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Validated All-in-One™ qPCR Primer for LGALS1(NM_002305.3) Search again
Product ID:
HQP010588
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
GAL1, GBP
Gene Description:
galectin 1
Target Gene Accession:
NM_002305.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. This gene product may act as an autocrine negative growth factor that regulates cell proliferation. [provided by RefSeq].
Gene References into function
- Galectin-1 possesses a cell growth-inhibitory site which is not part of the beta-galactoside binding site: a surface loop, comprising amino acid residues 25-30 and joining two internal beta-strands, forms part of the growth-inhibitory site.
- overexpressed in nasal polyps exposed to budesonide
- Galectin-1 has the ability to activate NADPH oxidase in neutrophils that have been exposed to inflammatory mediators and stress during extravasation in vivo.
- Receptor tyrosine phosphatase, CD45 binds galectin-1 but does not mediate its apoptotic signal in Jurkat cells
- Galectin-1 expression of human glioblastoma xenografts from the brains of nude mice revealed a higher level of galectin-1 in invasive areas. Galectin-1 enhances migration of tumor astrocytes and, therefore, their biological aggressiveness.
- Galectin-1 plays a role in binding to the pre-B cell receptor and forms a synapse
- galectin-1 is likely to be involved in the extracellular matrix assembly affecting incorporation of some components important for smooth muscle cell behavior
- galectin-1 induces surface exposure of phosphatidylserine and phagocytic recognition of leukocytes without inducing apoptosis
- Endogenous Gal-1 may be part of novel anti-inflammatory loop in which endothelium is the source of protein and migrating neutrophils the target for its anti-inflammatory action.
- Galectin-1 interacts with beta-1 subunit of integrin
- Galectin-1 activation in human hepatocellular carcinoma involves methylation-sensitive complex formations at the transcriptional upstream and downstream elements
- examined ability of stromal cells secreting galectin-1 to kill T cells. Although the stromal cells synthesized abundant galectin-1, the most of the galectin-1 remained bound to the cell surface, and stromal cell-associated galectin-1 killed bound T cells
- galectin-1 induces astrocyte differentiation and strongly inhibits astrocyte proliferation, and then the differentiated astrocytes greatly enhance their production of BDNF which may be a new mechanism for preventing neuronal loss after injury
- Galectin-1 plays a role in both cell-matrix interactions and the inhibition of Colo201 tumor cell proliferation in vitro; galectin-1 expressed in cells may be associated with apoptosis.
- Gal-1 signaling in activated T cells constitutes an important mechanism of tumor-immune escape
- Galectin-1-induced cell death proceeds via a caspase-independent pathway that involves a unique pattern of mitochondrial events.
- dGal-1 functions as a dimer to recognize terminal N-acetyllactosamine units on extended poly-N-acetyllactosamines on cell surfaces
- Gal-1 induces mitochondrial coalescence, budding, and fission accompanied by an increase and/or redistribution of fission-associated molecules
- Regulated expression of galectin-1 during T-cell activation involves Lck and Fyn kinases and signaling through MEK1/ERK, p38 MAP kinase and p70 S6 kinase.
- map of polymorphic sites within an 11-kb region containing the gene, including 14 SNPs and two genetic variations of other types detected in a Japanese population sample
- galectin-1 can cross-link HIV-1 and target cells and promote a firmer adhesion of the virus to the cell surface
- findings suggest a possible role for galectin-1 in anchoring microbial and cancer cells known to be rich in T antigen, in high serum IgA1 turn over and in tissue sequestering of IgA1 immune complexes
- galectin 1 may have a role in immunological functions of human mesenchymal stem cells
- Transient Ca(2+) fluxes contribute to a sustained redistribution of phosphatidylserines on neutrophils activated with fMLP and dimeric galecstin-1.
- gal-1 binds to specific N-glycans on Nipah virus (NiV) glycoproteins and aberrantly oligomerizes NiV-F and NiV-G, indicating a mechanism for fusion inhibition.
- galectin-1 shows apoptotic potential in both the epithelial tumour cell lines examined only with additional stress stimuli
- stable inhibition of galectin-1 expression alters the expression of a number of genes that either directly or indirectly influence adhesion, motility and invasion of human glioblastoma cells.
- data indicate that IL-12 down-regulates the expression of both gal-1 and CD7 in the microsomal fraction of peripheral blood mononuclear cells and cord blood CD4(+) cells
- HSV-1 may use galectin-1 as a weapon to kill activated T cells and evade specific immune responses
- ANXA1 and Gal-3 changed in their content and localization when neutrophils adhere to endothelia. In contrast, a decrease in the total amounts of Gal-1 was detected in migrated compared to non-migrated neutrophils.
- Results demonstrate that Galectin-1 is an endogenous factor that promotes the proliferation of neural stem cells in the
- Murine dendritic cells engineered to express transgenic galectin-1 in vivo represent a novel tool for differential control of the afferent and efferent arms of the T cell response.
- Galectin-1 binds to and activates monocyte-derived dendritic cells (MDDC) to become phenotypically and functionally mature DCs capable of enhanced chemotactic migration in an in vitro extracellular matrix model.
- Galectin 1 binds to VLA-5 integrins on bone marrow stromal cells and to VLA-4, VLA-5, and alpha4beta7 integrins on pre-B cells, forming a homogeneous lattice at the contact area between bone marrow pre-B and stromal cells.
