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CYGB encodes a globin protein found in vertebrate cells. Additionally we are shipping Cytoglobin Antibodies (53) and Cytoglobin Kits (10) and many more products for this protein.
Showing 10 out of 15 products:
Human CYGB Protein expressed in Escherichia coli (E. coli) - ABIN667790
Shivapurkar, Stastny, Okumura, Girard, Xie, Prinsen, Thunnissen, Wistuba, Czerniak, Frenkel, Roth, Liloglou, Xinarianos, Field, Minna, Gazdar: Cytoglobin, the newest member of the globin family, functions as a tumor suppressor gene. in Cancer research 2008
Show all 2 references for ABIN667790
Cygb, expressed in hepatic stellate cells during liver fibrosis, plays role in cancer development with nonalcoholic steatohepatitis.
Studied hepatic stellate cell cytoglobin involvement in acetaminophen induced hepatotoxicity through the regulation of CYP2E1 (show CYP2E1 Proteins).
cytoglobin serves an important role in muscle repair and regeneration
Cygb deficiency induces susceptibility to cancer development in the liver and lungs of mice exposed to N,N-diethylnitrosamine
The anatomical data indicate a role in NO signalling for cytoglobin and involvement in sleep-wake cycling for cytoglobin and neuroglobin (show NGB Proteins)
The nuclear localization of cytoglobin opens new perspectives for possible function(s) of globin-folded proteins as transcriptional regulators.
differential expression of cytoglobin argues against a general respiratory function of this molecule, but rather indicates a connective tissue-specific function
cytoglobin is significantly upregulated upon hypoxia and this is dependent on the tissue and severity of hypoxia
In the neuronal retina, cytoglobin is expressed in a subset of neurons of the ganglion cell and inner nuclear layers. Cytoglobin is also present in the inner plexiform layer, but absent from the pigment cells.
Cygb is an oxygen-responsive tissue hemoglobin expressed in distinct regions of thenormoxic and hypoxic brain and may play a key role in the response of the brain to ahypoxic insult.
DeltaNp63-CYGB axis is also present in lung and breast cancer cell lines, indicating that CYGB-mediated ROS (show ROS1 Proteins)-scavenging activity may also have a role in epithelial tumours
Propose a bipartite lipid binding model that rationalizes the modes of interactions of cytoglobin with phospholipids, the effects on structural re-arrangements and the peroxidase activity of the hemoprotein.
This review provides an overview of the proposed role of cytoglobin and explores its potential functional role as a biomarker for cancer and other diseases
Cygb stabilizes p53 (show TP53 Proteins) by inhibiting its ubiquitination and elicit cell cycle arrest in DNA damaged cells.
The cysteine redox state of the monomer controls histidine dissociation rate constants and hence extrinsic ligand binding in human cytoglobin.
The monomeric cytoglobin protein with an internal disulfide bond between the two cysteine residues Cys38 and Cys83, interacts with lipids to induce a change in haem co-ordination.
Protein multimerization may be a mechanism that triggers physiological functions of human cytoglobin.
Our data provides evidence that cytoglobin regulates the ovarian cancer cell proliferation and invasion.
Reduction of the internal disulfide bond between Cys (show DNAJC5 Proteins) 38 and 83 switches the ligand migration pathway in cytoglobin.
This gene encodes a globin protein found in vertebrate cells. The encoded protein is described as a hexacoordinate hemoglobin which binds ligand differently from the pentacoordinate hemoglobins involved in oxygen transport, and may be involved in protection during oxidative stress. This gene is located on chromosome 17 in the same region as a retinal gene which is mutated in progressive rod-cone degeneration, but in the opposite orientation.
, stellate cell activation associated protein
, stellate cell activation-associated protein