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

Angiotensin Converting Enzyme-2, His•Tag®, Human, Recombinant, NSO Cells: のSDS（安全データシート）、CoA（試験成績書）およびCoQ（品質証明書）、カタログなど製品関連の技術資料を入手いただけます。

同義語: ACE Homolog, ACEH, ACE-2

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176872
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概要

Replacement Information

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176872-10UGCN
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      		 ｶﾞﾗｽﾋﾞﾝ 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
      Quality LevelMQ100
      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
      Global Trade Item Number
      カタログ番号 GTIN
      176872-10UGCN 04055977222999

      Documentation

      Angiotensin Converting Enzyme-2, His•Tag®, Human, Recombinant, NSO Cells (M)SDS

      タイトル

      英語版製品安全データシート（(M)SDS） 

      Angiotensin Converting Enzyme-2, His•Tag®, Human, Recombinant, NSO Cells 試験成績書（CoA）

      タイトルロット番号
      176872

      参考資料

      参考資料の概要
      Tikellis, C., et al. 2003. Hypertension 41, 390.
      Tipnis, S.R., et al. 2000. J. Biol. Chem. 275, 33238.
      データシート

      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 Avoid freeze/thaw
      ≤ -70°C
      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.