Recombinant Human Hemoglobin subunit gamma-2(HBG2)

Code CSB-EP010156HU
Size US$2466
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Product Details

Purity Greater than 85% as determined by SDS-PAGE.
Target Names HBG2
Uniprot No. P69892
Research Area Cardiovascular
Alternative Names Abnormal hemoglobin; FLJ76540; G gamma globin; Gamma 2 globin; Gamma-2-globin; Hb F Ggamma; HBG 2; HBG2; HBG2_HUMAN; Hemoglobin gamma 2 chain; Hemoglobin gamma G; Hemoglobin gamma G chain; Hemoglobin gamma-2 chain; Hemoglobin gamma-G chain; Hemoglobin subunit gamma 2; Hemoglobin subunit gamma-2; Methemoglobin; OTTHUMP00000069638
Species Homo sapiens (Human)
Source E.coli
Expression Region 2-147aa
Target Protein Sequence GHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTGVASALSSRYH
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 23.0 kDa
Protein Length Full Length of Mature Protein
Tag Info N-terminal 10xHis-tagged and C-terminal Myc-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Q&A and Customer Reviews

 Q&A
Q:

Do you have them: HBG2 ?
I am looking for the control protein for HbH (β4) and Barts (γ4) · I am studying the haemoglobin variants and I couldn't able to find these two controls for my study. The closest protein I found is HBG1.HBG2 for barts and HBB for HbH. However, I am not sure whether this is the right protein to choose.

A:
Very nice to receive your inquiry. Recombinant Human Hemoglobin subunit gamma-2(HBG2)
CSB-YP010156HU >> Yeast
CSB-EP010156HU >> E.coli CSB-BP010156HU >> Baculovirus
CSB-MP010156HU >> Mammalian
Expression Region: 2-147aa; Full length of the mature protein.
Tag information:EP, BP, MP: N-terminal 10xHis-tagged and C-terminal Myc-tagged; YP: N-terminal 6xHis-tagged
Sequence:

GHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTGVASALSSRYH


Target Data

Function Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.
Gene References into Functions
  1. The results suggested that there was a significant relationship between high fetal hemoglobin levels and two variations (-309A/T and -369C/G) in Ggamma gene promotor. PMID: 29412791
  2. Genetic association studies provide a rationale for functional studies of HBG2 expression in wild-type and T/A/T haplotype erythroblasts and mechanistic studies like chromatin conformation capture experiments, to evaluate the role of chromatin looping as a mediator of the T/A/T haplotype effects on HbF. PMID: 27185208
  3. The frequency of rs7482144 was determined in Colombian sickle cell anemia patients. It indicated a West African ethnic background. PMID: 26849705
  4. In Portuguese beta-thalassemia carriers the HBG2 XmnI polymorphism is strongly associated with HbF levels. PMID: 25842369
  5. DNA polymorphisms at BCL11A, HBS1L-MYB and Xmn1-HBG2 site loci associated with fetal hemoglobin levels in sickle cell anemia patients from Northern Brazil. PMID: 25084696
  6. Its polymorphism effects HbF, HbE, MCV and MCH levels in Thai HbE carriers. PMID: 24474642
  7. Data indicate that the T to A conversion results in a leucine to histidine amino acid change at codon 105 of the (G)gamma-globin HBG2 gene and caused a hemoglobin (Hb) variant with lowered oxygen affinity. PMID: 24502349
  8. Hemoglobin gamma G plays a role in modifying clinical symptoms of beta-thalassemia innorthern Thailand. PMID: 25123009
  9. Hb F is regulated in inherited bone marrow failure syndromes by Xmn1-HBG2, as it is in the haemoglobinopathies. PMID: 23713742
  10. Our data suggest that a temporal repression mechanism is operative in the silencing of gamma-globin gene expression PMID: 23284307
  11. the study demonstrated that Egyptian beta-thalessemia patients have low frequency of positivity for the Xmnl polymorphism whether in heterozygous (+/-) or homozygous (+/+) state PMID: 22871617
  12. although the prevalence of Xmn1-(G)gamma polymorphism is high in beta thalassemia intermedia patients, it alone could not predict clinical severity of disease PMID: 21755589
  13. Chromatin looping between the Ggamma-globin gene and LCR HSs requires NF-E2. PMID: 21609963
  14. We identified a missense mutation in the fetal Ggamma-globin gene (HBG2) in a father and daughter with transient neonatal cyanosis and anemia. PMID: 21561349
  15. 12 molecules in the unit cell describe a right-handed helical filament having no polarity, which is different from the filament composed of HbS fibers, which is the only other well characterized fiber of human hemoglobin PMID: 21123872
  16. The polymorphisms -396_-391 del HBG2, -369 SNP HBG2 and -271 SNP HBG1 correlated with HbF levels, hence, it suggests an important role of HBG2 and HBG1 gene polymorphisms on the HbF synthesis. PMID: 20602015
  17. The recently identified chromatin factor Friend of Prmt1 (FOP) is a critical modulator of gamma-globin gene expression. PMID: 20688955
  18. A G>C substitution at position 479 of the (G)gamma-globin gene results in a glutamic acid to glutamine substitution at codon 101 of the (G)gamma-globin chain, a new gamma chain variant that we have named Hb F-Zhejiang PMID: 20113294
  19. Data suggest the G gamma-globin promoter is activated by cJun via an upstream cAMP response element. PMID: 19861239
  20. No statistically significant difference in the frequency of positive XmnI(G)gamma polymorphism was observed between thalassemia intermedia and thalassemia major patients. PMID: 19892574
  21. Data show that (G)Gamma-158(C-->T) had a strong association with moderately increased Hb F levels in beta-thalassemia heterozygotes in the Guangxi area of China. PMID: 15476181
  22. 3' flank of the Ggamma-globin gene contains multiple weak pause elements which, combined with the strong polyA signal the gene possesses, are likely to cause gradual termination across the 3' flank. PMID: 15798211
  23. A determinant linked to the XmnI restriction site which effects Ggamma-globin gene expression (and Hemoglobin F production) is active in beta-Thalassemic (anemic) adults but not in normal infants. PMID: 17365007
  24. analysis of heme uptake from human methemoglobin by the iron-regulated surface determinants system of Staphylococcus aureus PMID: 18467329
  25. HBG2:g-109G>T mutation has a functional role in increasing HBG2 transcription and is responsible for the hereditary persistence of fetal hemoglobin phenotype observed in our index cases PMID: 19050890

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Involvement in disease Cyanosis transient neonatal (TNCY)
Protein Families Globin family
Tissue Specificity Red blood cells.
Database Links

HGNC: 4832

OMIM: 142250

KEGG: hsa:3048

STRING: 9606.ENSP00000338082

UniGene: Hs.302145

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