wild type rbd (Sino Biological)
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96
Structured Review
Sino Biological
wild type rbd
Wild Type Rbd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 96/100, based on 211 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/wild+type+rbd/Ebola+virus+EBOV+(subtype+Bundibugyo%2C+strain+Uganda+2007)+Glycoprotein+%2F+GP-RBD+(Receptor+Binding+Domain)+Protein/10__1016_slash_j__microc__2025__113187-70-12-15
Average 96 stars, based on 211 article reviews
Wild Type Rbd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 96/100, based on 211 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/wild+type+rbd/Ebola+virus+EBOV+(subtype+Bundibugyo%2C+strain+Uganda+2007)+Glycoprotein+%2F+GP-RBD+(Receptor+Binding+Domain)+Protein/10__1016_slash_j__microc__2025__113187-70-12-15
Average 96 stars, based on 211 article reviews
wild type rbd - by Bioz Stars,
2026-09
96/100 stars
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Related Articles
Recombinant:Article Title: Precision mapping of the functional epitope of a SARS-CoV-2 neutralizing antibody via hydrogen–deuterium exchange mass spectrometry Article Snippet: The receptor-binding domain (RBD) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is pivotal in viral attachment and entry into host cells via interactions with the human angiotensin-converting enzyme 2 (hACE2) receptor; therefore, the RBD is a prime target for neutralizing antibodies.. Precise mapping of antibody epitopes within the RBD allows for targeted interference with viral entry mechanisms; thus, it is crucial for advancing therapeutic antibody development and vaccine design.. This study employed hydrogen–deuterium exchange mass spectrometry (HDX-MS) to define the epitope recognized by the potent neutralizing monoclonal antibody K102.1. Gentle:Article Title: Precision mapping of the functional epitope of a SARS-CoV-2 neutralizing antibody via hydrogen–deuterium exchange mass spectrometry Article Snippet: The receptor-binding domain (RBD) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is pivotal in viral attachment and entry into host cells via interactions with the human angiotensin-converting enzyme 2 (hACE2) receptor; therefore, the RBD is a prime target for neutralizing antibodies.. Precise mapping of antibody epitopes within the RBD allows for targeted interference with viral entry mechanisms; thus, it is crucial for advancing therapeutic antibody development and vaccine design.. This study employed hydrogen–deuterium exchange mass spectrometry (HDX-MS) to define the epitope recognized by the potent neutralizing monoclonal antibody K102.1. |