SAB2100035
Anti-ACSL4 antibody produced in rabbit
affinity isolated antibody
Synonym(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
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
74 kDa
species reactivity
rat, rabbit, guinea pig, mouse, bovine, human, dog, horse
concentration
0.5 mg - 1 mg/mL
technique(s)
western blot: suitable
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... ACSL4(2182)
Related Categories
General description
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.
Immunogen
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.
Biochem/physiol Actions
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.
Sequence
Synthetic peptide located within the following region: AKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVSKFGK
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
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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WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Find documentation for the products that you have recently purchased in the Document Library.
Acsl4 Dictates Ferroptosis Sensitivity by Shaping Cellular Lipid Composition
Doll S, et al.
Nature Chemical Biology, 13, 91-91 (2017)
The XLMR gene ACSL4 plays a role in dendritic spine architecture
Meloni I, et al.
Neuroscience, 159, 657-669 (2009)
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)
Xiaojia Guo et al.
Scientific reports, 13(1), 22255-22255 (2023-12-15)
Cisplatin (CP) induces acute kidney injury (AKI) whereby proximal tubules undergo regulated necrosis. Repair is almost complete after a single dose. We now demonstrate a role for Apolipoprotein B mRNA editing enzyme, catalytic polypeptide 1 (Apobec-1) that is prominently expressed
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)
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