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The results presented here show the major role of LAMP-2 in caveolin traffic and membrane repair and consequently in T. cruzi invasion.
The up-regulation of Rab11 (show RAB11A ELISA Kits), Rab7 (show RAB7A ELISA Kits), or RILP (show RILP ELISA Kits), but not its truncated form RILP (show RILP ELISA Kits)-C33 (show CD82 ELISA Kits), rescued LAMP2A-defective trafficking in cystinosis, whereas dominant-negative Rab11 (show RAB11A ELISA Kits) or Rab7 (show RAB7A ELISA Kits) impaired LAMP2A trafficking.
LAMP-2 in the central nervous system has a possible role in the degradation of the various macromolecules in lysosomes and an additional function concerning protection from oxidative stress, especially in the substantia nigra.
The absence of LAMP-2 in murine brain led to inflammation and abnormal behavior, including motor deficits and impaired learning.
Lamp-2 deficiency prevents high-fat diet-induced obese diabetes via enhancing energy expenditure.
These results suggest that VPS35 deficiency or mutation promotes Parkinson Disease (PD) pathogenesis, and reveals a crucial pathway, VPS35-Lamp2a-alpha-synuclein, to prevent PD pathogenesis.
LAMP proteins retain TAPL (show ABCB9 ELISA Kits) on the limiting membrane of endosomes and prevent its sorting to intraluminal vesicles.
Restoration of lysosome-associated membrane protein-2 levels synergizes with partial BECLIN-1 (show BECN1 ELISA Kits) knockdown to restore autophagosome processing and to attenuate cell death after hypoxia-reoxygenation.
results suggest that LAMP-2, its luminal domain in particular, plays a critical role in endosomal cholesterol transport and that this is distinct from the chaperone-mediated autophagy function of LAMP-2
Using LAMP1 (show LAMP1 ELISA Kits)/2 knock out cells the authors show that these two proteins are important for Trypanosoma cruzi infection of host cells, both in entrance and intracellular development, conceivably by being the major source of sialic acid for Trypanosoma cruzi.
Since effective regimens are readily available timely psychiatric evaluation is warranted in all newly diagnosed subjects with LAMP2 mutations, regardless of whether they show the typical Danon disease medical (cardiac) symptoms or not.
The authors show here that human LAMP1 (show LAMP1 ELISA Kits) and LAMP2 bind cholesterol in a manner that buries the cholesterol 3beta-hydroxyl group; they also bind tightly to NPC1 (show NPC1 ELISA Kits) and NPC2 (show NPC2 ELISA Kits) proteins that export cholesterol from lysosomes.
identified LAMP-2 as an endocytic receptor on monocyte-derived dendritic cells (MoDC) that routes cargo into unusual Ag processing pathways, which reduces surface expression of Ag-derived peptides while selectively enriching Ag within immunogenic exosome; this novel pathway has implications for the initiation of immune responses both locally and at distant sites
downregulation of FUT1 (show FUT1 ELISA Kits), which leads to the perinuclear localization of LAMP-1 (show LAMP1 ELISA Kits) and 2, is correlated with increased rate of autophagic flux by decreasing mTOR (show FRAP1 ELISA Kits) signaling and increasing autolysosome formation.
The results provide a new insight that LAMP-2 contributes to the ROS (show ROS1 ELISA Kits) clearance and cell death induced by Zn(2+) treatment, which would help us to get a better understanding of Zn(2+)-induced toxicity in respiratory system.
Genetic analysis identified 2 novel LAMP2 gene mutations. In Family A, a G-A transition (c.962G > A) leading to a nonsense mutation at codon 321 (p.Trp321Ter), and in Family B, a one-nucleotide insertion (c.973insC) leading to a full frame-shift (p.Pro324+24X) was detected in exon 8 of the LAMP2 gene.
the assembly modes of LAMP-1 (show LAMP1 ELISA Kits) and LAMP-2 are different, which may underlie their distinct functions
intracellular Salmonella recruit the host proteins LAMP-2A and Hsc73 (show HSPA8 ELISA Kits), key components of the host protein turnover pathway known as chaperone-mediated autophagy involved in transport of cytosolic proteins to the lysosome for degradation.
3 novel nonsense mutations (p.Q240X, p.S250X, and p.G22X) were found in LAMP2 associated with early onset Danon disease with hypertrophic cardiomyopathy. LAMP2 expression was absent in both cardiac and skeletal muscle samples of the first proband and severely decreased LAMP2 expression in the skeletal muscle samples of the second proband.
Increased expression of LAMP2 has been observed in peripheral blood mononuclear cells of coronary artery disease patients compared to the control group.
The protein encoded by this gene is a member of a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands. It may play a role in tumor cell metastasis. It may also function in the protection, maintenance, and adhesion of the lysosome. Alternative splicing of this gene results in multiple transcript variants encoding distinct proteins.
lysosome-associated membrane glycoprotein 2
, lysosomal-associated membrane protein 2
, Lysosome-associated membrane glycoprotein 2
, lysosome-associated membrane glycoprotein 2-like
, CD107 antigen-like family member B
, Lysosome-associated membrane protein 2
, Lamp II
, lysosomal membrane glycoprotein 2
, lysosomal membrane glycoprotein type B
, lysosome-associated membrane protein 2
, lysosome-associated membrane protein-2
, lysosome-associated membrane glycoprotein LAMP-2