GM130 (E9Z6S) Rabbit mAb #70767
- WB
- IF
Supporting Data
REACTIVITY | M R |
SENSITIVITY | Endogenous |
MW (kDa) | 140 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- M-Mouse
- R-Rat
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Immunofluorescence (Frozen) | 1:400 - 1:800 |
Immunofluorescence (Immunocytochemistry) | 1:1600 - 1:3200 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro77 of mouse GM130 protein.
Background
The Golgi apparatus functions in the modification, organization, and transport of proteins and membranes targeted to other parts of the cell, such as the plasma membrane, lysosomes, and endosomes. This regulated transport is important for appropriate protein localization, secretion, and signal transduction. Members of the Golgin family of proteins, including GM130, Giantin, p115, and GRASP65, are defined by their presence in the Golgi matrix and by their long coiled-coil domains. Golgin function, which is regulated in part by small GTPases of the Rab and Arl families, includes establishing and maintaining Golgi structure and transport (reviewed in 1). The Golgi cisternae are stacked and linked laterally to form a ribbon. GRASP65 and GM130 are required for membrane fusion events that mediate ribbon formation during Golgi assembly. These lateral fusion events allow for uniform distribution of Golgi enzymes (2). GM130 and Giantin interact with the transport factor p115 to facilitate endoplasmic reticulum (ER)-Golgi transport (3). GM130 is also involved in the transport of the ether-a-go-go-related (hERG) potassium ion channel. Inappropriate hERG localization may be an underlying cause of long QT syndrome, a hereditary and potentially fatal cardiac arrhythmia (4). Further, GM130 was implicated in signal transduction regulating invasion, migration, and cell polarization via its interaction with and activation of serine/threonine kinases YSK1 and Mst4 (5).
Limited Uses
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