Recombinant Human Cytoglobin Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1542

Recombinant Human Cytoglobin Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1542
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Product Overview

Tag His
Host Species Human
Accession AAH29798.1
Synonym HGB, STAP
Background Cytoglobin, also known as CYGB, is aglobinmolecule ubiquitously expressed in all tissues and most notably utilized in marine mammals. Its avtual function is still unknown. It is thought to be a method of protection under conditions ofhypoxia. The predicted function of cytoglobin is the transfer of oxygen from arterial blood to the brain. Cytoglobin is also present in chondroblasts and osteoblasts and shows a decreased level of expression upon differentiation to chondrocytes and osteocytes. Cytoglobin may facilitate diffusion of oxygen through tissues, scavengenitric oxideor reactive oxygen species, or serve a protective function duringoxidative stress.
Description A DNA sequence encoding the human CYGB (AAH29798.1) (Met1-Pro190) was expressed with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal His
AA Sequence Met1-Pro190
Molecular Weight The recombinant human CYGB consists of 205 a.a. and predicts a molecular mass of 23.2 KDa. It migrates as an approximately 26 KDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 20mM Tris, 100mM NaCl, 10% Glycerol, pH 8.0..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer.
Subcellular Location Cytoplasm.
Protein Families Globin family
Database References
Tissue Specificity Ubiquitously expressed. Highest expression in heart, stomach, bladder and small intestine.

