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A5588

Anti-polyHistidine−Alkaline Phosphatase antibody, Mouse monoclonal

Name: Anti-polyHistidine−Alkaline Phosphatase antibody, Mouse monoclonal
Brand: SIGMA

clone HIS-1, purified from hybridoma cell culture

Synonym(s):

Monoclonal Anti-polyHistidine, Monoclonal Anti-polyHistidine−Alkaline Phosphatase antibody produced in mouse, 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:

alkaline phosphatase conjugate

Clone:

HIS-1, monoclonal

Application:

Citations:

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biological source

mouse

Quality Level

200

conjugate

alkaline phosphatase conjugate

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

HIS-1, monoclonal

form

buffered aqueous glycerol solution

technique(s)

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

isotype

IgG2a

shipped in

wet ice

storage temp.

2-8°C

General description

The Monoclonal Anti-polyHistidine-Alkaline Phosphatase antibody recognizes native and denatured-reduced forms of synthetic polyhistidine or polyhistidine tagged fusion proteins. The product is reactive with fusion protein expressed by prokaryotic pET, pRSET and pTrc expression vectors.

Immunogen

recombinant polyHistidine tagged fusion protein.

Application

Antibody is suitable for ELISA, immunoblotting and dot blotting assays.

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

Solution in 0.05 M Tris buffer, pH 8.0, containing 1 mM MgCl₂, 1% bovine serum albumin, 50% glycerol and 15 mM sodium azide

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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Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Regulatory Information

常规特殊物品

低风险生物材料

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Certificates of Analysis (COA)

Lot/Batch Number

0000527506

0000430829

0000389409

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Optimization of production of the anti-keratin 8 single-chain Fv TS1-218 in Pichia pastoris using design of experiments.

Rozbeh Jafari et al.

Microbial cell factories, 10, 34-34 (2011-05-18)

Optimization of conditions during recombinant protein production for improved yield is a major goal for protein scientists. Typically this is achieved by changing single crucial factor settings one at a time while other factors are kept fixed through trial-and-error experimentation.

Application of a Short, Disordered N-Terminal Flagellin Segment, a Fully Functional Flagellar Type III Export Signal, to Expression of Secreted Proteins

Dobo,J et al.

Applied and Environmental Microbiology, 6(3), 891-899 (2010)

Characterization of a novel protein with homology to C-type lectins expressed by the Cotesia rubecula bracovirus in larvae of the lepidopteran host, Pieris rapae.

Richard Glatz et al.

The Journal of biological chemistry, 278(22), 19743-19750 (2003-03-20)

Polydnaviruses are essential for the survival of many Ichneumonoid endoparasitoids, providing active immune suppression of the host in which parasitoid larvae develop. The Cotesia rubecula bracovirus is unique among polydnaviruses in that only four major genes are detected in parasitized

Functional and informatics analysis enables glycosyltransferase activity prediction.

Min Yang et al.

Nature chemical biology, 14(12), 1109-1117 (2018-11-14)

The elucidation and prediction of how changes in a protein result in altered activities and selectivities remain a major challenge in chemistry. Two hurdles have prevented accurate family-wide models: obtaining (i) diverse datasets and (ii) suitable parameter frameworks that encapsulate

Coenzyme M biosynthesis in bacteria involves phosphate elimination by a functionally distinct member of the aspartase/fumarase superfamily.

Sarah E Partovi et al.

The Journal of biological chemistry, 293(14), 5236-5246 (2018-02-08)

For nearly 30 years, coenzyme M (CoM) was assumed to be present solely in methanogenic archaea. In the late 1990s, CoM was reported to play a role in bacterial propene metabolism, but no biosynthetic pathway for CoM has yet been

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Global Trade Item Number

SKU	GTIN
A5588-.5ML	04061833376065

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