Recombinant human LAMTOR4 protein
€0.00
In stock
SKU
ATGP2791
Description
LAMTOR4 is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Recombinant human LAMTOR4 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.Alternative Names
Ragulator complex protein LAMTOR4, C7orf59Concentration
0.25mg/ml (determined by Bradford assay)Concentration
Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 0.15M NaCl, 10% glycerol, 1mM DTTStorage: Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
LAMTOR4 is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Recombinant human LAMTOR4 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.Alternative Names
Ragulator complex protein LAMTOR4, C7orf59Concentration
0.25mg/ml (determined by Bradford assay)Concentration
Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 0.15M NaCl, 10% glycerol, 1mM DTTStorage: Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
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