Human MFAP5 / MAGP2 Protein (His Tag)

AAT9,MAGP-2,MAGP2,MFAP-5,MP25

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Catalog Number	P12648-H08H
Organism Species	Human
Host	Human Cells
Synonyms	AAT9,MAGP-2,MAGP2,MFAP-5,MP25
Molecular Weight	The recombinant human MFAP5 comprises 163 amino acids and has a predicted molecular mass of 18.7 kDa. The apparent molecular mass of the protein is approximately 54 and 29 kDa in SDS-PAGE under reducing conditions.
predicted N	Arg 22
SDS-PAGE
Purity	> (54.7+31.5) % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the human MFAP5 (Q13361) (Met1-Leu173) with a C-terminal polyhistidine tag was expressed.
Bio-activity
Research Area	Cardiovascular |Angiogenesis |Angiogenesis Growth Factor & Receptor
Formulation	Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	MFAP5, also known as MAGP2, is a component of the elastin-associated microfibrils. It belongs to the MFAP family. As a 25-kD microfibril-associated glycoprotein, MFAP5 is rich in serine and threonine residues. It stimulates the assembly of elastic fibers, a complex structure composed of a tropoelastin inner core and microfibril outer mantle comprising proteins such as fibrillins and microfibril-associated glycoproteins that guide tropoelastin deposition. MFAP5 also stabilizes type 1 procollagen and thus plays an important role in extracellular matrix homeostasis. It has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrils.
Reference	Hatzinikolas G, et al. (1998) The exon structure of the human MAGP-2 gene. Similarity with the MAGP-1 gene is confined to two exons encoding a cysteine-rich region. J Biol Chem. 273(45):29309-14. Gibson MA, et al. (1996) Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25). J Biol Chem. 271(2): 1096-103. Miyamoto A, et al. (2006) Microfibrillar proteins MAGP-1 and MAGP-2 induce Notch1 extracellular domain dissociation and receptor activation. J Biol Chem. 281(15):10089-97.