Recombinant Rat Hepcidin (HAMP) Protein (His-KSI)

Name: Recombinant Rat Hepcidin (HAMP) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-00188P
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 Rat Hepcidin (HAMP) Protein (His-KSI) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	Q99MH3
Target Symbol	HAMP
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	DTNFPICLFCCKCCKNSSCGLCCIT
Expression Range	60-84aa
Protein Length	Partial
Mol. Weight	18.1 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/SLC40A1, 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.; Has strong antimicrobial activity against E.coli ML35P N.cinerea and weaker against S.epidermidis, S.aureus and group b streptococcus bacteria. Active against the fungus C.albicans. No activity against P.aeruginosa.
Subcellular Location	Secreted.
Protein Families	Hepcidin family
Database References	KEGG: rno:84604 STRING: 10116.ENSRNOP00000028545 UniGene: PMID: 29147463 In experimental autoimmune encephalomyelitis, we recently found that chronic iron overload influences the course of disease. In females, iron overload accelerated the onset of disease, while in males it accelerated the progression of disease and increased mortality rate. We hypothesize that those differences arise on molecular level in different expression of stress response proteins hepcidin and metallothioneins. PMID: 28915963 Anti-hemojuvelin antibody corrects anemia caused by inappropriately high hepcidin levels PMID: 26944476 when a high erythropoietic stimulus occurs, hepcidin synthesis is mainly regulated by transferrin saturation; however, when the erythropoiesis rate reaches a specific threshold, extramedullary hematopoiesis is triggered, and the control of hepcidin synthesis is switched to matriptase-2, thus inhibiting hepcidin synthesis. PMID: 27282570 The data of in vitro and in vivo research evidenced on involvement of Hepc in formation of breast cancer cells malignant phenotype and their resistance to doxorubicin. PMID: 27356575 downregulation of ferroportin-1 and ceruloplasmin caused by hepcidin enhanced iron-dependent oxidative damage and may be the potential mechanism of subarachnoid hemorrhage . PMID: 27250827 liver iron overload was an important stimuli for hepcidin synthesis, stronger than the inhibitory effect of high rHuEPO doses; moreover, the findings raised the hypothesis that when high inflammation (triggering hepcidin expression) was associated with increased iron stores in hemodialysis patients, hepcidin expression was also upregulated via BMP6, enhancing hepcidin synthesis, leading, therefore, to worsening of anemia PMID: 26990350 Rats were treated with different dose levels of a monoclonal antibody that downregulates Hepcidin; results of this morphometric analysis in the liver showed that iron accumulation is not homogenous between liver lobes and the left lateral lobe was the most responsive lobe in the rat. PMID: 26839325 Hepcidin may be considered as a potential marker of impaired renal function. PMID: 26907911 a significant decrease of hepcidin expression is observed during late-pregnancy and early-lactation stages, suggesting the important regulatory role that hepcidin plays in iron metabolism during pregnancy and lactation PMID: 26788496 Study investigated the expression of hepcidin mRNA and protein in normal rat brain and to interpret the findings in the light of the properties of hepcidin as a peptide hormone with an essential role in systemic iron homeostasis PMID: 25896789 liver congestion induces hepcidin production, which may result in anemia and functional iron deficiency in some patients with heart failure. PMID: 25742771 Vitamin A deficiency reduced serum iron and transferrin saturation levels, increased spleen iron concentrations, reduced hepatic Hamp and kidney erythropoietin messenger RNA levels and up-regulated hepatic and spleen heme oxygenase-1 gene expression. PMID: 24998947 Data indicate that a moderate decrease in hepatic hepcidin mRNA content was observed in male rats. PMID: 24962641 inhibition of hepcidin may reduce many pathological changes seen in stress-induced depressive disorders. PMID: 25576700 This leads to a serum iron increase, which seems to stimulate hepcidin expression despite no evidence of inflammation, thus suggesting iron as the key modulator of hepcidin synthesis PMID: 25580431 Colitis increased local