Recombinant Mouse Endoglin / CD105 Protein (His Tag)

Name: Recombinant Mouse Endoglin / CD105 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1752
Availability: InStock

Collections: Cluster of differentiation (cd) proteins, Featured cd protein molecules, Recombinant proteins

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Product Overview

Tag	His
Host Species	Mouse
Accession	NP_031958.2
Synonym	AI528660, AI662476, CD105, Endo, S-endoglin
Background	Endoglin, also known as CD15, is a type I homodimeric transmembrane glycoprotein with a large, disulfide-linked, extracellular region and a short, constitutively phosphorylated cytoplasmic tail. Endoglin contains an RGD tripeptide which is a key recognition structure in cellular adhesion,,suggesting a critical role for endoglin in the binding of endothelial cells to integrins and/or other RGD receptors. Endoglin is highly expressed on vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta. It is also found on activated monocytes, mesenchymal stem cells and leukemic cells of lymphoid and myeloid lineages. As an accessory receptor for the TGF-beta superfamily ligands, endoglin binds TGF-beta1 and TGF-beta3 with high affinity not by itself but by associating with TGF-beta type II receptor (TbetaRII) and activates the downstream signal pathways. In addition, in human umbilical vein endothelial cells, ALK-1 is also a receptor kinase for endoglin threonine phosphorylation, and mutations in either of the two genes result in the autosomal-dominant vascular dysplasia, hereditary hemorrhagic telangiectasia (HHT). Endoglin has been regarded as a powerful biomarker of neovascularization, and is associated with several solid tumor types.
Description	A DNA sequence encoding the mouse CD105 (NP_031958.2) extracellular domain (Met 1-Gly 580) was expressed, with a C-terminal His tag.
Source	HEK293
Predicted N Terminal	Arg 27
AA Sequence	Met 1-Gly 580
Molecular Weight	The secreted recombinant mouse CD105 consists of 565 a.a. and has a calculated molecular mass of 61.2 kDa. As a result of glycosylation, the apparent molecular mass of the recombinant protein is approximately 65-70 kDa in SDS-PAGE under reducing conditions.
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 ability to bind Human ENG-Fc in functional Elisa.2. Measured by its ability to latent TGFB1-His in functional Elisa.3. Measured by its ability to mouse ENG-His in functional Elisa.4. Measured by its ability to inhibit BMP9-induced alkaline phosphatase production by MC3T3E1 mouse chondrogenic cells. David, L. et al. (2007) Blood 109:1953. The ED50 for this effect is typically 5-15 ng/mL in the presence of 2 ng/mL of recombiant human BMP9.
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.