Recombinant Mouse Hepcidin (HAMP) Protein (GST)

Name: Recombinant Mouse Hepcidin (HAMP) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-00381P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Hepcidin (HAMP) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9EQ21
Target Symbol	HAMP
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	DTNFPICIFCCKCCNNSQCGICCKT
Expression Range	59-83aa
Protein Length	Partial
Mol. Weight	29.4 kDa
Research Area	Others
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	Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. Acts by promoting endocytosis and degradation of ferroportin, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma. Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes.
Subcellular Location	Secreted.
Protein Families	Hepcidin family
Database References	KEGG: mmu:84506 STRING: 10090.ENSMUSP00000055404 UniGene: PMID: 29752985 Increased serum hepcidin contributes to the anemia of chronic kidney disease in a murine model. PMID: 27884972 bone marrow transplantation between wild-type and TLR4 knockout mice revealed that hepatic TLR4-dependent hepcidin expression was comparable to macrophage TLR4-dependent hepcidin expression induced by LPS PMID: 29217822 Hepc decreases in Cyp1b1-/- and gestational vitamin A deficiency mice resulted in stellate activation and lipogenesis suppression. PMID: 28583802 data indicate that unlike with many other infections, hepcidin is decreased following M.tb infection, and show that hepcidin ablation does not influence M.tb growth in vivo PMID: 29324800 Hepcidin expression involves epigenetic regulation by histone deacetylase 3. PMID: 28864822 Serum hepcidin levels were measured by competitive ELISA in wild-type and Inhbb-/- mice at baseline and 4 hours after LPS challenge. Although Smad1/5/8 signaling is not activated by inflammatory stimuli in the absence of activin B, this has no impact on the induction of hepcidin expression. PMID: 27903526 hepcidin mRNA upregulation depends on M1 macrophage polarization PMID: 27667162 Our data provide evidence that the interplay of these two hormones could help improve the understanding of the pathogenesis of atherosclerosis and NAFLD. PMID: 29158088 downregulation of hepcidin by siRNA increased iron uptake in bone and liver, which aggravated unloading-induced bone loss. PMID: 27686598 The authors generated mice with cardiomyocyte-specific deletion of hepcidin, or knock-in of hepcidin-resistant ferroportin. They find that while both models maintain normal systemic iron homeostasis, the mice nonetheless develop fatal contractile and metabolic dysfunction as a consequence of cardiomyocyte iron deficiency. PMID: 27897970 Acute tacrolimus treatment transiently increases hepcidin in wild-type mice. FKBP12 preferentially targets the BMP receptor ALK2. ALK2 mutants defective in binding FKBP12 increase hepcidin expression in a ligand-independent manner, through BMP-SMAD signaling. PMID: 28864813 Hamp1 mRNA and plasma hepcidin levels are not good predictors of tissue iron levels, at least in males PMID: 28798083 The lack of effect of erythropoietin on hepcidin expression in mask mice can not be explained by changes in erythroferrone synthesis, as splenic erythroferrone content increased after erythropoietin administration in both C57BL/6 and mask mice. PMID: 29073189 these results characterise a new model of rapidly inducible hepcidin disruption, and demonstrate the critical contribution of hepcidin to the hypoferraemia of inflammation PMID: 27423740 Hepatic gene expression of hepcidin is regulated in beta-thalassemia by ATOH8. PMID: 28405918 Endogenous hepcidin and its agonist mediate resistance to selected infections by clearing non-transferrin-bound iron. PMID: 28465342 the relationship between erythropoiesis and the candidate erythroid regulators, was examined. PMID: 28135344 Smad1 and Smad5 have overlapping functions to govern hepcidin transcription. Moreover, erythropoietin and erythroferrone target Smad1/5 signaling and require Smad1/5 to suppress hepcidin expression. PMID: 28438754 Genetic inactivation of hepatic angiocrine Bmp2 signaling in Stab2-Cre mice caused massive iron overload in the liver and increased serum iron levels and iron deposition in several organs similar to classic hereditary hemochromatosis; these changes were mediated by decreased hepatic expression of hepcidin, a key regulator of iron homeostasis. PMID: 27903529 These studies indicate that drug-like minihepcidins have a potential as future therapeutics for untransfused beta-thalassemia and polycythemia vera. PMID: 27154187 hepcidin induction by endoplasmic reticulum stress involves the central SMAD1/5/8 pathway PMID: 27483343 Increased hepcidin in transferrin-treated thalassemic mice correlates with increased liver BMP2 expression and decreased hepatocyte ERK activation. PMID: 26635037 The combined data presented here highlighted