176871
Angiotensin Converting Enzyme, His Tag , Human, Recombinant, NSO Cells
Synonym(s):
Hypertensinogen, Renin Substrate
Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
| Size/SKU | Availability | Price |
|---|---|---|
10 μg | Please contact Customer Service for Availability | €532.00 |
About This Item
NACRES:
NA.28
UNSPSC Code:
12352200
Form:
liquid
Storage condition:
OK to freeze
form
liquid
Quality Segment
specific activity
≥1 unit/µg protein
storage condition
OK to freeze
storage temp.
−70°C
General description
Recombinant, human ACE ectodomain (amino acids 30-1261) fused at the C-terminus to a HIS TAG® sequence and expressed in NSO cells. ACE is a zinc metallopeptidase that cleaves the C-terminal dipeptide from angiotensin I to produce the potent vasopressor octapeptide angiotensin II. ACE gene polymorphism has been a recent topic in Alzheimer′s disease studies. ACE is a type I membrane protein and exists in two isoforms, somatic and germinal. By SDS-PAGE, the apparent molecular weight of the glycosylated protein appears larger to be than 120 kDa under both reducing and non-reducing conditions.
Legal Information
HIS TAG is a registered trademark of Merck KGaA, Darmstadt, Germany
1 of 1
This Item | |||
|---|---|---|---|
| description - | description - | description recombinant, ≥10 U/mg, expressed in HEK 293 cells | description - |
| form liquid | form liquid | form lyophilized powder | form liquid |
| Quality Level 100 | Quality Level 100 | Quality Level 200 | Quality Level 100 |
| storage temp. −70°C | storage temp. −70°C | storage temp. −20°C | storage temp. - |
| storage condition OK to freeze | storage condition avoid repeated freeze/thaw cycles, OK to freeze | storage condition - | storage condition - |
| specific activity ≥1 unit/µg protein | specific activity ≥0.8 units/μg protein | specific activity ≥10 U/mg | specific activity - |
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.