Recombinant Rat DPP3 Protein

Name: Recombinant Rat DPP3 Protein
Brand: Beta LifeScience
SKU: BLK-03396P
Availability: InStock

Rat DPP3 on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.

Collections: All products, High-quality 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 Rat DPP3 Protein is expressed from E.coli with His tag at the N-terminus.It contains Ala2-Ala738.
Gene Background	Dipeptidyl peptidase III (DPP3) is a ubiquitously expressed zinc-dependent peptide cutting enzyme and selectively hydrolyses amide bonds to cleave N-terminal dipeptide fragments off of physiologically important oligopeptides. DPP3 has been found in a multitude of different types of cells and appears to be involved in various physiological processes (e.g. nociception, blood pressure control, protein turnover).
Accession	O55096
Target Symbol	DPP3
Synonyms	DPP III; Dipeptidyl peptidase 3; Enkephalinase B
Species	Rat
Expression System	E.coli
Purity	> 95% as determined by Bis-Tris PAGE;> 95% as determined by HPLC
Tag	N-His
Expression Range	Ala2-Ala738
Mol. Weight	The protein has a predicted MW of 84.00 kDa. The protein migrates to 70-80 kDa based on Bis-Tris PAGE result.
Form	Liquid
Formulation	Supplied as 0.22 um filtered solution in 20mM Tris, 150mM NaCl, 10%glycerol (pH 8.0).
Endotoxin	Less than 1 EU per ug by the LAL method.
Biotinylated	No
Shipping	Shipped with dry ice.
Storage	Valid for 12 months from date of receipt when stored at -80°C.； Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.

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.