ACSL4 antibody (AA 236-267)

Catalog No. ABIN2850437

This Rabbit Polyclonal antibody specifically detects ACSL4 in WB and IHC (p). It exhibits reactivity toward Human and has been mentioned in 11+ publications.

Quick Overview for ACSL4 antibody (AA 236-267) (ABIN2850437)

Target: ACSL4 (Acyl-CoA Synthetase Long-Chain Family Member 4 (ACSL4))

Reactivity: Human

Host: Rabbit

Clonality: Polyclonal

Conjugate: This ACSL4 antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))

Clone: RB04697

Product Details anti-ACSL4 Antibody

Binding Specificity: AA 236-267

Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.

Immunogen: This ACSL4 (FACL4) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 236-267 amino acids from the Central region of human ACSL4 (FACL4).

Isotype: Ig Fraction

Application Details

Application Notes: WB: 1:1000. IHC-P: 1:25

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: 4 °C,-20 °C

Storage Comment: Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots to prevent freeze-thaw cycles.

Expiry Date: 6 months

References for anti-ACSL4 antibody (ABIN2850437)

Shinjo, Jiang, Nameta, Suzuki, Kanai, Nomura, Goda: "Disruption of the mitochondria-associated ER membrane (MAM) plays a central role in palmitic acid-induced insulin resistance." in: Experimental cell research, Vol. 359, Issue 1, pp. 86-93, (2017) (PubMed).

Pera, Larrea, Guardia-Laguarta, Montesinos, Velasco, Agrawal, Xu, Chan, Di Paolo, Mehler, Perumal, Macaluso, Freyberg, Acin-Perez, Enriquez, Schon, Area-Gomez: "Increased localization of APP-C99 in mitochondria-associated ER membranes causes mitochondrial dysfunction in Alzheimer disease." in: The EMBO journal, Vol. 36, Issue 22, pp. 3356-3371, (2017) (PubMed).

Marzesco, Flötenmeyer, Bühler, Obermüller, Staufenbiel, Jucker, Baumann: "Highly potent intracellular membrane-associated Aβ seeds." in: Scientific reports, Vol. 6, pp. 28125, (2016) (PubMed).

Williamson, Wong, Bozidis, Zhang, Colberg-Poley et al.: "Isolation of Endoplasmic Reticulum, Mitochondria, and Mitochondria-Associated Membrane and Detergent Resistant Membrane Fractions from Transfected Cells and from Human Cytomegalovirus-Infected ..." in: Current protocols in cell biology, Vol. 68, pp. 3.27.1-33, (2016) (PubMed).

Zhang, Hildreth, Colberg-Poley: "Human cytomegalovirus inhibits apoptosis by proteasome-mediated degradation of Bax at endoplasmic reticulum-mitochondrion contacts." in: Journal of virology, Vol. 87, Issue 10, pp. 5657-68, (2013) (PubMed).

Zhang, Williamson, Wong, Bullough, Brown, Hathout, Colberg-Poley: "Quantitative proteomic analyses of human cytomegalovirus-induced restructuring of endoplasmic reticulum-mitochondrial contacts at late times of infection." in: Molecular & cellular proteomics : MCP, Vol. 10, Issue 10, pp. M111.009936, (2011) (PubMed).

Horner, Liu, Park, Briley, Gale: "Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 108, Issue 35, pp. 14590-5, (2011) (PubMed).

Williamson, Zhang, Colberg-Poley: "The human cytomegalovirus protein UL37 exon 1 associates with internal lipid rafts." in: Journal of virology, Vol. 85, Issue 5, pp. 2100-11, (2011) (PubMed).

Rodriguez, Bhat, Meloni, Ladd, Leslie, Doyne, Renieri, Dupont, Stevenson, Schwartz, Srivastava: "Intellectual disability, midface hypoplasia, facial hypotonia, and Alport syndrome are associated with a deletion in Xq22.3." in: American journal of medical genetics. Part A, Vol. 152A, Issue 3, pp. 713-7, (2010) (PubMed).

Area-Gomez, de Groof, Boldogh, Bird, Gibson, Koehler, Yu, Duff, Yaffe, Pon, Schon: "Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria." in: The American journal of pathology, Vol. 175, Issue 5, pp. 1810-6, (2009) (PubMed).

Simmen, Aslan, Blagoveshchenskaya, Thomas, Wan, Xiang, Feliciangeli, Hung, Crump, Thomas: "PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis." in: The EMBO journal, Vol. 24, Issue 4, pp. 717-29, (2005) (PubMed).

Target Details for ACSL4

Target: ACSL4 (Acyl-CoA Synthetase Long-Chain Family Member 4 (ACSL4))

Alternative Name: ACSL4 (FACL4)

Background: Long chain acyl-CoA synthetase (LACS), or long chain fatty acid-CoA ligase (FACL), converts free long chain fatty acids into fatty acyl-CoA esters, key intermediates in the synthesis of complex lipids. The FACL4 gene encodes a form of LACS and is expressed in several tissues, including brain. FACL4 cDNA from brain encodes a gene product that shows preference for arachidonic acid as a substrate when expressed in mammalian cells.1 The sequence of the predicted 670-amino acid human protein is 97 % identical to that of rat ACS4. FACL4 is highly expressed in adult human brain, especially in the cerebellum and hippocampus, similar to the mouse.2 A strong cytoplasmic staining was found in the Purkinje and granular cells of the cerebellum and the pyramidal layer of hippocampus, indicating that FACL4 is specifically expressed in neurons and not in glial cells. Two patients with Alport syndrome, elliptocytosis, and mental retardation carried a large deletion of the COL4A5 region that included FACL4.3 The absence of FACL4 might play a role in the development of mental retardation or other signs associated with Alport syndrome. Two point mutations, 1 missense and 1 splice site change, were reported in the FACL4 gene in 2 families with nonspecific mental retardation.2 Analysis of enzymatic activity in lymphoblastoid cell lines of affected individuals revealed low levels compared with normal cells, indicating that both mutations are null mutations.

Molecular Weight: 79188

Gene ID: 2182

NCBI Accession: NP_004449, NP_075266

UniProt: O60488