Recombinant Mouse Renin Protein (His Tag)

Name: Recombinant Mouse Renin Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4045
Availability: InStock

Collections: Enzymes, Protease, Recombinant proteins

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Product Overview

Tag	His
Host Species	Mouse
Accession	NP_112469.1
Synonym	D19352, Ren, Ren-1, Ren-A, Ren1, Ren1c, Ren1d, Rn-1, Rnr
Background	Renin-1, also known as Ren-1, Angiotensinogenase and Kidney renin, is a member of thepeptidase A1 family. Renin-1 is synthesized by the juxtaglomerular cells of the kidney in response to decreased blood pressure and sodium concentration. androgen and thyroid hormones influence levels of Renin-1 in mouse submandibular gland (SMG) primarily by regulating the amount of Renin-1 mRNA available for translation. Renin-1 is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. It is expressed at relatively low levels in mouse SMG and kidney. Ren-2 is expressed at high levels in the mouse SMG and at very low levels, if at all, in the kidney. Ren-1 and Ren-2 are closely linked on mouse chromosome 1, show extensive homology in coding and noncoding regions and provide a model for studying the regulation of gene expression.
Description	A DNA sequence encoding the pro form of mouse REN1 (NP_112469.1) (Met 1-Arg 402) was fused with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Leu 22
AA Sequence	Met 1-Arg 402
Molecular Weight	The recombinant mouse REN1 consists of 392 a.a. and has a predicted molecular mass of 43.2 kDa. As a result of glycosylation, the apparent molecular mass of rmREN1 is approximately 48-55 kDa in SDS-PAGE under reducing conditions.
Purity	>97% 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 cleave the fluorogenic peptide substrate 5-FAM/QXL-™ 520 (Peti-Peterdi, J. et al., 2009, Physiology 24:88.). The specific activity is > 20 pmoles/min/ug.2. Immobilized mouse REN1-His at 10ug/ml (100 ul/well) can bind biotinylated human AGT-His with a linear range of 31.25-250 ng/ml.
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.