Recombinant Human Galectin-10 Protein Summary
| Description |
A recombinant protein with a His-tag corresponding to amino acids 1 to 142 of Human Galectin-10
Source: E. coli Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MSLLPVPYTE AASLSTGSTV TIKGRPLACF LNEPYLQVDF HTEMKEESDI VFHFQVCFGR RVVMNSREYG AWKQQVESKN MPFQDGQEFE LSISVLPDKY QVMVNGQSSY TFDHRIKPEA VKMVQVWRDI SLTKFNVSYL KR |
| Preparation Method |
E.coli
|
| Protein/Peptide Type |
Recombinant Protein
|
| Gene |
CLC
|
| Purity |
>90%, by SDS-PAGE
|
Applications/Dilutions
| Application Notes |
The purity of this protein is > 90% by SDS-PAGE. Molecular weight is 18.6 kDa (162aa) confirmed by MALDI-TOF
|
| Theoretical MW |
18.6 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
| Storage |
Store at -80C. Avoid freeze-thaw cycles.
|
| Buffer |
20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol, 0.1M NaCl
|
| Concentration |
0.5 mg/ml
|
| Purity |
>90%, by SDS-PAGE
|
Alternate Names for Recombinant Human Galectin-10 Protein
- Charcot-Leyden crystal proteinLGALS10A
- CLC
- EC 3.1.1.5
- eosinophil lysophospholipase
- GAL10
- Gal-10
- galectin 10
- Galectin10
- Galectin-10
- LGALS10
- LPPL_HUMAN
- Lysolecithin acylhydrolase
- MGC149659
Background
Eosinophil lysophospholipase (CLC), also known as Galectin 10, act on biological membranes to regulate the multifunctional lysophospholipids. CLC is a lysophospholipase expressed in eosinophils and basophils. It hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. This protein may possess carbohydrate or IgE-binding activities. It is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. It may be associated with inflammation and some myeloid leukemias. Recombinant human CLC protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.