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Recombinant Human IBSP/Sialoprotein II Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Bioactivity

Order Details

Recombinant Human IBSP/Sialoprotein II Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of the MCF‑7 human breast cancer cells. When 5 x10 4 cells/well are added to recombinant human IBSP-coated plates (3 µg/mL with 100 µL/well), approximately 60‑80% will adhere after 30 minutes at 37° C.
Optimal concentration depends on cell type as well as the application or research objectives.
Chinese Hamster Ovary cell line, CHO-derived human IBSP/Sialoprotein II protein
Phe17-Gln317, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
Theoretical MW
34.7 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.
75-90 kDa, reducing conditions
Read Publications using
4014-SP in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in MES and NaCl.
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.


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

Alternate Names for Recombinant Human IBSP/Sialoprotein II Protein, CF

  • BNSP
  • Bone sialoprotein 2
  • Bone sialoprotein
  • BSP 2
  • BSP II
  • BSP
  • BSP2
  • BSP-II
  • Cell binding sialoprotein
  • IBSP
  • Integrin binding sialoprotein
  • SP II
  • SPII
  • SP-II


IBSP (integrin-binding sialoprotein; also BSP or bone sialoprotein (II)) is a 55 - 75 kDa, secreted, variably glycosylated, monomeric noncollagenous member of the SIBLING family of extracellular matrix (ECM) proteins (1 - 3). It is principally associated with the early stages of bone mineralization. BSP is synthesized as a 317 amino acid (aa) precursor that contains a 16 aa signal sequence and a 301 aa mature region (4 - 6). The mature segment is divided into a basic N-terminus (aa 17 - 62), a central region (aa 63 - 233), and an acidic C-terminus (aa 234 - 317) (7).

Functional segments associated with the mature molecule include a type I collagen binding domain (aa 19 - 46), two non-RGD cell binding sites (aa 30 - 57 and 261 - 281), an RGD alpha v beta 3 integrin-binding site (aa 286 - 288) and two potential hydroxyapatite (HAp) nucleation domains (aa 76 - 83 and 151 - 158) (3, 4, 8 - 11). HAp formation requires a BSP nucleation site composed of at least eight consecutive glutamic acid residues and, likely, a contribution from a BSP-associated co-nucleator (10, 12). BSP is highly glycosylated, sulfated, and phosphorylated. Phosphorylation may impact HAp growth, while carbohydrate may regulate cell adhesion (1, 3, 13). Mature human BSP is 70%, 72%, 78%, and 72% aa identical to porcine, rat, canine, and mouse BSP, respectively. BSP is synthesized by megakaryocytes/platelets, osteoblasts, osteocytes, odontoblasts, osteoclasts, and bone marrow stromal cells (14 - 17).

  1. Qin, C. et al. (2004) Crit. Rev. Oral Biol. Med. 15:126.
  2. Alford, A.I. and K.D. Hankenson (2006) Bone 38:749.
  3. Ganss, B. et al. (1999) Crit. Rev. Oral Biol. Med. 10:79.
  4. Fisher, L.W. et al. (1990) J. Biol. Chem. 265:2347.
  5. Kerr, J.M. et al. (1993) Genomics 17:408.
  6. Kim, R.H. et al. (1994) Matrix Biol. 14:31.
  7. Zaia, J. et al. (2001) Biochemistry 40:12983.
  8. Tye, C.E. et al. (2005) J. Biol. Chem. 280:13487.
  9. Stubbs, J.T. et al. (1997) J. Bone Miner. Res. 12:1210.
  10. Tye, C.E. et al. (2003) J. Biol. Chem. 278:7949.
  11. Miyauchi, A. et al. (1991) J. Biol. Chem. 266:20369.
  12. Hakki, S.S. et al. (2006) J. Periodontol. 77:167.
  13. Wazen, R.M. et al. (2007) J. Histochem. Cytochem. 55:35.
  14. Kacena, M.A. et al. (2006) Bone 39:978.
  15. Bianco, P. et al. (1991) Calcif. Tissue Int. 49:421.
  16. Chen, J. et al. (1992) J. Bone Miner. Res. 7:987.
  17. Kreke, M.R. et al. (2005) Bone 36:1047.

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Gene Symbol IBSP