Human Fetuin A / FETUA Protein, His Tag
Proteins and Peptides
- 貨號 Cat. No.
- FEA-H5221
- 規格 Size
- 100ug
- 品牌 Brand
- ACROBiosystems
- Species
- Human
- Conjugate
- Unconjugated
- Expression System
- HEK293
- Tag
- His Tag
Description
Source :
Human Fetuin A, His Tag (FEA-H5221) is expressed from human 293 cells (HEK293). It contains AA Ala 19 - Val 367 (Accession # P02765-1).
Molecule : Fetuin A
Synonyms : AHSG,FETUA,Fetuin A
Format : Powder
Category : Other Recombinant Proteins
Accession : NP_001613.2
Storage : -20℃
Shipping condition : Powder,RT
Molecular Weight : 38.2 kDa
Characteristics :
This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 38.2 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 :
Alpha-2-HS-glycoprotein (AHSG) is also known as Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, Fetuin-A (FETUA), is a glycoprotein that is composed of two subunits, the A and B chains, belongs to the cystatin family of proteases inhibitors and the fetuin class of plasma binding proteins. AHSG / Fetuin A is highly expressed in embryonic cells and adult hepatocytes, and is expressed to a lesser extent in monocytes/macrophages. Fetuins are carrier proteins like albumin. Fetuin-A / AHSG forms soluble complexes with calcium and phosphate and thus is a carrier of otherwise insoluble calcium phosphate. Thus AHSG / Fetuin A is a potent inhibitor of pathological calcification. Fetuin A / FETUA promotes phagocytosis of apoptotic cells and plays a role in bone development, calcium homeostasis and insulin sensitivity. Mice deficient in Fetuin-A show systemic calcification of soft tissues.
References :
(1) Jahnen-Dechent W., et al., 1994, Eur. J. Biochem. 226 (1): 59–69.
(2) Lee C., et al., 2009, Frontiers in Bioscience 14: 2911–2922.
(3) Heiss A., et al., 2008, J. Biol. Chem. 283 (21): 14815–25.
(4) Jahnen-Dechent W., et al., 2008, J. Mol. Med. 86 (4): 379–89.

