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Cat.No.: F1556
| Dilution |
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| Application |
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| IF |
| Reactivity |
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| Human |
| Source |
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| Mouse Monoclonal Antibody |
| Storage Buffer |
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| PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3 |
| Storage (from the date of receipt) |
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| -20°C (avoid freeze-thaw cycles), 2 years |
| Positive Control | HeLa cells; Hek293 cells |
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| Negative Control |
| Specificity |
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| Giantin (Golgi Marker) Antibody [F5N17] detects endogenous levels of total Giantin protein. |
| Clone |
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| F5N17 |
| Synonym(s) |
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| Golgin subfamily B member 1; 372 kDa Golgi complex-associated protein (GCP372); Giantin; Macrogolgin; GOLGB1 |
| Background |
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| Giantin (GOLGB1), also known as Giantin Golgi protein, is the largest mammalian golgin, a family of long coiled-coil proteins localized primarily to the cis/medial Golgi and serving as a key structural marker of Golgi integrity. Giantin consists of an extended rod-like coiled-coil cytoplasmic domain that forms a rigid scaffold, a C-terminal transmembrane anchor, and interaction motifs for proteins such as p115, GM130, GRASP65, Rab1, and SNAREs, enabling it to tether vesicles without reliance on specific key residues. It regulates Golgi architecture by inhibiting excessive fusion and interconnections between stacks and cisternae, ensuring the formation of discrete reaction compartments for sequential glycosylation; knockdown of Giantin leads to reduced fenestrae size and number, accelerated membrane protein diffusion, and increased cisternal connectivity, which slows intra-Golgi transport and impacts protein and lipid glycosylation. Biologically, Giantin tethers COPI vesicles to the cis-Golgi, facilitates ER-Golgi and intra-Golgi trafficking through complexes with coat proteins, and supports Golgi reassembly after mitosis or disruption by agents like brefeldin A or ethanol. It coordinates the secretory pathway for surface and lysosomal protein sorting, with its loss altering glycosylation patterns and cargo kinetics. Disease associations include Congenital Disorders of Glycosylation (CDG), connective tissue disorders, ciliopathies (from dynein-2 mislocalization), and impaired secretion due to trafficking defects. |
| References |
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