HBEGF (E5L5T) Rabbit mAb #27450
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 18, 21, 27 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
HBEGF (E5L5T) Rabbit mAb recognizes endogenous levels of total proHBEGF or mature HBEGF protein. This antibody also detects a 58 kDa band of unknown origin.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a recombinant protein fragment specific to human mature HBEGF protein.
Background
Heparin-binding EGF-like growth factor (HBEGF), also known as HB-EGF, belongs to the epidermal growth factor (EGF) family (1). The newly synthesized proHBEGF (about 27 kDa) has an N-terminal prodomain, a heparin-binding EGF domain, and a C-terminal transmembrane fragment (CTF). The heparin-binding region of HBEGF interacts with heparin residues in the extracellular matrix (ECM) and anchors the protein in the ECM. The proHBEGF is activated by the extracellular ADAM and MMP metalloproteases, shedding off its N-terminal prodomain and/or CTF, resulting in a 14-22 kDa product depending on different proteolytic processes. The mature HBEGF acts as a ligand for EGFR or ErbB4 receptors to activate downstream signaling pathways (2,3). The remaining membrane bound CTF is further internalized and binds to Bcl6 to regulate the related nuclear function (3). HBEGF has been shown to be involved in many physiological processes, such as placenta formation (4), heart development and function (5), and hematopoietic cell proliferation (6). The growth factor plays important roles in tissue inflammation, wound healing, and cancer development. Therefore, HBEGF is proposed as a therapeutic target in related diseases (7-10).
- Miyamoto, S. et al. (2006) Cancer Sci 97, 341-7.
- Tsujioka, H. et al. (2010) Anticancer Res 30, 3107-12.
- Higashiyama, S. et al. (2008) Cancer Sci 99, 214-20.
- Jessmon, P. et al. (2009) Mol Reprod Dev 76, 1116-27.
- Iwamoto, R. and Mekada, E. (2006) Cell Struct Funct 31, 1-14.
- Vinante, F. and Rigo, A. (2013) Toxins (Basel) 5, 1180-1201.
- Dao, D.T. et al. (2018) Am J Pathol 188, 2446-2456.
- Eapen, M.S. et al. (2019) Lab Invest 99, 150-157.
- Tsujioka, H. et al. (2011) Curr Opin Obstet Gynecol 23, 24-30.
- Miyata, K. et al. (2012) Anticancer Res 32, 2347-52.
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