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MAB2223

Sigma-Aldrich

Anti-DNP Antibody, clone 9H8.1

clone 9H8.1, from mouse

Sinónimos:

Dinitrophenol

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

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

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.

Specificity

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

Immunogen

KLH-conjugated DNP

Application

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

Quality

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.

Target description

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.

Physical form

Format: Purified

Analysis Note

Control
Oxyblot protein standards

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Jennifer B M Steffen et al.
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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.
Xiaoding Wang et al.
Cell death and differentiation, 25(12), 2181-2194 (2018-04-19)
Secretory and transmembrane proteins rely on proper function of the secretory pathway for folding, posttranslational modification, assembly, and secretion. Accumulation of misfolded proteins in the endoplasmic reticulum (ER) stimulates the unfolded protein response (UPR), which communicates between the ER and
Brígida R Pinho et al.
Free radical biology & medicine, 146, 372-382 (2019-11-22)
Abnormal protein homeostasis (proteostasis), dysfunctional mitochondria, and aberrant redox signalling are often associated in neurodegenerative disorders, such as Huntington's (HD), Alzheimer's and Parkinson's diseases. It remains incompletely understood, however, how changes in redox signalling affect proteostasis mechanisms, including protein degradation

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