Analytical Data
-
Gene name
FTH1
- Application
-
Alternative Names
FTH1;FTH;FTHL6;Ferritin heavy chain
-
Species
Human
-
Source
E. coli
-
Tag
N-6His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P02794
-
Expression Region
1-183aa
-
AA Sequence
MTTASTSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD CDDWESGLNA MECALHLEKN VNQSLLELHK LATDKNDPHL CDFIETHYLN EQVKAIKELG DHVTNLRKMG APESGLAEYL FDKHTLGDSD NES
-
Molecular Weight
21 kDa
-
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
Identification
Protein Description
FTH1, or Ferritin Heavy Chain 1, is a crucial protein involved in iron metabolism and oxidative stress responses within cells. As a component of the ferritin complex, FTH1 plays a significant role in the storage and regulation of iron, a vital element for various biological processes, including oxygen transport and DNA synthesis. Dysregulation of FTH1 has been linked to several diseases, including neurodegenerative disorders, cancer, and anemia, highlighting its importance in maintaining cellular homeostasis. In recent years, research has increasingly focused on the recombinant expression of FTH1 for various applications, including therapeutic strategies and biotechnology. The production of recombinant FTH1 allows for detailed functional studies, offering insights into its role in iron metabolism and its potential as a drug target. Furthermore, the engineered FTH1 proteins can be utilized in drug delivery systems, biosensors, and as biomarkers for disease diagnosis. Understanding the structure and function of FTH1 at the molecular level paves the way for innovative approaches in medicine and biotechnology, where precise modulation of iron metabolism can have significant therapeutic implications. Research into recombinant FTH1 continues to expand, revealing its multifaceted roles and potential in addressing health challenges related to iron homeostasis.











