Recombinant Human FLT4 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2115

Recombinant Human FLT4 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2115
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Product Overview

Tag His
Host Species Human
Accession NP_002011.2
Synonym FLT-4, FLT-41, FLT41, LMPH1A, PCL, VEGF Receptor 3, VEGFR-3, VEGFR3
Background Vascular endothelial growth factor receptor 3 (VEGFR3), also known as FLT-4, together with the other two members VEGFR1 (FLT-1) and VEGFR2 (KDR/Flk-1) are receptors for vascular endothelial growth factors (VEGF) and belong to the class III subfamily of receptor tyrosine kinases (RTKs). The VEGFR3 protein is expressed mainly on lymphatic vessels but it is also up-regulated in tumor angiogenesis. Mutations in VEGFR3 have been identified in patients with primary lymphoedema. The VEGF-C/VEGF-D/VEGFR3 signaling pathway may provide a target for antilymphangiogenic therapy in prostate cancer, breast cancer, gastric cancer, lung cancer, non-small cell lung cancer (NSCLC), and so on.Immune CheckpointImmunotherapyCancer ImmunotherapyTargeted Therapy
Description A DNA sequence encoding the extracellular domain (Met 1-Ile 776) of human VEGFR3 (NP_002011.2) was expressed with a C-terminal His tag.
Source HEK293
Predicted N Terminal Tyr 25 & Ser 473
AA Sequence Met 1-Ile 776
Molecular Weight The recombinant human VEGF R3 consists of 763 a.a. and predicts a molecular mass of 86 kDa. As a result of glycosylation, rhVEGFR3 migrates as an approximately 130 kDa in non-reduced SDS-PAGE.
Purity >97% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity 1. Measured by its binding ability in a functional ELISA.2. Immobilized human VEGF-C at 10 ug/mL (100 ul/well) can bind human VEGFR3-his. The EC50 of human VEGFR3-his is 0.011 ug/mL.3. Measured by its ability to bind human VEGF-D in a functional ELISA.
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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