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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for IBSP/Sialoprotein II Antibody
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).
Qin, C. et al. (2004) Crit. Rev. Oral Biol. Med. 15:126.
Alford, A.I. and K.D. Hankenson (2006) Bone 38:749.
Ganss, B. et al. (1999) Crit. Rev. Oral Biol. Med. 10:79.
Fisher, L.W. et al. (1990) J. Biol. Chem. 265:2347.
Kerr, J.M. et al. (1993) Genomics 17:408.
Kim, R.H. et al. (1994) Matrix Biol. 14:31.
Zaia, J. et al. (2001) Biochemistry 40:12983.
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.
Chen, J. et al. (1992) J. Bone Miner. Res. 7:987.
Kreke, M.R. et al. (2005) Bone 36:1047.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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