Chemerin-9 (149–157) – Catalog #B2026704

Chemerin-9 (Catalog #B2026704) is supplied as 1 mg of a lyophilized peptide fragment derived from full-length chemerin. The peptide corresponds to amino acids 149–157 of chemerin and is a potent, well-characterized agonist of the ChemR23 receptor (also known as CMKLR1, chemokine-like receptor 1). Chemerin-9 retains the full biological activity of the parent protein toward ChemR23 and is widely used in research on immune cell recruitment, inflammation resolution, and G protein-coupled receptor signaling.

Scientific Overview

Chemerin is a 143–amino-acid protein belonging to the C19 family of serine protease substrate proteins. It circulates as an inactive prochemerin and is activated in vivo and in vitro by serine proteases (including coagulation proteases, complement proteases, and leukocyte-derived proteases) that cleave the C-terminal region. Full-length chemerin and its proteolytic fragments bind to the G protein-coupled receptor ChemR23 (CMKLR1), which is expressed on immature dendritic cells, tissue macrophages, and non-classical (intermediate and patrolling) monocytes. The chemerin–ChemR23 axis plays a key role in immune homeostasis, promoting the recruitment and anti-inflammatory polarization of immune cells during inflammation resolution.

Chemerin-9, the 149–157 fragment, is the core bioactive domain of full-length chemerin. It is a potent agonist of ChemR23 and is substantially more stable than full-length chemerin, which is prone to further proteolytic processing in cellular assays. Because of its compact size, low molecular weight, and superior in vitro stability, Chemerin-9 has become the standard tool for studying ChemR23-mediated immune responses in cell culture and in vivo models.

Key applications include:

• Induction of immune cell chemotaxis toward ChemR23-expressing dendritic cells and macrophages
• Enhancement of phagocytosis in macrophages and dendritic cells via ChemR23 signaling
• Mechanistic studies of inflammation resolution pathways
• ChemR23 receptor antagonist screening and agonist characterization
• G protein-coupled receptor (GPCR) and G protein research

Usage & Handling Guidance

Dissolve the lyophilized peptide in sterile, ultrapure water or your assay buffer (phosphate-buffered saline, RPMI, or DMEM are all suitable). The peptide will readily dissolve; vortex or gently heat to speed dissolution if needed. Prepare a stock solution (typically 10 µM to 100 µM in PBS or assay medium), then aliquot and store frozen at –20°C or below to maintain stability. For cell culture assays, use stock solutions directly or dilute further into assay medium. For dose–response studies, titrate the peptide concentration from 0.1 nM to 1 µM depending on the assay and cell type.

• Stock solution preparation: Dissolve in ultrapure water or PBS to a known concentration (e.g., 100 µM). Store aliquots at –20°C.
• Cell culture concentration: Typical working concentrations range from 1–100 nM in cell-based assays. Optimize for your specific cell type and assay endpoint (e.g., chemotaxis, phagocytosis, cytokine production).
• Stability: The lyophilized powder is stable for at least 1–2 years when stored at –20°C. Reconstituted solutions are stable for several days at 2–8°C and for weeks at –20°C when stored with 0.02% sodium azide as a preservative.
• Sterile handling: For cell culture work, use aseptic technique and filter sterilize stock solutions (0.22 µm) if contamination is a concern.

What You Get

• 1 mg of lyophilized Chemerin-9 (149–157) peptide
• High purity, suitable for cell culture and biochemical assays
• A potent, well-characterized ChemR23 agonist for immune cell research
• For research use only (RUO)

Why Researchers Choose It

• Potent ChemR23 receptor agonist with full biological activity
• More stable than full-length chemerin in cell culture
• Compact, synthetic peptide suitable for standardized experiments
• Well-characterized in the immunology and GPCR literature
• Ideal for dose–response and mechanistic studies of immune signaling

Frequently Asked Questions (FAQ)

• What cells express ChemR23?
  ChemR23 is expressed on immature dendritic cells, tissue-resident macrophages, and non-classical (intermediate and patrolling) monocytes. Expression can also be induced on other cell types under certain inflammatory conditions. Use flow cytometry to confirm expression in your cell type of interest.
• How does Chemerin-9 compare to full-length chemerin?
  Chemerin-9 is the core bioactive domain of full-length chemerin and is a potent ChemR23 agonist. Unlike full-length chemerin, which can be further cleaved by proteases in cell culture medium, Chemerin-9 is resistant to proteolytic degradation, making it ideal for standardized cell assays.
• What assays can I use Chemerin-9 in?
  Chemerin-9 is well-suited for migration assays (Boyden chamber, real-time impedance), phagocytosis assays, cytokine production assays (ELISA, Luminex), flow cytometry-based activation marker detection, and binding assays on ChemR23-expressing cells or receptor-transfected cell lines.
• What is a typical working concentration?
  Most cell-based assays use Chemerin-9 in the range of 1–100 nM. Optimal concentration depends on your cell type, assay format, and endpoint. Start with 10 nM and titrate up or down as needed.
• Can I use Chemerin-9 in vivo?
  Yes, but because Chemerin-9 is a synthetic peptide, its pharmacokinetics in vivo may differ from full-length chemerin. Proteolytic stability in blood and tissue may also vary. For in vivo work, consult the literature for your specific organism and consider peptide-stabilizing modifications (e.g., PEGylation, D-amino acids).
• How should I store the reconstituted peptide?
  Store at –20°C or below. To preserve sterility, add 0.02% sodium azide. Once reconstituted, the peptide is stable for at least 1–2 weeks at 2–8°C and several months at –20°C.
• Can I get a COA or TDS?
  Yes. Request a quote or contact us and we will provide available lot documentation and information on peptide purity, mass spectrometry confirmation, and batch-specific storage guidance.

References

• Cash JL, Christian AR, Greaves DR. Chemerin peptides promote phagocytosis in a ChemR23- and Syk-dependent manner. J Immunol. 2010;184(9):5315-24.
• Luangsay S, Wittamer V, Bondue B, De Henau O, Rouger L, Brait M, Franssen JD, de Nadai P, Huaux F, Parmentier M. Mouse ChemR23 is expressed in dendritic cell subsets and macrophages, and mediates an anti-inflammatory activity of chemerin in a lung disease model. J Immunol. 2009;183(10):6489-99.
• Zhang X, Weiß T, Cheng MH, Chen S, Ambrosius CK, Czerniak AS, Li K, Feng M, Bahar I, Beck-Sickinger AG, Zhang C. Structural basis of G protein-Coupled receptor CMKLR1 activation and signaling induced by a chemerin-derived agonist. PLoS Biol. 2023;21(12):e3002188.
• Shimamura K, Matsuda M, Miyamoto Y, Yoshimoto R, Seo T, Tokita S. Identification of a stable chemerin analog with potent activity toward ChemR23. Peptides. 2009;30(8):1529-38.