recombinant human fsh (Sangon Biotech)
86
Structured Review
Sangon Biotech
recombinant human fsh
Recombinant Human Fsh, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+human+fsh/associated+human+microtube+monomers+protein+recombinant+tau/10__1016_slash_j__jddst__2026__108044-275-9-15
Average 86 stars, based on 1 article reviews
Recombinant Human Fsh, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+human+fsh/associated+human+microtube+monomers+protein+recombinant+tau/10__1016_slash_j__jddst__2026__108044-275-9-15
Average 86 stars, based on 1 article reviews
recombinant human fsh - by Bioz Stars,
2026-10
86/100 stars
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In Vivo:Article Title: Engineering and translational evaluation of A Novel Albumin-binding variable domain of heavy chain-only antibody for half-life extension Article Snippet: Therapeutic proteins often exhibit rapid clearance from circulation, necessitating frequent dosing and impairing patient adherence.. Here, we aimed to develop an albumin-binding VHH (variable domain of heavy chain-only antibody) to extend protein half-life via FcRn(neonatal Fc receptor)-mediated recycling, using folliclestimulating hormone (FSH) as a model. Anti-HSA VHHs were isolated from a naïve alpaca phage library (with cross-reactivity to cynomolgus serum albumin, Cyno-SA) and characterized via surface plasmon resonance (SPR) for binding affinity.. AlphaFold3-predicted VHH-HSA complex structures were validated by alanine-scanning mutagenesis. Analogues:Article Title: Engineering and translational evaluation of A Novel Albumin-binding variable domain of heavy chain-only antibody for half-life extension Article Snippet: Therapeutic proteins often exhibit rapid clearance from circulation, necessitating frequent dosing and impairing patient adherence.. Here, we aimed to develop an albumin-binding VHH (variable domain of heavy chain-only antibody) to extend protein half-life via FcRn(neonatal Fc receptor)-mediated recycling, using folliclestimulating hormone (FSH) as a model. Anti-HSA VHHs were isolated from a naïve alpaca phage library (with cross-reactivity to cynomolgus serum albumin, Cyno-SA) and characterized via surface plasmon resonance (SPR) for binding affinity.. AlphaFold3-predicted VHH-HSA complex structures were validated by alanine-scanning mutagenesis. Recombinant:Article Title: Engineering and translational evaluation of A Novel Albumin-binding variable domain of heavy chain-only antibody for half-life extension Article Snippet: Therapeutic proteins often exhibit rapid clearance from circulation, necessitating frequent dosing and impairing patient adherence.. Here, we aimed to develop an albumin-binding VHH (variable domain of heavy chain-only antibody) to extend protein half-life via FcRn(neonatal Fc receptor)-mediated recycling, using folliclestimulating hormone (FSH) as a model. Anti-HSA VHHs were isolated from a naïve alpaca phage library (with cross-reactivity to cynomolgus serum albumin, Cyno-SA) and characterized via surface plasmon resonance (SPR) for binding affinity.. AlphaFold3-predicted VHH-HSA complex structures were validated by alanine-scanning mutagenesis. |