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T0565

Sigma-Aldrich

3,3′,5,5′-Tetramethylbenzidine

TMB membrane substrate, chromogenic, liquid

Synonym(s):

TMB membrane substrate

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.83

product name

3,3′,5,5′-Tetramethylbenzidine (TMB) Liquid Substrate System for Membranes, ready to use solution

Quality Level

form

liquid

storage temp.

2-8°C

General description

3,3′,5,5′-Tetramethylbenzidine (TMB) is a chromogenic substrate for horseradish peroxidase (HRP) conjugates. It develops a permanent, insoluble, dark blue reaction product and is useful in colorimetric quantification.

Application

3,3′,5,5′-Tetramethylbenzidine (TMB) Liquid Substrate System for Membranes has been used as a chromogenic substrate in western blot analysis. It has also been used as a liquid substrate in enzyme-linked immunosorbent assay (ELISA).
3,3′,5,5′-Tetramethylbenzidine (TMB) Liquid Substrate System for Membranes has been used in:
  • enzyme-linked immune absorbent spot (ELISPOT) assay
  • as a substrate for IgG peroxidase
  • in the visualization of immunocomplexes

Physical form

Ready-to-use.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Muhammed M Salahuddin et al.
Current issues in molecular biology, 43(3), 2199-2209 (2021-12-24)
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Srdjan M Dragovic et al.
Cell host & microbe, 23(4), 523-535 (2018-04-13)
Plasmodium infection begins with the bite of an anopheline mosquito, when sporozoites along with saliva are injected into a vertebrate host. The role of the host responses to mosquito saliva components in malaria remains unclear. We observed that antisera against
Hesham Saeed et al.
Preparative biochemistry & biotechnology, 52(6), 668-680 (2021-10-07)
Microbial L-asparaginases are aminohydrolases that hydrolyze L-asparagine to L-aspartate. They are used to treat acute lymphoblastic leukemia and Hodgkin's lymphomas and in food industries. Increasing demand for L-ASNases is therefore needed. In the current study, the recombinant L-ASNase from Dickeya
immune response of multiparous hyper-immunized sows against peptides from non-structural and structural proteins of PRRSV
Rascon-Castelo E, et al.
Vaccines, 3(4), 973-987 (2015)
Testin (TES) as a candidate tumour suppressor and prognostic marker in human astrocytoma
Steponaitis G, et al.
Oncology Letters, 12(5), 3305-3311 (2016)

Articles

The field of proteomics is continually looking for new ways to investigate protein dynamics within complex biological samples. Recently, many researchers have begun to use RNA interference (RNAi) as a method of manipulating protein levels within their samples, but the ability to accurately determine these protein amounts remains a challenge. Fortunately, over the past decade, the field of proteomics has witnessed significant advances in the area of mass spectrometry. These advances, both in instrumentation and methodology, are providing researchers with sensitive assays for both identification and quantification of proteins within complex samples. This discussion will highlight some of these methodologies, namely the use of Multiple Reaction Monitoring (MRM) and Protein-AQUA.

NBT-BCIP substrate system aids in western blotting and immunohistological staining, producing a blue-purple insoluble end product.

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