. et al. (2011) J. Exp. Med. 208:2141.
- Friedman, R.S. et al. (2006) Nat. Immunol. 7:1101.
- Schumann, K. et al. (2010) Immunity 32:703.
- Pickens, S.R. et al. (2012) Arthritis Rheum. 64:2471.
- Sakai, N. et al. (2006) Proc. Natl. Acad. Sci. USA 103:14098.
- Damas, J.K. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:614.
- Biber, K. et al. (2011) EMBO J. 30:1864.
- Soto, H. et al. (1998) Proc. Natl. Acad. Sci. USA 95:8205.
- Vicari, A.P. et al. (2000) J. Immunol. 165:1992.
- Shields, J.D. et al. (2010) Science 328:749.
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