|Application ||WB, FC, IHC-P, E|
|Other Accession||Q9QZJ6, Q28022|
|Calculated MW||19612 Da|
|Antigen Region||133-160 aa|
|Other Names||Microfibrillar-associated protein 5, MFAP-5, MP25, Microfibril-associated glycoprotein 2, MAGP-2, MFAP5, MAGP2|
|Target/Specificity||This MFAP5 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 133-160 amino acids from the C-terminal region of human MFAP5.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MFAP5 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||May play a role in hematopoiesis. In the cardiovascular system, could regulate growth factors or participate in cell signaling in maintaining large vessel integrity (By similarity). Component of the elastin-associated microfibrils (PubMed:8557636).|
|Cellular Location||Secreted, extracellular space, extracellular matrix|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
MFAP5 is a 25-kD microfibril-associated glycoprotein which is rich in serine and threonine residues. The protein lacks a hydrophobic carboxyl terminus and proline-, glutamine-, and tyrosine-rich regions, which are characteristics of a related 31-kDa microfibril-associated glycoprotein (MFAP2). The close similarity between these two proteins is confined to a central region of 60 aa where precise alignment of 7 cysteine residues occurs. The structural differences suggest that this protein has some functions that are distinct from those of MFAP2.
Albig,A.R., Becenti,D.J. Microvasc. Res. 76 (1), 7-14 (2008)
Miyamoto,A., Lau,R. J. Biol. Chem. 281 (15), 10089-10097 (2006)
Penner,A.S., Rock,M.J. J. Biol. Chem. 277 (38), 35044-35049 (2002)
Hatzinikolas,G. J. Biol. Chem. 273 (45), 29309-29314 (1998)
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