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SAB2100035

Sigma-Aldrich

Anti-ACSL4 antibody produced in rabbit

affinity isolated antibody

Synonyme(s) :

Anti-ACS4, Anti-Acyl-CoA synthetase long-chain family member 4, Anti-FACL4, Anti-LACS4, Anti-MRX63, Anti-MRX68

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

74 kDa

Espèces réactives

rat, rabbit, guinea pig, mouse, bovine, human, dog, horse

Concentration

0.5 mg - 1 mg/mL

Technique(s)

western blot: suitable

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... ACSL4(2182)

Description générale

Acyl-CoA synthetase long-chain family member 4 (Acsl4) is encoded by the gene mapped to human chromosome Xq22.3−Xq23. Acsl4 is a member of the long-chain fatty-acid-coenzyme A ligase family. All the members of this family have different substrate specificity, subcellular localization, and tissue distribution. Alternative splicing of Acsl4 gene generates two transcript variants.

Immunogène

Synthetic peptide directed towards the N terminal region of human ACSL4

Application

Anti-ACSL4 antibody produced in rabbit has been used as a mitochondria-associated membrane (MAM) marker.

Actions biochimiques/physiologiques

ACSL4 is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme preferentially utilizes arachidonate as substrate. The absence of this enzyme may contribute to the mental retardation or Alport syndrome. Alternative splicing of this gene generates two transcript variants.
Long-chain fatty-acid-coenzyme A ligase family members convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby facilitate lipid biosynthesis and fatty acid degradation. Acsl4 plays a critical role in ferroptosis execution. It also contributes to the dendritic spine architecture. Acsl4 isozyme preferentially utilizes arachidonate as substrate. The absence of this enzyme may contribute to the non-syndromic X-linked mental retardation or Alport syndrome.

Séquence

Synthetic peptide located within the following region: AKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVSKFGK

Forme physique

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Acsl4 Dictates Ferroptosis Sensitivity by Shaping Cellular Lipid Composition
Doll S, et al.
Nature Chemical Biology, 13, 91-91 (2017)
N-Acetylcysteine prevents the spatial memory deficits and the redox-dependent RyR2 decrease displayed by an Alzheimer?s disease rat model
More JY, et al.
Frontiers in Aging Neuroscience, 10(4), 399-399 (2018)
AMMECR1: a single point mutation causes developmental delay, midface hypoplasia and elliptocytosis
Andreoletti G, et al.
Journal of medical Genetics, 54(4), 269-277 (2017)
The XLMR gene ACSL4 plays a role in dendritic spine architecture
Meloni I, et al.
Neuroscience, 159, 657-669 (2009)

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