Recombinant Human CD72 Protein

Name: Recombinant Human CD72 Protein
Brand: Beta LifeScience
SKU: BLK-00422P-100UG
Availability: InStock

Human CD72 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Collections: Car-nk targets proteins, High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Description	Recombinant Human CD72 Protein is expressed from HEK293 with His tag at the N-Terminus.It contains Arg117-Asp359.
Purity	> 95% as determined by Tris-Bis PAGE
Accession	P21854
Target Symbol	CD72
Species	Human
Expression System	HEK293
Tag	N-His
Expression Range	Arg117-Asp359
Mol. Weight	The protein has a predicted MW of 29.17 kDa. Due to glycosylation, the protein migrates to 32-40 kDa based on Tris-Bis PAGE result.
Form	Lyophilized
Formulation	Lyophilized from 0.22 um filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Endotoxin	Less than 1EU per ug by the LAL method.
Storage	Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Shipping	Shipped at ambient temperature.
Gene Background	CD72 (originally Lyb-2), a 45 kDa type II transmembrane glycoprotein. CD72 belongs to the calcium-dependent C-type lectin superfamily and shares sequence homology with CD23 (the B-cell-specific low-affinity Fc receptor for IgE) and the asialoglycoprotein receptors. It is expressed as a disulfide-linked homodimer from the pro-B through the mature B-cell stage, but it is downregulated on terminally differentiated plasma cells.

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

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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.