scholarly journals Development of a PCR-based dot blot assay for the detection of fowl adenovirus

2021 ◽  
pp. 101540
Author(s):  
Lidan Hou ◽  
Qi Su ◽  
Yawen Zhang ◽  
Dan Liu ◽  
Yaqing Mao ◽  
...  
Keyword(s):  
Dot Blot ◽  
Fowl Adenovirus ◽  
Dot Blot Assay

APPLICATION OF REAL-TIME PRC TECHNIQUE AND REVERSE DOT-BLOT FOR DETECTION THE HIGH RISK TYPES OF HUMAN PAPILLOMAVIRUS CAUSING CERVICAL CANCER

2017 ◽  
pp. 99-103
Author(s):  
Van Bao Thang Phan ◽  
Hoang Bach Nguyen ◽  
Van Thanh Nguyen ◽  
Thi Nhu Hoa Tran ◽  
Viet Quynh Tram Ngo
Keyword(s):  
Cervical Cancer ◽  
High Risk ◽  
Real Time ◽  
Real Time Pcr ◽  
Dot Blot ◽  
The Real ◽  
Dot Blot Assay ◽  
Hpv Types ◽  
High Risk Hpv ◽  
Reverse Dot Blot

Introduction: Infection with HPV is the main cause of cervical cancer. Determining HPV infection and the types of HPV plays an important role in diagnosis, treatment and prognosis of cervicitis/cervical cancer. Aims: Determining proportion of high-risk HPV types and the occurrence of coinfection with multiple HPV types. Methods: 177 women with cervicitis or abnormal Pap smear result were enrolled in the study. Performing the real-time PCR for detecting HPV and the reverse DOT-BLOT assay for determining type of HPV in cases of positive PCR. Results: 7 types of high-risk HPV was dectected, the majority of these types were HPV type 18 (74.6%) and HPV type 16 (37.6%); the proportion of infection with only one type of HPV was 30.4% and coinfection with multiple HPV types was higher (69.6%), the coinfected cases with 2 and 3 types were dominated (32.2% and 20.3%, respectively) and the coinfected cases with 4 and 5 types were rare. Conclusion: Use of the real-time PCR and reverse DOT-BLOT assay can determine the high-risk HPV types and the occurrence of coinfection with multiple HPV types. Key words: HPV type, Reverse DOT-BLOT, real-time PCR,PCR, cervical cancer

Use of monoclonal and polyclonal antibodies to detect prostatic acid phosphatase by immunoblotting.

1986 ◽  
Vol 32 (10) ◽  
pp. 1832-1835 ◽  
Author(s):  
P C Patel ◽  
L Aubin ◽  
J Côte
Keyword(s):  
Monoclonal Antibodies ◽  
Acid Phosphatase ◽  
Western Blot ◽  
Polyclonal Antibodies ◽  
Prostatic Acid Phosphatase ◽  
The Other ◽  
Dot Blot ◽  
Western Blots ◽  
Dot Blot Assay ◽  
Polyclonal Antisera

Abstract We investigated two techniques of immunoblotting--the Western blot and the dot blot--for use in detecting prostatic acid phosphatase (PAP, EC 3.1.3.2). We used polyclonal antisera to human PAP, produced in rabbits by hyperimmunization with purified PAP, and PAP-specific monoclonal antibodies in the immunoenzymatic protocols. We conclude that PAP can be readily detected by Western blots with use of polyclonal antisera, but not with monoclonal antibodies. On the other hand, using a dot blot assay, we could easily detect PAP with both polyclonal and monoclonal antibodies.

Quantitating Apoptosis by a Nonradioactive DNA Dot Blot Assay

1994 ◽  
Vol 221 (2) ◽  
pp. 431-433 ◽  
Author(s):  
A.O. Hueber ◽  
M. Pierres ◽  
H.T. He
Keyword(s):  
Dot Blot ◽  
Dot Blot Assay

Measurement of hygromycin B phosphotransferase activity in crude mammalian cell extracts by a simple dot-blot assay

Gene ◽  
1992 ◽  
Vol 112 (2) ◽  
pp. 257-260 ◽  
Author(s):  
Schandorf Sørensen Michael ◽  
Mogens Duch ◽  
Kirsten Paludan ◽  
Poul Jøgensen ◽  
Skou Pedersen Finn
Keyword(s):  
Mammalian Cell ◽  
Hygromycin B ◽  
Dot Blot ◽  
Cell Extracts ◽  
Dot Blot Assay

A Simple, Rapid and Non-Radiolabeled Immune Assay to Detect Anti-AChR Antibodies in Myasthenia Gravis

