Recombinant Human Hereditary Hemochromatosis Protein (HFE) Protein (His&Myc)

Name: Recombinant Human Hereditary Hemochromatosis Protein (HFE) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-02536P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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 Hereditary Hemochromatosis Protein (HFE) Protein (His&Myc) is produced by our E.coli expression system. This is a extracellular protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q30201
Target Symbol	HFE
Synonyms	dJ221C16.10.1; Hemochromatosis; Hemochromatosis protein; Hereditary hemochromatosis protein; Hereditary hemochromatosis protein HLA H; HFE 1; HFE; HFE_HUMAN; HFE1; HH; High Fe; HLA H; HLA-H; HLAH; MGC:150812; MGC10379; MGC103790; MHC class I like protein HFE; MVCD7; TFQTL2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	RLLRSHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDHESRRVEPRTPWVSSRISSQMWLQLSQSLKGWDHMFTVDFWTIMENHNHSKESHTLQVILGCEMQEDNSTEGYWKYGYDGQDHLEFCPDTLDWRAAEPRAWPTKLEWERHKIRARQNRAYLERDCPAQLQQLLELGRGVLDQQVPPLVKVTHHVTSSVTTLRCRALNYYPQNITMKWLKDKQPMDAKEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQVEHPGLDQPLIVIWEPSPSGTLV
Expression Range	23-306aa
Protein Length	Extracellular Domain
Mol. Weight	40.2 kDa
Research Area	Metabolism
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	Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin.
Subcellular Location	Cell membrane; Single-pass type I membrane protein.
Protein Families	MHC class I family
Database References	HGNC: 4886 OMIM: 176200 KEGG: hsa:3077 STRING: 9606.ENSP00000417404 UniGene: PMID: 11446670 mutational analysis of the transferrin receptor reveals overlapping HFE and transferrin binding sites PMID: 11800564 genotype and allele frequencies between neonates and referred patients for HFE molecular analysis PMID: 11809727 Association between MHC class I gene HFE polymorphisms and longevity PMID: 11857056 HFE gene implicated in this disorder has been identified on chromosome 6. the most prevalent mutation is a point mutation(histidine to aspartic acid)in iron overload has been controversial. PMID: 11869934 A previously undescribed nonsense mutation of the HFE gene PMID: 11903354 Distribution of HFE C282Y and H63D mutations in the Balearic Islands (NE Spain). PMID: 11903355 results suggest that wild-type HFE negatively modulates the endocytic uptake of transferrin PMID: 11940510 Frequency of the S65C mutation of HFE and iron overload in subjects heterozygous for C282Y. PMID: 11943417 REVIEW:Characteristics of the C282Y mutation in childhood ALL, in contrast to other cancers, is male-specific, lacks a gene-dosage effect, and exhibits associations suggesting the involvement of another HLA-linked gene in leukemia susceptibility. PMID: 12002748 Long term survival is excellent in C282Y homozygotes for the C282Y mutation of the hemochromatosis gene diagnosed and treated before the development of cirrhosis and diabetes PMID: 12045778 Individuals with mutations in the HFE gene show very few hemochromatosis-related symptoms. PMID: 12059121 The tighter association of the -467 polymorphism with the C282Y mutation is consistent with other data that suggest that the C282Y mutation has occurred relatively recently and that the H63D mutation is considerably older. PMID: 12064915 HFE mutations do not confer an additional risk of hepatic fibrosis in patients with nonalcoholic steatohepatitis PMID: 12085358 possession of the HFE gene 282Tyr allele may offer some protection against the development of Parkinson Disease. PMID: 12098643 polymorphism and its relation to type 2 diabetes mellitus in the Czech population PMID: 12148086 When combined with the C282Y mutation, the S65C mutation is associated with an increased risk of hemochromatosis. PMID: 12180078 HFE has two mutually exclusive functions, binding to TfR1 in competition with Tf, or inhibition of iron release from macrophages. PMID: 12429850 HFE mutations more common in patients than controls, and advanced degrees of fibrosis developed at younger ages with C282Y mutation. Patients with C282Y had higher mean hepatic iron concentrations, hepatic iron indices, and hepatic fibrosis scores. PMID: 12445428 These results suggest that the apparent iron-deficient phenotype elicited by haemochromatosis protein (HFE) is not linked to beta(2)microglobulin insufficiency. PMID: 12464008 an increased risk of osteoarthritis among individuals who are heterozygous for the C282Y HFE mutation. PMID: 12508400 Genotyping of the C282Y and H63D substitutions in the HFE gene provides a satisfactory marker since these genotypes are associated with ~90% of herditary hemochromatosis. PMID: 12512743 Subjects with any HFE gene mutation were more likely to have colon cancer than subjects with no HFE gene mutations. PMID: 12529348 The presence of HFE mutations is independently associated with iron loading and advanced fibrosis in patients with compensated liver disease from chronic hepatitis C, especially after controlling for duration of