hepcidin-25 expression, which was associated with the IL-6/Stat-3 signaling pathway PMID: 24764672 High hepcidin serum expression levels correlated with an impaired hematologic response to an erythropoiesis-stimulating agent in rats with anemia of chronic disease. PMID: 24895335 Hepcidin is increased in the hypertrophied heart of Dahl salt-sensitive rats. PMID: 24424338 Data indicate that Hepcidin expression is increased in response to serum treatment in liver cells. PMID: 25151311 Data suggest that hepcidin was a relevant indicator for renal I/R injury diagnosis. PMID: 23439664 hepcidin inhibits expression of iron release as well as iron uptake proteins in macrophages PMID: 22560353 Angelica sinensis polysaccharide significantly reduced hepcidin expression by inhibiting the expression of (SMAD4) in liver and stimulating the secretion of erythropoietin. PMID: 22985399 result strongly suggests that plasma Il-6 is involved in exercise-induced increase of hepcidin gene expression PMID: 22326661 We found that hepcidin mRNA levels were significantly reduced in the regenerating liver after the acute-phase response was completed. PMID: 22364558 Pathways for the regulation of hepcidin expression in anemia of chronic disease and iron deficiency anemia PMID: 21859731 Hepcidin controls iron uptake and release by regulating expression of iron transport proteins, implying the existence of a novel hepcidin-receptor on the membrane of astrocytes. PMID: 21438013 hepcidin is an important contributor to iron overload in cerebral ischemia PMID: 21957487 Downregulation of hepcidin (Hamp) gene, a key regulator of Fpn1 was accompanied by decreased levels of CCAAT/enhancer binding proteins alpha and beta, especially at the Hamp promoter. PMID: 21785164 Although liver Fe concentration was significantly higher in rats fed an Mg-deficient diet for 4 weeks than in rats fed a control diet, Hepcidin expression in the liver was comparable between the dietary groups. PMID: 21736832 hepcidin inhibits the expression of iron-absorption proteins and led to exercise-associated anemia. PMID: 21411831 Matriptase-2- and proprotein convertase-cleaved forms of hemojuvelin have different roles in the down-regulation of hepcidin expression PMID: 20937842 investigation of up-regulation of hepcidin in myocardium following myocardial infarction; comparison of ischemic tissue vs. remote myocardial tissue PMID: 20553779 With the increases of iron levels in diet, the levels of serum iron, serum ferretin, and transferrin saturation were gradually increased, and the hepcidin mRNA expression level in liver significantly increased. PMID: 18839536 regulation of hepatic transcription by C/EBPalpha PMID: 12183449 hepcidin mediates lipopolysaccharide-induced downregulation of intestinal ferroportin 1 expression and the hepcidin signaling pathway involves a pyrrolidinedithiocarbamate-sensitive step PMID: 14592944 In liver ischemia-reperfusion model of acute inflammation, mechanism(s) other than interleukin-6 signal transduction via signal transducers and activators of transcription-3 may be responsible for hepcidin induction. PMID: 15973703 HAMP expression differs in cultured as compared with freshly isolated hepatocytes, and decreases in iron-loaded hepatocytes in serum free-media, suggesting that additional serum factors influence HAMP expression. PMID: 16221503 Hepcidin may have an important role in cardiac diseases. PMID: 17363462 hepcidin may play a major, causative role in the change of FPN1 synthesis PMID: 18189270 Lipopolysaccharides induced a significant increase in the expression of hepcidin mRNA and protein in the cortex and substantia nigra. PMID: 18450970 IL-6-hepcidin axis is up-regulated by psychological stress in rats. PMID: 18541141 overproduction of HIF-1alpha and the activation of caspase-3 seem to be associated with iron deficiency and with inflammatory markers. Hepcidin seems to plays a key role in this mechanism. PMID: 18808386 Regulation of liver hepcidin expression by alcohol in vivo does not involve Kupffer cell activation or TNF-alpha signaling. PMID: 19008338 Phagocytosis upregulates hepcidin-gene expression and downregulates Hjv- and Fpn-1-gene expression within the liver. PMID: 19721414

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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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