Ferritin Human, FTL

Ferritin Human Recombinant, Light Chain
Cat. No.
BT8605
Source
Escherichia Coli.
Synonyms
Ferritin, FTL, MGC71996, Ferritin light chain.
Appearance
Sterile Filtered solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Ferritin Human Recombinant Light Chain produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20 kDa.

Product Specs

Introduction
Ferritin is a large, iron-storage protein made up of two types of subunits: light ferritin and heavy ferritin polypeptides. These subunits assemble in different ratios depending on the tissue. Ferritin's primary role is to capture and store iron in a soluble and safe form, preventing toxicity. It plays a crucial role in maintaining iron balance within cells. The light chain of ferritin is particularly important for iron storage, and defects in the gene responsible for its production are linked to neurological disorders and a condition known as hyperferritinemia-cataract syndrome.
Description
This product consists of the light chain of human ferritin, produced in E. coli bacteria. It is a single chain of 175 amino acids with a molecular weight of 20 kDa. The protein is not glycosylated, meaning it does not have sugar molecules attached.
Physical Appearance
Clear, sterile-filtered liquid.
Formulation
The protein is supplied in a solution at a concentration of 1 mg/ml in 20mM Tris-HCl buffer at pH 7.5.
Stability
For short-term storage (up to 4 weeks), keep at 4°C. For longer periods, freeze at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
The protein purity is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms
Ferritin, FTL, MGC71996, Ferritin light chain.
Source
Escherichia Coli.
Amino Acid Sequence
MSSQIRQNYS TDVEAAVNSL VNLYLQASYT YLSLGFYFDR DDVALEGVSH FFRELAEEKR EGYERLLKMQ NQRGGRALFQ DIKKPAEDEW GKTPDAMKAA MALEKKLNQA LLDLHALGSA RTDPHLCDFL ETHFLDEEVK LIKKMGDHLT NLHRLGGPEA GLGEYLFERL TLKHD.

Product Science Overview

Introduction

Ferritin is a crucial iron-storage protein found in both prokaryotes and eukaryotes. It plays a vital role in maintaining iron homeostasis within cells. Ferritin is composed of 24 subunits, which can be either heavy (H) or light (L) chains. The light chain of ferritin (FTL) is particularly significant due to its role in iron storage and detoxification.

Structure and Composition

Ferritin is a heteropolymer consisting of 24 subunits arranged in a spherical structure. The light chain (L-chain) and heavy chain (H-chain) subunits can vary in ratio, depending on the tissue type and physiological conditions. The L-chain is responsible for the nucleation and storage of iron in its ferric form (Fe^3+), while the H-chain catalyzes the oxidation of ferrous iron (Fe^2+) to ferric iron (Fe^3+) .

The recombinant human ferritin light chain (HuLF) is produced using recombinant DNA technology, typically expressed in systems such as Escherichia coli. This allows for the production of large quantities of the protein for research and therapeutic purposes .

Function

The primary function of the ferritin light chain is to store iron and regulate its release in a controlled manner. Iron is essential for various cellular processes, including oxygen transport, DNA synthesis, and electron transport. However, excess free iron can generate harmful free radicals through the Fenton reaction, leading to oxidative stress and cellular damage. Ferritin mitigates this risk by sequestering iron within its hollow spherical structure .

Biological Significance

Ferritin light chain plays a critical role in iron homeostasis and has been implicated in various physiological and pathological processes. It is involved in:

  • Iron Detoxification: By storing excess iron, ferritin prevents the formation of toxic free radicals.
  • Iron Transport: Ferritin releases iron in a controlled manner, ensuring a steady supply for cellular processes.
  • Neurodevelopment: Iron is crucial for the development of neurons and the synthesis of neurotransmitters. Ferritin light chain helps regulate iron availability during neurodevelopment .
Clinical Relevance

Mutations in the FTL gene, which encodes the ferritin light chain, can lead to disorders such as neurodegenerative diseases and hyperferritinemia-cataract syndrome. These conditions are often associated with oxidative stress caused by iron radicals .

Recombinant human ferritin light chain is used in research to study iron metabolism and related diseases. It also has potential therapeutic applications in treating conditions associated with iron overload or deficiency .

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