Recombinant Human FTL Protein (N-6His)

Name: Recombinant Human FTL Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-0884NP
Availability: InStock

BL-0884NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Ferritin Light Chain is produced by our E.coli expression system and the target gene encoding Met1-Asp175 is expressed with a 6His tag at the N-terminus.
Accession	P02792
Synonym	Ferritin L subunit; Ferritin light chain; FTL
Gene Background	Ferritin is a large, iron-storage heteropolymeric protein,which is expressed in most kinds of cells and co-assemble in different proportion in a tissue-specific manner. Ferritin has oligomer of 24 subunits and two types of subunits including light chain(FTL) and heavy chain. Ferritin can remove Fe (Ⅱ) from solution in the presence of oxygen and is very important for iron homeostasis. Iron is absorbed in the ferrous form and deposited as ferric hydroxides after oxidation. Iron is first oxidized to the ferric state for storage as ferric oxyhdroxide whithin the protein shell of ferritin. Thus, ferritin removes excess iron from the cell sap where it could otherwise participate in peroxidation mechanisms. Ferritin also plays a role in delivery of iron to cells and mediates iron uptake in capsule cells of the developing kidney.
Molecular Mass	21.45 KDa
Apmol Mass	20-25 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 250mM NaCl, 1mM EDTA, pH 9.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney.
Protein Families	Ferritin family
Database References	HGNC: 3999 OMIM: 134790 KEGG: hsa:2512 STRING: 9606.ENSP00000366525 UniGene: PMID: 27372204 Determining serum ferritin is a convenient and nonexpensive method to determine the outcome of the treatment of the cases with oral squamous cell carcinoma . Its potential as prognostic marker could not be overlooked PMID: 28862225 The functional significance of the observed patch of carboxylate side chains and resulting metallocluster for biomineralization emerges from the lower iron oxidation rate measured in the E60AE61AE64A variant of human L-ferritin, leading to the proposal that the observed metallocluster corresponds to the suggested, but yet unobserved, nucleation site of L-ferritin PMID: 28202724 The clinical measurement of ferritin in cerebrospinal fluid is a better biomarker than serum levels of ferritin for diagnosing and assessing the progression of amyotrophic lateral sclerosis patients. PMID: 27804118 Our patient's transferrin saturation was 27% and HFE analysis revealed that she had neither H63D nor C282Y mutations that are known to predispose to hemochromatosis. Besides being an iron storage protein, ferritin is also one of the so-called acute phase proteins PMID: 28636169 This is the first Australian report of the c.-167 C>T mutation in a large family with multiple affected individuals. PMID: 27096259 Baseline serum ferritin (SF) did not influence bloodstream infections (BSIs), but higher levels resulted in more invasive fungal infections (IFIs) PMID: 28585071 High serum ferritin expression is associated with metabolic syndrome. PMID: 27390880 Hepatitis E virus ORF1 encoded macro domain protein interacts with light chain subunit of human ferritin and inhibits its secretion. PMID: 27170377 indicate an important role of ferritin light chains in neurodegeneration PMID: 26994418 This study demostrated that FTL mutation progressive brain iron dysregulation, morphological signs of early neurodegeneration and motor coordination deficits show PMID: 25447222 FTL expression was higher in glioblastoma than in low-grade glioma, and decreased expression of FTL correlated with increased survival in glioblastoma patients. PMID: 26871431 FTL gene mutation and persistent hyperferritinemia without iron deficiency anemia after phlebotomy PMID: 25720123 Ferritin plasma levels increased significantly following stem cell transplantation in graft rejection patients. PMID: 26611853 Single nucleotide polymorphisms in HAMP, BMP2, FTL and SLC40A1 genes have phenotype-modifying roles in hereditary hemochromatosis type 1. PMID: 25976471 Genome-wide association study identifies variants in PMS1 associated with serum ferritin in a Chinese population. PMID: 25162662 Urine ferritin levels are elevated significantly in systemic lupus erythematosus and correlate with disease activity. PMID: 22871034 findings expand the genetic and clinical diversity of neuroferritinopathy and suggest CSF ferritin levels as a novel potential biochemical marker for the diagnosis of neuroferritinopathy. PMID: 24825732 Plasma hepcidin-25 and ferritin light chain levels correlate with a malignant breast cancer diagnosis. PMID: 24306042 provide a new mechanism for selective autophagy of ferritin and reveal a previously unappreciated role for autophagy and NCOA4 in the control of iron homeostasis in vivo PMID: 25327288 Genetic testing confirmed the diagnosis of hereditary hyperferritinemia cataract syndrome (HHCS), demonstrating a C39>G (c.