JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB13808

Anti-Bacillus anthracis protective antigen 抗体

Anti-Bacillus anthracis protective antigen antibody

Be the first to review this product! Submit a review

|

(6 Publications)

Rabbit Polyclonal Bacillus anthracis protective antigen antibody. Suitable for WB and reacts with Recombinant fragment - Bacillus anthracis samples. Cited in 6 publications.

別名を表示する

pag, pXO1-110, BXA0164, GBAA_pXO1_0164, pagA, Protective antigen, PA, Anthrax toxins translocating protein, PA-83, PA83

1 Images
Western blot - Anti-Bacillus anthracis protective antigen antibody (AB13808)
  • WB

Unknown

Western blot - Anti-Bacillus anthracis protective antigen antibody (AB13808)

Western blot analysis of Anthrax PA in recombinant protein using ab13808 (lane B) at 1 : 1000 dilution. Lane A shows the pre-bleed.

All lanes:

Western blot - Anti-Bacillus anthracis protective antigen antibody (ab13808)

false

Key facts

宿主種

Rabbit

クローン性

Polyclonal

アイソタイプ

IgG

キャリアフリー

No

交差種

Bacillus anthracis

アプリケーション

WB

applications

style
left-column

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Bacillus anthracis": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Recombinant fragment - Bacillus anthracis": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/1000", "WB-species-notes": "<p></p>" } } }
style
left-column
style
left-column
style
left-column

出荷温度及び保存条件

製品の状態
Liquid
精製度
Whole antiserum
バッファー組成
Preservative: 0.05% Sodium azide Constituents: PBS, 0.05% BSA
出荷温度
Blue Ice
短期保存期間
1-2 weeks
短期保存温度
+4°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
style
left-column

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

Bacillus anthracis protective antigen often referred to as PA plays an important role in the mechanism of anthrax toxin's entry into host cells. PA weighs approximately 83 kDa and is an essential component of B. anthracis the bacterium causing anthrax. It expresses on the surface of the bacteria and exists in the extracellular environment. Within the anthrax toxin complex PA functions mechanically by binding to host cell receptors and facilitating the entry of other anthrax toxin components lethal factor (LF) and edema factor (EF) into the host cells.
Biological function summary

Bacillus anthracis protective antigen behaves as a part of a complex specifically the anthrax toxin composed of LF EF and PA itself. PA binds to host cell’s receptors such as ANTXR1 and ANTXR2. Once PA attaches to these receptors it undergoes proteolytic cleavage to heptamer formation allowing the assembly of the toxin complex. This heptamer serves as a platform for LF and EF which subsequently translocate into the host cell's cytosol disrupting cellular processes and immune responses.

Pathways

Bacillus anthracis protective antigen operates primarily in endocytic and intracellular trafficking pathways. The binding and cleavage of PA on the host cell surface enable endocytosis of the toxin complex through clathrin-mediated pathways. This interaction with cellular components is critical for facilitating the entry of LF and EF which relate to pathways involving cellular signaling and immune response suppression. These processes highlight PA’s role in efficiently hijacking host cellular machinery for pathogenic activity.

Bacillus anthracis protective antigen is chiefly associated with anthrax a severe and sometimes lethal disease. The action of PA in the anthrax toxin contributes to systemic issues such as shock and multi-organ dysfunction. Within this context PA’s interaction with LF and EF directly correlates with the virulence and lethality of the anthrax pathogen. Understanding PA and its interactions provides invaluable insight for developing therapeutic interventions and effective anthrax antibodies aimed at neutralizing the effects of the toxin.
style
left-column
style
left-column

製品プロトコール

For this product, it's our understanding that no specific protocols are required. You can visit:
style
left-column

