Analytical Data
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Gene name
RGM-C
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简介
RGM-C Protein, a BMP coreceptor, crucially modulates BMP signaling and regulates hepcidin (HAMP) expression, impacting iron homeostasis. It interacts with BMP2, BMP4, BMP6, BMPR1B, and TMPRSS6, forming a molecular network that collectively mediates BMP-related signaling pathways and iron regulation. RGM-C Protein, Human (Biotinylated, HEK293, Avi) is the recombinant human-derived RGM-C protein, expressed by HEK293, with C-Avi labeled tag.
- Application
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Alternative Names
Hemojuvelin; Rgmc; DL-M; HFE2; HFE2AMGC23953; HJV; JH; RGMC; RGM-C
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Species
Human
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Source
HEK293
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Tag
C-Avi
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6ZVN8-1
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Expression Region
Q36-D400
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Protein Length
Full Length of Isoform-1 Mature Protein
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Molecular Weight
55-60 kDa & 30-40 kDa & 20-25 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Serum albumin, primarily produced by the liver, is the most abundant protein in human plasma and plays a crucial role in maintaining oncotic pressure, transporting various molecules, and acting as a reservoir for hormones and drugs. Research into recombinant human serum albumin (rHSA) has gained significant attention due to its potential therapeutic applications and advantages over traditional plasma-derived albumin. The production of rHSA offers a safer alternative, eliminating risks related to bloodborne pathogens, while also allowing for large-scale production and purification in controlled environments. Furthermore, rHSA can be engineered for enhanced stability and extended half-life, providing improved efficacy for drug delivery systems. Studies have demonstrated its use in various clinical settings, including liver disease, critical care, and as a carrier for therapeutics in cancer treatment. Recent advancements in biotechnology, such as genetic engineering and novel expression systems, have facilitated the development of rHSA with superior properties, leading to an increased interest in its application in medicine. Investigating the structure-function relationship of rHSA is essential for optimizing its performance and understanding its interaction with other biomolecules. As the demand for safer and more efficient therapeutics continues to rise, rHSA remains a pivotal focus in both academic and industrial research, promising to revolutionize treatment protocols and improve patient outcomes in the future.
