Recombinant Human LGALS1 Protein (C-6His)

Name: Recombinant Human LGALS1 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1220NP
Availability: InStock

BL-1220NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Galectin-1 is produced by our E.coli expression system and the target gene encoding Ala2-Asp135 is expressed with a 6His tag at the C-terminus.
Accession	P09382
Synonym	Galectin-1; Gal-1; 14 kDa Laminin-Binding Protein; HLBP14; 14 kDa Lectin; Beta-Galactoside-Binding Lectin L-14-I; Galaptin; HBL; HPL; Lactose-Binding Lectin 1; Lectin Galactoside-Binding Soluble 1; Putative MAPK-Activating Protein PM12; S-Lac Lectin 1; LGALS1
Gene Background	Galectin-1 is a member of growing family of evolutionary conserved animal lectins. Galectin-1 is widely expressed in many cells and tissues. Galectins consists of a Galectin domain and two Beta-galactoside binding domains. Galectin-1 can binds LGALS3BP and interacts with CD2, CD3, CD4, CD7, CD43 and CD45. Galectin-1 may act as an autocrine negative growth factor which regulates apoptosis, cell proliferation and cell differentiation. In addition, Galectin-1 plays improtant roles in immunosuppressive and antiinflammatory properties.
Molecular Mass	15.78 KDa
Apmol Mass	15 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Citrate, 8% Trehalose, 4% Mannitol, 50mM NaCl, 1mM TCEP, 0.05% Tween 80, pH 4.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis.
Subcellular Location	Secreted, extracellular space, extracellular matrix. Cytoplasm. Secreted.
Database References	HGNC: 6561 OMIM: 150570 KEGG: hsa:3956 STRING: 9606.ENSP00000215909 UniGene: PMID: 30453284 Association of galectin-1 expression with eosinophilic infiltration of the tumor tissue in stomach and colorectal cancer was detected. PMID: 29926280 Study shows that recombinant Galectin-1 (Gal-1) could promote the differentiation and invasion of Trophoblast stem cells (TSCs), suggesting that some of Ishikawa cells secretion increase the expression of Gal-1 in TSCs during implantation, which then induced trophoblast differentiation and invasion in vitro. PMID: 28826368 In conclusion, these findings suggest that the serum levels of Gal-1, Gal-3, and Gal-9 may be associated with large artery atherosclerotic stroke. PMID: 28112232 High LGALS1 expression is associated with fibrosis in chronic pancreatitis and pancreatic cancer. PMID: 29328490 Pancreatic stellate cells promote cancer proliferation, migration, and invasion via Gal1-driven pathways. Gene-expression analyses of pancreatic tumor cells exposed to Gal1 reveal modulation of multiple regulatory pathways involved in tumor progression. PMID: 29615514 Studies indicate tumor-derived galectin-1, galectin-3 and galectin-9 in various cancers and anticancer therapies that target these molecules [Review]. PMID: 29389859 The expression level of galectin-1 affects survival in patients with glioblastoma multiforme treated with adjuvant radiotherapy PMID: 29378529 Results show that Galectin-1 teams up with Galectin-3 to induce inflammatory/pro-degradative gene signature in human chondrocytes affecting the progression of osteoarthritis. Also, Galectin-3 was found to induce a pro-degradative-inflammatory gene signature in human chondrocytes, teaming up with Galectin-1 in the pathogenesis of osteoarthritis. PMID: 27982117 We also found a subset of prostate cancer patient-derived xenografts and prostate cancer patient samples with mild HO-1 and low Gal-1 expression levels. These results highlight a novel function of a human-used drug as a means of boosting the antitumor response PMID: 28512172 Gal-1, Gal-3 and Gal-9 galectin expression was higher in the myenteric plexus ganglia of chagasic patients PMID: 28554765 Results have shown that Gal-1 in the farnesyl-bound form acquires the ability to form self-clusters, and the galactoside-binding pocket of Gal-1 in the FTS-bound form plays an important role in self-cluster formation. PMID: 27624845 Our findings support the introduction of galectin-1 as a reliable diagnostic marker for thyroid carcinomas. Its involvement in cell proliferation, migration, invasion and tumor growth also intimate functional involvement of galectin-1 in the progression of thyroid carcinoma, suggesting its potential as a therapeutic target PMID: 28677745 This study showed that obese children had significantly higher galectin-1 levels in proportion to fat mass in obese cases than those in healthy children, which may be interpreted as a compensatory increase in an attempt to improve glucose metabolism. PMID: 28728946 We further demonstrated using the NMR-based hydrogen-deuterium exchange (HDX) that lactose binding increases the exchange rates of residues located on the opposite side of the ligand-binding pocket for hGal1 and hGal8(NTD), indicative of allostery. Additionally, lactose binding induces significant stabilisation of hGal8(CTD) across the entire domain PMID: 28813004 our findings indicate that galectin-1 plays a pivotal role in the regulation of key processes in cancer cells, such as migration, invasion, and chemoresistance, by modulating FAK and ERK signaling and survivin level. PMID: 28415760 Gal-3 staining in the nucleus could be a new positive prognosticator for ovarian cancer. PMID: 28594391 Gal-1 may offer an additional therapeutic target linking anti-angiogenesis and immune checkpoint blockade. PMID: 28473314 markedly increased brain Gal-1 and S-nitrosylated Gal-1 both in scrapie-infected rodents and human prion diseases. PMID: 27211330 Gal-1 knockdown dramatically improved drug sensitivity of breast cancer by reducing P-glycoprotein (P-gp) expression via