Species Reactivity
Human
Specificity
Detects human Galectin-3 in direct ELISAs and Western blots. In direct ELISAs, approximately 50% cross-reactivity with recombinant mouse Galectin-3 is observed and less than 1% cross-reactivity with recombinant human (rh) Galectin-1, rhGalectin-2, rhGalectin-4, rhGalectin-7, and rhGalectin-8 is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
E. coli-derived recombinant human Galectin‑3
Ala2-Ile250
Accession # P17931.5
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Label
Unconjugated
Western Blot
0.1 µg/mL
See below
Simple Western
10 µg/mL
See below
Immunohistochemistry
5-15 µg/mL
See below
CyTOF-ready
Ready to be labeled using established conjugation methods. No BSA or other carrier proteins that could interfere with conjugation.
Intracellular Staining by Flow Cytometry
2.5 µg/106 cells
Human PBMCs fixed with paraformaldehyde and permeabilized with saponin
Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
Shipping
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. - 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
- Rabinovich, A. et al. (2002) Trends in Immunol. 23:313.
- Rabinovich, A. et al. (2002) J. Leukocyte Biology 71:741.
- Hughes, R.C. (2001) Biochimie 83:667.
- R&D Systems Cytokine Bulletin; Summer 2002.
- Gorski, J.P. et al. (2002) J. Biol. Chem. 277:18840.
Entrez Gene IDs:
3958 (Human); 16854 (Mouse)
Alternate Names:
AGE-R3; Carbohydrate-binding protein 35; CBP 35,35 kDa lectin; CBP35; GAL3; Gal-3; galactin-3; Galactose-specific lectin 3; Galactoside-binding protein; GALBPCBP35; Galectin3; Galectin-3; GALIG; IgE-binding protein; L29; L31; L-31; Laminin-binding protein; Lectin L-29; lectin, galactoside-binding, soluble, 3; LGALS2; LGALS3; Mac-2 antigen; Mac-2; MAC2GAL3
Background:
The galectins constitute a large family of carbohydrate-binding proteins with specificity for N-acetyl-lactosamine-containing glycoproteins. At least 14 mammalian galectins, which share structural similarities in their carbohydrate recognition domains (CRD), have been identified. The galectins have been classified into the prototype galectins (-1, -2, -5, -7, -10, -11, -13, -14), which contain one CRD and exist either as a monomer or a noncovalent homodimer; the chimera galectins (Galectin-3) containing one CRD linked to a nonlectin domain; and the tandem-repeat galectins (-4, -6, -8, -9, -12) consisting of two CRDs joined by a linker peptide. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified non-classical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell-surface glycoproteins (1-4). Galectin-3, also known as Mac-2, L29, CBP35, andepsilon BP, is a chimera galectin that has a tendency to dimerize. Besides the soluble protein, alternatively spliced forms of chicken Galectin-3 containing a transmembrane-spanning domain and a leucine zipper motif have been reported. Galectin-3 is expressed in tumor cells, macrophages, activated T cells, osteoclasts, epithelial cells, and fibroblasts. It binds various matrix glycoproteins including laminin, fibronectin, LAMPS, 90K/Mac-2BP, MP20, and CEA. Galectin-3 promotes cell growth and proliferation for many cell types. Galectin-3 acts intracellularly to prevent apoptosis. Depending on the cell types, Galectin-3 exhibits pro- or anti-adhesive properties. Galectin-3 has proinflammatory activities in vitro and in vivo. It induces pro-inflammatory and inhibits Th2 type cytokine production. Galectin-3 chemoattracts monocytes and macrophages. It activates and degranulates basophils and mast cells. Elevated circulating levels of Galectin-3 has been show to correlate with the malignant potential of several types of cancer, suggesting that Galectin-3 is also involved in tumor growth and metastasis. Human and mouse Galectin-3 shares approximately 80% amino acid sequence similarity (1-5).
R&D Systems位于美国的明尼苏达州,一直致力于生物制品的开发与生产。公司成立之初主要生产用于医院及临床应用的血控品。1997年,公司推出第一个产品--富血小板血浆质控品;1981年,公司成为全球第二家生产含血小板全血控品的供应商。40多年的发展中,R&D Systems仍持续开发各种血控品产品。
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天然蛋白类产品的成功推广,加速了R&D Systems在细胞因子市场的开拓。公司于1985年形成Growth Factor事业部(现Biotechnology事业部)。Biotechnology事业部的目标是生产和营销重组人细胞因子。与天然来源提取蛋白相比较,DNA重组技术生产的蛋白产品其成本更低,产量更高,完全摆脱原料的限制。1989年,Biotechnology事业部开始开发抗细胞因子的单克隆和多克隆抗体,并于1990年开发了第一个ELISA试剂盒。
2014年2月10日,R&D Systems的母公司宣布命名为Bio-Techne. Bio-Techne旗下包括R&D Systems, Novus Biologicals, BiosPacific, Tocris Bioscience, Boston Biochem和Bionostics。