Recombinant Human Renin
Product name: | Recombinant Human Renin |
Source: | Human Cells |
Purity: | Greater than 95% as determined by reducing SDS-PAGE. |
Buffer Formulation: | Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4. |
Applications: | Applications:SDS-PAGE; WB; ELISA; IP. |
Storage: | Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months. |
UOM: | 100ug/50ug/200ug/1mg/1g |
Source | Human Cells |
Description | Recombinant Human Renin is produced by our Mammalian expression system and the target gene encoding Leu24-Arg406 is expressed with a 10His tag at the C-terminus. |
Names | Renin; Angiotensinogenase; REN |
Accession # | P00797 |
Formulation | Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4. |
Shipping |
The product is shipped at ambient temperature. |
Reconstitution |
Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 μg/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
Storage |
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
Purity |
Greater than 95% as determined by reducing SDS-PAGE. |
Endotoxin | Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test. |
Amino Acid Sequence |
LPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYG EIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGT VSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGV LKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLC EDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSA DYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALARGGGGSHH HHHHHHHH
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Background | Renin is a member of the aspartyl proteinase family produced largely in part by the juxtaglomerular cells in the kidney. Renin is produced as prorenin with 43 pro residues at the N-terminal of mature Renin. The inactive prorenin becomes activated proteolytically by trypsin, cathepsin B, or other proteinases. Renin also has a very high selectivity for substrates due to a long peptide recognition on either side of the peptide bond undergoing cleavage. An octapeptide substrate was the minimum length to be cleaved by Renin. Renin plays a crucial role in the regulation of blood pressure and salt balance through the cleavage of angiotensinogen,which is the only known physiological substrate of Renin. Renin releases the decapeptide angiotensin I, which in turn is further converted to vasoactive hormone angiotensin II by angiotensin converting enzyme (ACE). |