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

Complement C5a, His•Tag®, Human, Recombinant, E. coli is made by fusing recombinant C5a to a His•Tag® sequence. The recombinant protein is not further processed to remove the additional sequence.

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
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Overview

Replacement Information
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.


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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 LevelMQ200
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
Global Trade Item Number
Catalogue Number GTIN
234397 0

Documentation

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

TitleLot Number
234397

References

Reference overview
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 Avoid freeze/thaw
≤ -70°C
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.