Clinically Tested Bacteria-derived Fth Recombinant Protein Lyophilized Unlock 55% Savings [Ck1rh4HU]
Bacteria-Derived FTH Recombinant Protein Lyophilized from Innovative Research has been recombinantly produced in E.coli. The protein formulation is lyophilized from a 0.2 ?m filtered solution of 20mM PB; 150mM NaCl; pH 7.4. with a purity of > 95 %
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Clinically Tested Bacteria-derived Fth Recombinant Protein Lyophilized Unlock 55% Savings [Ck1rh4HU]
Clinically Tested Bacteria-derived Fth Recombinant Protein Lyophilized Unlock 55% Savings [Ck1rh4HU] from Innovative Research has been recombinantly produced in E.coli. The protein formulation is lyophilized from a 0.2 ?m filtered solution of 20mM PB; 150mM NaCl; pH 7.4. with a purity of > 95 % as determined by reducing SDS-PAGE..
More Details:
- Species: Human
- Target: FTH
- Purity: > 95 % as determined by reducing SDS-PAGE..< 1.0 EU per ug as determined by the LAL method.
- Source: E.coli
- Storage Conditions: Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8? for 2-7 days. Aliquots of reconstituted samples are stable at < -20? for 3 months.
Ferritin heavy polypeptide 1(FTH1); is a ubiquitous intracellular protein which stores iron in a soluble; non-toxic; readily available form. FTH1 has ferroxidase activity and is important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Ferritin is composed of 24 subunits of the light and heavy ferritin chains. It plays a role in delivery of iron to cells and mediates iron uptake in capsule cells of the developing kidney. Variation of ferritin subunit composition may affect iron absorption and release in different tissues. Deficiency of ferritin proteins may cause several neurodegenerative diseases. Almost all living organisms can produce this protein; including algae; bacteria; higher plants; and animals.
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For research use only.
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