AGGF1 antibody
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935106861
info@markelab.com
name
AGGF1 antibody
category
Primary Antibodies
provider
FineTest
reference
FNab00212
tested applications
ELISA, WB, IHC
Description
Promotes angiogenesis and the proliferation of endothelial cells. Able to bind to endothelial cells and promote cell proliferation, suggesting that it may act in an autocrine fashion.
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | angiogenic factor with G patch and FHA domains 1 (AGGF1) |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Recommended Dilution | WB: 1:500-1:2000; IHC: 1:10-1:100 |
| Clonality | polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | 84-100 kDa |
| Purity | ≥95% as determined by SDS-PAGE |
| Purification | Immunogen affinity purified |
| Size 1 | 100µg |
| Form | liquid |
| Tested Applications | ELISA, WB, IHC |
| Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
| UniProt ID | Q8N302 |
| Gene ID | 55109 |
| Alias | GPATC7,GPATCH7 |
| Background | Antibody anti-AGGF1 |
| Status | RUO |
| Note | Mol. Weight 84-100 kDa |
Descripción
AGGF1, which stands for Angiogenic Factor with G-patch and FHA domains 1, is a protein that plays a role in angiogenesis, the process of forming new blood vessels from existing ones. AGGF1 is involved in the regulation of endothelial cell proliferation and migration, which are essential steps in angiogenesis.AGGF1 is classified as an angiogenic factor, meaning it promotes the growth and development of blood vessels. The G-patch domain is a conserved motif found in a variety of RNA-binding proteins. Proteins containing G-patch domains are implicated in RNA metabolism, including pre-mRNA splicing, mRNA processing, and RNA export. While the specific role of the G-patch domain in AGGF1 is not fully understood, it suggests a potential involvement in RNA-related processes or interactions. The FHA (Forkhead-associated) domain is a protein module involved in protein-protein interactions and phosphorylation-dependent signaling pathways. FHA domains can bind to phosphorylated serine or threonine residues on target proteins, thereby mediating protein-protein interactions and signaling events. In the context of AGGF1, the FHA domain may participate in protein-protein interactions that regulate its function in angiogenesis.
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