Introduction of GJA3
Gap junction alpha-3 protein (GJA3) is a protein encoded by the GJA3 gene. It is also known as connexin 46 (cx46). Cx46 is a connexin isoform of 46 kDa. One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
|Basic Information of GJA3|
|Protein Name||Gap junction alpha-3 protein|
|Organism||Homo sapiens (Human)|
Function of GJA3 Membrane Protein
GJA3 is expressed in folliculostellate, TtT/GF and endocrine cells. In the cytoplasm, GJA3 is primarily involved in lysosomes. Different sizes of GJA3 molecules are fully restored in the TtT/GF cell nuclear fraction. It is an intrinsic membrane protein. The localization of the full-length GJA3 molecule in the nucleus is interesting because this process requires the protein to be separated from the membrane in advance and inserted during the synthesis of the ER. So far, either GJA3 or connexin 50 mutations have been associated with congenital cataracts. These proteins are believed to be modified with fiber cell age. However, limited work has been done on specific lens attachment modifications. GJA3 proved to be important in the growth of normal lens and maintenance of lens transparency. Specifically, mutations in the GJA3 gene are involved in the development of cataracts. In addition, disruption of the GJA3 gene led to the development of nuclear cataracts. Cx46 is a phosphorylated protein and truncated in the lens nucleus.
Fig.1 The membrane topology of GJA3. (Beyer, 2013)
Application of GJA3 Membrane Protein in Literature
These results indicate that glutathione diffuses from cortical fiber cells to the nucleus via gap junction channels formed by GJA3.
The article suggests that GJA3 is associated with cellular activities such as cell growth or proliferation in the anterior pituitary.
The data show that expression and phosphorylation of GJA3 and Cx50 are complementary in seminiferous tubules.
These results suggest that mutation of this highly conserved residue on the cytoplasmic loop domain of GJA3 enhances its interaction with the C-terminus, resulting in a reduction of gap junction channel function, but increased hemichannel function.
This article indicated that gap junction plaque formation by GJA3 in differentiating lens fiber cells is influenced by the actin-spectrin and beaded intermediate filament networks.
GJA3 Preparation Options
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