MAP1LC3A antibody (cleaved)

Catalog No. ABIN2849553

Product Details anti-MAP1LC3A Antibody

Target: MAP1LC3A (Microtubule-Associated Protein 1 Light Chain 3 alpha (MAP1LC3A))

Binding Specificity: AA 89-120, cleaved

Reactivity: Human, Mouse

Host: Rabbit

Clonality: Polyclonal

Conjugate: This MAP1LC3A antibody is un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunocytochemistry (ICC)

Predicted Reactivity: Zf, B, Rat

Purification: This antibody is purified through a protein A column, followed by peptide affinity purification.

Immunogen: This Cleaved LC3A antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 89-120 amino acids from human Cleaved LC3A or LC3B.

Clone: RB38908

Isotype: IgG

Application Details

Application Notes: IF: 1:25. IF: 1:25. WB: 1:500. WB: 1:500. WB: 1:500. WB: 1:500. WB: 1:1000

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.

Handling Advice: Avoid freeze-thaw cycles.

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.

Expiry Date: 6 months

References for anti-MAP1LC3A antibody (ABIN2849553)

Giatromanolaki, Sivridis, Kalamida, Koukourakis: "Transcription Factor EB Expression in Early Breast Cancer Relates to Lysosomal/Autophagosomal Markers and Prognosis." in: Clinical breast cancer, Vol. 17, Issue 3, pp. e119-e125, (2018) (PubMed).

Tavera-Mendoza, Westerling, Libby, Marusyk, Cato, Cassani, Cameron, Ficarro, Marto, Klawitter, Brown: "Vitamin D receptor regulates autophagy in the normal mammary gland and in luminal breast cancer cells." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 114, Issue 11, pp. E2186-E2194, (2018) (PubMed).

Bingel, Koeneke, Ridinger, Bittmann, Sill, Peterziel, Wrobel, Rettig, Milde, Fernekorn, Weise, Schober, Witt, Oehme: "Three-dimensional tumor cell growth stimulates autophagic flux and recapitulates chemotherapy resistance." in: Cell death & disease, Vol. 8, Issue 8, pp. e3013, (2018) (PubMed).

Miyamoto, Takano, Aoyama, Soyama, Yoshikawa, Tsuda, Furuya: "Inhibition of autophagy protein LC3A as a therapeutic target in ovarian clear cell carcinomas." in: Journal of gynecologic oncology, Vol. 28, Issue 3, pp. e33, (2017) (PubMed).

Martinet, Roth, De Meyer: "Standard Immunohistochemical Assays to Assess Autophagy in Mammalian Tissue." in: Cells, Vol. 6, Issue 3, (2017) (PubMed).

Shrestha, Assani, Rinehardt, Albastroiu, Zhang, Shell, Amer, Schlesinger, Kopp: "Cysteamine-mediated clearance of antibiotic-resistant pathogens in human cystic fibrosis macrophages." in: PLoS ONE, Vol. 12, Issue 10, pp. e0186169, (2017) (PubMed).

Giatromanolaki, Kalamida, Sivridis, Karagounis, Gatter, Harris, Koukourakis: "Increased expression of transcription factor EB (TFEB) is associated with autophagy, migratory phenotype and poor prognosis in non-small cell lung cancer." in: Lung cancer (Amsterdam, Netherlands), Vol. 90, Issue 1, pp. 98-105, (2016) (PubMed).

Tanaka, Whelan, Chandramouleeswaran, Kagawa, Rustgi, Noguchi, Guha, Srinivasan, Amanuma, Ohashi, Muto, Klein-Szanto, Noguchi, Avadhani, Nakagawa: "ALDH2 modulates autophagy flux to regulate acetaldehyde-mediated toxicity thresholds." in: American journal of cancer research, Vol. 6, Issue 4, pp. 781-96, (2016) (PubMed).

Vanoli, Necchi, Barozzi, Manca, Pecci, Solcia: "Chaperone molecules concentrate together with the ubiquitin-proteasome system inside particulate cytoplasmic structures: possible role in metabolism of misfolded proteins." in: Histochemistry and cell biology, Vol. 144, Issue 2, pp. 179-84, (2015) (PubMed).

Pecci, Necchi, Barozzi, Vitali, Boveri, Elena, Bernasconi, Noris, Solcia: "Particulate cytoplasmic structures with high concentration of ubiquitin-proteasome accumulate in myeloid neoplasms." in: Journal of hematology & oncology, Vol. 8, pp. 71, (2015) (PubMed).

Kong, Whelan, Laczkó, Dang, Caro Monroig, Soroush, Falcone, Amaravadi, Rustgi, Ginsberg, Falk, Nakagawa, Lynch: "Autophagy levels are elevated in barrett's esophagus and promote cell survival from acid and oxidative stress." in: Molecular carcinogenesis, (2015) (PubMed).

