Antibody data
- Antibody Data
- Antigen structure
- References [4]
- Comments [0]
- Validations [0]
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- Product number
- ABIN2451995 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Heparin-Binding EGF-Like Growth Factor (HBEGF) (Bound), (EGF Like Domain), (Soluble) antibody
- Antibody type
- Monoclonal
- Antigen
- RecombinanthumanHB-EGFectodomainexpressed inSF21 cell
- Reactivity
- Human
- Host
- Mouse
- Epitope
- EGF Like Domain,Soluble,Bound
- Isotype
- IgG
- Antibody clone number
- 4G10
- Vial size
- 50 μg
- Storage
- Upon arrival centrifuge briefly, aliquote and store at -20 C.
Submitted references Heparin-binding EGF-like growth factor is a promising target for ovarian cancer therapy.
EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF.
Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity.
A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF.
Miyamoto S, Hirata M, Yamazaki A, Kageyama T, Hasuwa H, Mizushima H, Tanaka Y, Yagi H, Sonoda K, Kai M, Kanoh H, Nakano H, Mekada E
Cancer research 2004 Aug 15;64(16):5720-7
Cancer research 2004 Aug 15;64(16):5720-7
EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF.
Prenzel N, Zwick E, Daub H, Leserer M, Abraham R, Wallasch C, Ullrich A
Nature 1999 Dec 23-30;402(6764):884-8
Nature 1999 Dec 23-30;402(6764):884-8
Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity.
Iwamoto R, Higashiyama S, Mitamura T, Taniguchi N, Klagsbrun M, Mekada E
The EMBO journal 1994 May 15;13(10):2322-30
The EMBO journal 1994 May 15;13(10):2322-30
A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF.
Higashiyama S, Abraham JA, Miller J, Fiddes JC, Klagsbrun M
Science (New York, N.Y.) 1991 Feb 22;251(4996):936-9
Science (New York, N.Y.) 1991 Feb 22;251(4996):936-9
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