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Human MAP1LC3A Protein expressed in Wheat germ - ABIN1310152
Martinet, Schrijvers, Timmermans, Bult, De Meyer: Immunohistochemical analysis of macroautophagy: recommendations and limitations. in Autophagy 2013
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we report that autophagy is associated with apoptosis processes, involving LC3 and TRIF (show TRIM69 Proteins)-colocation in human HCC (show FAM126A Proteins) cells. Regulation of autophagy and the TLR3 (show TLR3 Proteins)-TRIF (show TRIM69 Proteins) pathway may be effective in the treatment of liver cancer.
The autophagy induced by 2-PCPA requires LC3-II processing machinery..2-PCPA treatment induces the change of global gene expression program, including a series of autophagy-related genes, such as SQSTM1/p62 (show SQSTM1 Proteins). Taken together, our data indicate that KDM1A/LSD1 (show KDM1A Proteins) inhibitors induce autophagy through affecting the expression of autophagy-related genes and in a BECN1 (show BECN1 Proteins)-independent manner
LC3 and p62/SQSTM1 (show SQSTM1 Proteins) have roles in early-stage non-small cell lung cancer
Hotspot mutations in the arginine-rich stretch in MAP1LC3A resulting in reduced cleavage of MAP1LC3A by ATG4B (show ATG4B Proteins) both in vitro and in vivo, suggesting a functional implication of this gene mutation in cancer development.
FYCO1 (show FYCO1 Proteins) and MAP1LC3A interact through a novel binding mode that involves Atg8 (show GABARAPL2 Proteins)-family proteins
analysis of soluble SQSTM1 (show SQSTM1 Proteins) complexes and soluble complexes formed between SQSTM1 (show SQSTM1 Proteins) oligomers and LC3 using a combination of fluorescence microscopy-based biophysical approaches in living cells
we found that ATG14 interacted with Ulk1 and LC3, and knock down of Ulk1 prevented the lipidation of LC3 and autophagy in HeLa-ATG14 cells. We also identified a phosphatidylethanolamine (PE) binding region in ATG14, and the addition of Ulk1 to Hela-ATG14 cells decreased the ATG14-PE interaction.
Legionella pneumophila RavZ extracts LC3-PE from the membrane before deconjugation. RavZ initially recognizes the LC3 molecule on membranes via its N-terminal LC3-interacting region (LIR (show CD300C Proteins)) motif.
The results are consistent with a model in which RPIA (show RPIA Proteins) suppresses autophagy and LC3 processing by modulation of redox signaling.
can act as a negative mediator in autophagy through stimulation of the AKT (show AKT1 Proteins)-MTORC1 pathway and direct interaction with LC3.
the conjugation of ubiquitin-like LC3 homologs to the phospholipids of membranes may change the destiny of the membranes beyond degradation through lysosomal fusion
paxillin (show PXN Proteins) interacts with processed LC3 through a conserved LIR (show CD300C Proteins) motif in the amino-terminal end of paxillin (show PXN Proteins) and that this interaction is regulated by oncogenic SRC (show SRC Proteins) activity.
These results suggest that the Golgi complex may serve as a membrane platform for noncanonical autophagy where V-ATPase (show ATP6V1H Proteins) is (show ATP11A Proteins) a key player.
LC3 was down regulated in the hypothalamus of diabetic mice.
LC3 overexpression in 3T3-L1 preadipocytes stimulates adipocyte differentiation via direct modulation of RKIP (show PEBP1 Proteins)-dependent ERK1 (show MAPK3 Proteins) activity.
Development of LC3/GABARAP (show GABARAP Proteins) sensors containing a LIR (show CD300C Proteins) and a hydrophobic domain to monitor autophagy.
These findings demonstrate that LC3 contributes to melanogenesis by increasing ERK (show EPHB2 Proteins)-dependent MITF (show MITF Proteins) expression, thereby providing a mechanistic insight into the signaling network that links autophagy to melanogenesis.
LC3 is exploited by coxsackievirus in both autophagy-dependent and -independent manners in vivo
LC3 overexpression thus exerts neuroprotection through increasing alpha7nAChR expression for eAbeta binding and further enhancing autophagic activity for Abeta (show APP Proteins) clearance in vitro and in vivo.
Hedgehog (show SHH Proteins) signaling is required for the Lc3 synthase (show B3GNT5 Proteins) expression in embryonic lens
LC3 is localized in porcine oocytes during in vitro maturation.
Data suggest that expression of MAP1LC3A in graafian follicle/granulosa cell/theca cell is distinct in normal pigs versus miniature pigs; expression of MAP1LC3A is higher in normal pigs than in miniature pigs; MAP1LC3A may be marker of autophagy.
Data indicate that the expression of MAP1LC3A, B and autophagy-associated genes (ATG5 (show ATG5 Proteins), mTOR (show FRAP1 Proteins), Beclin-1 (show BECN1 Proteins)) was increased in normal pigs, while decreased in miniature pigs.
MAP1A and MAP1B are microtubule-associated proteins which mediate the physical interactions between microtubules and components of the cytoskeleton. MAP1A and MAP1B each consist of a heavy chain subunit and multiple light chain subunits. The protein encoded by this gene is one of the light chain subunits and can associate with either MAP1A or MAP1B. Two transcript variants encoding different isoforms have been found for this gene. The expression of variant 1 is suppressed in many tumor cell lines, suggesting that may be involved in carcinogenesis.
microtubule-associated protein 1 light chain 3 alpha
, 35-alpha calcimedin
, Annexin III (Lipocortin III)
, lipocortin III
, placental anticoagulant protein III
, MAP1 light chain 3-like protein 1
, MAP1A/1B light chain 3 A
, MAP1A/MAP1B LC3 A
, MAP1A/MAP1B light chain 3 A
, autophagy-related ubiquitin-like modifier LC3 A
, microtubule-associated proteins 1A/1B light chain 3
, microtubule-associated proteins 1A/1B light chain 3A
, autophagy-related protein LC3 A
, microtubule-associated protein 1-light chain 3A
, microtubule-associated proteins 1A/1B light chain 3B
, UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5A
, UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
, beta-1,3-N-acetylglucosaminyltransferase 5A
, lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase A
, lactotriaosylceramide synthase A
, lc(3)Cer synthase A
, lc3 synthase A