Product Catalog



> Recombinant Protein > E.Coli Expressed > Rat LGALS1 / Galectin-1 Protein (Native) Rat LGALS1 / Galectin-1 Protein (Native)
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 80248-RNAE |
|
YES |
|
![]() |
|
Lectin, galactoside-binding, soluble, 1 Protein Datasheet
LGALS1 / Galectin-1 Protein Price Inquiry ( Available Sizes )
- 500μg: Inquiring Price;
- ≥1mg Bulk: Inquiring Price
LGALS1 / Galectin-1 Protein Product Information
| Synonym : | Galectin1, Lgals1 |
| Protein Construction: | A DNA sequence encoding the rat Galectin1 (P11762) (Ala2-Glu135) was expressed and purified. |
| Source: | Rat |
| Expression Host: | E.coli |
LGALS1 / Galectin-1 Protein QC Testing
| Purity: | > 95 % as determined by SDS-PAGE | SDS-PAGE:![]() LGALS1 / Galectin-1 protein |
| Endotoxin: | Please contact us for more information. | |
| Stability: | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal: | Ala 2 | |
| Molecular Mass: |
The recombinant rat Galectin1 consists of 135 amino acids and has a predicted molecular mass of 14.9 kDa. As a result of glycosylation, the apparent molecular mass of the recombinant protein is approximately 16 kDa in SDS-PAGE under reducing conditions. |
|
| Formulation: | Lyophilized from sterile PBS, pH 7.5.
|
LGALS1 / Galectin-1 Protein Usage Guide
| Storage: | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution: | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
LGALS1 / Galectin-1 Protein Related Products & Topics
Related Areas:
Cardiovascular>>Angiogenesis>>Adhesion Molecules in Angiogenesis>>Galectin-1
Cancer>>Angiogenesis>>Adhesion Molecules in Angiogenesis>>Galectin-1
Immunology>>Adhesion Molecule>>Lectin>> Galectin-1
Proteins:
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Galectin-1/GAL1/LGALS1 | Human | Galectin-1 Protein, Recombinant, with Native | 10290-HNAE |
| Galectin-1/GAL1/LGALS1 | Human | Galectin-1 / GAL1 Protein (Low Endotoxin), Recombinant, with Native | 10290-HNAE-E |
| Galectin-1/GAL1/LGALS1 | Mouse | Galectin-1 Protein, Recombinant, with Native | 50100-MNAE |
| Galectin-1/GAL1/LGALS1 | Rat | LGALS1 / Galectin-1 Protein, Recombinant, with Native | 80248-RNAE |
Antibodies:
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Galectin-1/GAL1/LGALS1 | Human | Galectin-1 Antibody (Antigen Affinity Purified) | 10290-RP02 |
LGALS1 / Galectin-1 Protein Description
Galectin-1 (Gal-1, GAL1), the first identified member of the β-galactoside-binding animal lectin family, and exists as a homodimer of a single carbohydrate-recognition domain. Galectin-1 is expressed in a variety of cell types, including thymic epithelial cells, endothelial cells, dendritic cells, macrophages, fibroblasts, and bone marrow stromal cells. There is increased galectin-1 expression in many types of cancer, including colon, breast, ovary and prostate carcinomas. 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. It is revealed that Galectin-1 can induce apoptosis of activated human T cells and human T leukaemia cell lines, while resting T cells also bound galectin-1, but did not undergo apoptosis. Galectin-1 modulates inflammatory responses and contributes to tumor progression and immune cell homeostasis. Galectin-1 regulates the inflammatory responses of neutrophils, mast cells, and macrophages and also associates with components of the complement system. Galectin-1 is thus suggested to act as an autocrine negative regulatory “cytokine,” killing T cells to terminate an immune response.
References
- Nozomu Nishi. et al., 2008, Glycobiology. 18 (12): 1065-73.
- Jiale He. et al., 2004, The Journal of Biological Chemistry. 279 (6): 4705-12.
- Santiago Di Lella. et al., 2009, Biochemistry. 48 (4): 786-91.
- Nicola TINARI1. et al., 2001, Int J Cancer: 91: 167-72.
- Magali Fouillit. et al., 2000, Glycobiology. 10 (4): 413-9.

+86-400-890-9989







