Human COMP / TSP5 Protein, His Tag

Proteins and Peptides

貨號 Cat. No.
COP-H5220
規格 Size
100ug
品牌 Brand
ACROBiosystems
Species
Human
Conjugate
Unconjugated
Expression System
HEK293
Tag
His Tag

Description




Source : 


Human COMP, His Tag (COP-H5220) is expressed from human 293 cells (HEK293). It contains AA Gln 21 - Ala 757 (Accession # AAI25093).


 

Molecule : COMP


 

Synonyms : COMP,TSP5,EDM1,EPD1,MED,PSACH,THBS5


 

Format : Powder


 

Category : Bio-Markers & CD Antigens


 

Accession : AAI25093


 

Storage : -20℃


 

Shipping condition : Powder,RT


 

Molecular Weight : 81.9 kDa


 

Characteristics :


This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 81.9 kDa. The protein migrates as 110-130 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.


 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.


 

Buffer : 50 mM Tris, 150 mM NaCl, pH7.5


 

Description :


Cartilage oligomeric matrix protein (COMP) is also known as Thrombospondin-5 (TSP5), EDM1, EPD1, MED, PSACH, THBS5, which belongs to the thrombospondin family. COMP / TSP5 contains 4 EGF-like domains, 1 TSP C-terminal (TSPC) domain, 8 TSP type-3 repeats. Abundantly expressed in the chondrocyte extracellular matrix, and is also found in bone, tendon, ligament and synovium and blood vessels. COMP may play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. COMP can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Thrombospondin-5 could play a role in the pathogenesis of osteoarthritis. COMP is a marker of cartilage turnover.


 

References :


(1) Chen F.-H., et al., 2006, J. Biol. Chem. 280:32655-32661.
(2) Koelling S., et al., 2006, Arthritis Res. Ther. 8:R56-R56.
(3) Gagarina V., et al., 2008, J. Biol. Chem. 283:648-659.
(4) Petersen, G., et al., 2009, Osteoarthritis and Cartilage 18 (1): 34–40.





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