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Recombinant Mouse Galectin-2, CF (50 ug)
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咨询Recombinant Mouse Galectin-2 Protein, CF Summary
- R&D Systems HEK293-derived Recombinant Mouse Galectin-2 Protein (8579-GA)
- Quality control testing to verify active proteins with lot specific assays by in-house scientists
- All R&D Systems proteins are covered with a 100% guarantee
Product Specifications
Ser2-Glu130
Analysis
Product Datasheets
8579-GA
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
8579-GA
| Formulation | Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl, EDTA, DTT and Trehalose. |
| Reconstitution | Reconstitute at 400 μg/mL in water. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: Galectin-2
Galectin-2 is an approximately 14 kDa, homodimeric carbohydrate-binding protein of the S-type lectin family (1, 2). Like other prototype Galectins, Galectin-2 consists of a single carbohydrate-recognition domain (CRD) (3). Mouse Galectin-2 shares 86% and 66% amino acid sequence identity with rat and human Galectin-2, respectively. Galectin-2 is primarily expressed in the digestive tract and skin of mice (4-6). It can be S-nitrosylated with S-nitrosoglutathione in mouse gastric mucosa (7).
S-nitrosylation prevents Galectin-2 inactivation by hydrogen peroxide, suggesting that this modification protects Galectin-2 function against oxidative stress (8). Galectin-2 appears to have a role in immune responses. Galectin-2 mRNA and protein levels are down-regulated following infection with H. felis (9). Additionally, Galectin-2 treatment has been shown to reduce MHC class I-restricted immune responses and ameliorate acute and chronic experimental colitis in mice by inducing apoptosis of T cells (6, 10). Galectin-2 may also play a role in cancer since circulating levels of human Galectin-2 are elevated in colon and breast cancer patients (11).
- Hokama, A. et al. (2008) World J. Gastroenterol. 14:5133.
- Barondes, S.H. et al. (1994) Cell 76:597.
- Hirabayashi, J. and K. Kasai (1993) Glycobiology 3:297.
- Nio, J. et al. (2005) J. Histochem. Cytochem. 53:1323.
- Nio-Kobayashi, J. et al. (2009) J. Histochem. Cytochem. 57:41.
- Loser, K. et al. (2009) J. Immunol. 182:5419.
- Ohtake, K. et al. (2009) J. Proteomics 72:750.
- Tamura, M. et al. (2015) Biochem. Biophys. Res. Commun. 457:712.
- Takaishi, S. and T.C. Wang (2007) Cancer Sci. 98:284.
- Paclik, D. et al. (2008) J. Mol. Med. 86:1395.
- Chen, C. et al. (2014) Br. J. Cancer 110:741.
Background: Galectin-2
Galectin-2 is an approximately 14 kDa, homodimeric carbohydrate-binding protein of the S-type lectin family (1, 2). Like other prototype Galectins, Galectin-2 consists of a single carbohydrate-recognition domain (CRD) (3). Mouse Galectin-2 shares 86% and 66% amino acid sequence identity with rat and human Galectin-2, respectively. Galectin-2 is primarily expressed in the digestive tract and skin of mice (4-6). It can be S-nitrosylated with S-nitrosoglutathione in mouse gastric mucosa (7).
S-nitrosylation prevents Galectin-2 inactivation by hydrogen peroxide, suggesting that this modification protects Galectin-2 function against oxidative stress (8). Galectin-2 appears to have a role in immune responses. Galectin-2 mRNA and protein levels are down-regulated following infection with H. felis (9). Additionally, Galectin-2 treatment has been shown to reduce MHC class I-restricted immune responses and ameliorate acute and chronic experimental colitis in mice by inducing apoptosis of T cells (6, 10). Galectin-2 may also play a role in cancer since circulating levels of human Galectin-2 are elevated in colon and breast cancer patients (11).
- Hokama, A. et al. (2008) World J. Gastroenterol. 14:5133.
- Barondes, S.H. et al. (1994) Cell 76:597.
- Hirabayashi, J. and K. Kasai (1993) Glycobiology 3:297.
- Nio, J. et al. (2005) J. Histochem. Cytochem. 53:1323.
- Nio-Kobayashi, J. et al. (2009) J. Histochem. Cytochem. 57:41.
- Loser, K. et al. (2009) J. Immunol. 182:5419.
- Ohtake, K. et al. (2009) J. Proteomics 72:750.
- Tamura, M. et al. (2015) Biochem. Biophys. Res. Commun. 457:712.
- Takaishi, S. and T.C. Wang (2007) Cancer Sci. 98:284.
- Paclik, D. et al. (2008) J. Mol. Med. 86:1395.
- Chen, C. et al. (2014) Br. J. Cancer 110:741.