Human Galectin-7 / LGALS7 Protein (GST Tag)

GAL7,LGALS7A

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Catalog Number	P12000-H09E
Organism Species	Human
Host	E. coli
Synonyms	GAL7,LGALS7A
Molecular Weight	The recombinant human LGALS7/GST chimera consists of 366 amino acids and has a predicted molecular mass of 41.8 kDa. It migrates as an approxiamtely 40 KDa band in SDS-PAGE under reducing conditions.
predicted N	Met
SDS-PAGE
Purity	> 92 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the human LGALS7 (P47929) (Ser 2-Phe 136) was fused with the GST tag at the N-terminus.
Bio-activity	Measured by its ability to agglutinate human red blood cells. The ED₅₀ for this effect is typically 0.01-0.05 μg/mL.
Research Area	Cancer \|Invasion microenvironment \|Adhesion molecule \|Cell adhesion \|Lectin \|Galectin \|
Formulation	Lyophilized from sterile PBS, pH 7.5 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	LGALS7, also known as Galectin-7, is a member of the galectins family. The galectins are a family of beta-galactoside-binding proteins. There are at least 14 identified members in this family. Galectins share similarities in the CRD (the carbohydrate recognition domain). They are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are implicated in modulating cell-cell and cell-matrix interactions. LGALS7 contains 1 galectin domain and is mainly expressed in stratified squamous epithelium. Galectin-7 could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. LGALS7 is a pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release.
Reference	Villeneuve C, et al. (2011) Mitochondrial proteomic approach reveals galectin-7 as a novel BCL-2 binding protein in human cells. Mol Biol Cell. 22(7):999-1013. Rondanino C, et al. (2011) Galectin-7 modulates the length of the primary cilia and wound repair in polarized kidney epithelial cells. Am J Physiol Renal Physiol. 301(3):F622-33. Masuyer G, et al. (2012) Inhibition mechanism of human galectin-7 by a novel galactose-benzylphosphate inhibitor. FEBS J. 279(2):193-202. Magnaldo T, et al. (1995) Galectin-7, a human 14-kDa S-lectin, specifically expressed in keratinocytes and sensitive to retinoic acid. Dev Biol. 168(2):259-71. Madsen P, et al. (1995) Cloning, expression, and chromosome mapping of human galectin-7. J Biol Chem. 270(11):5823-29.