Recombinant Mouse CNDP1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1347

Recombinant Mouse CNDP1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1347
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Product Overview

Tag His
Host Species Mouse
Accession Q8BUG2
Synonym AI746433, Cn1
Background CNDP1, also known as carnosine dipeptidase 1, glutamate carboxypeptidase-like protein 2 (CPGL-2) or carnosinase 1 (CN1), is a member of the M2 metalloprotease family. The CNDP1 gene contains trinucleotide (CTG) repeat length polymorphism in the coding region, which has been demonstrated to be associated with susceptibility to developing diabetic nephropathy, for carnosine protection against the adverse effects of high glucose levels on renal cells. In humans, CNDP1 is secreted from the liver into the serum. In other mammals, including rodents, CNDP1 is expressed exclusively within the kidney and lacks a signal peptide. CNDP1 protein is a secreted homodimeric dipeptidase that specifically hydrolyzes L-carnosine (beta-alanyl-L-histidine), and is identified as human carnosinase expressed in the brain. CNDP1 has been associated with diabetic nephropathy in Europeans and European Americans, but not African-Americans. It was identified and confirmed as a risk factor, were cross-sectional and mostly in patients with type 2 diabetes. The polymorphisms of CNDP1 can be excluded as a risk factor for nephropathy in type 1 diabetes. In addition, CNDP1 is also suggested to be implicated in the actions of neuroprotection and neurotransmiting.
Description A DNA sequence encoding the mouse CNDP1 (Q8BUG2) (Met 1-Tyr 492) was expressed, with an N-terminal signal peptide and a C-terminal His tag.
Source HEK293
Predicted N Terminal Met 1
AA Sequence Met 1-Tyr 492
Molecular Weight The secreted recombinant mouse CNDP1 comprises 503 a.a. and has a calculated molecular mass of 56.5 kDa. As a result of glycosylation, the apparent molecular mass of the recombinant protein is approximately 55 kDa in SDS-PAGE under reducing conditions.
Purity >93% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its ability to cleave carnosine (β-Ala-L-His)in a two-step assay.The specific activity is > 250 pmoles/min/ug.
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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