Recombinant Human TMED1 Fc Chimera Protein, CF

When Recombinant TMED1 Fc Chimera (Catalog # 2243-TM)is coated at 0.5 μg/mL, Recombinant Human ST2/IL‑1 R4 Fc Chimera (Catalog # 523-ST) binds with an ED50 of 0.6‑3.6 μg/mL.

2 μg/lane of Recombinant Human TMED1 Fc was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 56-62 kDa and 110-120 kDa, respectively.

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

Recombinant Human TMED1 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human TMED1 Fc Chimera is coated at 0.5 µg/mL, 100 μL/well, Recombinant Human ST2/IL‑1 R4 Fc Chimera (Catalog # 523-ST) binds with an ED₅₀ of 0.6-3.6 μg/mL
• Source: Human embryonic kidney cell, HEK293-derived human TMED1 protein
  

  Human TMED1 (Ala24-Asn194) Accession # Q13445	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q13445
• N-terminal Sequence: Ala24
• Structure / Form: Disulfide-linked homodimer
• 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: 46 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: 56-62 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °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 500 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 TMED1 Fc Chimera Protein, CF

• IL1RL1-Binding Protein
• Il1rl1l
• IL1RL1LG
• IL-1RL1LG
• IL1RL1LGIL1RL1-binding protein
• Interleukin 1 Receptor-Like 1 Ligand
• Interleukin-1 receptor-like 1 ligand
• Ly84l
• MGC1270
• P24g1
• P24gamma1
• Putative T1/ST2 receptor-binding protein
• ST2L
• T1/ST2 receptor binding protein
• TMED1
• Tp24
• transmembrane emp24 domain containing 1
• transmembrane emp24 domain-containing protein 1
• transmembrane emp24 protein transport domain containing 1

Background

TMED1 (Transmembrane Emp24 domain-containing protein 1) is a member of the TMED family of proteins (gene name TMED1). The TMED family of proteins are localized to membranes of the early secretory pathway, including the endoplasmic reticulum and Golgi, and function in vesicular protein trafficking (1, 2). TMED1 is a 59 kDa monomer and has been reported to exist as homodimer (3). TMED1 is composed of a 23 amino acid (aa) signal sequence, a 171 aa extra cellular domain, a 21 aa transmembrane domain, and a 12 aa cytoplasmic domain. The extracellular domain contains an 83 aa GOLD (Golgi Dynamics) domain, and COPI and COPII binding motifs are found in the cytoplasmic domain (1-3, 5). Human TMED1 shares 97% sequence identity with mouse, bovine, and rat homologs within the 171 aa extracellular domain. The beta -strand-rich GOLD domain has been specifically identified to be involved in intracellular protein trafficking (1, 4, 5). TMED1 is important in regulating innate immune signaling through its interaction with ST2L. Specifically, the GOLD domain in TMED1 interacts with the TIR domain of ST2L, a receptor for IL‑33 (1). This interaction promotes ST2L association with IL-33, allowing downstream signaling cascade activating MAP kinases, p38, and JNK (1, 6). Studies have shown knockdown of TMED-1 in HUVECs impairs the IL-33 induced response resulting in reduction of IL-6 and IL-8 productions (1).

1. Connolly, D. et al. (2013) J Biol Chem. 288:5616.
2. Gour, N. and Lajoie, S. (2018) Curr Allergy Ashma Rep. 16:65.
3. Jenne, N. (2002) J Biol Chem. 277:46504.
4. Anantharaman, V. and Aravind, L. (2002) Genome Biol. 3:research0023
5. Gomez-Navarro, N. and Miller, E. (2016) J Cell Biol. 215:769.
6. Hardman, C. and Ogg, G. (2016). Curr Opin Immunol. 42:16.

Bioinformatics

• Uniprot:
  • Q13445()