Recombinant Human EFEMP1/Fibulin-3 protein is a Human Full Length protein, in the 1 to 493 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes (Recombinant protein). |
Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth.
FBLN3, FBNL, EFEMP1, EGF-containing fibulin-like extracellular matrix protein 1, Extracellular protein S1-5, Fibrillin-like protein, Fibulin-3, FIBL-3
Recombinant Human EFEMP1/Fibulin-3 protein is a Human Full Length protein, in the 1 to 493 aa range, expressed in Wheat germ and suitable for SDS-PAGE, ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.3% Glutathione
Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth.
Belongs to the fibulin family.
This product was previously labelled as EFEMP1.
EFEMP1 also known as Fibulin-3 is a member of the fibulin family involved in extracellular matrix (ECM) organization. The protein's mass is approximately 55 kDa. It is expressed in various tissues but researchers find it most common in the eye lung and arterial walls. As a secreted glycoprotein Fibulin-3 plays a vital role in maintaining structural integrity and elasticity in connective tissues.
EFEMP1/Fibulin-3 participates in ECM modulation and cell signaling. It interacts with other ECM components such as fibronectin and collagen contributing to structural assembly and stability. Although not prominently part of multi-protein complexes Fibulin-3 influences cellular adhesion and migration impacting tissue development and repair mechanisms. Researchers observe its expression during embryogenesis suggesting a role in developmental processes.
EFEMP1/Fibulin-3 integrates into matrix-related pathways impacting tissue architecture. It plays a role in the EGF (Epidermal Growth Factor) signaling pathway which is important for various cell survival and proliferation processes. Fibulin-3 exhibits functional relationships with proteins like fibronectin and integrins within these pathways highlighting its importance in mediating cell-matrix interactions and influencing signal transduction cascades.
EFEMP1/Fibulin-3 has notable connections with certain pathologies. Malfunctions in its expression or structure can relate to age-related macular degeneration and various forms of cancer including mesothelioma. In these diseases Fibulin-3 interacts with proteins such as matrix metalloproteinases which degrade extracellular matrix proteins thereby influencing tumor progression and ECM remodeling in affected tissues.
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12.5% SDS-PAGE showing ab114651 at approximately 79.97kDa stained with Coomassie Blue.
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