Recombinant Mouse IBSP/Sialoprotein II Protein, CF

Catalog # Availability Size / Price Qty
6225-SP-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Mouse IBSP/Sialoprotein II Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by the ability of the immobilized protein to support the adhesion of the MCF‑7 human breast cancer cells. When 5 x 104 cells/well are added to recombinant mouse 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.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse IBSP/Sialoprotein II protein
Met1-Gln324, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Phe17
Predicted Molecular Mass
34.9 kDa
SDS-PAGE
70-90 kDa, reducing conditions

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6225-SP

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

6225-SP

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 200 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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Background: IBSP/Sialoprotein II

IBSP (integrin‑binding sialoprotein; also BSP or bone sialoprotein II) is a 55 ‑ 75 kDa, secreted, variably glycosylated, monomeric non‑collagenous member of the SIBLING family of extracellular matrix (ECM) proteins (1 ‑ 3). It is principally associated with the early stages of bone mineralization. Mouse BSP is synthesized as a 324 amino acid (aa) precursor that contains a 16 aa signal sequence and a 308 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 regions that are potential hydroxyapatite (HAp) nucleation domains (aa 76 ‑ 83 and 151 ‑ 158) (3, 4, 8 ‑ 12). HAp formation requires a BSP nucleation site composed of at least eight consecutive glutamic acid residues and, likely, a contribution from a BSP‑associated conucleator (10, 13). BSP is highly glycosylated, sulfated and phosphorylated. Phosphorylation promotes HAp nucleation, while carbohydrate may regulate cell adhesion (1, 3, 14). Interaction with integrins stimulates cell migration and survival, and has been implicated in bone metastasis of cancers, especially those of breast and prostate (15). Mature mouse BSP shares 90% aa identity with rat, 70% with human, 67% with canine, equine and porcine, and 64% with bovine BSP, respectively. BSP is synthesized by megakaryocytes/platelets, osteoblasts, osteocytes, odontoblasts, osteoclasts and bone marrow stromal cells (16 ‑ 19).

References
  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. Wazen, R.M. et al. (2007) J. Histochem. Cytochem. 55:35.
  13. Hakki, S.S. et al. (2006) J. Periodontol. 77:167.
  14. Baht, G.S. et al. (2010) Biochem. J. 428:385.
  15. Gordon, J.A.R. et al. (2009) J. Cell. Biochem. 107:1118.
  16. Kacena, M.A. et al. (2006) Bone 39:978.
  17. Bianco, P. et al. (1991) Calcif. Tissue Int. 49:421.
  18. Chen, J. et al. (1992) J. Bone Miner. Res. 7:987.
  19. Kreke, M.R. et al. (2005) Bone 36:1047.
Long Name
Integrin-binding Sialoprotein
Entrez Gene IDs
3381 (Human); 15891 (Mouse); 24477 (Rat)
Alternate Names
BNSP; Bone sialoprotein 2; Bone sialoprotein; BSP 2; BSP II; BSP; BSP2; BSPII; BSP-II; Cell binding sialoprotein; IBSP; Integrin binding sialoprotein; SP II; SPII; SP-II

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