LGALS4 Human

Galectin-4 Human Recombinant
Cat. No.
BT10946
Source
Escherichia Coli.
Synonyms
Galectin-4, Gal-4, Lactose-binding lectin 4, L-36 lactose-binding protein, L36LBP, Antigen NY-CO-27, LGALS4, lectin galactoside-binding soluble 4, GAL4.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Galectin-4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 38.1kDa.
Galectin-4 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Galectin-4, a member of the galectin family, consists of two carbohydrate recognition domains with similar peptide chains. This family of beta-galactoside-binding proteins plays a crucial role in regulating cell-cell and cell-matrix interactions, ultimately inhibiting chronic inflammation, graft-versus-host disease (GVHD), and allergic responses. LGALS4 expression is primarily observed in the small intestine, colon, and rectum, with underexpression noted in colorectal cancer. Functionally, LGALS4 acts as an endogenous ligand for glycosphingolipids containing 3-O-sulfated Gal residues and binds to cholesterol-3-sulfate, contributing to cell adhesion. It plays a vital role in crosslinking the lateral cell membranes of surface-lining epithelial cells, enhancing epithelial integrity against mechanical stress within the bowel. Furthermore, LGALS4 influences intestinal inflammation by selectively regulating the cell cycle and apoptosis of peripheral and mucosal T-cells through a caspase-independent pathway. Notably, LGALS4 blockade has been shown to reduce TNF-alpha inhibitor-induced T-cell death, and it can decrease the secretion of pro-inflammatory cytokines like IL-6 and IL-17.
Description
Produced in E. coli, this Galectin-4 is a non-glycosylated polypeptide chain comprising 343 amino acids (with amino acids 1-323 present) and possessing a molecular weight of 38.1 kDa. A 20 amino acid His-Tag is fused to the N-terminus of the protein, which is then purified using proprietary chromatographic methods.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
This LGALS4 protein solution is formulated with 20mM Tris-HCl at a pH of 8, 1mM DTT, and 10% glycerol.
Stability
For optimal storage, keep at 4°C if the entire vial will be utilized within 2-4 weeks. For longer storage, freeze at -20°C. To further ensure stability during long-term storage, the addition of a carrier protein like HSA or BSA (0.1%) is recommended. Repeated freezing and thawing cycles should be avoided.
Purity
The purity of this product is greater than 95%, as assessed by SDS-PAGE.
Synonyms
Galectin-4, Gal-4, Lactose-binding lectin 4, L-36 lactose-binding protein, L36LBP, Antigen NY-CO-27, LGALS4, lectin galactoside-binding soluble 4, GAL4.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAYVPAPGYQ PTYNPTLPYY QPIPGGLNVG MSVYIQGVAS EHMKRFFVNF VVGQDPGSDV AFHFNPRFDG WDKVVFNTLQ GGKWGSEERK RSMPFKKGAA FELVFIVLAE HYKVVVNGNP FYEYGHRLPL QMVTHLQVDG DLQLQSINFI GGQPLRPQGP PMMPPYPGPG HCHQQLNSLP TMEGPPTFNP PVPYFGRLQG GLTARRTIII KGYVPPTGKS FAINFKVGSS GDIALHINPR MGNGTVVRNS LLNGSWGSEE KKITHNPFGP GQFFDLSIRC GLDRFKVYAN GQHLFDFAHR LSAFQRVDTL EIQGDVTLSY VQI.

Product Science Overview

Discovery and Structure

Galectin-4 was initially discovered as a soluble 17-kDa lectin in rat intestinal extracts by Leffler et al. in 1989 . Subsequent cDNA cloning revealed that it is a 36-kDa protein . The protein is mostly expressed in epithelial cells of the intestinal tract and is secreted extracellularly .

Function and Binding Specificity

Galectin-4 has been implicated in various biological processes, primarily due to its ability to bind specific carbohydrate structures. It has a unique carbohydrate binding specificity and interacts with O-linked sulfoglycans . For instance, it shows high-affinity binding to SO3–→3Galβ1→3GalNAc pyranoside . This specificity suggests that galectin-4 plays a role in cell adhesion and signaling.

Clinical Relevance

Galectin-4 is not only found throughout the gastrointestinal tract but is also present in well-differentiated breast and liver carcinomas . This makes it a potential biomarker for certain types of cancer. Additionally, its ability to agglutinate human red blood cells and bind to specific glycoproteins indicates its potential use in diagnostic and therapeutic applications .

Recombinant Production

Recombinant human galectin-4 is typically produced in E. coli and purified to high levels of purity . It is available in both carrier-free and carrier-containing formulations, depending on the intended application . The carrier-free version is recommended for applications where the presence of bovine serum albumin (BSA) could interfere, such as in certain cell culture or ELISA assays .

Storage and Stability

Recombinant human galectin-4 is usually lyophilized and should be reconstituted in sterile PBS. It is stable for up to 12 months when stored at -20 to -70°C and for shorter periods at 2 to 8°C after reconstitution .

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