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Merck

A7058

Anti-polyHistidine−Peroxidase antibody, Mouse monoclonal

clone HIS-1, purified from hybridoma cell culture

Synonym(s):

Monoclonal Anti-polyHistidine, Monoclonal 6 His epitope tag, Monoclonal 6xHis-tag, Monoclonal HHHHHH epitope tag, Monoclonal Hexa His tag, Monoclonal His-tag, Monoclonal His6 tag, Monoclonal Histidine tagged, Monoclonal Poly-His-tag

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About This Item

NACRES:
NA.56
UNSPSC Code:
12352203
Conjugate:
peroxidase conjugate
Clone:
HIS-1, monoclonal
Application:
WB
Citations:
105

Key Documents

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biological source

mouse

conjugate

peroxidase conjugate

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

HIS-1, monoclonal

form

lyophilized powder

packaging

vial of 0.5 mL

concentration

5-11 mg/mL

technique(s)

western blot: 1:2,000 using lysates of Escherichia coli induced to express a 6xHis tagged protein

isotype

IgG2a

storage temp.

2-8°C

target post-translational modification

unmodified

Quality Level

200

Related Categories

General description

The monoclonal anti-polyHistidine Peroxidase Conjugate antibody recognizes native and denatured forms of synthetic polyhistidine or polyhistidine-tagged fusion proteins. The product is reactive with fusion proteins expressed by prokaryotic pET, pRSET and pTrc expression vectors.

Immunogen

recombinant polyHistidine tagged fusion protein.

Application

Antibody suitable for immunoblotting. Working dilution 1:20



Also suitable for dot blot assays and ELISA

Biochem/physiol Actions

The antibody recognizes synthetic polyHistidine, as well as native or denatured, reduced forms of proteins tagged with 6X histidines, expressed in selected vectors.

Physical form

Lyophilized from 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 0.05% MIT.

Preparation Note

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).
The antibody conjugate should be reconstituted with 0.5 ml deionized water.

Other Notes

2024 CiteAb Award Winner for Supplier Succeeding in Parkinson′s Research

Legal Information

This Product is covered by patent DE 19507166 and foreign equivalents exclusively licensed to QIAGEN GmbH, Qiagen Strasse 1, D-40724 Hilden, Germany.

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pictograms

Exclamation mark
GHS07

signalword

Warning

hcodes

H317

Hazard Classifications

Skin Sens. 1

Storage Class

12 - Non Combustible Liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
059M4839V
21190358
088M4865V
21180441
077M4847V

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Vincenzo Lionetti et al.
BMC plant biology, 15, 6-6 (2015-01-20)
Fusarium graminearum, one of the causal agents of Fusarium Head Blight (FHB, scab), leads to severe losses in grain yield and quality due to the production of mycotoxins which are harmful to human and livestock. Different traits for FHB resistance
Laurence Guglielmi et al.
Methods in molecular biology (Clifton, N.J.), 562, 215-224 (2009-06-26)
The most frequently used approach to produce single-chain Fv fragments (scFv) and Fab in Escherichia coli is to express them in the periplasm of the bacteria. We present here an alternative procedure that uses cytoplasmic expression of soluble active scFv.
Xiao-Xia Xia et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(32), 14059-14063 (2010-07-28)
Spider dragline silk is a remarkably strong fiber that makes it attractive for numerous applications. Much has thus been done to make similar fibers by biomimic spinning of recombinant dragline silk proteins. However, success is limited in part due to
Philippe Thullier et al.
PloS one, 8(5), e65855-e65855 (2013-06-07)
The lethal toxin (LT) of Bacillus anthracis, composed of the protective antigen (PA) and the lethal factor (LF), plays an essential role in anthrax pathogenesis. PA also interacts with the edema factor (EF, 20% identity with LF) to form the
Rita Figueira et al.
Scientific reports, 5, 17524-17524 (2015-12-02)
The Escherichia coli eukaryote-like serine/threonine kinase, encoded by yeaG, is expressed in response to diverse stresses, including nitrogen (N) starvation. A role for yeaG in bacterial stress response is unknown. Here we reveal for the first time that wild-type E.
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