Recombinant Human SLURP2 Fc Chimera Protein, CF

When Recombinant HumanNicotinic Acetylcholine R alpha 7/CHRNA7 (Novus Catalog # H00001139) is immobilized at 1 µg/mL (100 µL/well), RecombinantHuman SLURP2 Fc Chimera (Catalog # 10035-SP) binds with an ED50 of 1‑6 μg/mL.

2 μg/lane of Recombinant Human SLURP2 Fc Chimera was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 36-43 kDa and 70-85 kDa, respectively.

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

Recombinant Human SLURP2 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Nicotinic Acetylcholine R alpha 7/CHRNA7 (Novus Catalog # H00001139) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human SLURP2 Fc Chimera binds with an ED₅₀ of 1-6 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human SLURP2 protein
  

  MD	Human IgG1 (Pro100-Lys330)	IEGR	Human SLURP2 (Ile23-Asp97) Accession # P0DP57
  N-terminus			C-terminus

• Accession #: P0DP57
• N-terminal Sequence: Met
• 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:
  • Bioactivity2
• Theoretical MW: 35 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: 36-43 kDa, 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 °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 SLURP2 Fc Chimera Protein, CF

• secreted LY6/PLAUR domain-containing protein 2
• secreted Ly-6/uPAR domain-containing protein 2
• secreted Ly6/uPAR related protein 2
• secreted Ly-6/uPAR-related protein 2
• SLURP2
• SLURP-2

Background

Secreted Ly-6/uPAR domain-containing protein 2 (SLURP2) is expressed primarily in epithelial and immune cells and regulates growth and differentiation of epithelial cells (1, 2). It is part of the Ly6/neurotoxin superfamily and contains the ‘three-finger' UPAR/Ly6 domain, which has a beta -structural core and three protruding loops (2, 3). Mature SLURP2 is a secreted protein which is comprised of 75 amino acids. Human SLURP2 shares 65% and 25% aa identity with mouse and rat SLURP2, respectively. SLURP2 is demonstrated to lessen the tumorigenic activity of nitrosamines on Het-1A cells (4), reduce inflammation on human intestinal epithelial cells and Immunocytes such as CEM and U937 (5). SLURP2 can interact with alpha 3, alpha 4, alpha 5, alpha 7, beta 2, beta 4, and possibly alpha 6 nicotinic acetylcholine receptors (nAChRs) as well as M1 and M3 muscarinic acetylcholine receptors (3, 6). In addition, SLURP2 controls the proliferation of keratinocytes and epithelial cancer cells via nAChRs on the cell surface (1, 6, 7). It has been suggested SLURP2 may be involved in the pathophysiology of psoriasis through its role in keratinocyte hyper-proliferation and/or T cell differentiation/activation (8).

1. Arredondo, J. et al. (2006) J. Cell. Physiol. 208:238.
2. Moriwaki, Y. et al. (2015) Int. Immunopharmacol. 29:71.
3. Lyukmanova, E.N. et al. (2016) Sci. Rep. 6:30698.
4. Arredondo, J. et al. (2007) Life. Sci. 80:2243.
5. Chernyavsky, AI. et al. (2014) Biomed. Res. Int. 2014:609086.
6. Lyukmanova, E.N. et al. (2014) Acta. Naturae. 6:60.
7. Lyukmanova, E.N. et al. (2018) Br. J. Pharmacol. 175:1973.
8. Tsuji, H. et al. (2003) Genomics 81:26.

Bioinformatics

• Uniprot:
  • P0DP57()