Probable multifunctional globin with a hexacoordinated heme iron required for the catalysis of various reactions depending on redox condition of the cell as well as oxygen availability (PubMed:11893755, PubMed:12359339, PubMed:15165856, PubMed:19147491, PubMed:20511233, PubMed:28393874, PubMed:28671819, PubMed:29128400, PubMed:33576020, PubMed:34930834). Has a nitric oxide dioxygenase (NOD) activity and is most probably involved in cell-mediated and oxygen-dependent nitric oxide consumption (PubMed:19147491, PubMed:20511233, PubMed:28393874, PubMed:28671819). By scavenging this second messenger may regulate several biological processes including endothelium-mediated vasodilation and vascular tone (PubMed:19147491, PubMed:28393874). Under normoxic conditions functions as a nitric oxide dioxygenase (NOD) but under hypoxic conditions the globin may switch its function to that of a nitrite (NO2) reductase (NiR), generating nitric oxide (PubMed:29128400). Could also have peroxidase and superoxide dismutase activities, detoxifying reactive oxygen species and protecting cells against oxidative stress (PubMed:12359339, PubMed:33576020, PubMed:34930834). Also binds dioxygen with low affinity and could function as an oxygen sensor but has probably no function as a respiratory oxygen carrier (PubMed:11893755, PubMed:15299006, PubMed:20553503).

Cytoglobin (Histoglobin) (HGb) (Nitric oxygen dioxygenase CYGB) (NOD) (EC 1.14.12.-) (Nitrite reductase CYGB) (EC 1.7.-.-) (Pseudoperoxidase CYGB) (EC 1.11.1.-) (Stellate cell activation-associated protein) (Superoxide dismutase CYGB) (EC 1.15.1.1)
CYGB STAP HGB; STAP

Q8WWM9

Human, Mouse, Rat

WB

WB 1:250-500

21.2 kDa

Mouse

Full length human recombinant protein of human CYGB (NP_599030) produced in HEK293T cell.

Monoclonal

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Store at -20 °C. Stable for 12 months from date of receipt.