Recombinant Mouse CD48 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1026

Recombinant Mouse CD48 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1026
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Product Overview

Tag His
Host Species Mouse
Accession NP_031675.1
Synonym CD48 antigen, B-lymphocyte activation marker BLAST-1, BCM1 surface antigen, Leukocyte antigen MEM-102, SLAM family member 2, SLAMF2, Signaling lymphocytic activation molecule 2, TCT.1.
Background CD48, is a GPI-linked protein which belongs to the CD2 family of immunoglobulin superfamily molecules. CD48 is capable to transduce signals and can likewise trigger signaling through CD2 or 2B4. CD48 to CD2 interactions advocate T cell activation and class replacing to IgG2a in B cells. In addition, high affinity of CD48 to 2B4, interactions may either promote or inhibit NK cell as well as cytotoxic T cell (CTL) activation. CD48 does not contain a transmembrane domain, though it is held at the cell surface by a GPI anchor through a C-terminal domain which possibly split to produce a soluble form of the receptor.
Description A DNA sequence encoding the mouse CD48 (NP_031675.1) without the propeptide, corresponding to the amino acids (Met 1-Arg 216) was produced with a C-terminal His tag.
Source HEK293
Predicted N Terminal Phe 23
AA Sequence Met 1-Arg 216
Molecular Weight The secreted recombinant mouse CD48 consists of 205 amino acids and has a calculated molecular mass of 23.7 kDa. As a result of glycosylation, the apparent molecular mass of the recombinant protein is approximately 45-60 kDa in SDS-PAGE under reducing conditions.
Purity Greater than 85% 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 2B4 in a functional ELISA.2. Measured by its ability to bind biotinylated recombinant mouse CD2 in a functional ELISA.
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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