Analytical Data
-
Gene name
HJV
- Application
-
Alternative Names
HJV;HFE2;RGMC;Hemojuvelin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q6ZVN8
-
Expression Region
36-400aa
-
AA Sequence
QCKIL RCNAEYVSST LSLRGGGSSG ALRGGGGGGR GGGVGSGGLC RALRSYALCT RRTARTCRGD LAFHSAVHGI EDLMIQHNCS RQGPTAPPPP RGPALPGAGS GLPAPDPCDY EGRFSRLHGR PPGFLHCASF GDPHVRSFHH HFHTCRVQGA WPLLDNDFLF VQATSSPMAL GANATATRKL TIIFKNMQEC IDQKVYQAEV DNLPVAFEDG SINGGDRPGG SSLSIQTANP GNHVEIQAAY IGTTIIIRQT AGQLSFSIKV AEDVAMAFSA EQDLQLCVGG CPPSQRLSRS ERNRRGAITI DTARRLCKEG LPVEDAYFHS CVFDVLISGD PNFTVAAQAA LEDARAFLPD LEKLHLFPSD
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
HJV (Hemojuvelin) is a crucial protein involved in iron homeostasis and regulation of hepcidin, a key hormone that modulates iron absorption and distribution in the body. Abnormalities in HJV function can lead to iron overload disorders, such as hereditary hemochromatosis, and are implicated in various pathologies, including anemia and inflammation. The study of HJV recombinant proteins has gained importance in understanding its molecular mechanisms and potential therapeutic applications. By expressing and purifying HJV in a recombinant form, researchers aim to investigate its structure-function relationships and the pathways through which it regulates hepcidin expression. Furthermore, the availability of recombinant HJV allows for the development of targeted interventions for iron-related diseases and helps in elucidating the complex interplay between iron metabolism and systemic inflammation. This research is essential not only for advancing basic biomedical knowledge but also for developing potential strategies for treating conditions associated with iron dysregulation. Overall, HJV recombinant protein studies hold promise for contributing to novel diagnostic and therapeutic modalities aimed at managing iron homeostasis disorders.











