Recombinant Human CD226 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0809

Recombinant Human CD226 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0809
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Product Overview

Tag His
Host Species Human
Accession NP_006557.2
Synonym DNAM-1/CD226 CD226 antigen; DNAX accessory molecule 1; DNAM-1; CD226; DNAM1
Background Human DNAX accessory molecule 1 (DNAM-1/CD226) is a 65 kDa type I transmembrane glycoprotein in the immunoglobulin superfamily. Mature human DNAM-1 contains an extracellular domain (ECD) with two Ig-like C2-set domains and a cytoplasmic region that contains motifs for binding PDZ domains and band 4.1 family proteins. DNAM-1 is expressed on multiple lymphoid and myeloid cells and interacts with CD155 and CD112. Ligation of DNAM-1 promotes the activation of NK cells, CD8+ T cells, and mast cells, dendritic cell maturation, megakaryocyte and activated platelet adhesion to vascular endothelial cells, and monocyte extravasation; it inhibits the forrmation of osteoclasts. Plateletendothelium, interactions mediated by DNAM-1, enable the metastasis of tumor cells to the lung.
Description A DNA sequence encoding the human DNAM1 (NP_006557.2) extracellular domain (Met 1-Asn 247) was fused with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Glu 19
AA Sequence Met 1-Asn 247
Molecular Weight The recombinant human DNAM1 comprises 240 amino acids and has a predicted molecular mass of 27.6 kDa. As a result of glycosylation, rh DNAM1 migrates with an apparent molecular mass of 40-50 kDa in SDS-PAGE under reducing conditions.
Purity Greater than 97% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its binding ability in a functional ELISA. Immobilized human CD226 at 2 ug/ml (100 ul/well) can bind human CD112 with a linear ranger of 6.4-800 ng/ml.
Formulation Lyophilized from sterile PBS, pH 7.4
Stability Recombinnat Proteins are stable for up to 1 year from date of receipt at -70°C
Usage For Research Use Only
Storage Store recombinant 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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