Recombinant Human C13orf7 protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

C13orf7 also known as LOC388268 is a protein with a molecular mass of approximately 26 kDa. This protein is expressed in various human tissues making it a significant target for research in multiple biological contexts. Currently researchers have identified C13orf7 through gene sequencing and have recognized its potential roles in cellular processes although further studies are needed to clarify its mechanical activities. Understanding its expression patterns across tissues can provide insights into its functional significance in different cell types.

Biological function summary

The function of C13orf7 suggests involvement in important cellular functions where it may facilitate interactions that affect cellular homeostasis and response. It's hypothesized to engage as part of multiprotein complexes that influence cellular dynamics although the specific partners and complex memberships remain under investigation. Cellular models lacking C13orf7 display altered phenotypes indicating its importance for maintaining normal cellular processes.

Pathways

Studies connect C13orf7 to pathways like the MAPK signaling pathway which regulates various cellular activities including proliferation and apoptosis. Researchers have noted interactions with kinases like ERK1/2 highlighting a role for C13orf7 in modulating signal transduction and cellular responses. The Wnt signaling pathway also appears to be influenced by C13orf7 particularly affecting β-catenin which further implicates it in cell growth and differentiation processes.

Researchers have explored links between C13orf7 and specific conditions such as cancer and neurodegenerative diseases. Mutations or dysregulation of C13orf7 may correlate with tumorigenesis where it might interact with tumor suppressor genes or oncogenes. In neurodegenerative contexts abnormalities in C13orf7 expression or function may influence pathways involving amyloid precursor proteins contributing to neuronal cell death or dysfunction. Identifying these connections could lead to novel therapeutic targets.