Review




Structured Review

Galectin Therapeutics human galectin 4
Human Galectin 4, supplied by Galectin Therapeutics, 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/human+galectin-4/lgals3/pm41865671-89-4-7
Average 86 stars, based on 1 article reviews
human galectin 4 - by Bioz Stars, 2026-10
86/100 stars

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Related Articles

Binding Assay:

Article Title: Structural characterization of human galectin-4 C-terminal domain: elucidating the molecular basis for recognition of glycosphingolipids, sulfated saccharides and blood group antigens.
Article Snippet: doi:10.1111/febs.13348 Human galectin-4 is a lectin that is expressed mainly in the gastrointestinal tract and exhibits metastasis-promoting roles in some cancers.. Its tandemrepeat nature exhibits two distinct carbohydrate recognition domains allowing crosslinking by simultaneous binding to sulfated and non-sulfated (but not sialylated) glycosphingolipids and glycoproteins, facilitating stabilization of lipid rafts.. Critically, galectin-4 exerts favourable or unfavourable effects depending upon the cancer.

Article Title: Functions and Inhibition of Galectin-7, an Emerging Target in Cellular Pathophysiology
Article Snippet: Tandem-repeat galectins (human galectin-4, -8, -9, and -12) contain two CRDs that are connected by a short peptide linker that can range from 5 up to 70 amino acids.

Article Title: Conformations of the type-1 lacto- N -biose I unit in protein complex structures
Article Snippet: The PDB contains LNB or LNT structures bound to human galectins (galectin-1, galectin-3, galectin-4, galectin-7 and galectin-8) as a part of a lacto-series of glycosphingolipids.

Fluorescence:

Article Title: Structural characterization of human galectin-4 C-terminal domain: elucidating the molecular basis for recognition of glycosphingolipids, sulfated saccharides and blood group antigens.
Article Snippet: doi:10.1111/febs.13348 Human galectin-4 is a lectin that is expressed mainly in the gastrointestinal tract and exhibits metastasis-promoting roles in some cancers.. Its tandemrepeat nature exhibits two distinct carbohydrate recognition domains allowing crosslinking by simultaneous binding to sulfated and non-sulfated (but not sialylated) glycosphingolipids and glycoproteins, facilitating stabilization of lipid rafts.. Critically, galectin-4 exerts favourable or unfavourable effects depending upon the cancer.

Article Title: Functions and Inhibition of Galectin-7, an Emerging Target in Cellular Pathophysiology
Article Snippet: Tandem-repeat galectins (human galectin-4, -8, -9, and -12) contain two CRDs that are connected by a short peptide linker that can range from 5 up to 70 amino acids.

Article Title: Conformations of the type-1 lacto- N -biose I unit in protein complex structures
Article Snippet: The PDB contains LNB or LNT structures bound to human galectins (galectin-1, galectin-3, galectin-4, galectin-7 and galectin-8) as a part of a lacto-series of glycosphingolipids.

Bacteria:

Article Title: Structural characterization of human galectin-4 C-terminal domain: elucidating the molecular basis for recognition of glycosphingolipids, sulfated saccharides and blood group antigens.
Article Snippet: doi:10.1111/febs.13348 Human galectin-4 is a lectin that is expressed mainly in the gastrointestinal tract and exhibits metastasis-promoting roles in some cancers.. Its tandemrepeat nature exhibits two distinct carbohydrate recognition domains allowing crosslinking by simultaneous binding to sulfated and non-sulfated (but not sialylated) glycosphingolipids and glycoproteins, facilitating stabilization of lipid rafts.. Critically, galectin-4 exerts favourable or unfavourable effects depending upon the cancer.

Article Title: Functions and Inhibition of Galectin-7, an Emerging Target in Cellular Pathophysiology
Article Snippet: Tandem-repeat galectins (human galectin-4, -8, -9, and -12) contain two CRDs that are connected by a short peptide linker that can range from 5 up to 70 amino acids.

Article Title: Conformations of the type-1 lacto- N -biose I unit in protein complex structures
Article Snippet: The PDB contains LNB or LNT structures bound to human galectins (galectin-1, galectin-3, galectin-4, galectin-7 and galectin-8) as a part of a lacto-series of glycosphingolipids.



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