Recombinant Human FTH Protein (N-6His)

Name: Recombinant Human FTH Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-0885NP
Availability: InStock

BL-0885NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Ferritin Heavy Chain is produced by our E.coli expression system and the target gene encoding Met1-Ser183 is expressed with a 6His tag at the N-terminus.
Accession	P02794
Synonym	Ferritin heavy chain; FTH1; FTH; FTHL6; Ferritin H subunit; Cell proliferation-inducing gene 15 protein
Gene Background	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.
Molecular Mass	23.4 KDa
Apmol Mass	22 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 1mM EDTA, pH 8.0.
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. Has ferroxidase activity. 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: 3976 OMIM: 134770 KEGG: hsa:2495 STRING: 9606.ENSP00000273550 UniGene: PMID: 29457657 High serum ferritin (SF) and the overall survival of allogeneic hematopoietic SF was only significantly associated with prolonged RBC transfusion dependence post-transplantation. PMID: 29046127 the role of FTH1 in the FIH control of HIF-1 activity, is reported. PMID: 29580991 Study demonstrate that the amounts of ferritin heavy subunit are inversely correlated, in K562 cells, to H19/miR-675 levels, and that this phenomenon may be largely attributed to the increase in ROS production induced by the FHC silencing. PMID: 29544765 Findings indicate that induction of EMT, increased migration and survival depend, in MCF-7 and H460 cells, on the release of FHC control on two pathways, namely the iron/ROS metabolism and CXCR4/CXCL12 axis. PMID: 28774348 ferritin heavy chain has a role in ovarian cancer stem cell expansion and epithelial to mesenchymal transition PMID: 27566559 Report in vivo magnetic resonance imaging of xenografted neuroblastoma tumors using FTH1 reporter gene expression controlled by a tet-on switch. PMID: 27732930 The H-ferritin could bind up to 24 NCOA4(383-522) fragments forming highly stable and insoluble complexes. The binding was partially inhibited only by Fe(II) among the various divalent metal ions analyzed. The iron-dependent, highly-specific formation of the remarkably stable H-ferritin-NCOA4 complex shown in this work may be important for the characterization of the mechanism of ferritinophagy. PMID: 28754384 Recombinant human H-chain ferritin nanocages were characterized by transmission electron microscopy and dynamic light scattering. These results indicate that H-chain ferritin is able to self-assemble into nanocages with a narrow size distribution. PMID: 26853188 Among myelodysplastic syndromes patients only, CD163 + macrophage density and HO1 and H-ferritin expression by CD163 + macrophages increased in tandem with marrow iron. High HO1 was significantly associated with shorter overall survival. PMID: 26758041 Low levels of FTH-positive tumor cells and microglia/macrophages were associated with poor survival in anaplastic astrocytomas, while high amounts of FTL-positive microglia/macrophages had a negative prognostic value PMID: 28837569 there is no significant relationship between serum ferritin concentrations and depressive symptoms among Chinese adults. PMID: 27611581 Data suggest that, in homopolymeric H-subunit ferritin (HuHF), iron oxidation proceeds with a 2:1 Fe(II):O(2) stoichiometry at iron level of 2 Fe(II) atoms/H-subunit with generation of H2O2; L-subunit-rich heteropolymeric ferritin also facilitates iron oxidation at the ferroxidase center and additionally promotes oxidation at the mineral surface once iron-binding capacity has been exceeded. PMID: 28636371 Elevated serum ferritin levels are associated with hematologic malignancies. PMID: 25124580 Ferritin light chain and ferritin heavy chain are required for the neural differentiation of bone marrow-derived mesenchymal stem cells under extremely low-frequency electromagnetic field. PMID: 26602884 Human FTH1 is a general pro-survival sequence. PMID: 26886577 H-ferritin tissue expression and the number of CD68+/H-ferritin+ cells were increased in the lymph nodes of adult-onset Still's disease patients, and these results correlated significantly with disease severity PMID: 26540556 Stopped-flow kinetics assays revealed that human H ferritin has different levels of activity compared with its R. catesbeiana counterpart PMID: 26327381 Studies indicate that the the best characterized cytosolic ferritins in mammals are encoded by two genes, FTH and FTL, with four exons and similar structures. PMID: 26518749 high cytoplasmic FTH1 was associated