Renin Protein, Mouse, Recombinant (His Tag)

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Renin Protein, Mouse, Recombinant (His Tag): Product Information

Purity
> 97 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
1. Measured by its ability to cleave the fluorogenic peptide substrate 5­FAM/QXL™ 520 (Peti­Peterdi, J. et al., 2009, Physiology 24:88.). The specific activity is > 20 pmoles/min/μg.
2. Immobilized mouse REN1-His (Cat: 50279-M08H) at 10ug/ml (100 μl/well) can bind biotinylated human AGT-His (Cat: 10994-H08H) with a linear range of 31.25-250 ng/ml.
Protein Construction
A DNA sequence encoding the pro form of mouse REN1 (NP_112469.1) (Met 1-Arg 402) was fused with a polyhistidine tag at the C-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Mouse
Predicted N Terminal
Leu 22
Molecule Mass
The recombinant mouse REN1 consists of 392 amino acids 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.
Formulation
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Renin Protein, Mouse, Recombinant (His Tag): Images

Renin Protein, Mouse, Recombinant (His Tag): Alternative Names

D19352 Protein, Mouse; Ren Protein, Mouse; Ren-1 Protein, Mouse; Ren-2 Protein, Mouse; Ren-A Protein, Mouse; Ren-B Protein, Mouse; Ren1 Protein, Mouse; Ren1c Protein, Mouse; Ren1d Protein, Mouse; Ren2 Protein, Mouse; Rn-1 Protein, Mouse; Rn-2 Protein, Mouse; Rnr Protein, Mouse

Renin Background Information

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.
Full Name
renin
References
  • McKeon F.D., et al.,(1986), Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319:463-468.
  • Fisher D.Z., et al., (1986), cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.Proc. Natl. Acad. Sci. U.S.A. 83:6450-6454.
  • Sylvius N., et al.,(2005), In vivo and in vitro examination of the functional significances of novel lamin gene mutations in heart failure patients.J. Med. Genet. 42:639-647.
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