Recombinant Human IBSP/Sialoprotein II Protein (Catalog # 4014-SP) supports the adhesion of MCF‑7 human breast cancer cells. The ED50 for this effect is 0.0600-0.600 µg/mL.
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. The ED50 of this effect is 0.0600 - 0.600 μg/mL
Source
Chinese Hamster Ovary cell line, CHO-derived human IBSP/Sialoprotein II protein Phe17-Gln317, with a C-terminal 10-His tag
>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.
Applications/Dilutions
Dilutions
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.
SDS-PAGE
75-90 kDa, reducing conditions
Publications
Read Publications using 4014-SP in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in MES and NaCl.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
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
BSPII
BSP-II
Cell binding sialoprotein
IBSP
Integrin binding sialoprotein
SP II
SPII
SP-II
Background
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).
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Tye, C.E. et al. (2005) J. Biol. Chem. 280:13487.
Stubbs, J.T. et al. (1997) J. Bone Miner. Res. 12:1210.
Tye, C.E. et al. (2003) J. Biol. Chem. 278:7949.
Miyauchi, A. et al. (1991) J. Biol. Chem. 266:20369.
Hakki, S.S. et al. (2006) J. Periodontol. 77:167.
Wazen, R.M. et al. (2007) J. Histochem. Cytochem. 55:35.
Kacena, M.A. et al. (2006) Bone 39:978.
Bianco, P. et al. (1991) Calcif. Tissue Int. 49:421.
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