with favorable prognosis whereas nuclear FTH1 staining was associated with adverse prognosis in triple negative breast cancer PMID: 24742827 The goals of this study were to evaluate the multilineage differentiation ability of human mesenchymal stem cells expressing an MRI reporter, human ferritin heavy chain (FTH). PMID: 25448225 Data suggest that iron-independent effects of ferritin in myeloma should be prospectively investigated in preclinical and clinical studies. PMID: 24512320 Significant differences were seen in the levels of serum iron and hepcidin but not ferritin between the -582A>G hepcidin polymorphism genotypes. PMID: 25134646 High ferritin expression is associated with malignant phenotype of breast cancer. PMID: 25265351 High serum ferritin levels are associated with pancreatic cancer. PMID: 24446242 FTH provides metabolic adaptation to tissue Fe overload. [Review] PMID: 24124891 Tumor necrosis factor-alpha attenuates starvation-induced apoptosis through upregulation of ferritin heavy chain in hepatocellular carcinoma cells. PMID: 24066693 Elevated serum ferritin level is associated with the incident type 2 diabetes in healthy Korean men. PMID: 24098686 Children with autism spectrum disorders have significantly lower ferritin levels compared with controls and higher levels of sleep fragmentation and periodic limb movements. PMID: 24053984 Data indicate that serum highest TNF-alpha and IL-6 and higher ferritin are among those with intense steatosis. PMID: 23892696 Traumatic brain injury upregulates ferritin-heavy-chain in pericontusional cortex. PMID: 23079850 Increased levels of serum ferritin are adversely associated with cardiac function following myocardial infarction treated with percutaneous coronary intervention. PMID: 23079089 In normal bone marrow, ferritin H antibody stained early erythroid precursors and macrophages. In leukemic bone marrow, ferritin H was selectively expressed in erythroid blasts (M6), whereas all other blasts were negative. PMID: 23611361 The present study provides information about the metal binding sites of human H-chain ferritin and the pathway of ferrous ions (Fe2+) from the cytoplasm to the interior of the ferritin nanocage. PMID: 23344859 Serum ferritin levels in infectious diseases was lower than those in hematologic diseases. PMID: 23324584 Data indicate that ferritin levels and hyperuricemia are two independently significant factors associated with alanine aminotransferase (ALT) elevation among obese adolescents. PMID: 23119080 Increased levels of ferritin and decreased total antioxidant status indicated increasing inflammation in chronic hepatitis C. PMID: 22760008 H-ferritin overexpression promotes radiation-induced leukemia/lymphoma. PMID: 22843505 The hepcidin:ferritin ratio is reduced in relation to increasing fibrosis in chronic liver disease. PMID: 22676252 To study whether the human ferritin heavy chain (FTH1) can be expressed in Hansenula polymorpha, we integrated an expression cassette for FTH1, analyzed the protein expression, and also designed a FTH1-PTH fusion protein. PMID: 22212821 Induction of ferritin heavy chain expression results in severe inhibition of apoB-100 secretion from hepatoma cells during HCV infection. PMID: 22443280 Survivin inhibition by an interacting recombinant peptide, derived from the human ferritin heavy chain, impedes tumor cell growth PMID: 22426960 Elevated serum ferrin in infants is associated with congenital hypothyroidism. PMID: 22768652 Data provide useful insights into biomineralization of ferritin under in vivo fever conditions as well as in biomimetic synthesis of nanomaterials using ferritin. PMID: 22020807 FTH1 can inhibit the activation of the JNK signaling pathway and can bind to Daxx, inhibiting Daxx-mediated apoptosis. PMID: 21573799 H ferritin silenced human metastatic melanoma cells are characterized by a decreased growth activity, a reduced invasiveness, and a reduced cell adhesion capability. PMID: 22043922 There was a positive correlation between reactive oxygen species levels and serum ferritin levels in myelodysplastic syndrome patients PMID: 22117997 results showed the association of secreted IL-10, FHC and iron homoeostasis in Chlamydia trachomatis-infected HeLa-229 cells PMID: 21413929 FTH1 is a functional target gene of the BACH1 transcription factor according to ChIP-seq and knockdown analysis in HEK 293 cells. PMID: 21555518 Results illustrate how silencing H-ferritin can effectively sensitize tumors to chemotherapy. PMID: 21385903

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.