biological source
goat
antibody form
purified antibody
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized
does not contain
preservative
species reactivity
human
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze, avoid repeated freeze/thaw cycles
isotype
IgG
shipped in
ambient
storage temp.
−20°C
Quality Level
Gene Information
human ... HBEGF(1839)
General description
Anti-Heparin Binding Epidermal Growth Factor (Ab-1), goat polyclonal, recognizes the ~19-23 kDa HB-EGF in vascular smooth muscle cells. It is validated for use in ELISA, WB & neutralization studies.
Purified goat polyclonal antibody. Recognizes the ~19-23 kDa (apparent MW) heparin binding epidermal growth factor protein.
Recognizes the ~19-23 kDa HB-EGF protein in vascular smooth muscle cells.
Immunogen
purified, recombinant, human HB-EGF
Application
ELISA (0.5-1 µg/ml, see comments)
Immunoblotting (1-2 µg/ml)
Neutralization Studies (see comments)
Immunoblotting (1-2 µg/ml)
Neutralization Studies (see comments)
Physical form
Lyophilized from sterile filtered solution in PBS, 5% trehalose, 100 µg BSA.
Preparation Note
Reconstitute the lyophilized antibody with sterile PBS, pH 7.4, or sterile 20 mM Tris-saline (20 mM Tris containing 0.15 M NaCl), pH 7.4, to yield a final concentration of 0.25 mg/ml. Lyophilized antibody should be resuspended at 4°C with occasional gentle mixing for at least 2 h. Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C. Avoid freeze/thaw cycles of solutions.
Analysis Note
Positive Control
Vascular smooth muscle cells
Vascular smooth muscle cells
Other Notes
Davis-Fleischer, K.M. et al. 1998. Front. Biosci.3, D288.
Ouchi, N., et al. 1997. Biochem. J.328, 923.
Raab, G. and Klagsbrun M. 1997. Biochim. Biophys. Acta1333, F179.
Suzuki, M., et al. 1997. J. Biol. Chem.272, 31730.
Nakata, A., et al. 1996. Circulation94, 2778.
Miyagawa, J., et al. 1995. J. Clin. Invest.95, 404.
Ouchi, N., et al. 1997. Biochem. J.328, 923.
Raab, G. and Klagsbrun M. 1997. Biochim. Biophys. Acta1333, F179.
Suzuki, M., et al. 1997. J. Biol. Chem.272, 31730.
Nakata, A., et al. 1996. Circulation94, 2778.
Miyagawa, J., et al. 1995. J. Clin. Invest.95, 404.
This antibody has been selected for its ability to neutralize the biological activity of human recombinant HB-EGF. It will not neutralize the biological activity of EGF, TGF-α or amphiregulin. The exact concentration of antibody required to neutralize human recombinant HB-EGF activity is dependent on the cytokine concentration, cell type, growth conditions, and the type of activity studied. Suggested neutralization concentration required to yield one-half maximal inhibition of HB-EGF activity is ~3-6 µg/ml in the presence of 10 ng/ml of human recombinant HB-EGF using a Balb/3T3 cell line. For immunoblotting, the detection limit for human recombinant HB-EGF is ~0.5 ng/lane under non-reducing and reducing conditions. For ELISA, the detection limit for human recombinant HB-EGF is ~0.03 ng/well. This antibody exhibits no cross-reactivity with other cytokines when tested in ELISA. Antibody should be titrated for optimal results in individual systems.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Harmful (C)
未找到合适的产品?
试试我们的产品选型工具.
Kevin C Parvaresh et al.
Experimental physiology, 95(11), 1098-1106 (2010-08-11)
Skeletal muscle hypertrophy requires the co-ordinated expression of locally acting growth factors that promote myofibre growth and concurrent adaptive changes in the microvasculature. These studies tested the hypothesis that vascular endothelial growth factor (VEGF) and heparin-binding epidermal growth factor (HB-EGF)
Deepti B Ramnarain et al.
Cancer research, 66(2), 867-874 (2006-01-21)
The epidermal growth factor receptor (EGFR) gene is commonly amplified and rearranged in glioblastoma multiforme leading to overexpression of wild-type and mutant EGFRs. Expression of wild-type EGFR ligands, such as transforming growth factor-alpha (TGF-alpha) or heparin-binding EGF (HB-EGF), is also
Pal Göoz et al.
Biochemical and biophysical research communications, 380(1), 33-38 (2009-01-20)
Modulation of angiogenesis is a promising approach for treating a wide variety of human diseases including ischemic heart disease and cancer. In this study, we show that ADAM-17 is an important regulator of several key steps during angiogenesis. Knocking down
我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系客户支持