Recombinant Human VEGFD Protein (His Tag)

Name: Recombinant Human VEGFD Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4791
Availability: InStock

Collections: Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NP_004460.1
Synonym	VEGF-D, VEGFD
Background	Vascular endothelial growth factor D (VEGF-D), also known as C-fos induced growth factor (FIGF), belongs to the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family. FIGF protein is active in angiogenesis, lymphangiogenesis, and endothelial cell growth. FIGF protein is secreted as a non-covelent homodimer in an antiparallel fashion. Human FIGF protein is expressed in adult lung, heart, muscle, and small intestine, and is most abundantly expressed in fetal lungs and skin. FIGF protein is structurally and functionally similar to VEGF-C. Therefore, FIGF protein binds and activates VEGFR-2 (Flk1) and VEGFR-3 (Flt4) receptors, and may particularly be involved in cancers, such as breast cancer, epithelial ovarian carcinoma and so on.
Description	A DNA sequence encoding the mature form of human VEGFD (NP_004460.1) corresponding to amino acid (Phe 93-Ser 201) was expressed with a C-terminal His tag.
Source	HEK293
Predicted N Terminal	Phe 93
AA Sequence	Phe 93-Ser 201
Molecular Weight	The recombinant mature form of human VEGFD consists of 120 a.a. and has a predicted molecular mass of 13.6 kDa. In SDS-PAGE under reducing conditions, it migrates with an apparent molecular mass of 20-22 kDa due to glycosylation.
Purity	>95% as determined by SDS-PAGE and SEC-HPLC Analysis.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC).The ED50 for this effect is 0.3-1.6 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.