Recombinant Mouse IBSP/Sialoprotein II Protein, CF
Recombinant Mouse IBSP/Sialoprotein II Protein, CF Summary
Product Specifications
Optimal concentration depends on cell type as well as the application or research objectives.
Met1-Gln324, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
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Reconstitution Calculator
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).
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- Alford, A.I. and K.D. Hankenson (2006) Bone 38:749.
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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.
- Wazen, R.M. et al. (2007) J. Histochem. Cytochem. 55:35.
- Hakki, S.S. et al. (2006) J. Periodontol. 77:167.
- Baht, G.S. et al. (2010) Biochem. J. 428:385.
- Gordon, J.A.R. et al. (2009) J. Cell. Biochem. 107:1118.
- 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.
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