MAB2223

Anti-DNP Antibody, clone 9H8.1

Name: Anti-DNP Antibody, clone 9H8.1
Brand: MM

clone 9H8.1, from mouse

Synonym(s):

Dinitrophenol

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About This Item

UNSPSC Code:

12352203

NACRES:

NA.41

eCl@ss:

32160702

Product Name

Anti-DNP Antibody, clone 9H8.1, clone 9H8.1, from mouse

biological source

mouse

antibody form

purified immunoglobulin

clone

9H8.1, monoclonal

species reactivity (predicted by homology)

all

technique(s)

western blot: suitable

isotype

IgG1κ

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

100

Application

This Anti-DNP Antibody, clone 9H8.1 is validated for use in WB for the detection of DNP.

Analysis Note

Control
Oxyblot protein standards

Evaluated by Western Blot in Oxyblot protein standards.

Western Blot Analysis: 0.5 µg/mL of this antibody detected DNP on 10 µg of Oxyblot protein standards.

Biochem/physiol Actions

Demonstrated to react with a DNP moiety in a wider range of species. This antibody′s reactivity is expected to be species independent.

General description

Dinitrophenol (DNP) is a small water-soluble, hydrophobic ligand that binds to transthyretin at acidic pH and also reduces the formation of amyloid fibril. DNP levels of 100 mg/l or more is greatly toxic to acclimated bacteria. DNP has been associated with possible therapies for neurodegenerative and neurological disorders.

Various kDa observed. The Oxyblot protein standards (S7151) were used to test this antibody. These standards are phosphorylase B, BSA, OVA, Carbonic Anhydrase, and trypsin inhibitor which all contain 1-3 DNP residues per protein.

Immunogen

KLH-conjugated DNP

Physical form

Format: Purified

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Combined effects of salinity and intermittent hypoxia on mitochondrial capacity and reactive oxygen species efflux in the Pacific oyster, Crassostrea gigas.

Jennifer B M Steffen et al.

The Journal of experimental biology, 226(15) (2023-07-20)

Coastal environments commonly experience fluctuations in salinity and hypoxia-reoxygenation (H/R) stress that can negatively affect mitochondrial functions of marine organisms. Although intertidal bivalves are adapted to these conditions, the mechanisms that sustain mitochondrial integrity and function are not well understood.

Mitochondrial responses to constant and cyclic hypoxia depend on the oxidized fuel in a hypoxia-tolerant marine bivalve Crassostrea gigas.

Linda Adzigbli et al.

Scientific reports, 14(1), 9658-9658 (2024-04-27)

Sessile benthic organisms like oysters inhabit the intertidal zone, subject to alternating hypoxia and reoxygenation (H/R) episodes during tidal movements, impacting respiratory chain activities and metabolome compositions. We investigated the effects of constant severe hypoxia (90 min at ~ 0% O2 ) followed

Novel Antibody-Peptide Binding Assay Indicates Presence of Immunoglobulins against EGFR Phospho-Site S1166 in High-Grade Glioma.

Lona Zeneyedpour et al.

International journal of molecular sciences, 23(9) (2022-05-15)

We investigated the feasibility of detecting the presence of specific autoantibodies against potential tumor-associated peptide antigens by enriching these antibody-peptide complexes using Melon Gel resin and mass spectrometry. Our goal was to find tumor-associated phospho-sites that trigger immunoreactions and raise

A new ex vivo model of the bone tissue response to the hyperglycemic environment - The embryonic chicken femur organotypic culture in high glucose conditions.

Rita Araújo et al.

Bone, 158, 116355-116355 (2022-02-14)

Diabetes mellitus (DM) embrace a group of chronic metabolic conditions with a high morbidity, causing deleterious effects in different tissues and organs, including bone. Hyperglycemia seems to be one of the most contributing etiological factors of bone-related alterations, altering metabolic

Molecular and clinical effects of aromatase inhibitor therapy on skeletal muscle function in early-stage breast cancer.

Tara A Seibert et al.

Scientific reports, 14(1), 1029-1029 (2024-01-11)

We evaluated biochemical changes in skeletal muscle of women with breast cancer initiating aromatase inhibitors (AI), including oxidation of ryanodine receptor RyR1 and loss of stabilizing protein calstabin1, and detailed measures of muscle function. Fifteen postmenopausal women with stage I-III breast

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Global Trade Item Number

SKU	GTIN
MAB2223	04053252528323

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