Gene Functions References

  1. The results obtained in this study (1) show that plasma-produced reactive oxygen and nitrogen species can extensively oxidize proteins and (2) that the oxidation status of two redox-active cysteines lead to different conformations of CYGB. PMID: 30081385
  2. Endothelial cells facilitate the ability of smooth muscle cells to metabolize nitric oxide through upregulation of cytoglobin. PMID: 29969687
  3. FGF2 initiates CYGB transcription via the JNK pathway. PMID: 28916723
  4. the study reveals a novel mechanism for the regulated expression of Cygb and also assigns a new role to Cygb in cell cycle control. PMID: 28948618
  5. Data suggest that cytochrome b5 (CYB5) and cytochrome b5 reductase 3 (CYB5R3) can reduce human cytoglobin (CYGB) and zebrafish cytoglobins at rates up to 250-fold higher than those reported for the known physiological substrates, hemoglobin and myoglobin; the three proteins (CYB5+CYB5R3+CYGB) appear to constitute a metabolon involved in generation of nitric oxide. PMID: 28671819
  6. DeltaNp63-CYGB axis is also present in lung and breast cancer cell lines, indicating that CYGB-mediated ROS-scavenging activity may also have a role in epithelial tumours PMID: 26096935
  7. 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. PMID: 26928591
  8. 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 PMID: 26339645
  9. Cygb, expressed in hepatic stellate cells during liver fibrosis, plays role in cancer development with nonalcoholic steatohepatitis. PMID: 25665792
  10. Cygb stabilizes p53 by inhibiting its ubiquitination and elicit cell cycle arrest in DNA damaged cells. PMID: 25269893
  11. The cysteine redox state of the monomer controls histidine dissociation rate constants and hence extrinsic ligand binding in human cytoglobin. PMID: 25601563
  12. 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. PMID: 25327890
  13. Protein multimerization may be a mechanism that triggers physiological functions of human cytoglobin. PMID: 24632414
  14. Our data provides evidence that cytoglobin regulates the ovarian cancer cell proliferation and invasion. PMID: 24737588
  15. This review outlines the current understanding of Cygb's involvement in tumor hypoxia and discusses its role in tumorigenesis. PMID: 24816917
  16. Molecular dynamics studies of four cytoglobinCO models indicated that the distal E7 residue was a crucial influence on the dynamics of cytoglobinCO in terms of loop fluctuations, cavity rearrangement, and slight heme motion. PMID: 24037220
  17. Reduction of the internal disulfide bond between Cys 38 and 83 switches the ligand migration pathway in cytoglobin. PMID: 24008134
  18. Cytoglobin is expressed in hepatic stellate cells, but not in myofibroblasts, in normal and fibrotic human liver, so it thus a useful marker to distinguish these cells. PMID: 24296877
  19. Results show that CYGB revealed Tumor Suppressor Gene properties in normoxia but promoted tumourigenic potential of the cells exposed to stress, suggesting a bimodal function in lung tumourigenesis. PMID: 23591990
  20. Reduction of Cygb by cellular reductants enables Cygb to efficiently regulate nitric oxide metabolism in the vascular wall in an oxygen-dependent manner. PMID: 23710929
  21. Report cytoglobin expression in human brain. PMID: 23160832
  22. A substantial change in both protein dynamics and inner cavities is observed upon transition from the CO-liganded to the pentacoordinated and bis-histidyl hexacoordinated species, which could be exploited as a signalling state. PMID: 23308092
  23. Cygb-mediated nitrite reduction can play an important role in NO generation and soluble guanylyl cyclase activation under hypoxic conditions PMID: 22896706
  24. This suggests that Cytoglobin is likely not important for global neuronal protection following ischemia and the role of Cytoglobin in relation to endogenous neuroprotection remains unresolved. PMID: 22750003
  25. Coexistence of Cygb with efficient reductants in tissues allows Cygb to function as an oxygen-dependent regulator of nitric oxide (NO) decay. A related kinetic model predicts the NO consumption rate. PMID: 22577939
  26. normal physiological concentrations of cytoglobin do not offer cytoprotection from reactive oxygen species PMID: 22359545
  27. Cytoglobin, a protein that can be induced in response to oxidative stress, is elevated in most atrophic foci in adenocarcinoma of the prostate, suggesting hypoxic, and/or oxidative damage. PMID: 22025306
  28. knockdown of cytoglobin expression can sensitize human glioma cells to oxidative stress PMID: 21631290
  29. Binding of ferric cytoglobin to lipids and their subsequent transformation may be integral to the physiological function of cytoglobin, generating cell signalling lipid molecules under an oxidative environment. PMID: 21171964
  30. Cygb has a nitric-oxide dioxygenase function and ascorbate and cytochrome b(5) have roles as reductants PMID: 20511233
  31. Cytoglobin displays biphasic kinetics after the photolysis of CO, as a result of competition with an internal protein ligand, the E7 distal histidine. PMID: 20553503
  32. A ubiquitously expressed human hexacoordinate hemoglobin PMID: 11893755
  33. vertebrate myoglobins are in fact a specialized intracellular globin that evolved in adaptation to the special needs of muscle cells PMID: 11919282
  34. cloned, deduced amino acid sequence and expressed in diseased liver tissue where stellate cells were present PMID: 12359339
  35. characterization of the heme environmental structure of this protein, a fourth globin in humans PMID: 12718557
  36. differential expression of cytoglobin argues against a general respiratory function of this molecule, but rather indicates a connective tissue-specific function PMID: 14660570
  37. hereditary neuralgic amyotrophy is not caused by point mutations of cytoglobin PMID: 15052627
  38. Results describe the crystal structure of cytoglobin, which displays heme hexa-coordination. PMID: 15095869
  39. reporting of X-ray crystallographic structure PMID: 15165856
  40. Cytoglobin is a novel candidate tumour suppressor gene highly methylated in upper aero-digestive tract squamous cancer PMID: 16449996
  41. We now show that cytoglobin gene expression in oesophageal biopsies from tylotic patients is dramatically reduced by approximately 70% compared with normal oesophagus. Furthermore, both alleles are equally repressed PMID: 16510494
  42. Results provide the first evidence to suggest the implication of CYGB in the pathogenesis of non-small cell lung cancer. PMID: 16698880
  43. The structure of a new crystal form of cytoglobin reveals a new dimerization arrangement of cytoglobin. PMID: 16699195
  44. Pomoter elements of human CYGB gene are located between -1113 to -10 relative to the translation start site. PMID: 16797742
  45. hypoxia responsive elements (HREs) at positions -141, -144 and -448 were essential for activation of CYGB expression under hypoxic conditions. The binding of hypoxia inducible factor protein to the HREs was confirmed. PMID: 17936249
  46. A role for cytoglobin in cytoprotection of neuronal cells from oxidative-related damage. PMID: 18353768
  47. Data constitute the first direct functional evidence for CYGB, the newest member of the globin family, as a tumor suppressor gene. PMID: 18794132
  48. cytoglobin contributes to cell-mediated NO dioxygenation and represents an important NO sink in the vascular wall. PMID: 19147491
  49. CYGB gene is regulated by both promoter methylation and tumour hypoxia in HNSCC and that increased expression of this gene correlates with clincopathological measures of a tumour's biological aggression. PMID: 19568272


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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