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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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can act as a negative mediator in autophagy through stimulation of the AKT (show AKT1 Proteins)-MTORC1 pathway and direct interaction with LC3.
Data show that p62 interaction with LC3, leading to the delivery of p62 and its cargoes to the autophagosome.
LC3 puncta were still present in the granular layer of nonlesional psoriatic epidermis but at a much lower level compared with healthy adult epidermis, whereas in lesional psoriatic skin, LC3 was not expressed at all.
Results suggest that P. gingivalis internalization is not necessary for LC3 lipidation.
Development of LC3/GABARAP (show GABARAP Proteins) sensors containing a LIR (show CD300C Proteins) and a hydrophobic domain to monitor autophagy.
Aldo was revealed to induce autophagy, as indicated by the increased conversion from microtubuleassociated protein 1A/1Blight chain 3 (LC3)I to LC3II, the increased expression levels of autophagyrelated gene 7 (Atg7) and the increased degradation of p62, which was accompanied by MC proliferation
LC3 overexpression is associated with colorectal cancer.
these findings were reversed with the LC3I/II-shPTEN treatment. Therefore, the loss of PTEN may promote the development of primary resistance to trastuzumab in breast cancer via autophagy defects
autophagy of cytoplasmic bulk cargo was completely LC3 independent.
Results of our present study demonstrated that beclin 1 (show BECN1 Proteins) and LC3 immunoreactivity increased in carcinoma cells following exemestane treatment and that the status of pre-treatment stromal beclin 1 (show BECN1 Proteins) is associated with higher carcinoma cell proliferation and poor clinical and pathological responses to NAE
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.
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.
we describe basic protocols to measure the levels of endogenous LC3 and p62 by immunoblotting in cultured mammalian cells
Clusterin (show CLU Proteins) facilitates stress-induced lipidation of LC3 and autophagosome biogenesis to enhance cancer cell survival.
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