Assani, Tazi, Amer, Kopp: "IFN-? stimulates autophagy-mediated clearance of Burkholderia cenocepacia in human cystic fibrosis macrophages." in: PLoS ONE, Vol. 9, Issue 5, pp. e96681, (2014) (PubMed).

Armani, Cinti, Marzolla, Morgan, Cranston, Antelmi, Carpinelli, Canese, Pagotto, Quarta, Malorni, Matarrese, Marconi, Fabbri, Rosano, Cinti, Young, Caprio: "Mineralocorticoid receptor antagonism induces browning of white adipose tissue through impairment of autophagy and prevents adipocyte dysfunction in high-fat-diet-fed mice." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 28, Issue 8, pp. 3745-57, (2014) (PubMed).

Liao, Sun, Wang, Huang, Liu, Liao, Shi: "LC3A-positive "stone-like" structures predict an adverse prognosis of gastric cancer." in: Anatomical record (Hoboken, N.J. : 2007), Vol. 297, Issue 4, pp. 653-62, (2014) (PubMed).

Sivridis, Koukourakis, Mendrinos, Touloupidis, Giatromanolaki: "Patterns of autophagy in urothelial cell carcinomas--the significance of "stone-like" structures (SLS) in transurethral resection biopsies." in: Urologic oncology, Vol. 31, Issue 7, pp. 1254-60, (2013) (PubMed).

Koukourakis, Giatromanolaki, Zois, Sivridis: "LC3 immunostaining pitfalls." in: Histopathology, Vol. 62, Issue 6, pp. 962-3, (2013) (PubMed).

Giatromanolaki, Koukourakis, Pouliliou, Gatter, Pezzella, Harris, Sivridis: "Overexpression of LC3A autophagy protein in follicular and diffuse large B-cell lymphomas." in: Hematology/oncology and stem cell therapy, Vol. 6, Issue 1, pp. 20-5, (2013) (PubMed).

Radtke, English, Rondeau, Leib, Lippé, Desjardins: "Inhibition of the host translation shutoff response by herpes simplex virus 1 triggers nuclear envelope-derived autophagy." in: Journal of virology, Vol. 87, Issue 7, pp. 3990-7, (2013) (PubMed).

Abdulrahman, Khweek, Akhter, Caution, Tazi, Hassan, Zhang, Rowland, Malhotra, Aeffner, Davis, Valvano, Amer: "Depletion of the ubiquitin-binding adaptor molecule SQSTM1/p62 from macrophages harboring cftr ?F508 mutation improves the delivery of Burkholderia cenocepacia to the autophagic machinery." in: The Journal of biological chemistry, Vol. 288, Issue 3, pp. 2049-58, (2013) (PubMed).

Giatromanolaki, Sivridis, Mendrinos, Koutsopoulos, Koukourakis: "Autophagy proteins in prostate cancer: relation with anaerobic metabolism and Gleason score." in: Urologic oncology, Vol. 32, Issue 1, pp. 39.e11-8, (2013) (PubMed).

Target Details for MAP1LC3A

Target: MAP1LC3A (Microtubule-Associated Protein 1 Light Chain 3 alpha (MAP1LC3A))

Alternative Name: LC3A (MAP1LC3A Products)

Synonyms: ATG8E antibody, LC3 antibody, LC3A antibody, MAP1ALC3 antibody, MAP1BLC3 antibody, 1010001H21Rik antibody, 4922501H04Rik antibody, LC3a antibody, MGC69006 antibody, zgc:77094 antibody, MGC89867 antibody, MAP1LC3A antibody, map1lc3a antibody, microtubule associated protein 1 light chain 3 alpha antibody, microtubule-associated protein 1 light chain 3 alpha antibody, microtubule associated protein 1 light chain 3 alpha S homeolog antibody, MAP1LC3A antibody, Map1lc3a antibody, map1lc3a.S antibody, map1lc3a antibody

Background: Macroautophagy is the major inducible pathway for the general turnover of cytoplasmic constituents in eukaryotic cells, it is also responsible for the degradation of active cytoplasmic enzymes and organelles during nutrient starvation. Macroautophagy involves the formation of double-membrane bound autophagosomes which enclose the cytoplasmic constituent targeted for degradation in a membrane bound structure, which then fuse with the lysosome (or vacuole) releasing a single-membrane bound autophagic bodies which are then degraded within the lysosome (or vacuole). MAP1A and MAP1B are microtubule-associated proteins which mediate the physical interactions between microtubules and components of the cytoskeleton. These proteins are involved in formation of autophagosomal vacuoles (autophagosomes). MAP1A and MAP1B each consist of a heavy chain subunit and multiple light chain subunits. MAP1LC3a is one of the light chain subunits and can associate with either MAP1A or MAP1B. The precursor molecule is cleaved by APG4B/ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II.

Gene ID: 84557

NCBI Accession: NP_115903, NP_852610

UniProt: Q9H492, Q9GZQ8

Pathways: Autophagy