Recombinant Human JAM-A Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3040

Recombinant Human JAM-A Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3040
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Product Overview

Tag His
Host Species Human
Accession NP_058642.1
Synonym CD321, JAM, JAM1, JAMA, JCAM, KAT, PAM-1
Background Junctional adhesion molecule-A (JAM-A), also known as F11 receptor (F11R) or Cluster of Differentiation 321 (CD321), is a transmembrane protein expressed at tight junctions of epithelial and endothelial cells, as well as on circulating leukocytes. JAM-A protein serves as a serotype-independent receptor for mammalian orthoreoviruses (reoviruses). It is also a ligand for the integrin LFA1, involves in leukocyte transmigration. As a cell adhesion molecule of the immunoglobulin superfamily, JAM-A protein involves in platelet adhesion, secretion and aggregation, and plays a crucial role in inflammatory thrombosis and atherosclerosis. In addition, it may be a potential therapeutic target for breast cancer.
Description A DNA sequence encoding the extracellular domain (Met 1-Ala 242) of human JAM-A (NP_058642.1) precursor was expressed with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Ser 28
AA Sequence Met 1-Ala 242
Molecular Weight The secreted recombinant human JAM-A comprises 227 a.a. and has a calculated molecular mass of 25 kDa. As a result of glycosylation, it migrates with the molecular mass of approximately 28-32 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 Measured by the ability of the immobilized protein to support the adhesion of Jurkat human acute T cell leukemia cells.When 8 x 104 cells/well are added to JAM-A-Fc coated plates (2.5ug/mL, 100 uL/well)in the presence of 20 ng/mL PMA, approximately 30-40% will adhere after 30 minutes at 37°C.
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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