Anti-Golgin-97 [CDF4]

The Golgi complex is an intricate cytoplasmic organelle that has a major function in the processing, transporting, and sorting of intracellular proteins following synthesis in the rough endoplasmic reticulum. Golgins are Golgi-localized proteins with extensive coiled-coil structure throughout the entire polypeptide which serve as tethering molecules or matrix proteins for the cisternal architecture of Golgi […]

Contributors

Inventor Institute
Martin Fritzler University of Calgary
Cat. #: 157877
Unit size: 100 ug
Research Fields: Cell biology
Application: IF ; WB
Target: Golgin 97
Reactivity: Human ; Rabbit
Host: Mouse
Class: Monoclonal
Alternate name: Golgin subfamily A member 1
Product description: The Golgi complex is an intricate cytoplasmic organelle that has a major function in the processing, transporting, and sorting of intracellular proteins following synthesis in the rough endoplasmic reticulum. Golgins are Golgi-localized proteins with extensive coiled-coil structure throughout the entire polypeptide which serve as tethering molecules or matrix proteins for the cisternal architecture of Golgi apparatus. Glogins belonging to the Glutamate receptor-interacting protein (GRIP) family are targeted to the trans-face of the Golgi by their C-terminal GRIP domains and play an essential role as tethering molecules for tubulovesicular carriers of the trans-Golgi Network (TGN).Golgin-97 resides on the cytoplasmic face of the Golgi and plays an essential role as tethering molecules on the TGN for retrograde traffic from the early and/or recycling endosomes. As a GRIP family member, Golgin-97 maintains cell polarity. Binding to the Golgi membrane is mediated by the G protein family member Arl1, and this pathway is a key regulatory process for endosome–TGN traffic.
Conjugation: Unconjugated
Molecular weight: 88
Target background: The Golgi complex is an intricate cytoplasmic organelle that has a major function in the processing, transporting, and sorting of intracellular proteins following synthesis in the rough endoplasmic reticulum. Golgins are Golgi-localized proteins with extensive coiled-coil structure throughout the entire polypeptide which serve as tethering molecules or matrix proteins for the cisternal architecture of Golgi apparatus. Glogins belonging to the Glutamate receptor-interacting protein (GRIP) family are targeted to the trans-face of the Golgi by their C-terminal GRIP domains and play an essential role as tethering molecules for tubulovesicular carriers of the trans-Golgi Network (TGN).Golgin-97 resides on the cytoplasmic face of the Golgi and plays an essential role as tethering molecules on the TGN for retrograde traffic from the early and/or recycling endosomes. As a GRIP family member, Golgin-97 maintains cell polarity. Binding to the Golgi membrane is mediated by the G protein family member Arl1, and this pathway is a key regulatory process for endosome–TGN traffic.
Format: Liquid
Shipping conditions: Dry ice
References:

Nozawa et al. 2009. Cell Biol Int. 33(2):148-57. PMID: 19000931.

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