2018 ◽  
Vol 50 (3) ◽  
pp. 229-235 ◽  
Author(s):  
Suresh Bokoliya ◽  
Shripad Patil ◽  
Madhu Nagappa ◽  
Arun Taly
Keyword(s):  
Myasthenia Gravis ◽  
Case Control Study ◽  
Enzyme Linked Immunosorbent Assay ◽  
Test Results ◽  
Dot Blot ◽  
Dot Blot Assay ◽  
Healthy Control ◽  
Neurological Illnesses ◽  
Control Study ◽  
Immune Assay

AbstractObjectiveTo assess the practicality of dot-blot testing for rapid and sensitive detection of the antiacetylcholine receptor (anti-AChR) antibodies in myasthenia gravis (MG).MethodsIn this case-control study, we tested serum specimens of 85 patients with MG, 85 healthy control individuals, and 85 patients without MG who have other autoimmune and neurological illnesses. All the serum specimens were tested for anti-AChR antibodies using 3 assays: in-house enzyme-linked immunosorbent assay (ELISA), the dot-blot assay, and commercial ELISA.ResultsIn-house ELISA, commercial ELISA, and dot-blot test results were positive for anti-AChR antibodies in 65 (76.5%) patients with MG. The results of all 3 tests were negative for anti-AChR antibodies in healthy controls and patients without MG. We observed perfect concordance (K = 1, P <.001) between all 3 tests. In-house ELISA correlated significantly (r = 0.873, P <.001) with commercial ELISA. In-house ELISA and the dot-blot test demonstrated similar diagnostic performance in detecting anti-AChR antibodies.ConclusionsThe dot-blot assay is a simple, nonradioactive immune assay for rapid detection of anti-AChR antibodies in MG.

scholarly journals P3-072: QUANTITATIVE MEASUREMENT OF AMYLOID BETA OLIGOMER IN MOUSE BRAIN USING DOT BLOT ASSAY

2019 ◽  
Vol 15 ◽  
pp. P953-P954
Author(s):  
Akiko Amano ◽  
Nobuo Sanjo ◽  
Makoto Nakakido ◽  
Kouhei Tsumoto ◽  
Etsuro Matsubara ◽  
...  
Keyword(s):  
Mouse Brain ◽  
Amyloid Beta ◽  
Quantitative Measurement ◽  
Dot Blot ◽  
Dot Blot Assay

scholarly journals Contribution of factor VIII light-chain residues 2007–2016 to an activated protein C-interactive site

2013 ◽  
Vol 109 (02) ◽  
pp. 187-198 ◽  
Author(s):  
Masahiro Takeyama ◽  
Hironao Wakabayashi ◽  
Philip Fay
Keyword(s):  
Light Chain ◽  
Protein C ◽  
Activated Protein C ◽  
Fluid Phase ◽  
Fold Increase ◽  
Binding Assays ◽  
Dot Blot ◽  
Binding Studies ◽  
Dot Blot Assay ◽  
Dot Blotting

SummaryAlthough factor (F) VIIIa is inactivated by activated protein C (APC) through cleavages in the FVIII heavy chain-derived A1 (Arg336) and A2 subunits (Arg562), the FVIII light chain (LC) contributes to catalysis by binding the enzyme. ELISA-based binding assays showed that FVIII and FVIII LC bound to immobilised active site-modified APC (DEGRAPC) (apparent K d ~270 nM and 1.0 μM, respectively). Fluid-phase binding studies using fluorescence indicated an estimated K d of ~590 nM for acrylodan-labelled LC binding to DEGR-APC. Furthermore, FVIII LC effectively competed with FVIIIa in blocking APC-catalysed cleavage at Arg336 (K i = 709 nM). A binding site previously identified near the C-terminal end of the A3 domain (residues 2007–2016) of FVIII LC was subjected to Ala-scanning mutagenesis. FXa generation assays and western and dot blotting were employed to assess the contribution of these residues to FVIIIa interactions with APC. Virtually all variants tested showed reductions in the rates of APC-catalysed inactivation of the cofactor and cleavage at the primary inactivation site (Arg336), with maximal reductions in inactivation rates (~3-fold relative to WT) and cleavage rates (~3 to ~9-fold relative to WT) observed for the Met2010Ala, Ser2011Ala, and Leu2013Ala variants. Titration of FVIIIa substrate concentration monitoring cleavage by a dot blot assay indicated that these variants also showed ~3-fold increases relative to WT while a double mutant (Met2010Ala/Ser2011Ala) showed a >4-fold increase in K m. These results show a contribution of a number of residues within the 2007–2016 sequence, and in particular residues Met2010, Ser2011, and Leu2013 to an APC-interactive site.

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