176872 | Angiotensin Converting Enzyme-2, His•Tag®, Human, Recombinant, NSO Cells

176872
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      176872-10UG
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          Glass bottle 10 μg
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          Description
          OverviewRecombinant, human ACE-2 ectodomain (amino acids 1-740) fused at the C-terminus to a His•Tag® sequence and expressed in NSO cells. Native ACE-2 is an integral membrane zinc metalloprotease that can be inhibited by EDTA. ACE-2 cleaves angiotensins I and II. Plays an important role in regulating cardiovascular and renal functions. By SDS-PAGE, the apparent molecular mass of the glycosylated protein is ~120 kDa under either reducing or non-reducing condition.
          Catalogue Number176872
          Brand Family Calbiochem®
          SynonymsACE Homolog, ACEH, ACE-2
          References
          ReferencesTikellis, C., et al. 2003. Hypertension 41, 390.
          Tipnis, S.R., et al. 2000. J. Biol. Chem. 275, 33238.
          Product Information
          Unit of DefinitionOne unit is defined as the amount of enzyme that will cleave 1 nmol MCA-YVADAPK(DNP)-OH per min at 25°C, pH 7.5.
          FormLiquid
          Applications
          Biological Information
          Purity≥90% by SDS-PAGE
          Specific Activity≥0.8 unit/µg protein
          Concentration Label Please refer to vial label for lot-specific concentration
          Physicochemical Information
          ContaminantsEndotoxins: ≤1.0 EU/µg ACE-2
          Dimensions
          Materials Information
          Toxicological Information
          Safety Information according to GHS
          Safety Information
          Product Usage Statements
          Storage and Shipping Information
          Ship Code Dry Ice Only
          Toxicity Standard Handling
          Storage ≤ -70°C
          Avoid freeze/thaw Avoid freeze/thaw
          Do not freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          176872

          References

          Reference overview
          Tikellis, C., et al. 2003. Hypertension 41, 390.
          Tipnis, S.R., et al. 2000. J. Biol. Chem. 275, 33238.
          Data Sheet

          Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

          Revision14-April-2008 RFH
          SynonymsACE Homolog, ACEH, ACE-2
          DescriptionRecombinant, human ACE-2 ectodomain (amino acids 1-740) fused at the C-terminus to a His•Tag® sequence and expressed in NSO cells. ACE-2 cleaves angiotensins I and II as a carboxypeptidase and plays an important role in regulating cardiovascular and renal functions. Native ACE-2 is an integral membrane zinc metalloprotease whose activity is inhibited by EDTA. By SDS-PAGE, the apparent molecular mass of the glycosylated protein is ~120 kDa under either reducing or non-reducing conditions.
          FormLiquid
          Concentration Label Please refer to vial label for lot-specific concentration
          Purity≥90% by SDS-PAGE
          ContaminantsEndotoxins: ≤1.0 EU/µg ACE-2
          Specific activity≥0.8 unit/µg protein
          Unit definitionOne unit is defined as the amount of enzyme that will cleave 1 nmol MCA-YVADAPK(DNP)-OH per min at 25°C, pH 7.5.
          Storage ≤ -70°C
          Avoid freeze/thaw
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
          Toxicity Standard Handling
          ReferencesTikellis, C., et al. 2003. Hypertension 41, 390.
          Tipnis, S.R., et al. 2000. J. Biol. Chem. 275, 33238.