anti-Fras1 Related Extracellular Matrix Protein 2 (FREM2) Antibodies

Human Fras1 Related Extracellular Matrix Protein 2 (FREM2) interaction partners

1. Based on these data, we conclude that deficiency of FREM2, and possibly FRAS1, are associated with an increased risk of developing Congenital diaphragmatic hernia (CDH) and that loss of the FREM1/FREM2/FRAS1 complex, or its function, leads to anterior sac CDH development through its effects on mesothelial fold progression

2. Our results showed that p.Arg2167Trp had a weaker effect in interrupting interactions between FREM2 and FREM1 than FS-associated missense mutation p.Glu1972Lys. Overall, our data demonstrate that the homozygous mutation p.Arg2167Trp in FREM2 causes isolated Cryptophthalmos(CO), which will facilitate our better understanding of the molecular mechanisms underlying the disease

3. FREM2 is thus proposed as a novel GB biomarker and a putative biomarker of glioblastoma stem cells. Both FREM2 and SPRY1 are expressed on the surface of the GB cells, while SPRY1 alone was found overexpressed in the cytosol of non-malignant astrocytes.

4. In 15 of 590 families, we identified recessive mutations in the genes FRAS1, FREM2, GRIP1, FREM1, ITGA8, and GREM1, all of which function in the interaction of the ureteric bud and the metanephric mesenchyme.

5. Amplification of the FREM2 gene is associated with mesenchymal differentiation in gliosarcoma.

6. Heterozygous missense mutations in FREM2 cause non-syndromic congenital abnormalities of the kidney and urinary tract in humans.

7. report on 2 fetuses affected by Fraser syndrome (FS); a homozygous IVS14 + 1G -- A mutation in FREM2 was indentified; present report provides additional evidence that FS may be caused by complete or near-complete lack or loss of function of FREM2 protein

8. 1 new mutation in FREM2 was identified in families with Fraser syndrome.

Mouse (Murine) Fras1 Related Extracellular Matrix Protein 2 (FREM2) interaction partners

1. Report Fras1 up-regulation/Frem down-regulation in nephrons from mice with polycystic kidney disease and Frem2 mutations.

2. The QBRICK, together with Frem2, defines the ability of BMs to bind integrin 81 through modulating the BM assembly of nephronectin, thereby regulating the integrin 81-mediated signals transmitted from the ureteric buds to the metanephric mesenchyme.

3. expression of Frem2 may dynamically alter the extracellular matrix to provide a substrate for cell migration and rearrangements during embryogenesis

4. QBRICK/Frem1, Fras1, and Frem2 interactions at the basement membrane have roles in preventing Fraser syndrome-like defects

5. Study reports a comparative analysis of the spatiotemporal localization of Fras1, Frem1, Frem2 and Frem3 proteins during mouse embryonic development.

6. Fras1 is not only essential as a component of a macromolecular complex for the extracellular stabilization of Frem2 but it is also required for its proper intracellular trafficking and export from embryonic epithelial cells.

7. The localization pattern of Fras1 and Frem2 was indistinguishable, while both proteins along with Frem3 could be detected even in the absence of Frem1.