Recombinant Human TREM-1 Fc Chimera Avi-tag Protein, CF

Measured by its binding ability in a functional ELISA. When Recombinant Human PGLYRP1/PGRP-S Protein (2590-PGB) is immobilized at 1 μg/mL (100 μL well), Biotinylated Recombinant Human TREM‑1 Fc Chimera Avi-tag Protein (Catalog # AVI1278) binds with an ED50 of 15.0‑150 ng/mL.

2 μg/lane of Biotinylated Recombinant Human TREM‑1 Fc Chimera Avi-tag Protein (Catalog # AVI1278) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 60-78 kDa and 110-150 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human TREM-1 Fc Chimera Avi-tag Protein, CF Summary

• Additional Information: Biotinylated
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human PGLYRP1/PGRP-S Protein (Catalog # 2590-PGB) is immobilized at 1 μg/mL (100 μL well), Biotinylated Recombinant Human TREM‑1 Fc Chimera Avi-tag (Catalog # AVI1278) binds with an ED₅₀ of 15.0-150 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human TREM-1 protein
  

  Human TREM-1 (Ala21-Arg200) Accession # Q9NP99.1	IEGRMD	Human IgG1 (Pro100-Lys330)	Avi-tag
  N-terminus			C-terminus

• Accession #: Q9NP99.1
• N-terminal Sequence: Ala21
• Structure / Form: Disulfide-linked homodimer
  Biotinylated via Avi-tag
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 49 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: 60-78 kDa, under reducing conditions.

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 PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 250 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human TREM-1 Fc Chimera Avi-tag Protein, CF

• CD354 antigen
• CD354
• TREM1
• TREM-1
• TREM-1Triggering receptor expressed on monocytes 1
• triggering receptor expressed on myeloid cells 1
• triggering-receptor TREM1

Background

TREM-1 (Triggering Receptor Expressed on Myeloid cells) is a type I transmembrane protein having a single Ig-like domain. It associates with the adapter protein, DAP12, to deliver an activating signal. Several other TREM family members have been reported that are structurally similar but share less than 30% amino acid identity. TREM-1 is expressed on blood neutrophils and a subset of monocytes, and expression is up-regulated by bacterial LPS. The natural ligand for TREM-1 has not been identified. However, engagement of TREM-1 with an agonist monoclonal antibody leads to expression of IL-8, MCP-1 and TNF-alpha , suggesting that this receptor plays an important role in inflammatory responses. TREM-1 is expressed at high levels on neutrophils of patients with microbial sepsis and in mice with LPS‑induced shock. Blockade of TREM-1 with a TREM‑1/Fc fusion protein protected mice against LPS‑induced shock. Human and mouse TREM-1 share approximately 42% amino acid sequence homology (1 - 3). Our Avi-tag Biotinylated human TREM-1 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

1. Bouchon, A. (2000) J. Immunol. 164:4991.
2. Bouchon, A. (2001) Nature 410:1103.
3. Nathan, C. and A. Ding (2001) Nature Med. 7:530.

Bioinformatics

• Uniprot:
  • Q9NP99.1()