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.





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