Recombinant Cynomolgus c-MET Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-1336

Recombinant Cynomolgus c-MET Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-1336
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Product Overview

Tag Fc
Host Species Cynomolgus
Accession NP_001162100.1
Background Hepatocyte growth factor receptor (HGFR), also known as c-Met or mesenchymal-epithelial transition factor (MET), is a receptor tyrosine kinase (RTK) that has been shown to be overexpressed and/or mutated in a variety of malignancies. HGFR protein is produced as a single-chain precursor, and HGF is the only known ligand. Normal HGF/HGFR signaling is essential for embryonic development, tissue repair or wound healing, whereas aberrantly active HGFR has been strongly implicated in tumorigenesis, particularly in the development of invasive and metastatic phenotypes. HGFR protein is a multifaceted regulator of growth, motility, and invasion, and is normally expressed by cells of epithelial origin. Preclinical studies suggest that targeting aberrant HGFR signaling could be an attractive therapy in cancer.Immune CheckpointImmunotherapyCancer ImmunotherapyTargeted Therapy
Description A DNA sequence encoding the cynomolgus/rhesus MET (NP_001162100.1) (Met1-Thr932) was expressed with the Fc region of human IgG1 at the C-terminus. Cynomolgus and Rhesus MET sequences are identical.
Source HEK293
Predicted N Terminal Glu 25
AA Sequence Met1-Thr932
Molecular Weight The recombinant cynomolgus/rhesus MET comprises 1146 a.a. and has a calculated molecular mass of 128.3 KDa. The apparent molecular mass of it is approximately 100.2 and 42.5 KDa in SDS-PAGE under reducing conditions.
Purity (66.7+31.5)% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Immobilized Cynomolgus HGF at 10 ug/ml (100 ul/well) can bind Cynomolgus MET-Fc, EC50 of Cynomolgus MET-Fc is 0.04-0.09 ug/ml.
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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