Recombinant Mouse CD52 Fc Chimera Protein, CF

When Recombinant Human Siglec-10 Fc Chimera (2130-SL) is immobilized at 2.5 μg/mL (100 μL/well), the concentration of Recombinant Mouse CD52 Fc Chimera (Catalog # 10712-CD) that produces 50% of the optimal binding response is found to be approximately 1.5-7.5 μg/mL.

2 μg/lane of Recombinant Mouse CD52 Fc Chimera (Catalog # 10712-CD) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 32-42 kDa and 64-84 kDa, respectively.

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

Recombinant Mouse CD52 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Siglec-10 Fc Chimera Protein (Catalog # 2130-SL) is immobilized at 2.5 μg/mL (100 µL/well), the concentration of Recombinant Mouse CD52 Fc Chimera (Catalog # 10712-CD) that produces 50% of the optimal binding response is found to be approximately 1.5-7.5 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse CD52 protein

  Mouse CD52 (Thr27-Ser47) Accession # Q64389.1

  IEGRMDP

  Mouse IgG 2a (Glu98-Lys330)

  N-terminus

  C-terminus

• Accession #: Q64389.1
• N-terminal Sequence: Thr27
• 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: 29 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: 32-36 kDa & 38-42 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 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• 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 Mouse CD52 Fc Chimera Protein, CF

• Cambridge pathology 1 antigen
• CAMPATH-1 antigen
• CAMPATH-1
• CD52 antigen (CAMPATH-1 antigen)
• CD52 antigen
• CD52 molecule
• CD52
• CDW52 antigen (CAMPATH-1 antigen)
• CDw52
• Epididymal secretory protein E5
• He5
• HEL-S-171mP
• Human epididymis-specific protein 5

Background

CD52, also known as CAMPATH-1 antigen, HE5, and gp20, is a cell surface glycoprotein that can be targeted to induce immune suppression by complement-mediated cell lysis (1, 2). Mature mouse CD52 is a short peptide that is tethered to the cell surface with a GPI linkage (1, 2). CD52 carries a large N-linked carbohydrate moiety which increases the molecular weight significantly (3-5). Mouse CD52 shares only 23% and 16% amino acid identity with rat and human CD52, respectively. CD52 is expressed on lymphocytes, monocytes, monocycte-derived dendritic cells, eosinophils, and neutrophils (6-8), as well as on mature spermatozoa and epithelial cells lining the male genital tract (5, 9, 10). It protects sperm against anti-sperm antibodies by binding to C1q and inhibiting complement activation (11). CD52 ligation on CD4+ T cells induces a suppressive population of cells that release soluble CD52 which then binds to Siglec-10 (12-14). This interaction inhibits the proliferation of activated T cells and the cytotoxic function of autoimmune CD8+ T cells in type 1 diabetes (13).

1. Morris, P.J. et al. (2006) Transplantation. 81:1361.
2. Hu, Y. et al. (2009) Immunol. 128:260.
3. Xia, M.Q. et al. (1991) Eur. J. Immunol. 21:1677.
4. Treumann, A. et al. (1995) J. Biol. Chem. 270:6088.
5. Schroter, S. et al. (1999) J. Biol. Chem. 274:29862.
6. Ratzinger, G. et al. (2003) Blood 101:1422.
7. Elsner, J. et al. (1996) Blood 88:4684.
8. Ambrose, L.R. et al. (2009) Blood 114:3052.
9. Focarelli, R. et al. (1998) Mol. Hum. Reprod. 4:119.
10. Koyama, K. et al. (2009) J. Reprod. Immunol. 83:56.
11. Hardiyanto, L. et al. (2012) J. Reprod. Immunol. 94:142.
12. Watanabe, T. et al. (2006) Clin. Immunol. 120:247.
13. Bandala-Sanchez, E. et al. (2013) Nat. Immunol. 14:741.
14. Toh, B.-H. et al. (2013) Cell. Mol. Immunol. 10:379.

Bioinformatics

• Uniprot:
  • Q64389.1()