The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.
The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.
|Rat LGALS1 ORF mammalian expression plasmid, C-GFPSpark tag||RG80248-ACG|
|Rat LGALS1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||RG80248-ACR|
|Rat LGALS1 ORF mammalian expression plasmid, C-Flag tag||RG80248-CF|
|Rat LGALS1 ORF mammalian expression plasmid, C-His tag||RG80248-CH|
|Rat LGALS1 ORF mammalian expression plasmid, C-Myc tag||RG80248-CM|
|Rat LGALS1 ORF mammalian expression plasmid, C-HA tag||RG80248-CY|
|Rat LGALS1 ORF mammalian expression plasmid, N-Flag tag||RG80248-NF|
|Rat LGALS1 ORF mammalian expression plasmid, N-His tag||RG80248-NH|
|Rat LGALS1 ORF mammalian expression plasmid, N-Myc tag||RG80248-NM|
|Rat LGALS1 ORF mammalian expression plasmid, N-HA tag||RG80248-NY|
|Rat LGALS1 natural ORF mammalian expression plasmid||RG80248-UT|
|Learn more about expression Vectors|
Galectin-1 (Gal-1, GAL1), is a member of the galectins, a family of animal lectins ranging from Caenorhabditis elegans to humans, which is defined by their affinity for beta-galactosides and by significant sequence similarity in the carbohydrate-binding site. It is a homodimer with a subunit molecular mass of 14.5 kDa, which contains six cysteine residues per subunit. The cysteine residues should be in a free state in order to maintain a molecular structure that is capable of showing lectin activity. This endogenous lectin widely expressed at sites of inflammation and tumour growth, has been postulated as an attractive immunosuppressive agent to restore immune cell tolerance and homeostasis in autoimmune and inflammatory settings. On the other hand, galectin-1 contributes to different steps of tumour progression including cell adhesion, migration and tumour-immune escape, suggesting that blockade of galectin-1 might result in therapeutic benefits in cancer. Several potential glycoprotein ligands for galectin-1 have been identified, including lysosome-associated membrane glycoproteins and fibronectin, laminin, as well as T-cell glycoproteins CD43 and CD45. Evidence points to Gal-1 and its ligands as one of the master regulators of such immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host-pathogen interactions.