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SAB4300966

Sigma-Aldrich

Anti-MT2A antibody produced in rabbit

affinity isolated antibody

Synonyme(s) :

MT2

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100 MG
MYR 689.00
1 G
MYR 1,746.00

MYR 689.00


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100 MG
MYR 689.00
1 G
MYR 1,746.00

About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

MYR 689.00


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Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

human

Concentration

1 mg/mL

Technique(s)

immunohistochemistry: 1:25- 1:100

Isotype

IgG

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Cet article
SAB1402848HPA006214SAB4301632
Anti-TTI1 affinity isolated antibody

SAB4301632

Anti-TTI1

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

100

antibody form

affinity isolated antibody

antibody form

purified immunoglobulin

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

biological source

rabbit

biological source

mouse

biological source

rabbit

biological source

rabbit

technique(s)

immunohistochemistry: 1:25- 1:100

technique(s)

capture ELISA: suitable, immunofluorescence: suitable, indirect ELISA: suitable, western blot: 1-5 μg/mL

technique(s)

immunoblotting: 0.04-0.4 μg/mL, immunofluorescence: 0.25-2 μg/mL, immunohistochemistry: 1:50-1:200

technique(s)

immunohistochemistry: 1:25-1:100

Gene Information

human ... MT2A(4502)

Gene Information

human ... MT2A(4502)

Gene Information

human ... MTA2(9219)

Gene Information

human ... TTI1(9675)

UniProt accession no.

P02795

UniProt accession no.

P02795

UniProt accession no.

O94776

UniProt accession no.

O43156

Spécificité

The antibody detects endogenous levels of total MT2A protein.

Immunogène

Full length fusion protein

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Forme physique

Rabbit IgG in pH7.3 PBS, 0.05% NaN3, 50% Glycerol.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), 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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

M F Pardo et al.
Journal of agricultural and food chemistry, 48(9), 3795-3800 (2000-09-20)
A new plant endopeptidase was obtained from unripe fruits of Bromelia balansae Mez (Bromeliaceae). Crude extracts were partially purified by ethanol fractionation. This preparation (redissolved ethanol precipitate, REP) showed maximum activity at pH 8.8-9.2, was very stable even at high
Paul V Attwood et al.
Analytical biochemistry, 334(2), 382-389 (2004-10-21)
Mass spectrometry offers a potential means of measuring virtually all enzyme-catalyzed reactions by simultaneously measuring the concentrations of substrates, products, and intermediates where there are differences in mass between them. To perform these measurements the reaction mixture must be aged
M F Pardo et al.
Biological chemistry, 382(5), 871-874 (2001-08-24)
Unripe fruit extracts of Bromelia balansae Mez (Bromeliaceae), whose principal endopeptidase is balansain I (isolated for anion exchange chromatography: pI = 5.45, molecular weight = 23192), exhibit a pH profile with a maximum activity around pH 9.0 and are inhibited
Susana R Morcelle et al.
Fitoterapia, 75(5), 480-493 (2004-07-21)
As part of a screening of latex endopeptidases from plants growing in Argentina, the presence of proteolytic activity in the latex of Funastrum clausum stems is reported. The proteases present in the crude extract showed the main characteristics of the
N E Mackenzie et al.
The Biochemical journal, 219(2), 437-444 (1984-04-15)
The kinetics of the trypsin-catalysed hydrolysis of the highly specific substrate N alpha-benzyloxycarbonyl-L-lysine p-nitrophenyl ester were studied under cryoenzymological conditions by 13C-n.m.r. spectroscopy at pH approx. 3.0. The kinetics of this reaction are shown to be in agreement with similar

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