Galectin-8 Protein, Rat (GST)

Galectin-8 belongs to the family of animal lectins that bind to different glycoconjugates. Galectin-8 inhibits MTOR and AMPK signaling pathways to induce autophagy in response to lysosomal damage. Galectin-8 is highly expressed in a variety of tumors. Galectin-8 Protein, Rat (GST) is the recombinant rat-derived Galectin-8 protein, expressed by E. coli , with N-GST labeled tag. The total length of Galectin-8 Protein, Rat (GST) is 316 a.a., with molecular weight of ~63.2 kDa.

Galectin-8 belongs to the family of animal lectins that bind to different glycoconjugates. As a secreted protein, Galectin-8 is found in body fluids or the serum of patients with breast cancer and those with colon cancer. Extracellular Galectin-8 promotes cell adhesion by binding to cell adhesion molecules such as integrins CD44, CD166 and Podoplanin. Galectin-8 performs its intracellular function by marking the vacuoles invaded by pathogens to be destroyed by autophagy. Galectin-8 inhibited MTOR and AMPK in response to lysosomal injury induced autophagy in membrane disturbances. Galectin-8 is highly expressed in a variety of tumors^[1][2][3].

Rat

E. coli

N-GST

Q6IN24 (M1-W316)

116641  [NCBI]

Approximately 63.2 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.