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MW 225.3 Da. Superoxide dismutase (SOD) and NF-κB inhibitor. Nitric oxide (NO) spin-trapping reagent when complexed with Fe2+. Active in vivo and in vitro.

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Chemical Structure - Diethyldithiocarbamic acid sodium salt trihydrate, SOD and NF-kappaB inhibitor (AB144752), expandable thumbnail

Key facts

CAS number
20624-25-3
Form
Solid
Molecular weight
225.3 Da
Molecular formula
C5H16NNaO3S2
PubChem identifier
517546
Nature
Synthetic

Alternative names

Recommended products

MW 225.3 Da. Superoxide dismutase (SOD) and NF-κB inhibitor. Nitric oxide (NO) spin-trapping reagent when complexed with Fe2+. Active in vivo and in vitro.

Key facts

PubChem identifier
517546
Solubility

Soluble in water to 75mM.

Biochemical name
Sodium diethyldithiocarbamate trihydrate
Biological description

Superoxide dismutase (SOD) and NF-κB inhibitor. Nitric oxide (NO) spin-trapping reagent when complexed with Fe2+. Active in vivo and in vitro.

Canonical SMILES
CCN(CC)C(=S)[S-].O.O.O.[Na+]
InChI
InChI=1S/C5H11NS2.Na.3H2O/c1-3-6(4-2)5(7)8;;;;/h3-4H2,1-2H3,(H,7,8);;3*1H2/q;+1;;;/p-1
InChIKey
WWGXHTXOZKVJDN-UHFFFAOYSA-M
IUPAC name
sodium;N,N-diethylcarbamodithioate;trihydrate

Storage

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate long-term storage conditions
+4°C
Storage information
The product can be stored for up to 12 months

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.
Activity summary

Hsp27 also known as HSPB1 is a small heat shock protein with a molecular weight of approximately 27 kilodaltons. This protein is expressed in various tissues including muscle heart and brain. It functions as a molecular chaperone that stabilizes unfolded proteins preventing their aggregation. Hsp27 undergoes phosphorylation at specific residues which modulates its chaperone activity and interaction with other proteins.

Biological function summary

Hsp27 plays a critical role in cellular stress response by regulating actin cytoskeleton dynamics and inhibiting apoptosis. It forms part of a complex that includes other proteins such as alphaB-crystallin. This complex facilitates the reorganization of proteins under stress conditions enhancing cell survival during oxidative stress or thermal shock. Hsp27 also modulates inflammatory responses and has been shown to affect cell migration.

Pathways

Hsp27 integrates into the apoptosis and inflammation pathways. It interacts with apoptotic machinery such as caspase proteins to protect cells by hindering apoptosome formation. Additionally Hsp27 can engage with pathways involving the nuclear factor-kappa B (NF-kB) impacting inflammatory signaling. CPTC (carboxyl-pyrene-trioctylamine) can modulate these pathways by altering Hsp27 function and interactions.

Associated diseases and disorders

Hsp27 has connections to neurodegenerative diseases and cancer. In neurodegenerative conditions such as Alzheimer's disease its chaperone activity is thought to protect neurons from misfolded protein aggregates. In cancer Hsp27 supports tumor cell survival and resistance to chemotherapy by interacting with proteins like Akt and p53. These interactions highlight the complex role of Hsp27 in modulating cellular responses in various pathological states.

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1 product image

  • Chemical Structure - Diethyldithiocarbamic acid sodium salt trihydrate, SOD and NF-kappaB inhibitor (ab144752), expandable thumbnail

    Chemical Structure - Diethyldithiocarbamic acid sodium salt trihydrate, SOD and NF-kappaB inhibitor (ab144752)

    2D chemical structure image of ab144752, Diethyldithiocarbamic acid sodium salt trihydrate, SOD and NF-kappaB inhibitor

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Product protocols

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