Recombinant Human CXCL17/VCC-1 Protein


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Recombinant Human CXCL17/VCC-1 Protein Summary

Details of Functionality
Measured by its ability to induce VEGF expression in mouse endothelial cells. Weinstein, E.J. et al. (2006) BBRC 350:74. The ED50 for this effect is 1-5 µg/mL.
E. coli-derived human CXCL17/VCC-1 protein
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


Theoretical MW
11.3 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.
Read Publications using
4207-DM in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human CXCL17/VCC-1 Protein

  • Chemokine (C-X-C Motif) Ligand 17
  • C-X-C Motif Chemokine 17
  • CXCL17
  • Dcip1
  • Dendritic Cell And Monocyte Chemokine-Like Protein
  • DMC
  • UNQ473
  • VCC1
  • VCC-1
  • VEGF Coregulated Chemokine 1
  • VEGF Co-Regulated Chemokine 1


Dendritic cell and monocyte chemokine-like protein (DMC), also known as VEGF-correlated chemokine-1 (VCC-1) and CXCL17, is a novel secreted molecule that belongs to the intercrine alpha (or CXC) family of chemokines (1, 2). It has no predicted N‑glycosylation sites, so cleavage of a 22 amino acid (aa) signal sequence likely results in a mature human DMC of 97 aa and 11 kDa. DMC is constitutively produced by bronchiolar, mammary, and intestinal epithelium, vascular endothelial cells, and multiple tumor types (1, 2, 3). It induces the chemotaxis of quiescent, but not LPS-activated, peripheral blood monocytes and dendritic cells, and also is noted to specifically bind to these cells (1). DMC expression is increased in endothelial cells when they are induced to form tubes in vitro (2). Transgenic overexpression in NIH3T3 cells causes up‑regulation of proteins such as VEGF and FGF basic, and increases cell growth rate and tumorigenicity (2). DMC and two other chemokines that play roles in angiogenesis, CXCL1/GRO and CXCL8/IL-8, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors (2). DMC is therefore suggested to play a role in tumor angiogenesis. Mature human DMC shares 73%, 71% and 64% amino acid sequence identity with bovine, mouse and rat DMC, respectively.
  1. Pisabarro, M. T. et al. (2006) J. Immunol. 176:2069.
  2. Weinstein, E. J. et al. (2006) Biochem. Biophys. Res. Commun. 350:74.
  3. Mu, X. et al. (2009) Acta Biochim. Biophys. Sin 41:632.

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Gene Symbol CXCL17