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Recombinant Human Hemojuvelin/HFE2 Protein (His Tag)

£585.60 – £732.00 excluding VAT

SKU FAS-031623-P Category Tag

Hemojuvelin, also known as HFE2, is a membrane-bound and soluble protein which belongs to the repulsive guidance molecule (RGM) family. It is known that RGMs function through Neogenin, a homologue of the Netrin receptor deleted in colon cancer. In mammals, RGM family consists of three glycoproteins which have discrete expression patterns and functions (RGM-A, RGM-B, and RGM-C). Hemojuvelin is expressed in adult and fetal liver, heart, and skeletal muscle. Hemojuvelin acts as a bone morphogenetic protein (BMP) coreceptor. Enhancement of BMP signaling regulates hepcidin (HAMP) expression and iron metabolism. It plays a key role in iron metabolism. Hemojuvelin represents the cellular receptor for hepcidin. It may be a component of the signaling pathway which activates hepcidin or it may act as a modulator of hepcidin expression. Defects in hemojuvelin are the cause of hemochromatosis type 2A, also known as juvenile hemochromatosis (JH).

Size

100µg
Active Protein
Activity
Protein Construction

A DNA sequence encoding the mature form of human HFE2 isoform a (Q6ZVN8-1) (Met 1-Ser 399) was fused with a polyhistidine tag at the C-terminus.
Sequence

Met 1-Ser 399
Fusion Tag

C-His
Accession

Q6ZVN8-1
Species

Human
Expressed Host

Baculovirus-Insect Cells
Shipping

This product is provided as lyophilized powder which is shipped with ice packs.
Purity

> 95 % as determined by reducing SDS-PAGE.
Endotoxin

< 1.0 EU per µg as determined by the LAL method.
Stability and Storage

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Mol Mass

40 kDa
AP Mol Mass

20, 34 and 44 kDa
Formulation

Lyophilized from sterile PBS, 500mM NaCl, pH 7.0, 10% gly
Research Areas
Reconstitution

Please refer to the printed manual for detailed information.

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