inhibiting the Raf-1/AP-1 pathway, providing a novel therapeutic target to overcome MDR in breast cancer. PMID: 28212576 the immunosuppressive microenvironment promoted by hepatic stellate cell-derived galectin-1 in hepatocellular carcinoma can be inhibited by miR-22 PMID: 27494859 Galectin-1 promotes invasion and epithelial mesenchymal transformation in gastric cancer cells via activation of the non-canonical Hh pathway in Gli-1 dependent manner. PMID: 27835885 Gal-1 level retained independent predictive influence on the risk of developing cGvHD PMID: 27214079 this study identified 131 Gal-3 and 15 Gal-1 interactors by galectin pulldown experiments combined with quantitative proteomics. PMID: 28576849 we found that galectin-1 was a novel modulator of MDR1 by proteomic analysis of a model system of leukemia cell lines PMID: 27050374 Data found Gal-1 to induce EMT and gastric cancer (GC) cell migration and invasion. Also, Gal-1 up-regulated Gli1 expression and beta1 integrin was responsible for Gal-1-induced Gli1 expression and EMT. PMID: 27836001 Galectin-1-driven production of SDF-1 in pancreatic stellate cells through activation of NF-kappaB promotes metastasis in pancreatic ductal adenocarcinoma. PMID: 28336327 Gal-1 expression by MM cells was upregulated in hypoxic conditions and stable knockdown of hypoxia inducible factor-1alpha significantly downregulated its expression PMID: 27311934 Gal1 may be a useful marker for determining whether morphologic changes in oral cells are reactive or neoplastic PMID: 26980012 The aim of this study was to analyze the syncytium formation abilities of BeWo cells that were gal-1 silenced. PMID: 26418280 Studies provide evidence that galectin-1 belongs to the group of potential pathogenic molecules in systemic lupus erythematosus. [review] PMID: 28100106 an intact dimer interface of Gal-1 is required for it to positively regulate H-rasG12V nanoclustering, but negatively K-rasG12V nanoclustering. PMID: 27087647 Our results suggest that Gal-1 and ASPP2 functionally compete in nanocluster for active Ras on the plasma membrane. ASPP2 dominates the biological outcome, thus switching from a Gal-1 supported growth-promoting setting to a senescence inducing and stemness suppressive program in cancer cells. Our results support Ras nanocluster as major integrators of tumour fate decision events. PMID: 27437940 Galectin-1 and Galectin-3 are novel-binding partners for human FVIII. Gal-1 binding can influence the procoagulant activity of FVIII. PMID: 27013611 Proteomics of the interstitial fluid in subcutaneous adipose tissue in vivo identified a novel adipokine, galectin-1, with a potential role in the pathophysiology of type 2 diabetes. PMID: 27282870 Suggest that galectin-1 is a protective factor against the development of digital vasculopathy in systemic sclerosis. PMID: 24517166 This study demonstrated that TLR-mediated PI3K activation modulated the invasion and metastasis of ovarian cancer through the production of galectin-1. PMID: 28350104 Gal-1-regulated carcinoma-associated fibroblast activation promotes breast cancer cell metastasis by upregulating MMP-9 expression. PMID: 27025601 It is a beta-galactose-binding animal lectin and known to be distributed throughout the body. PMID: 27590897 Our functional analyses of galectin-1 in urinary bladder urothelial carcinoma provided novel insights into the critical role of galectin-1 in tumor progression and invasion. These results revealed that silencing the galectin-1-mediated MAPK signaling pathway presented a novel strategy for bladder cancer therapy. PMID: 27440446 the TLR4/Gal-1 signaling pathway regulates lactate-mediated EMT processes through the activation of ADAM10 and ADAM17 in colon cancer cells. PMID: 27837433 These findings suggest that Gal-1 plays an important role in immune escape of gingival squamous cell carcinoma cells, and Gal-1 expression level may be a useful clinicopathological prognostic marker for this cancer. PMID: 28108653 Galectin-1 gene silencing would improve the sensitivity of A549/DDP cells to cisplatin in vivo and in vitro. PMID: 27392028 In this study, gal-1, -2, -3 and -13 were investigated systematically in the trophoblast and decidua compartment of intrauterine growth restriction (IUGR) placentas and normal third trimester control placentas and stratified by fetal gender and gestational age. Gal-1 Expression Shows No Significant Changes in IUGR Placentas in Villous Trophoblasts. PMID: 27070577 Galectin-1 overexpression activates the FAK/PI3K/AKT pathway by upregulating expression of alphavbeta3 integrin, leading to enhanced hepatocellular carcinoma invasion via epithelial-mesenchymal transition and sorafenib resistance. PMID: 27100895 results show that HELLP syndrome is associated with increased circulating levels of gal-1 PMID: 26956510 The integrative analysis of galectins(Gal-1, -3, -4, -9) discriminated IBD from other intestinal inflammatory conditions and could be used as potential mucosal biomarker PMID: 26891020 Galectin-1 was undetectable in normal and ulcerative colitis colonic epithelium, while galectin-2, galectin-3, and galectin-4 were strongly expressed. PMID: 26885508 Tumor-driven, unremitting expression of Satb1 in activated Zbtb46+ inflammatory dendritic cells that infiltrate ovarian tumors results in an immunosuppressive phenotype characterized by increased secretion of tumor-promoting Galectin-1 and IL-6. PMID: 26876172 Epithelial immunostaining for galectin-1 tended to be elevated in fallopian tubes from women with ectopic pregnancy. PMID: 26359845

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.