Recombinant Human GOLPH4/GPP130 protein
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Recombinant Human GOLPH4/GPP130 protein is a Human Fragment protein, in the 473 to 568 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
GIMPC, GOLPH4, GPP130, GOLIM4, Golgi integral membrane protein 4, Golgi phosphoprotein 4, Golgi-localized phosphoprotein of 130 kDa, GIMPc, Golgi phosphoprotein of 130 kDa
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human GOLPH4/GPP130 protein (AB162146)
ab162146 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The role of GOLPH4 centers around its involvement in the protein trafficking process within cells. It acts as part of the complex tasked with maintaining Golgi organization which is important for facilitating accurate cargo sorting and delivery. GOLPH4's location and structure enable it to interact with motor proteins and other Golgi matrix proteins aiding in vesicle tethering and fusion processes.
Pathways
GOLPH4 is involved in essential cellular pathways such as the secretion and endocytic trafficking pathways. It interacts with other Golgi-resident proteins like GM130 and giantin which are essential for the movement of materials through the Golgi and to their final destinations. These pathways ensure that proteins and lipids reach their intended areas within the cell or are secreted to the extracellular space which is important for maintaining cellular function and homeostasis.
Specifications
Form
Liquid
General info
Function
Plays a role in endosome to Golgi protein trafficking; mediates protein transport along the late endosome-bypass pathway from the early endosome to the Golgi.
Sequence similarities
Belongs to the GOLIM4 family.
Post-translational modifications
Phosphorylated probably by c-AMP-dependent kinases in its lumenal part.. O-glycosylated; modified by sialic acid residues.. N-glycosylated; N-glycans are probably of the complex type and modified by sialic acid residues.
Subcellular localisation
Endosome membrane
Target data
Product promise
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