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Product Overview
Product Name Mouse Complement C5 Protein
Catalog Number orb653662
ReactivityMouse
ConjugationUnconjugated
Endotoxins 1.0 EU per μg
Target Complement C5
Alternative Names
Product Properties
Form/Appearance Powder
Preservatives PBS, pH7.4
Storage -20°C to -70°C for 12 months in lyophilized state; -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Tag C-10×His
Note For research use only.
Purity 95%
MW 73.5 kDa (β chain) & 114.6 kDa (α chain)
Source Mouse Complement C5, His Tag (orb653662) is expressed from human 293 cells (HEK293). It contains AA Gln 19 - Glu 1680 (Accession # P06684-1).
Biological Origin Mouse
Expression Region Gln 19 - Glu 1680
Activity Immobilized Mouse Complement C5, His Tag at 2 μg/mL (100 μL/well) can bind Monoclonal Anti-Human C5a Human Antibody, Human IgG1 with a linear range of 0.1-13 ng/mL (QC tested).
Product Description

Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. C5 precursor is first processed by the removal of 4 basic residues, forming two chains, beta and alpha, linked by a disulfide bond. C5 convertase activates C5 by cleaving the alpha chain, releasing C5a anaphylatoxin and generating C5b (beta chain + alpha' chain). Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled. The C5a anaphylatoxin interacts with C5AR1 and tick complement inhibitor. C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation.

Application Notes
Application Notes This protein carries a polyhistidine tag at the C-terminus. The mature form of Complement C5 is a disulfide-linked heterodimer composed of proteolytically cleaved α and β chain. Each α and β chain has a calculated MW of 73.5 kDa (β chain) and 114.6 kDa (α chain). The protein migrates as 66 kDa (β chain) and 100 kDa (α chain) under reducing (R) condition (SDS-PAGE) due to glycosylation.
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