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The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Additionally we are shipping Golgin A2 Antibodies (112) and many more products for this protein.
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Therefore, we confirmed the associations among Golgi function, fibrosis, and autophagy. Moreover, GOLGA2 knockout mice may be a potentially valuable animal model for studying autophagy-induced fibrosis.
the GM130-deficient mouse provides a valuable model for investigating the etiology of human globozoospermia.
In oocyte meiosis, GM130 localization and expression patterns are regulated by FMNL1 (show FMNL1 Proteins).
GM130 regulates microtubule organization and might cooperate with the MAPK (show MAPK1 Proteins) pathway to play roles in spindle organization, migration and asymmetric division during mouse oocyte maturation
GM130 upregulated expression of the key epithelial-mesenchymal transformation regulator Snail (SNAI1 (show SNAI1 Proteins)), which mediated EMT (show ITK Proteins) activation and cell invasion by GM130.
the study identified GM130 as a novel target of Coxsackievirus B3 (CVB3), which may implicate in the pathogenesis of CVB3-induced acute pancreatitis.
We describe the first human patient with a homozygous apparently loss of function mutation in GOLGA2. The phenotype is a neuromuscular disorder characterized by developmental delay, seizures, progressive microcephaly, and muscular dystrophy.
Data show that WAC (show WAC Proteins) directly binds to GM130 and that this binding is required for autophagosome formation through interacting with GABARAP (show GABARAP Proteins) regulating its subcellular localization.
Mutagenesis experiments support these structural observations and demonstrate that they are required for GRASP65 (show GORASP1 Proteins)-GM130 association.
Depletion of GM130 increases cellular velocity and increases the invasiveness of breast cancer cells, therefore supporting the view that alterations of polarity contribute to tumor progression.
GM130 is a parallel homotetramer with a flexible rod-like structure with I- and Y-shaped conformations.
H-ERG (show KCNH2 Proteins) trafficking was impaired by H2O2 after 48 h treatment, accompanied by reciprocal changes of expression between miR-17-5p seed miRNAs and several chaperones (Hsp70 (show HSP70 Proteins), Hsc70 (show HSPA8 Proteins), CANX (show CANX Proteins), and Golga20)
Induction of autophagy by shGOLGA2 may induce cell death rather than cell survival. Downregulation of GOLGA2/GM130 may be a potential therapeutic option for lung cancer.
GM130 is involved in the control of glycosylation, cell cycle progression, cell polarization and directed cell migration, according to this review.
The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions between the Golgi and microtubules are thought to be important for the reorganization of the Golgi after it fragments during mitosis. This gene encodes one of the golgins, a family of proteins localized to the Golgi. This encoded protein has been postulated to play roles in the stacking of Golgi cisternae and in vesicular transport. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of these variants has not been determined.
, golgin subfamily A member 2-like
, Golgin subfamily A member 2-like
, 130 kDa cis-Golgi matrix protein
, Golgin subfamily A member 2
, SY11 protein
, cis-Golgi matrix protein GM130
, golgi autoantigen, golgin subfamily a, 2
, GM130 autoantigen
, Golgi matrix protein GM130