Analytical Data
-
Gene name
FBN3
- Application
-
Alternative Names
FBN3；KIAA1776；Fibrillin-3
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q75N90
-
Expression Region
全长
-
AA Sequence
full
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
FBN3, or Fibulin-3, is a member of the fibulin family of extracellular matrix proteins, which play crucial roles in various biological processes, including tissue development, cell adhesion, and signaling. This protein has garnered attention within the research community due to its involvement in ocular and connective tissue disorders, particularly its association with age-related macular degeneration (AMD) and other degenerative diseases. Understanding the structure and function of FBN3 is essential for elucidating its role in these pathologies, as well as its potential as a therapeutic target. Recent studies have focused on the recombinant expression of FBN3 to investigate its molecular properties, interactions with other matrix components, and the mechanisms underlying its functional properties. By generating recombinant FBN3, researchers aim to develop innovative strategies for drug design and gene therapy, thereby addressing the unmet clinical needs of diseases linked to this protein. The ongoing exploration of FBN3's role in disease processes enhances our knowledge of extracellular matrix biology and may lead to novel therapeutic avenues for treating conditions associated with its dysfunction.
