Human MFG-E8 Antibody Summary
Leu24-Cys387
Accession # Q08431
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of Human MFG‑E8 by Western Blot. Western blot shows lysates of human milk. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Human MFG-E8 Monoclonal Antibody (Catalog # MAB2767) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for MFG-E8 at approximately 45 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Detection of Human MFG‑E8 by Simple WesternTM. Simple Western lane view shows recombinant human (rh) MFG-E8, loaded at 50 ng/mL, and human milk, loaded at 0.2 mg/mL. A specific band was detected for MFG‑E8 at approximately 57-58 kDa (as indicated) using 50 µg/mL of Mouse Anti-Human MFG‑E8 Monoclonal Antibody (Catalog # MAB2767). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: MFG-E8
Milk Fat Globulin Protein E8 (MFG-E8), also known as Lactadherin, MP47, breast epithelial antigen BA46, and SED1, is a 66‑75 kDa pleiotropic secreted glycoprotein that promotes mammary gland morphogenesis, angiogenesis, and tumor progression. MFG-E8 also plays an important role in tissue homeostasis and the prevention of inflammation (1). Human MGF-E8 contains one N-terminal EGF-like domain and two C‑terminal F5/8-type discoidin-like domains (2). It shares 63% and 61% aa sequence identity with comparable regions of mouse and rat MFG-E8, respectively. Shorter isoforms of human MFG-E8 may have N-terminal deletions (beginning near the end of the first discoidin-like domain), internal deletions (lacking either the EGF-like domain or the central region of the second discoidin-like domain), or C‑terminal deletions (truncated within the second discoidin-like domain) (3). A 50 aa internal proteolytic fragment of human MFG-E8 (known as Medin) is a major component of aortic medial amyloid deposits (4). MFG-E8 is released into the milk in complex with lipid-containing milk fat globules. It is also found in multiple other cell types including endothelial cells and smooth muscle cells of the vasculature, immature dendritic cells, at the acrosomal cap of testicular and epididymal sperm, and in epithelial cells of the endometrium (1). MFG-E8 binds to the Integrins alpha V beta 3 and alpha V beta 5 and potentiates the angiogenic action of VEGF through VEGF R2 (5, 6). It reduces inflammation and tissue damage in a variety of settings. MFG-E8 functions as a bridge between phosphatidylserine on apoptotic cells and Integrin alpha V beta 3 on phagocytes, leading to the clearance of apoptotic debris (7). It mediates the engulfment of apoptotic bodies in atherosclerotic plaques and prion-infected brain (8, 9) and of apoptotic B cells during germinal center reactions (10, 11). MFG-E8 also promotes the removal of excess Collagen in fibrotic lungs and the regeneration of damaged intestinal epithelia (12, 13). Its tissue-protective role impairs anti‑tumor immunity and chemotherapy-induced apoptosis (14). MFG-E8 in the breastmilk blocks rotavirus infection in nursing babies (15).
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- Yamaguchi, H. et al. (2010) Eur. J. Immunol. 40:1778.
- Haggqvist, B. et al. (1999) Proc. Natl. Acad. Sci. USA 96:8669.
- Silvestre, J.-S. et al. (2005) Nat. Med. 11:499.
- Borges, E. et al. (2000) J. Biol. Chem. 275:39867.
- Hanayama, R. et al. (2002) Nature 417:182.
- Ait-Oufella, H. et al. (2007) Circulation 115:2168.
- Kranich, J. et al. (2010) J. Exp. Med. 207:2271.
- Hanayama, R. et al. (2004) Science 304:1147.
- Kranich, J. et al. (2010) J. Exp. Med. 205:1293.
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- Jinushi, M. et al. (2009) J. Exp. Med. 206:1317.
- Kvistgaard, A.S. et al. (2004) J. Dairy Sci. 87:4088.
Product Datasheets
Citations for Human MFG-E8 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Oncogene-regulated release of extracellular vesicles
Authors: Seda Kilinc, Rebekka Paisner, Roman Camarda, Suprit Gupta, Olga Momcilovic, Rebecca A. Kohnz et al.
Developmental Cell
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Buoyant Density Fractionation of Small Extracellular Vesicle Sub-populations Derived from Mammalian Cells
Authors: Morayma M Temoche-Diaz, Matthew J Shurtleff, Randy Schekman
BIO-PROTOCOL
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Distinct mechanisms of microRNA sorting into cancer cell-derived extracellular vesicle subtypes
Authors: Morayma M Temoche-Diaz, Matthew J Shurtleff, Ryan M Nottingham, Jun Yao, Raj P Fadadu, Alan M Lambowitz et al.
eLife
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MFG-E8 activates proliferation of vascular smooth muscle cells via integrin signaling
Authors: Mingyi Wang, Zongming Fu, James Wu, Jing Zhang, Liqun Jiang, Benjamin Khazan et al.
Aging Cell
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Comparative proteomic analysis of rat aorta in a subtotal nephrectomy model.
Authors: Lin YP, Hsu ME, Chiou YY
Proteomics, 2010-07-01;10(13):2429-43.
Species: Human
Sample Types: Serum
Applications: ELISA Development
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