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Recombinant Human IBSP/Sialoprotein II Protein, CF

Catalog #: 4014-SP
5 Citations Datasheet / COA / SDS
Catalog # Availability Size / Price Qty
4014-SP-050
Recombinant Human IBSP/Sialoprotein II Protein Bioactivity.
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Citations (5)
FAQs
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human IBSP/Sialoprotein II Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<1.0 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. 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
Accession #
AAC95490
N-terminal Sequence
Analysis
Phe17
Predicted Molecular Mass
34.7 kDa
SDS-PAGE
75-90 kDa, reducing conditions

Product Datasheets

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4014-SP

Product Datasheet
COA
SDS

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.

4014-SP

Formulation Lyophilized from a 0.2 μm filtered solution in MES and NaCl.
Reconstitution Reconstitute at 100 μg/mL in sterile 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.

Scientific Data

Bioactivity View Larger

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.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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 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).

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. 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.
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

Citations for Recombinant Human IBSP/Sialoprotein II Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

5 Citations: Showing 1 - 5
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  1. Identification of anti-citrullinated osteopontin antibodies and increased inflammatory response by enhancement of osteopontin binding to fibroblast-like synoviocytes in rheumatoid arthritis
    Authors: A Umemoto, T Kuwada, K Murata, M Shiokawa, S Ota, Y Murotani, A Itamoto, K Nishitani, H Yoshitomi, T Fujii, A Onishi, H Onizawa, K Murakami, M Tanaka, H Ito, H Seno, A Morinobu, S Matsuda
    Arthritis Research & Therapy, 2023-02-17;25(1):25.
    Species: Human, N/A
    Sample Types: Antibody, Protein
    Applications: Bioassay, ELISA Capture
  2. A molecular interactome of the glioblastoma perivascular niche reveals integrin binding sialoprotein as a mediator of tumor cell migration
    Authors: Y Ghochani, SD Muthukrish, A Sohrabi, R Kawaguchi, MC Condro, S Bastola, F Gao, Y Qin, J Mottahedeh, ML Iruela-Ari, N Rao, DR Laks, LM Liau, GW Mathern, SA Goldman, ST Carmichael, I Nakano, G Coppola, SK Seidlits, HI Kornblum
    Cell Reports, 2022-10-18;41(3):111511.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Micropatterning biomineralization with immobilized mother of pearl proteins
    Authors: KA White, VJ Cali, RM Olabisi
    Scientific Reports, 2021-01-25;11(1):2141.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  4. Proteolytic processing of osteopontin by PHEX and accumulation of osteopontin fragments in Hyp mouse bone, the murine model of X-linked hypophosphatemia.
    Authors: Barros N, Hoac B, Neves R, Addison W, Assis D, Murshed M, Carmona A, McKee M
    J Bone Miner Res, 2013-03-01;28(3):688-99.
    Applications: Bioassay
  5. Effect of Lamin A/C Knockdown on Osteoblast Differentiation and Function.
    Authors: Akter R, Rivas D, Geneau G, Drissi H, Duque G
    J. Bone Miner. Res., 2009-02-01;0(0):.
    Applications: Western Blot

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