disease. PMID: 12557137 C282Y or H63D heterozygosity is an independent risk factor for liver fibrosis and cirrhosis in HCV infected individuals. Screening for HFE mutations should be considered in HCV infection. PMID: 12586300 Results suggest that the H63D mutation in the hereditary hemochromatosis HFE gene may play a role in the pathogenesis of late onset type 2 diabetes. PMID: 12601293 In patients with rheumatoid arthritis, 2/24 (8.34%) were found to be positive for the C282Y mutation in the case of heterozygosis compared with 3/24 (12.5%) of patients with spondylarthritis. PMID: 12635863 The presence of TfR2 and absence of TfR1 suggests that HFE may serve a different function in platelets compared with the other HFE-positive cell types. PMID: 12656741 Interacts with transferrin receptors in endosomes PMID: 12667138 HFE C282Y and H63D are determinants of iron parameters in the elderly and will be effective in detecting individuals at high risk of hemochromatosis. PMID: 12673276 HFE and APOE genotypes are different between Alzheimer's disease patients, high cognitive impairment and low cognitive impairment PMID: 12707938 this study does not support the suggestion that H63D mutations may anticipate sporadic AD clinical presentation in susceptible individuals. PMID: 12714262 trend for an increased frequency of H63D allele in centenarian women PMID: 12714263 In a population of 1279 Caucasians with angiographically confirmed coronary status, there is no evidence of an association between the C282Y mutation in the haemochromatosis gene and prevalence of coronary artery disease and myocardial infarction PMID: 12746412 The mild iron overload associated with heterozygosity for C282Y HFE mutation confers susceptibility to nonalcoholic fatty liver disease PMID: 12779071 We see no evidence for over-representation of iron loading HFE alleles in type 2 diabetes mellitus PMID: 12783844 study performed in two samples of genetically homogeneous patients and controls does not support the suggestion that HFE mutations may be associated with acute myocardial infarction in susceptible individuals PMID: 12850485 REVIEW: C282Y mutant gene product failed to associate with 2-microglobulin and significantly reduced cell surface expression of the HFE-2m complex, thereby affecting the interaction with TfR and its interaction with transferrin. PMID: 9869618 871 healthy unrelated subjects in Poland were collected to assess the relevant frequencies. Each subject was genotyped for the C282Y and H63D mutations using a PCR-based protocol PMID: 11386022 Overall, this increased understanding of the role of HFE in the immune response sets the stage for better treatment and management of hereditary hemochromatosis and other iron-related diseases, as well as of the immune defects related to this condition. PMID: 28474781 Results show that cystic fibrosis (CF) patients who carry a HFE gene mutation, particularly the C282Y substitution, demonstrate accelerated lung function and worsening of disease suggesting that HFE C282Y mutation is associated with CF severity and progression. PMID: 30291871 This study showed that the Iron related hemochromatosis (HFE) gene mutations in Friedreich Ataxia patients. PMID: 27814974 p.Cys282Tyr homozygous women are diagnosed HFE Hemochromatosis at a later age than men, and thus corroborates the existence of a difference in the expression of this genotype between men and women. Nevertheless, these results do not confirm the protective effect typically attributed to pregnancy to explain the slower iron accumulation in women. PMID: 29454332 HFE could be a potential susceptibility gene for isolated recurrent aphthous oral ulcers PMID: 28950260 HFE mutation is associated with a lower level of aerobic capacity, even in the absence of iron accumulation. PMID: 29362711 Three single nucleotide polymorphisms associated with iron regulation were genotyped in multiple sclerosis : two in the human hereditary hemochromatosis protein gene HFE: rs1800562 (C282Y mutation) and rs1799945 (H63D mutation), as well as the rs1049296 SNP in the transferrin gene (C2 mutation). We only observed a higher prevalence of TF-C2 in multiple sclerosis patients PMID: 29201641 The HFE gene including both coding and boundary intronic regions were sequenced and polymorphisms were identified in 304 Brazilian individuals, encompassing healthy individuals and patients exhibiting hereditary or acquired iron overload. PMID: 28727322 homozygosity for the HLA-A*03 allele significantly increases the risk of excessive iron loading in Norwegian p.C282Y homozygous male patients. PMID: 28678636 genetic association studies in cohort of infants in Spain: Data suggest that serum hepcidin levels increase in infants during first year of life and are positively associated with iron status only in infants with wild-type HFE gene (not in infants with genetic polymorphisms C282Y, H63D, and S65C). PMID: 29404719 HFE stability is pH-dependent. PMID: 27174123

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.