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Merck
CN

SAB4200799

Anti-Shiga Toxin 1, B Subunit-FITC antibody, Mouse monoclonal

clone 13C4, purified from hybridoma cell culture

别名:

Anti-SLT-1 B subunit, Anti-SLT-1b, Verocytotoxin 1 subunit B, Anti-Shiga-like toxin 1 subunit B, Anti-Verotoxin 1 subunit B, Anti-stxB

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关于此项目

NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
FITC conjugate
Clone:
13C4, monoclonal
Application:
FACS
Citations:
3
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biological source

mouse

conjugate

FITC conjugate

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

13C4, monoclonal

description

Research area: Microbiome

form

buffered aqueous solution

species reactivity

E. coli

storage condition

protect from light

concentration

~1 mg/mL

technique(s)

flow cytometry: 2-4 μg/test using human RAMOS cells pretreated with recombinant Shiga toxin 1, B subunit

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

General description

Monoclonal Anti-Shiga Toxin 1, B Subunit-FITC (mouse IgG1 isotype) is derived from the hybridoma 13C4 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice. The Shiga toxins are a family of related protein toxins secreted by certain types of bacteria. Shiga toxin (Stx) is produced by Shigella dysenteriae; whereas, the Shiga-like toxins, Stx1 and Stx2, with a few known isoforms, are secreted by specific strains of Escherichia coli named Shiga-toxin-producing E. coli (STEC) such as E. coli O157:H7. Stx1 is identical to Stx and the Stx2 isoforms shares 60% similarity with STX. Howevere, the toxin structure is conserved. Shiga toxins consist of two polypeptides: A and B.

Immunogen

Purifed Shiga-like toxin from E. coli H30.

Application

Anti-Shiga Toxin 1, B Subunit-FITC antibody, Mouse monoclonal may be used in flow cytometry.

Biochem/physiol Actions

Monoclonal Anti-Shiga Toxin 1, B Subunit -FITC recognizes the B subunit of Shiga holotoxin.
The STX catalytic A subunit has RNA N-glycosidase activity that inhibits eukaryotic protein synthesis. The B subunits form a pentamer, which recognizes and binds to the functional cell-surface receptor globotriaosylceramide [Gb3, Galα (1-4)-Galβ (1-4)-Glcβ1-ceramide]. Shiga toxins are implicated in bloody diarrhea and hemorrhagic colitis in humans, which may lead to fatal systemic complications. Gb3 is overexpressed in membranes of numerous tumor cells, therefore, STxB binding to Gb3 receptors may be useful in cancer cell imaging.

Physical form

Supplied as a solution in 0.01 M phosphate buffered saline pH 7.4 and 15 mM sodium azide as a preservative.

Preparation Note

For continuous use, store at 2–8 °C protected from light for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours. Protect from prolonged exposure to light.

Other Notes

In order to obtain best results in different techniques and preparations we recommend determining optimal working concentration by titration test.

Disclaimer

Unless otherwise stated in our catalog, 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.

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存储类别

12 - Non Combustible Liquids

wgk

WGK 3

法规信息

低风险生物材料
常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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访问文档库

Shiga toxins 1 and 2 translocate differently across polarized intestinal epithelial cells
Hurley BP, et al.
Infection and Immunity, 67(12), 6670-6677 (1999)
Shiga toxin (Stx) classification, structure, and function
Melton-Celsa AR
Microbiology spectrum, 37-53 (2015)
Shiga toxin and its use in targeted cancer therapy and imaging
Engedal N, et al.
Microbial Biotechnology, 4(1), 32-46 (2011)

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