LGALS1 Human

Galectin-1 Human Recombinant
Cat. No.
BT9991
Source
Escherichia Coli.
Synonyms
Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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

LGALS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids and having a molecular mass of 14.7kDa.
The LGALS1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Galectins are a family of proteins that bind to beta-galactosides and are involved in regulating interactions between cells and between cells and the extracellular matrix. Galectin-1, a member of this family, acts as an autocrine negative growth factor, regulating cell proliferation, apoptosis, and differentiation. It achieves this by binding to cell surface receptors such as CD45, CD3, and CD4, inhibiting the activity of CD45 protein phosphatase and consequently, the dephosphorylation of lyn kinase. Galectin-1 and its binding partners play a crucial role in immune regulation, influencing T-cell homeostasis, survival, immune disorders, inflammation, allergies, and host-pathogen interactions. The presence of elevated levels of Galectin-1 in tumors or their surrounding tissues is often indicative of malignant progression, potentially contributing to metastasis, local tissue invasion, and tumor immune evasion. Interestingly, oxidized Galectin-1 plays a significant role in central nervous system regeneration following injury. These properties suggest that targeted delivery or overexpression of Galectin-1 could be a promising therapeutic strategy for inflammation-related diseases, neurodegenerative conditions, and muscular dystrophies. Conversely, inhibiting Galectin-1 expression could be a valuable approach to combat cancer progression. Therefore, Galectin-1 represents a promising molecular target for developing novel therapeutic interventions. Notably, there is a high degree of homology (88%) between human and mouse Galectin-1.
Description
Recombinant human LGALS1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 135 amino acids, resulting in a molecular weight of 14.7 kDa. The purification of LGALS1 is achieved through proprietary chromatographic techniques.
Physical Appearance
White, sterile-filtered powder obtained by lyophilization (freeze-drying).
Formulation
The Galectin-1 protein was lyophilized from a 1 mg/ml solution buffered with 10 mM sodium phosphate at a pH of 7.5.
Solubility
It is recommended to reconstitute the lyophilized LGALS1 in sterile, 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Stability
Lyophilized recombinant Galectin-1, though stable at room temperature for up to 3 weeks, should ideally be stored in a dry environment below -18°C. Upon reconstitution, Galectin-1 should be stored at 4°C for short-term use (2-7 days). For long-term storage, it is recommended to store it below -18°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
The purity is determined to be greater than 95.0% using SDS-PAGE analysis.
Biological Activity
The biological activity of human Galectin-1 is assessed based on its ability to induce chemotaxis in human THP-1 cells. Detectable activity is observed at concentrations starting from 100 ng/ml, corresponding to a specific activity of 1.0 x 10^4 units/mg.
Protein Content
Protein content is determined using UV spectroscopy at 280 nm, employing an absorbance value of 0.59 as the extinction coefficient for a 0.1% (1 mg/ml) solution. This value is calculated using the PC GENE computer analysis program, which analyzes protein sequences (IntelliGenetics).
Synonyms
Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.
Source
Escherichia Coli.
Amino Acid Sequence
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD.

Product Science Overview

Structure and Expression

Galectin-1 is a “proto-type” galectin, meaning it consists of a single polypeptide chain with one carbohydrate recognition domain (CRD) that can dimerize . The human Galectin-1 protein is encoded by the LGALS1 gene and is expressed in various tissues, including the endometrial stromal cells throughout the menstrual cycle .

Biological Functions

Galectin-1 exhibits broad anti-inflammatory and pro-resolving activities by targeting multiple immune cell types. It acts as a resolution-associated molecular pattern (RAMP) by counteracting the synthesis of pro-inflammatory cytokines, inhibiting neutrophil trafficking, targeting eosinophil migration and survival, and suppressing mast cell degranulation . Additionally, Galectin-1 controls T cell and B cell compartments by modulating receptor clustering and signaling, thus serving as a negative-regulatory checkpoint that reprograms cellular activation, differentiation, and survival .

Therapeutic Potential

Due to its regulatory functions, Galectin-1 has been studied for its potential therapeutic applications in various conditions, including acute and chronic inflammation, autoimmune diseases, allergic inflammation, pregnancy, cancer, and infections . Therapeutic strategies aimed at targeting Galectin-1–glycan interactions could help overcome cancer immunosuppression and reinforce antimicrobial immunity, while stimulation of Galectin-1–driven immunoregulatory circuits could mitigate excessive inflammation .

Recombinant Human Galectin-1

Recombinant human Galectin-1 is typically expressed in and purified from E. coli . It is used in various research applications to study its biological functions and therapeutic potential. The recombinant protein is often formulated with or without carrier proteins like Bovine Serum Albumin (BSA) to enhance stability and shelf-life .

Applications in Research

Recombinant human Galectin-1 is widely used in research to investigate its role in immune regulation, cell signaling, and disease mechanisms. It has been shown to induce apoptosis of activated T cells and leukemic T cell lines, making it a valuable tool in cancer research .

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