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Dog (Canine) Polyclonal MAP1LC3A Primary Antibody for ELISA, FACS - ABIN250719
Zhang, Yu, Pan, Hu, Hao, Cai, Zhu, Yu, Xie, Ma, Yuan: Small molecule regulators of autophagy identified by an image-based high-throughput screen. in Proceedings of the National Academy of Sciences of the United States of America 2007
Show all 226 Pubmed References
Cow (Bovine) Polyclonal MAP1LC3A Primary Antibody for FACS, ICC - ABIN446593
Dehay, Bové, Rodríguez-Muela, Perier, Recasens, Boya, Vila: Pathogenic lysosomal depletion in Parkinson's disease. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2010
Show all 17 Pubmed References
Dog (Canine) Polyclonal MAP1LC3A Primary Antibody for ELISA, ICC - ABIN250720
Kabeya, Mizushima, Ueno, Yamamoto, Kirisako, Noda, Kominami, Ohsumi, Yoshimori: LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. in The EMBO journal 2000
Show all 6 Pubmed References
Dog (Canine) Polyclonal MAP1LC3A Primary Antibody for ELISA, IHC (fro) - ABIN250721
Mizushima, Yamamoto, Hatano, Kobayashi, Kabeya, Suzuki, Tokuhisa, Ohsumi, Yoshimori: Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. in The Journal of cell biology 2001
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Human Polyclonal MAP1LC3A Primary Antibody for DB, ELISA - ABIN548604
Lum, DeBerardinis, Thompson: Autophagy in metazoans: cell survival in the land of plenty. in Nature reviews. Molecular cell biology 2005
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Human Polyclonal MAP1LC3A Primary Antibody for IF (p), IHC (p) - ABIN1714263
Chen, Wei, Nie, Lin, Tian, Liu, Yu, Cheng, Yan, Wang, Liu, Deng, Lai, Zhou, Zhang, Lin, Chen: ?-Asarone prevents autophagy and synaptic loss by reducing ROCK expression in asenescence-accelerated prone 8 mice. in Brain research 2014
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Human Polyclonal MAP1LC3A Primary Antibody for WB - ABIN1883177
Gladue, ODonnell, Baker-Branstetter, Holinka, Pacheco, Fernandez-Sainz, Lu, Brocchi, Baxt, Piccone, Rodriguez, Borca: Foot-and-mouth disease virus nonstructural protein 2C interacts with Beclin1, modulating virus replication. in Journal of virology 2012
Cow (Bovine) Polyclonal MAP1LC3A Primary Antibody for IHC, WB - ABIN2784522
Taylor, Kirkegaard: Modification of cellular autophagy protein LC3 by poliovirus. in Journal of virology 2007
Human Polyclonal MAP1LC3A Primary Antibody for DB, EIA - ABIN1449623
Su, Chao, Huang, Weng, Jeng, Lai: Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy. in Journal of virology 2011
Show all 9 Pubmed References
Human Polyclonal MAP1LC3A Primary Antibody for IF, WB - ABIN6683067
Li, Zhao, Wang, Shao, Wang, Wang, Xing: Regulation of autophagy factors by oxidative stress and cardiac enzymes imbalance during arsenic or/and copper induced cardiotoxicity in Gallus gallus. in Ecotoxicology and environmental safety 2018
LC3 may influence the perineural invasion and prognosis of pancreatic cancer through ubiquitin C
p66SHC is a novel regulator of autophagy and mitophagy in B cells and recruits LC3-II. This implies p66SHC-mediated coordination of autophagy and apoptosis in B cell survival and differentiation.
LC3 and STRAP regulate actin filament assembly by JMY during autophagosome formation.
Data reveal that the stability and cargo recognition ability of LC3 are highly dependent on its acetylation. Acetylation blocked LC3's interaction with p62 preventing the mis-targeting of p62 to nonautophagic LC3 and thus permitting the efficient degradation of autophagic cargoes. Acetylation also inhibited LC3 proteasome-dependent degradation, thus maintaining LC3 as a long-lived protein that could be used as a reserve.
Flightless-I functions as a checkpoint protein for selective autophagy by interacting with p62 to block its recognition of LC3, leading to tumorigenesis in breast cancer.
Data reveal the nuanced role of the ATG14 ALPS in membrane curvature sensing, suggesting that the ALPS has additional roles in supporting LC3 lipidation.
A new molecular mechanism has been described in uterine sarcoma, by which miR-152 and miR-24 promote autophagy by activating SIRT1 and deacetylating LC3.
PHB2 forms a ternary protein complex with sequestosome 1 (SQSTM1) and LC3, leading to loading of LC3 onto the damaged mitochondria.
The distribution of nuclear LC3 can be a novel way for further studying death of acute myeloid leukemia (AML) cells,and the regulatory molecules may be new targets for treating AML.
calreticulin induces autophagy by interacting with microtubule-associated protein 1A/1B-light chain 3 (LC3). Confocal microscopy revealed that the colocalization of calreticulin and LC3 at the autophagosome was enhanced under ER stress conditions.
