DESCRIPTION
Source E. coliderived
Ala2Thr323
Accession # BAA31542
Nterminal
Sequence
Analysis
Ala2
Structure / Form Monomer
Predicted Molecular
Mass
35.8 kDa
SPECIFICATIONS
SDSPAGE
34 kDa, reducing conditions
Activity Measured by its ability to induce apoptosis of Jurkat human acute T cell leukemia cells. Lu, L.H. et al. （2007） J. Biochem. 141:157.
The ED50 for this effect is typically 15
ug/mL.
Measured by its ability to agglutinate human red blood cells. Hadari, Y.R. et al. （2000） J. Cell Sci. 113:2385.
The ED50 for this effect is typically 2.5-12.5 μg/mL.
Endotoxin Level <1.0 EU per 1 μg of the protein by the LAL method.
Purity >95%, by SDSPAGE
under reducing conditions and visualized by silver stain.
Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl, EDTA, DTT and Trehalose. See Certificate of Analysis for details.
PREPARATION AND STORAGE
Reconstitution Reconstitute at 100 μg/mL in water.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediay at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freezethaw
cycles.
l 12 months from date of receipt, 20
to 70
°C as supplied.
l 1 month, 2 to 8 °C under sterile conditions after reconstitution.
l 3 months, 20
to 70
°C under sterile conditions after reconstitution.
BACKGROUND
Galectins comprise a family of multifunctional carbohydratebinding
proteins with specificity for N-acetyllactosaminecontaining
glycoproteins. At least 14
mammalian Galectins share structural similarities in their carbohydrate recognition domains （CRD）, forming three groups: prototype （one CRD）, tandemrepeat
（two
CRDs）, and chimeric （one CRD, unique N-terminus） （1, 2）. Full length Galectin 9
is a widely expressed 39 kDa tandemrepeat
Galectin that contains two CRDs
connected by a linker region （3）. Progressive deletion within the linker region generates a 36 kDa isoform, also known as Ecalectin or UAT, as well as a 35 kDa
isoform （4）. This recombinant protein corresponds to the Ecalectin isoform of human Galectin9
and shares 70% and 73% aa sequence identity with the corresponding
regions of mouse and rat Galectin9,
respectively. Galectin9
exhibits a wide range of activities. All three isoforms function as eosinophil chemoattractants （5, 6）. This
activity is destroyed by thrombinmediated
cleavage within the linker region of the long isoform, although the Ecalectin isoform is resistant to thrombin （7）. Galectin9
binds to carbohydrate moieties of IgE, thereby preventing immune complex formation, mast cell degranulation, and asthmatic and cutaneous anaphylaxis reactions
（8）. Independent of its lectin properties, Galectin9
induces the maturation of dendritic cells which promote Th1 polarization （9）. Galectin9
induces cellular apoptosis in
part by direct binding to TIM3
（10, 11）. Its interaction with TIM3
inhibits Th1 cell and CD8+ cytotoxic T cell responses and also promotes regulatory T cell
differentiation and activity （11, 12）. Galectin9
suppresses tumor cell metastasis by interfering with the associations between hyaluronic acid and CD44 and between
VCAM1
and Integrin α4β1 （13）. The Ecalectin isoform （UAT; urate transporter） can also be expressed as an integral membrane protein and mediate the cellular efflux
of urate （14）.
References:
1. Yang, RY
. et al. （2008） Expert Rev. Mol. Med. 10:e17.
2. Elola, M. T. et al. （2007） Cell. Mol. Life Sci. 64:1679.
3. Tureci, O. et al. （1997） J. Biol. Chem. 272:6416.
4. Chabot, S. et al. （2002） Glycobiology 12:111.
5. Matsumoto, R. et al. （2002） J. Immunol. 168:1961.
6. Sato, M. et al. （2002） Glycobiology 12:191.
7. Nishi, N. et al. （2006） Glycobiology 16:15C.
8. Niki, T. et al. （2009） J. Biol. Chem. 284:32344.
9. Dai, S.Y
. et al. （2005） J. Immunol. 175:2974.
10. Seki, M. et al. （2007） Arthritis Rheum. 56:3968.
11. Zhu, C. et al. （2005） Nat. Immunol. 6:1245.
12. Sehrawat, S. et al. （2010） PloS Pathogens 6:e1000882.
13. Nobumoto, A. et al. （2008） Glycobiology 18:735.
14. LealPinto,
E. et al. （2002） Am. J. Physiol. Renal Physiol. 283:F150.