Recombinant Human Peroxiredoxin-1/PRDX1 (N, C-6His)

Product code: 32-8343

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Available Pack Size(s)

  •   10 µg

  •  50 µg

  • $321.00 

  • $371.00 

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Shipping Info:

For estimated delivery dates, please contact us at [email protected]


Amount : 50 µg
Content : Supplied as a 0.2 µm filtered solution of PBS, 10% glycerol, 0.1mM DTT,pH 6.0.
Storage condition : Store at -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.
AA sequence : MGSSHHHHHHSSGLVPRGSHMSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQKLEHHHHHH
Gene : PRDX1
Gene ID : 5052
Uniprot ID : Q06830
Source: E. coli.
MW :25.3kD.
Recombinant Human Peroxiredoxin-1 is produced by our E.coli expression system and the target gene encoding Met1-Lys199 is expressed with a 6His tag at the N-terminus, 6His tag at the C-terminus. Peroxiredoxin-1(PRDX1) contains 1 thioredoxin domain and belongs to the AhpC/TSA family. PRDX1 constitutively expressed in most human cells and it is induced to higher levels upon serum stimulation in untransformed and transformed cells. PRDX1 is involved in redox regulation of the cell. It reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin and play an important role in eliminating peroxides generated during metabolism. PRDX1 might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. It reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. It may contribute to the antiviral activity of CD8(+) T-cells and have a proliferative effect in cancer development or progression.

Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

Subcellular location: Cytoplasm, Melanosome
Post transnational modification: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.
BioGrid: 111089. 133 interactions.
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