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AB141762

HELSS, inhibitor of Ca2+ independent PLA2

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MW 317.18 Da, Purity >98%. Potent, irreversible, selective inhibitor of Ca2+ independent PLA2 (IC50 = 1 μM). Active *in vivo.*.
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Chemical Structure - HELSS, inhibitor of Ca2+ independent PLA2 (AB141762)
  • Chemical Structure

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Chemical Structure - HELSS, inhibitor of Ca2+ independent PLA2 (AB141762)

2D chemical structure image of ab141762, HELSS, inhibitor of Ca2+ independent PLA2

Key facts

CAS number

88070-98-8

Purity

>98%

Form

Solid

form

Molecular weight

317.18 Da

Molecular formula

C<sub>1</sub><sub>6</sub>H<sub>1</sub><sub>3</sub>BrO<sub>2</sub>

PubChem

5940264

Nature

Synthetic

Solubility

Soluble in DMSO to 75 mM

Biochemical name

Bromoenol lactone

Biological description

Potent, irreversible, selective inhibitor of Ca2+ independent PLA2 (IC50 = 1 μM). Active *in vivo.*

Canonical smiles

C1CC(=CBr)OC(=O)C1C2=CC=CC3=CC=CC=C32

Isomeric smiles

C1C/C(=C\Br)/OC(=O)C1C2=CC=CC3=CC=CC=C32

InChi

InChI=1S/C16H13BrO2/c17-10-12-8-9-15(16(18)19-12)14-7-3-5-11-4-1-2-6-13(11)14/h1-7,10,15H,8-9H2/b12-10+

InChiKey

BYUCSFWXCMTYOI-ZRDIBKRKSA-N

IUPAC Name

(6E)-6-(bromomethylidene)-3-naphthalen-1-yloxan-2-one

Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Store under desiccating conditions|The product can be stored for up to 12 months

Supplementary information

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

ALDH1A1 also known as retinal dehydrogenase 1 is a cytosolic enzyme with a molecular mass of approximately 55 kDa. It plays a mechanical role in the oxidation of retinal to retinoic acid which is important for a variety of biological processes. This enzyme is mostly expressed in the liver corneal epithelium and the brain. FAAH1 also known as fatty acid amide hydrolase is another enzyme related to the degradation of fatty acid amides like anandamide. FAAH1 is around 63 kDa and is present in high levels in the brain and liver. Both proteins maintain important enzymatic functions within their respective tissues.
Biological function summary

ALDH1A1 and FAAH1 participate in distinct metabolic pathways that help regulate key physiological activities. ALDH1A1 is involved in the synthesis of retinoic acid an active metabolite of vitamin A which is essential for vision immune function and cellular differentiation. FAAH1 while part of a different pathway plays a role in breaking down endocannabinoids. These two proteins not only regulate important biochemical reactions but also serve in maintaining metabolic balance.

Pathways

ALDH1A1 fits into the retinoic acid signaling pathway critical for cellular growth and differentiation. FAAH1 is involved in the endocannabinoid signaling pathway influencing mood pain sensation and appetite. Both enzymes despite being part of separate pathways emphasize the regulation of metabolites important to physiological homeostasis. ALDH1A1 shares interactions through the retinoid pathway with other enzymes like CYP26A1. FAAH1 interacts with cannabinoid receptors affected by the net concentration of endocannabinoids.

ALDH1A1 relates to alcohol use disorder due to its function in alcohol metabolism. Alterations in ALDH1A1 activity can result in varying susceptibility to alcohol-related liver toxicity. FAAH1 has connections to anxiety disorders as changes in endocannabinoid levels impact anxiety-like behaviors. Through disease contexts ALDH1A1 and FAAH1 link to key regulatory proteins like ALDH2 and CB1 receptor respectively influencing disease progression and potential therapeutic interventions.

Product protocols

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