a crucial role of ERFE in regulating hepcidin expression and systematic iron homeostasis under phenylhydrazine-induced hemolytic anemia. PMID: 27067488 The results suggest that physiologic hepcidin levels are insufficient to alter Fpn levels within the retinal pigment epithelium and Muller cells, but may limit iron transport into the retina from vascular endothelial cells. PMID: 26506980 In TNF(DeltaARE/+) and IL-10(-/-)-mice hepatic hepcidin expression and protein content was significantly lower than in corresponding wild-types. PMID: 26302924 In Angiotensin II treated mice, duodenal divalent metal transporter-1 and ferroportin expression levels were increased and hepatic hepcidin mRNA expression and serum hepcidin concentration were reduced. PMID: 25096756 results clarify how commensal bacteria affect hepcidin expression and reveal a novel connection between IL-1beta and activation of BMP signaling. PMID: 26515063 Activation of TLR4 signaling and NF-small ka, CyrillicB are involved in the suppression of hepcidin gene transcription by alcohol in the presence of inflammation in the liver. PMID: 25232250 Study describes extensive blood vessel damage in Alzheimer's disease brain and a reduction in hepcidin and ferroportin levels PMID: 24252754 Hepatic hepcidin plays an important role in sepsis through regulation of iron metabolism PMID: 25264597 Hepc1(-/-) mice had a phenotype of low bone mass and alteration of the bone microarchitecture, most likely caused by a decreased osteoblastic activity PMID: 24652331 Hepcidin mRNA expression was increased in the D-galactose (D-gal) group, decreased in the caloric restriction (CR) group, and was basically unchanged in the D-gal-CR group. PMID: 24044515 results provide evidence that HFE induces hepcidin expression via the BMP pathway: HFE interacts with ALK3 to stabilize ALK3 protein and increase ALK3 expression at the cell surface. PMID: 24904118 Data suggest that hepcidin-1 expression is up-regulated in obesity in visceral/subcutaneous adipose tissue (but down-regulated in liver); hepcidin may play local roles in modulating both iron metabolism and inflammation in adipose tissue. PMID: 24418880 Hepcidin expression is upregulated in interleukin (IL)-10-deficient mice and downregulated in wild-type mice with dextran sulfate sodium-induced colitis. PMID: 24973448 this study shows that the liver-specific KO mice fully recapitulate the severe iron overload phenotype observed in the total KO mice, with increased plasma iron and massive parenchymal iron accumulation. PMID: 24646470 Results indicate a negative role of hepcidin in modulating liver regeneration. PMID: 24123375 The Hamp1 and interleukin-6 knock out genotype resulted in improved erythropoiesis in aged mice. PMID: 23996485 Hepcidin deficiency resulted in a marked reduction of bone load-bearing capacity likely through enhancing bone resorption, suggesting a direct correlation between hepcidin deficiency and bone loss. PMID: 24561287 Hepcidin regulates intrarenal iron handling at the distal nephron. PMID: 23615502 Data suggest that Hamp1 expression in liver can be regulated by dietary factors (here, down-regulated by a hematinic dietary supplement, black soyabean seed coat extract). PMID: 24387766 Identify a link between glucose and iron homeostasis, showing that hepcidin is a gluconeogenic sensor in mice during starvation. PMID: 24361124 Direct transcriptional suppression of hepcidin gene (HAMP) expression mediated by 1,25-dihydroxyvitamin D binding to the vitamin D receptor causes decrease in hepcidin mRNA levels PMID: 24204002 The Brucella abortus model shows multifactorial pathogenesis of inflammatory anemia including iron restriction from increased hepcidin, transient suppression of erythropoiesis, and shortened erythrocyte lifespan. PMID: 24357728 Knockout mice exhibited different patterns in the development and resolution of anemia, supporting the notion that interleukin 6 and hepcidin play distinct roles in modulating erythropoiesis in anemia of inflammation. PMID: 24357729 Exogenous mouse IgG1 Fc fused to the N terminus of mouse IL-22 induced hepcidin production. Ab-mediated blockade of hepcidin partially reversed the effects on iron biology caused by IL-22R stimulation. PMID: 23836059 Iron overload increased pro-hepcidin that remained high in hypoxia. PMID: 23656253 A model is proposed that suggests that unlike proteases, which are irreversibly bound to activated alpha2M, hepcidin remains labile and available to down-regulate Fpn1. PMID: 23846698 role of hepcidin in the setting of hypoferremia during acute inflammation PMID: 23637785

FAQs

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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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Recombinant Mouse Hepcidin (HAMP) Protein (GST)

Recombinant Mouse Hepcidin (HAMP) Protein (GST)

Product Overview

Target Details

FAQs