ターゲットの情報

Protective antigen constitutes one of the three proteins composing the anthrax toxin; it mediates attachment to host cells and translocation of edema factor (EF) and lethal factor (LF) into the host cytoplasm (PubMed : 11700562, PubMed : 14507921, PubMed : 15243628, PubMed : 15326297). PA associated with LF forms the lethal toxin (LeTx) and causes death when injected; PA associated with EF forms the edema toxin (EdTx) and produces edema (PubMed : 1651334). PA induces immunity to infection with anthrax (PubMed : 11544370).. Protective antigen. Mediates the attachment to host cells by binding host cell receptors ANTXR1 and ANTXR2 (PubMed : 11700562, PubMed : 14507921, PubMed : 15243628, PubMed : 15326297). Following host cell surface attachment, PA is cleaved by FURIN to generate the PA-63 (Protective antigen PA-63) form, which constitutes the mature form of the protein that oligomerizes and forms a pore to translocate the enzymatic toxin components edema factor (EF) and lethal factor (LF) into the host cytosol (PubMed : 11700562, PubMed : 15243628, PubMed : 15326297).. Protective antigen PA-63. Mature form that oligomerizes and forms a pore to translocate the enzymatic toxin components edema factor (EF) and lethal factor (LF) into the host cytosol (PubMed : 15243628, PubMed : 15326297). Following attachment to host cell receptors and cleavage by FURIN, homooligomerizes to form ring-shaped oligomers that are in a pre-pore conformation, and associates with EF and LF (PubMed : 10085027, PubMed : 12117959, PubMed : 15313199). Toxin-leaded complexes are then endocytosed in a clathrin-dependent process, followed by a conformational change of oligomerized PA-63 from the pre-pore to pore state, which is triggered by the low pH in the endosome (PubMed : 10085027, PubMed : 12551953, PubMed : 15326297, PubMed : 20221438). Once active, the pore mediates unfolding of EF and LF, which pass through the pore and translocate into the host cytosol (PubMed : 16051798, PubMed : 21037566, PubMed : 32047164, PubMed : 32521227, PubMed : 32810181).
See full target information pagA
style
left-column

文献 (6)

Recent publications for all applications. Explore the full list and refine your search

Analytical chemistry 92:7845-7851 PubMed32437125

2020

Dual-Readout Sandwich Immunoassay for Device-Free and Highly Sensitive Anthrax Biomarker Detection.

Applications

Unspecified application

Species

Unspecified reactive species

Isaac N Larkin,Viswanadham Garimella,Gokay Yamankurt,Alexander W Scott,Hang Xing,Chad A Mirkin

Journal of bacteriology 202: PubMed32071095

2020

Increased Excess Intracellular Cyclic di-AMP Levels Impair Growth and Virulence of Bacillus anthracis.

Applications

Unspecified application

Species

Unspecified reactive species

Jia Hu,Gaobo Zhang,Leiqin Liang,Chengfeng Lei,Xiulian Sun

Journal of controlled release : official journal of the Controlled Release Society 220:316-328 PubMed26546271

2015

Disarmed anthrax toxin delivers antisense oligonucleotides and siRNA with high efficiency and low toxicity.

Applications

Unspecified application

Species

Unspecified reactive species

Paul D R Dyer,Thomas R Shepherd,Alexander S Gollings,Susan A Shorter,Monique A M Gorringe-Pattrick,Chun-Kit Tang,Beatrice N Cattoz,Les Baillie,Peter C Griffiths,Simon C W Richardson

Letters in applied microbiology 54:306-12 PubMed22268495

2012

Comparative analysis of virulence factors secreted by Bacillus anthracis Sterne at host body temperature.

Applications

Unspecified application

Species

Unspecified reactive species

S K Kim,S Shahid,S H Kim,J H Park,H T Lee,K H Jung,Y G Chai

Infection and immunity 79:3012-9 PubMed21576337

2011

Bacillus cereus G9241 makes anthrax toxin and capsule like highly virulent B. anthracis Ames but behaves like attenuated toxigenic nonencapsulated B. anthracis Sterne in rabbits and mice.

Applications

WB

Species

Unspecified reactive species

Melissa K Wilson,James M Vergis,Farhang Alem,John R Palmer,Andrea M Keane-Myers,Trupti N Brahmbhatt,Christy L Ventura,Alison D O'Brien

Proceedings of the National Academy of Sciences of 107:15583-8 PubMed20713715

2010

Heterodimeric integrin complexes containing beta1-integrin promote internalization and lethality of anthrax toxin.

Applications

WB

Species

Unspecified reactive species

Mikhail Martchenko,Sun-Young Jeong,Stanley N Cohen
View all publications
style
left-column
style
left-column

Abcam product promise

当社は、高品質な試薬を通じてお客様の研究を力強くサポートすることをお約束いたします。ご使用いただく各段階で、常にお客様をサポートできる体制を整えております。万が一、製品が期待通りに機能しない場合は、「Abcam Product Promise」による当社保証制度に基づき、安心してご利用いただけます。
保証に関する詳細については利用規約をご確認ください。
style
left-column
style
right-column

関連製品

Select an associated product type
Alternative Product
Primary Antibodies

AB21268

Anti-Bacillus anthracis protective antigen antibody

primary-antibodies

bacillus-anthracis-protective-antigen-antibody-ab21268

0

(0 reviews)

style
bg-slate-100

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com