Recombinant Mouse APN Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-2637NP
BL-2637NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-2637NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Mouse APN Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-2637NP
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 Mouse Aminopeptidase N is produced by our Mammalian expression system and the target gene encoding Lys69­Ser966 is expressed with a 6His tag at the C-terminus.
Accession P97449
Synonym Aminopeptidase N; ANPEP; AP-M; APN; AP-N; CD13 antigen; CD13; CD13APN; PEPN; PEPNhAPN
Gene Background ANPEP gene encodes aminopeptidase N (APN) also known as microsomal aminopeptiase, alanyl aminopeptidase, aminopeptidase M, CD13, or membrane protein p161, is a member of the peptidase M1 family. Widely expressed in many cells, tissues and species, APN cleaves the N-terminal amino acids from bioactive peptides, leading to their inactivation or degradation. Probably plays a role in regulating growth and differentiation of early B-lineage cells. It also may play a role in the catabolic pathway of the renin-angiotensin system. It degrades vasoconstricting angiotensin II into angiotensin III and therefore helps to regulate blood pressure.
Molecular Mass 103.6 KDa
Apmol Mass 110-130 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

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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