Human Osteopontin (OPN) Protein, His Tag
Proteins and Peptides
- 貨號 Cat. No.
- OPN-H5227
- 規格 Size
- 100ug
- 品牌 Brand
- ACROBiosystems
- Species
- Human
- Conjugate
- Unconjugated
- Expression System
- HEK293
- Tag
- His Tag
Description
Source :
Human Osteopontin, His Tag (OPN-H5227) is expressed from human 293 cells (HEK293). It contains AA Ile 17 - Asn 300 (Accession # AAH07016).
Molecule : Osteopontin
Synonyms : SPP1,BNSP,OPN,Uropontin,Nephropontin,Osteopontin,BSP-1,ETA-1,BSPI
Format : Powder
Category : Other Recombinant Proteins
Accession : AAH07016
Storage : -20℃
Shipping condition : Powder,RT
Molecular Weight : 33.0 kDa
Characteristics :
This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 33.0 kDa. The protein migrates as 45-55 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Endotoxin Level : Less than 1.0 EU per μg by the LAL method.
Buffer : PBS, pH7.4
Description :
Osteopontin (OPN) is also known as Secreted phosphoprotein 1 (SPP1), Bone sialoprotein 1, Nephropontin, Urinary stone protein, Uropontin, BNSP, which belongs to the osteopontin family. OPN / SPP1 is a highly negatively charged, extracellular matrix protein that lacks an extensive secondary structure. Full length OPN (OPN-FL) can be modified by thrombin cleavage, which exposes a cryptic sequence, SVVYGLR on the cleaved form of the protein known as OPN-R. Osteopontin / SPP-1 is biosynthesized by a variety of tissue types. OPN is the ligand for integrin alpha-V/beta-3. OPN / SPP1 binds tightly to hydroxyapatite and appears to form an integral part of the mineralized matrix. OPN / SPP1 probably important to cell-matrix interaction. OPN / SPP1 acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity.
References :
(1) Wang KX., et al., 2008, Cytokine Growth Factor Rev. 19 (5-6): 333–45.
(2) Laffón A., et al., 1991, J. Clin. Invest. 88 (2): 546–52.
(3) Christensen B., et al., 2005, Biochem. J. 390:285-292.

