Recombinant Human Ferritin Light Chain (FTL) Protein (His)

Name: Recombinant Human Ferritin Light Chain (FTL) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06405P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Ferritin Light Chain (FTL) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P02792
Target Symbol	FTL
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD
Expression Range	2-175aa
Protein Length	Full Length of Mature Protein
Mol. Weight	24.0 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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