- Galectin 1 induces surface phosphatidylserine exposure in a carbohydrate-dependent fashion in activated, but not resting, human neutrophils and in several leukocyte cell lines.
- galectin-1 regulates tumor angiogenesis and is a target for angiostatic cancer therapy
- galectin-1, is overexpressed in regulatory T cells, and that expression is increased after activation
- galectin-1 expression on stromal cells increases with the histopathologic grade of cervical tissues
- Our results provide evidence of a novel unrecognized role for galectin-1 in the control of monocyte/macrophage physiology with potential implications at the crossroad of innate and adaptive immunity.
- Galectin-1 was found to be negatively regulated by transfection with TP53 in a glioblastoma cell line.
- roles of galectin-1 in cancer-associated stroma and in tumor immune privilege
- galectin-1 has a role in recurrence in laryngeal squamous cell carcinomas
- Galectin-1 mediated suppression of Epstein-Barr virus specific T-cell immunity is associated with Hodgkin lymphoma
- investigated the solvation properties of the carbohydrate recognition domain of galectin-1 by means of molecular dynamics simulations
- p16INK4a modulates glycomic profile and galectin-1 expression to increase susceptibility to carbohydrate-dependent induction of anoikis in pancreatic carcinoma cells
- Data show that galectin-1, an endogenous lectin produced by arterial cells, binds lipoprotein(a) [Lp(a)] in situ.
- This study sheds light on the molecular mechanisms whereby betaGBP can control cell proliferation and, by extension, may potentially control tumorigenesis by controlling PI3K.
- galectin-1 has a role in O-glycosylation regulation of LNCaP prostate cancer cell susceptibility to apoptosis
- MUC1, TF and galectin might have important roles in endometrial pathogenesis and malignant transformation.
- Results suggest a possible role for galectin-1 in the pathogenesis of primary glomerulopathies in children as a kind of podocyte-related self-protective activity and probably involvement of epithelial cells of Bowman's capsule in inflammatory processes.
- galectin-1, an endogenous lectin with immunoregulatory properties, plays a key role in human platelet activation and function.
- X-ray diffraction data enabled assignment of unit-cell parameters for crystals grown under 2 conditions, one belongs to a tetragonal crystal system and the other was determined as monoclinic P2(1), representing 2 new crystal forms of human galectin-1.
- Gal-1 can directly bind to NRP1 on endothelial cells, and can promote the NRP1/VEGFR-2-mediated signaling pathway as well as NRP1-mediated biological activities.
- Galectin-9 and galectin-1 require different glycan ligands and glycoprotein receptors to trigger T cell death.
- Gal-1 and Gal-3 induce differential responses in T cells and neutrophils; Gal-1 induces IL-10 production and attenuates interferon-gamma production in activated T cells.
- An association was seen between the level of presence of galectins-1 and -7 and neoplastic progression of hypopharyngeal and laryngeal squamous cell carcinomas.
- These results suggest that decreasing Gal-1 expression (e.g. through brain delivery of nonviral infusions of anti-Gal-1 siRNA in patients) can represent an additional therapeutic strategy for glioblastoma.
- Gal1 and c-Jun serve as diagnostic biomarkers that delineate classical Hodgkin lymphoma and anaplastic large cell lymphoma from other lymphomas with shared morphologic and/or molecular features.
- Placental galectin-1 mRNA expression was significantly higher in severe preeclampsia than in controls; Trophoblasts had the most intense galectin-1 immunostaining
- Internalization of Gal-1 depends on its lectin activity and follows dual pathways involving clathrin-coated vesicles and raft-dependent endocytosis.
- Serum levels of galectins-1 and -3 are relatively high in patients with thyroid malignancy but there is considerable overlap in serum galectin-3 concentrations between those with benign and malignant nodular thyroid disease
- Dimeric galectin-1 (dGal-1) preferentially binds to and signals through glycoproteins containing complex-type N-glycans in at least some leukocyte subsets
- carbohydrate-binding and the splicing activities of Gal1 can be dissociated and therefore, saccharide-binding, per se, is not required for the splicing activity
- Galectin-1 appears to modulate migration and invasion in human glioma cell lines and may play a role in tumor progression and invasiveness in human gliomas
- Galectin-1 decreases Smad3-complex from binding to the SBE, down-regulating transcription of COL1A2 in TGF-beta1-stimulated renal epithelial cells.
- The structure of cysteine-less Gal-1 is almost identical to that of wild-type human Gal-1
- Galectin-1 plays a role in promoting immunoglobulin production during plasma cell differentiation.
- GnT-Vb-mediated glycosylation of RPTPbeta promotes galectin-1 binding and RPTPbeta levels of retention on the cell surface.
- These studies identify galectin-1 as a cross-regulatory cytokine that selectively antagonizes Th1 survival, while promoting TCR-induced Th2 cytokine production.
- secretion of galectin-1 by dNKs and other decidual cells contributes to the generation of an immune-privileged environment at the maternal-fetal interface
- These data suggest that HTLV-I Tax increases galectin-1 expression and that this modulation could play an important role in HTLV-I infection by stabilizing both cell-to-cell and virus-cell interactions.
- Use of ultraviolet resonance Raman spectroscopy and calculated water radial distribution functions show that, while no large structural changes in Gal-1 protein follow lactose binding, substantial solvent reorganization occurs.
