P8170
Protein G−Peroxidase from Streptococcus sp.
recombinant, expressed in unspecified host, lyophilized powder
Synonyme(s) :
Protein G−HRP from Streptococcus sp.
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Form:
lyophilized powder
Recombinant:
expressed in unspecified host
Service technique
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Laissez-nous vous aiderQuality Level
recombinant
expressed in unspecified host
conjugate
peroxidase conjugate
form
lyophilized powder
technique(s)
direct ELISA: 1:100,000 using human IgG
storage temp.
−20°C
General description
Protein G is a bacterial cell wall protein, which has high affinity for immunoglobulin G (IgG). It is isolated from group G streptococcal strains. Peroxidase from Streptococcus sp. is used to maintain the H2O2 homeostasis in cells. It aids the regulation of ABC Mn2+-permease complex (psaBCA) genes.
Application
Protein G- Peroxidase from Streptococcus sp. has been used in indirect ELISA and immunoblotting.
Biochem/physiol Actions
The product binds IgG for most mammalian species (excluding feline) and can be used in ELISA or immunohistochemical formats. Protein was determined to be at 250-350ug per 250ug vial by UV absorbance. Reactive to chicken IgG as well.
Preparation Note
Labeled with peroxidase type VI by a modification of the procedure of O′Sullivan, M.S., et al., FEBS Lett., 95, 311 (1978) which favors low molecular weight conjugates. Conjugate is purified by gel filtration.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Evaluation of a modified Rose Bengal test and an indirect enzyme-linked immunosorbent assay for the diagnosis of Brucella melitensis infection in sheep
Ferreira AC, et al.
Veterninary Research, 34(3), 297-305 (2003)
Thiol peroxidase is an important component of Streptococcus pneumoniae in oxygenated environments
Hajaj B, et al.
Infection and Immunity, IAI-00126 (2012)
Dimitra Zarafeta et al.
Frontiers in microbiology, 7, 1779-1779 (2016-12-03)
Lipolytic enzymes that retain high levels of catalytic activity when exposed to a variety of denaturing conditions are of high importance for a number of biotechnological applications. In this study, we aimed to identify new lipolytic enzymes, which are highly