234397 Complement C5a, His·Tag®, Human, Recombinant, E. coli

234397
가격을 검색할 수 없습니다
Minimum Quantity needs to be mulitiple of
가격 문의 추가 정보
()이 할인됨
 
가격 문의
재고 없음재고 없음
예상 출고 가능일 
단종품
제한된 수량 가능
재고여부 확인
    Remaining: will advise
      Remaining: will advise
      추천사항
      고객 서비스로 문의
      Contact Customer Service
      가격 및 재고 조회

      개요

      Replacement Information

      가격 및 재고여부

      카탈로그 번호 재고 정보패킹 포장 단위 가격(VAT 별도) 수량
      234397-100UGCN
      재고 정보 검색...
      재고 없음재고 없음
      예상 출고 가능일 
      단종품
      제한된 수량 가능
      재고여부 확인
        Remaining: will advise
          Remaining: will advise
          추천사항
          고객 서비스로 문의
          Contact Customer Service

          Plastic ampoule 100 μg
          가격 검색...
          가격을 검색할 수 없습니다
          Minimum Quantity needs to be mulitiple of
          가격 문의 추가 정보
          ()이 할인됨
           
          가격 문의
          Description
          OverviewRecombinant, human C5a complement (74 amino acids) fused at the N-terminus to a His•Tag® sequence and a proprietary vector sequence necessary for expression and expressed in E. coli. The recombinant protein is not further processed to remove the additional sequence. Activation of complement by either pathway results in the formation of C5-cleaving enzymes (C5 convertases) on target surfaces. The C5 convertase enzymes cleave the C5 α-chain at peptide bond 74 resulting in the production and release of the C5a glycopeptide. C5a is the most biologically active of the three complement-derived anaphylatoxins. C5a expresses a wide variety of biogical activities which include: inflammatory cell chemotaxis, smooth muscle contraction, and release reactions of neutrophils, mast cells, and macrophages.


          Available in Bulk - request a quote!
          Catalogue Number234397
          Brand Family Calbiochem®
          References
          ReferencesCarney, D.F. and Hugli, T.E. 1993. Protein Sci. 2, 1391.
          Hugli, T.E., et al. 1981. Mol. Cell. Biochem. 41, 59.
          Product Information
          FormLyophilized solid
          Quality LevelMQ100
          Applications
          Biological Information
          Biological activityExhibits equal activity to that of serum-derived C5a based on a myeloperoxidase release assay.
          Purity≥95% by SDS-PAGE
          Physicochemical Information
          ContaminantsEndotoxins: ≤0.1 ng/µg protein
          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 reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 3 months at -70°C.
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          Complement C5a, His·Tag®, Human, Recombinant, E. coli Certificates of Analysis

          TitleLot Number
          234397

          References

          참고문헌 보기
          Carney, D.F. and Hugli, T.E. 1993. Protein Sci. 2, 1391.
          Hugli, T.E., et al. 1981. Mol. Cell. Biochem. 41, 59.
          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.

          Revision22-May-2009 JSW
          DescriptionRecombinant, human C5 a complement (74 amino acids) fused at the N-terminus to a His•Tag® sequence and a proprietary vector sequence necessary for expression and expressed in E. coli. The recombinant protein is not further processed to remove the additional sequences. Activation of complement by either pathway results in the formation of C5-cleaving enzymes (C5 convertase) on target surfaces. The C5 convertase enzymes cleave the C5a chain at peptide bond 74, resulting in the production and release of the C5a glycopeptide. C5a is the most biologically active of the three complement-derived anaphylatoxins. C5a exhibits a wide variety of biological activities, including inflammatory cell chemotaxis, smooth muscle contraction, and degranulation of neutrophils, mast cells, and macrophages.
          FormLyophilized solid
          Purity≥95% by SDS-PAGE
          ContaminantsEndotoxins: ≤0.1 ng/µg protein
          Biological activityExhibits equal activity to that of serum-derived C5a based on a myeloperoxidase release assay.
          SolubilityReconstitute in sterile H₂O containing 2.5 mg/ml BSA.
          Storage ≤ -70°C
          Avoid freeze/thaw
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 3 months at -70°C.
          Toxicity Standard Handling
          ReferencesCarney, D.F. and Hugli, T.E. 1993. Protein Sci. 2, 1391.
          Hugli, T.E., et al. 1981. Mol. Cell. Biochem. 41, 59.