CYGB Antibody

Code CSB-PA006376LA01HU
Size US$166
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  • Immunohistochemistry of paraffin-embedded human skeletal muscle tissue using CSB-PA006376LA01HU at dilution of 1:100

  • Immunofluorescent analysis of HepG2 cells using CSB-PA006376LA01HU at dilution of 1:100 and Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L)

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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) CYGB Polyclonal antibody
Uniprot No.
Target Names
CYGB
Alternative Names
Cygb antibody; CYGB_HUMAN antibody; Cytoglobin antibody; Hgb antibody; Histoglobin antibody; STAP antibody; Stellate cell activation associated protein antibody; Stellate cell activation-associated protein antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Cytoglobin protein (1-190AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated

The CYGB Antibody (Product code: CSB-PA006376LA01HU) is Non-conjugated. For CYGB Antibody with conjugates, please check the following table.

Available Conjugates
Conjugate Product Code Product Name Application
HRP CSB-PA006376LB01HU CYGB Antibody, HRP conjugated ELISA
FITC CSB-PA006376LC01HU CYGB Antibody, FITC conjugated
Biotin CSB-PA006376LD01HU CYGB Antibody, Biotin conjugated ELISA
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Tested Applications
ELISA, IHC, IF
Recommended Dilution
Application Recommended Dilution
IHC 1:20-1:200
IF 1:50-1:200
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Customer Reviews and Q&A

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Target Background

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

HGNC: 16505

OMIM: 608759

KEGG: hsa:114757

STRING: 9606.ENSP00000293230

UniGene: Hs.95120

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