High expression of LC3, beclin 1 and p62 was significantly more frequent in high-grade gliomas than in low-grade.Kaplan-Meier analyses revealed that LC3, p62 and autophagy status were significantly associated with poorer survival.
These results unambiguously demonstrate that IcsB is required for double-membrane vacuole escape during cell-to-cell spread, regardless of LC3 recruitment, and do not support the previously proposed notion that autophagy counters Shigella flexneri dissemination.
Absence of MAP1LC3A disrupts the autophagic pathway and leads to the failure of aggresome vimentin cage degradation in primary choroid plexus carcinoma.
High LC3 expression is associated with Glioma.
Intense autophagic activity, as assessed by LC3A immunostaining and Stone-like structures quantification, is a strong prognostic marker in gastric cancer and can be useful for clinical application.
show that the WD repeat-containing C-terminal domain (WD40 CTD) of ATG16L1 is essential for LC3 recruitment to endolysosomal membranes during non-canonical autophagy
Expression and Clinical Significance of LC-3 and P62 in Non-small Cell Lung Cancer
The results suggest that autophagy-associated proteins LC3A, LC3B, and Beclin-1 might be potential biomarkers for subclassification, differentiation, and local metastasis in primary lung tumor.
High LC3 Expression is Associated with Cancer Progression and Chemo-Resistance in Esophageal Squamous Cell Carcinoma.
Data suggest that, in patients with diabetic kidney disease, urinary excretion of mRNAs for MAP1LC3A, WIPI2, and RB1CC1 is down-regulated as compared to healthy control subjects; these transcripts may serve as urinary autophagy biomarkers. (MAP1LC3A = microtubule associated protein 1 light chain 3; WIPI2 = WD repeat domain phosphoinositide-interacting protein 2; RB1CC1 = RB1 inducible coiled-coil 1)
Inhibiting ROS production in Nlrx1 (-/-) macrophages almost completely abolishes H. capsulatum-induced LC3 conversion.
aberrant accumulation of mitochondria in Neuro-2a cells may be attributed to insufficient BNIP3-mediated mitophagy due to poor interaction between BNIP3 and LC3-II. ... our data indicated for the first time that impaired autophagy degradation and inefficient BNIP3-mediated mitophagy may constitute mechanisms underlying neuronal cell damage during chronic hypoxia.
Data suggest a direct link between microtubule-associated protein 1-light chain 3 (LC3)-associated phagocytosis (LAP) formation and IKK alpha (IKKalpha) recruitment downstream of -like receptor 9 (TLR9) activation that is necessary to facilitate type I IFN production.
Enforced expression of CDC20 in cardiomyocytes and in the heart aggravated the hypertrophic response. Furthermore, the authors found that CDC20 directly targeted LC3, a key regulator of autophagy, and promoted LC3 ubiquitination and degradation by the proteasome, which inhibited autophagy leading to cardiac hypertrophy.
In mouse RPE and neural retina, LC3A and LC3B were expressed at approximately equivalent levels.
During the liver stage of a malaria infection, plasmodium UIS3 binds host microtubule-associated protein 1 light chain 3 (LC3) through a non-canonical interaction with a specialized surface on LC3 where host proteins with essential functions during autophagy also bind. UIS3 acts as a autophagy inhibitor by competing with host LC3-interacting proteins for LC3 binding.
The LC3-decorated vacuoles are bound by an apparently undamaged single membrane, and fail to associate with the molecules implicated in selective autophagy, such as ubiquitin or adaptors.
With increasing age, expression of the autophagy proteins ATG5 and LC3 in meniscus and articular cartilage was significantly reduced by 24 months.
the conjugation of ubiquitin-like LC3 homologs to the phospholipids of membranes may change the destiny of the membranes beyond degradation through lysosomal fusion
analysis of soluble SQSTM1 complexes and soluble complexes formed between SQSTM1 oligomers and LC3 using a combination of fluorescence microscopy-based biophysical approaches in living cells
paxillin interacts with processed LC3 through a conserved LIR motif in the amino-terminal end of paxillin and that this interaction is regulated by oncogenic SRC activity.
These results suggest that the Golgi complex may serve as a membrane platform for noncanonical autophagy where V-ATPase is 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-dependent ERK1 activity.
Development of LC3/GABARAP sensors containing a LIR and a hydrophobic domain to monitor autophagy.
These findings demonstrate that LC3 contributes to melanogenesis by increasing ERK-dependent MITF 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 clearance in vitro and in vivo.
we describe basic protocols to measure the levels of endogenous LC3 and p62 by immunoblotting in cultured mammalian cells
Clusterin facilitates stress-induced lipidation of LC3 and autophagosome biogenesis to enhance cancer cell survival.
A study of the expression of BECN1, LC3-II, and LAMP1 throughout the luteal phase of the estrous cycle in order to assess autophagy during corpus luteum development is reported.
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, mTOR, Beclin-1) 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.
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 3 alpha
, microtubule-associated protein 1-light chain 3A