Generation and Characterization of Monoclonal Antibodies Against Channel Catfish Virus

Hybridoma ◽  
2011 ◽  
Vol 30 (6) ◽  
pp. 555-558 ◽  
Author(s):  
Bing Wu ◽  
Bibo Zhu ◽  
Yuling Luo ◽  
Min Wang ◽  
Yuanan Lu ◽  
...  
2010 ◽  
Vol 135 (3-4) ◽  
pp. 325-328 ◽  
Author(s):  
Eva-Stina Edholm ◽  
Edward D. Hudgens ◽  
Dannielle Tompkins ◽  
Manoranjan Sahoo ◽  
Bailey Burkhalter ◽  
...  

2008 ◽  
Vol 126 (1-2) ◽  
pp. 120-130 ◽  
Author(s):  
Mohadetheh Moulana ◽  
Jason Evenhuis ◽  
Mark Albertino ◽  
Ulla Godwin ◽  
Evgueni I. Kountikov ◽  
...  

2018 ◽  
Vol 163 (9) ◽  
pp. 2503-2506
Author(s):  
Hongli Jing ◽  
Min Zhang ◽  
Shaoqiang Wu ◽  
Xiangmei Lin ◽  
Longying Gao ◽  
...  

1998 ◽  
Vol 79 (01) ◽  
pp. 104-109 ◽  
Author(s):  
Osamu Takamiya

SummaryMurine monoclonal antibodies (designated hVII-B101/B1, hVIIDC2/D4 and hVII-DC6/3D8) directed against human factor VII (FVII) were prepared and characterized, with more extensive characterization of hVII-B101/B1 that did not bind reduced FVIIa. The immunoglobulin of the three monoclonal antibodies consisted of IgG1. These antibodies did not inhibit procoagulant activities of other vitamin K-dependent coagulation factors except FVII and did not cross-react with proteins in the immunoblotting test. hVII-DC2/D4 recognized the light chain after reduction of FVIIa with 2-mercaptoethanol, and hVIIDC6/3D8 the heavy chain. hVII-B101/B1 bound FVII without Ca2+, and possessed stronger affinity for FVII in the presence of Ca2+. The Kd for hVII-B101/B1 to FVII was 1.75 x 10–10 M in the presence of 5 mM CaCl2. The antibody inhibited the binding of FVII to tissue factor in the presence of Ca2+. hVII-B101/B1 also inhibited the activation of FX by the complex of FVIIa and tissue factor in the presence of Ca2+. Furthermore, immunoblotting revealed that hVII-B101/B1 reacted with non-reduced γ-carboxyglutaminic acid (Gla)-domainless-FVII and/or FVIIa. hVII-B101/B1 showed a similar pattern to that of non-reduced proteolytic fragments of FVII by trypsin with hVII-DC2/D4 on immunoblotting test. hVII-B101/B1 reacted differently with the FVII from the dysfunctional FVII variant, FVII Shinjo, which has a substitution of Gln for Arg at residue 79 in the first epidermal growth factor (1st EGF)-like domain (Takamiya O, et al. Haemosta 25, 89-97,1995) compared with normal FVII, when used as a solid phase-antibody for ELISA by the sandwich method. hVII-B101/B1 did not react with a series of short peptide sequences near position 79 in the first EGF-like domain on the solid-phase support for epitope scanning. These results suggested that the specific epitope of the antibody, hVII-B101/B1, was located in the three-dimensional structure near position 79 in the first EGF-like domain of human FVII.


2012 ◽  
Vol 36 (2) ◽  
pp. 314
Author(s):  
Jian-feng LU ◽  
Chang-wei MENG ◽  
Jin LI ◽  
Zi-hui GONG ◽  
Lin LIN ◽  
...  

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