-161C>G) mutation into FTL gene. PMID: 24983587 A c.-171C>G mutation in the iron-regulatory element of FTL was found in 2 members of a Spanish family with hyperferritinemia-cataract syndrome. PMID: 24022025 Elevated cerebrospinal ferritin reliably (but unspecifically) indicates severe central nervous system disease. PMID: 24821637 Through combining serum ferritin and MS spectral data, the diagnosis sensitivity and specificity of our model for prewarning severe aGVHD (III~IV degrees aGVHD) before transplant all increased to 90.0% PMID: 24195075 Increased levels of ferritin light chain protein is associated with breast cancer. PMID: 23969999 Together, our results suggest that iron can increase gamma-secretase activity through promoting the level of FTL that interacts with and stabilizes PEN-2 PMID: 23685131 Elevated levels of ferritin are associated with type 2 diabetes mellitus. PMID: 23381919 Data show the transcriptional regulation of the human ferritin gene by coordinated regulation of Nrf2 and protein arginine methyltransferases PRMT1 and PRMT4. PMID: 23699174 Noncoding G-to-T transversion (c.-168G>T) located in the iron response element (IRE) of the gene coding for ferritin light chain (FTL) cosegregated with cataract in the family. PMID: 23592921 The Badalona 36C > U and Heidelberg 52 G > C mutations within the L-ferritin Iron-Responsive Element only mildly alter the binding capacity of the Iron Regulatory Proteins but are still causative for hyperferritinaemia cataract syndrome. PMID: 23421845 Elevation in ferritin is associated with response to trastuzumab in breast cancer. PMID: 23300545 Plasma levels of FLT and S100A9 proteins are up-regulated and CNDP1 levels are down-regulated in patients with glioblastoma. PMID: 23029420 data demonstrate an enhanced propensity of mutant ferritin to undergo iron-catalyzed oxidative damage and support this as a mechanism causing disruption of ferritin structure and iron mishandling that contribute to pathology of hereditary ferritinopathy PMID: 22348978 Two novel missense L-ferritin variants are associated with hyperglycosylation, p.Gln26Ile and p.Ala27Val, and with benign hyperferritinemia in two unrelated patients. PMID: 22535864 High ferritin is associated with poor treatment response in hematological neoplasms. PMID: 22248276 The data strongly suggest that FTL and SCCA1 may serve as coreceptors in HBV cellular attachment and virus entry into hepatocytes. PMID: 22359459 Molecular genetic analysis revealed point mutations within the FTL IRE. PMID: 22020773 genetic variations in the HFE gene, but not plasma ferritin may have a role in coronary heart disease in Chinese PMID: 21696736 Genetic analysis revealed mutation G32A in Pedigree 1 and mutation G32T in Pedigree 2, both heterozygous and located in the iron-responsive element of the ferritin light chain mRNA in hyperferritinemia cataract syndrome. PMID: 21907119 FTL is a target gene of the BACH1 transcription factor according to ChIP-seq analysis in HEK 293 cells. PMID: 21555518 In the family with hyperferritinemia cataract syndrome a G-->C heterozygous mutation at position +32 of FTL was identified. PMID: 21541272 Somatic mutations in the iron response elements (IRE) of the L-ferritin gene are infrequent in the age-related cataract. PMID: 21139976 This protein has been found differentially expressed in thalami from patients with schizophrenia. PMID: 20471030 Toluene diisocyanate (TDI) regulates haem oxygenase-1/ferritin expression: implications for toluene diisocyanate-induced asthma. PMID: 20345975 biochemical and crystallographic characterization of pathogenic FTL mutant p.Phe167SerfsX26 showing that it is a functional ferritin with an altered conformation of the C terminus PMID: 20159981 This protein has been found differentially expressed in the anterior cingulate cortex from patients with schizophrenia PMID: 20381070 indicate that cellular iron imbalance and oxidative damage produced by the over-expression in of two pathogenic L-ferritin variants are primary causes of cell death, while aggregate formation is a secondary effect PMID: 19781644 the x-ray crystallographic structure and report functional studies of ferritin homopolymers formed from the mutant FTL polypeptide PMID: 19923220 Finding not only supports direct evidence for a regulatory role of L-ferritin in neuroectodermal cell pigmentation but also integrates a new player within a complicated network governing iron homeostasis in the dopamine neurons of substantia nigra. PMID: 19318681 The genetic defects in the FTL gene are unlikely to be a common cause of typical PD, at least in a North America population. PMID: 12459518

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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