Recombinant Strepococcus Protein G [HRP]

Name: Recombinant Strepococcus Protein G [HRP]
SKU: DAG678
Rating: 5 (1 reviews)

Strepococcus Protein G [HRP], recombinant protein from E. coli

COA

SDS

Datasheet

Summary

Product Overview

RecombinantStaphylococcus Protein Gconjugatedto Horseradish Peroxidase (HRP) and expressed in E.coli.

Specificity

ProteinG binds to the Fc portion of immunoglobulin G subclasses (IgGs) from a broadrange of species including human and mouse, and does not bind IgA, IgE, IgMor serum albumin.

Nature

Recombinant

Tag/Conjugate

HRP

Preservative

None

Storage

2-8°C short term, -20°C long term

Introduction

Streptomyces is the largest genus of Actinobacteria and the type genus of the family Streptomycetaceae. Over 500 species of Streptomyces bacteria have been described. As with the other Actinobacteria, streptomycetes are Gram-positive, and have genomes with high GC content. Found predominantly in soil and decaying vegetation, most streptomycetes produce spores, and are noted for their distinct "earthy" odor that results from production of a volatile metabolite, geosmin.

Antigen Description

Protein G is animmunoglobulin-binding protein expressed in group C and G Streptococcalbacteria much like Protein A but with differing specificities. It is a 65-kDa(G148 protein G) and a 58 kDa (C40 protein G) cell surface protein that hasfound application in purifying antibodies through its binding to the Fcregion. The native molecule also binds albumin, however, because serumalbumin is a major contaminant of antibody sources, the albumin binding sitehas been removed from recombinant forms of Protein G.

Keywords

Spg; IgG binding protein G; Immunoglobulin G binding protein G [Precursor]; Protein G; Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus protein G; Staphylococcal Protein A; Staphylococcal; Protein A; Immunoglo

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Documents

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References

Topical Therapy with Antisense Tumor Necrosis Factor Alpha Using Novel beta-Glucan-Based Drug Delivery System Ameliorates Intestinal Inflammation

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

Authors: Sakisaka, Hideto; Takedatsu, Hidetoshi; Mitsuyama, Keiichi; Mochizuki, Shinichi; Sakurai, Kazuo; Sakisaka, Shotaro; Hirai, Fumihito

Abstract

Anti-tumor necrosis factor alpha (TNF-alpha) antibodies are effective in patients with inflammatory bowel disease (IBD). However, the effect is not optimal because a sufficient concentration of antibodies cannot be maintained at the site of inflammation. Thus, a macromolecular complex was developed with schizophyllan (SPG) and antisense oligonucleotides. In the present study, an SPG-antisense TNF-alpha complex was prepared, and its therapeutic efficacy was examined using a dextran sodium sulfate (DSS)-induced colitis model. The TNF-alpha production in CD11b+ macrophages significantly increased in the colon of DSS-treated mice. Dectin-1, a receptor of SPG, binds with SPG and is subsequently taken into the cells via phagocytosis. The expression of dectin-1 by CD11b+ macrophages significantly increased in DSS-treated mice. Flow cytometry revealed that the uptake of SPG-antisense TNF-alpha in the macrophages was efficient. TNF-alpha production was suppressed significantly by SPG-antisense TNF-alpha in vitro, which was administered via enema to evaluate its efficacy. The intrarectal administration of SPG-antisense TNF-alpha ameliorated the intestinal inflammation. In this study, we showed that the delivery system that conjugates SPG and antisense can have higher therapeutic efficacy. Thus, the new therapeutic approach presented in this study may be used in the management of IBD.

Highly sensitive fluorescence-linked immunosorbent assay based on aggregation-induced emission luminogens incorporated nanobeads

BIOSENSORS & BIOELECTRONICS

Authors: Wu, Weijie; Shen, Mengfei; Liu, Xinyi; Shen, Lisong; Ke, Xing; Li, Wanwan

Abstract

Aggregation-induced emission luminogens (AIEgens) have attracted considerable interest for application towards the development of various biosensors due to their unique optical properties. However, the major challenge associated with generating a suitable fluorescent signal for constructing an AIEgens-based immunoassay platform, is the complex surface modification and additional chemical reaction required to activate the AIE process. This work reports a novel AIEgens nanobeads-based fluorescence-linked immunosorbent assay (FLISA) platform wherein the fluorescent labels are hexaphenylsilole (HPS) nanobeads, which were synthesized through Shirasu porous glass (SPG) membrane emulsification method and could provide a strong, direct fluorescent signal without any pretreatment. Moreover, the particle-based signal amplification effect affords this platform significantly improved detection sensitivity for carcinoembryonic antigen (CEA) quantitation. Compared to FLISA which uses R-phycoerythrin (PE) or commercial green QDs nanobeads as fluorescent labels, this AlEgens nanobeads-based FLISA platform exhibits detection sensitivity improved up to 45-fold and 12-fold, respectively. Clinical validation experiments applying this AIEgens nanobeads-based FLISA immunoassay platform to analyze human serum samples produce results consistent with those obtained by the clinical gold-standard method, electrochemiluminescence immunoassay (ECLIA). The strong photobleaching resistance and excellent fluorescent stability of the HPS nanobeads negate the need for light shielding, which improves the efficiency and makes the operating conditions more comfortable. Thus, this AIEgens nanobeads-based FLISA platform, with attractive features including direct fluorescent signal generation and significant signal amplification, creates a new, versatile route for the application of AIEgens in biosensors and clinical diagnosis.