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Your Position: Home > Recombinant Protein > E.Coli Expressed > Rat LGALS1 / Galectin-1 Protein (Native)

Rat LGALS1 / Galectin-1 Protein (Native) PDF Download

Catalog Size (Price) Quantity In Stock Operation Other Information
80248-RNAE
  YES          

Protein Production & Purification Service

Lectin, galactoside-binding, soluble, 1 Protein Datasheet

 

LGALS1 / Galectin-1 Protein Price Inquiry ( Available Sizes )

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:
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.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.

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

  1. Nozomu Nishi. et al., 2008, Glycobiology. 18 (12): 1065-73.
  2. Jiale He. et al., 2004, The Journal of Biological Chemistry. 279 (6): 4705-12.
  3. Santiago Di Lella. et al., 2009, Biochemistry. 48 (4): 786-91.
  4. Nicola TINARI1. et al., 2001, Int J Cancer: 91: 167-72.
  5. Magali Fouillit. et al., 2000, Glycobiology. 10 (4): 413-9.