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

234397
Purchase on Sigma-Aldrich

Descripción

Replacement Information

Products

Número de referenciaEmbalaje Cant./Env.
234397-100UG Ampolla de plást. 100 μg
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
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 Ficha datos de seguridad (MSDS)

Título

Ficha técnica de seguridad del material (MSDS) 

Complement C5a, His·Tag®, Human, Recombinant, E. coli Certificados de análisis

CargoNúmero de lote
234397

Referencias bibliográficas

Visión general referencias
Carney, D.F. and Hugli, T.E. 1993. Protein Sci. 2, 1391.
Hugli, T.E., et al. 1981. Mol. Cell. Biochem. 41, 59.
Ficha técnica

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.