Results 1 to 10 of about 628,463 (260)

Single Domain Antibody application in bacterial infection diagnosis and neutralization

open access: yesFrontiers in Immunology, 2022
Increasing antibiotic resistance to bacterial infections causes a serious threat to human health. Efficient detection and treatment strategies are the keys to preventing and reducing bacterial infections. Due to the high affinity and antigen specificity,
Qian Qin   +11 more
doaj   +3 more sources

Single-domain antibody-based protein degrader for synucleinopathies [PDF]

open access: yesMolecular Neurodegeneration
Synucleinopathies are a group of neurodegenerative diseases characterized by the accumulation of α-synuclein (α-syn) in the brain, leading to motor and neuropsychiatric symptoms.
Yixiang Jiang   +7 more
doaj   +2 more sources

Single domain antibody: Development and application in biotechnology and biopharma. [PDF]

open access: yesImmunol Rev
SummaryHeavy‐chain antibodies (HCAbs) are a unique type of antibodies devoid of light chains, and comprised of two heavy chains‐only that recognize their cognate antigen by virtue of a single variable domain also referred to as VHH, single domain antibody (sdAb), or nanobody (Nb). These functional HCAbs, serendipitous discovered about three decades ago,
Yu T   +4 more
europepmc   +4 more sources

Bamboo Shark as a Small Animal Model for Single Domain Antibody Production

open access: yesFrontiers in Bioengineering and Biotechnology, 2021
The development of shark single domain antibodies (sdAbs) is hindered by the high cost and tediousness of large-sized shark farming. Here, we demonstrated white-spotted bamboo sharks (Chiloscyllium plagiosum) being cultivated commercially as a promising ...
Likun Wei   +24 more
doaj   +3 more sources

Development of a Chicken Immunoglobulin Heavy Chain Variable Region (VH) Single-Domain Antibody (sdAb) Against Calsequestrin (CSQ) and Its Application [PDF]

open access: yesAntibodies
Background/Objectives: Calsequestrin (CSQ) is a calcium-binding protein that is highly soluble and can serve as a solubility-enhancing fusion tag in recombinant protein expression.
Sun Lee   +8 more
doaj   +2 more sources

Immunogenicity and humanization of single‐domain antibodies [PDF]

open access: yesThe FEBS Journal, 2021
Single‐domain antibodies (sdAbs), the autonomous variable domains of camelid and shark heavy‐chain antibodies, have many desirable properties as components of biologic drugs. However, their sequences may increase the risk of immunogenicity and antidrug antibody (ADA) development in humans, and thus, sdAbs are routinely humanized during development ...
Rossotti, Martin A.   +3 more
openaire   +2 more sources

Single-domain antibodies make a difference [PDF]

open access: yesScience, 2021
A double hit with one antibody construct may avoid viral ...
Xavier, Saelens, Bert, Schepens
openaire   +2 more sources

Single-domain antibody screening by is PLA-seq

open access: yesLife Science Alliance, 2022
This study describes a high-sensitive, high-throughput single-domain antibody library screening approach, which is applicable for any given interested protein at single-cell resolution by is PLA-seq.
Yueyuan Yin   +6 more
doaj   +1 more source

Preparation and identification of a single domain antibody specific for adenovirus vectors and its application to the immunoaffinity purification of adenoviruses

open access: yesAMB Express, 2022
Adenovirus belongs to the family of Adenoviridae. As a vaccine carrier, it has high safety and stimulates the body to produce cellular immunity and humoral immunity.
Yi Cheng   +8 more
doaj   +1 more source

Novel single-domain antibodies against the EGFR domain III epitope exhibit the anti-tumor effect

open access: yesJournal of Translational Medicine, 2020
Background Monoclonal antibodies (mAbs) have been used for cancer therapy. They are large and have some disadvantages limiting their use. Smaller antibody fragments are needed as their alternatives. A fully human single-domain antibody (sdAb) has a small
Tao Chen   +3 more
doaj   +1 more source

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