Recombinant Human Hemoglobin Subunit Gamma-2 (HBG2) Protein (His&Myc)

Name: Recombinant Human Hemoglobin Subunit Gamma-2 (HBG2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-11248P
Availability: InStock

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HBG2.

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Product Overview

Description	Recombinant Human Hemoglobin Subunit Gamma-2 (HBG2) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P69892
Target Symbol	HBG2
Synonyms	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)
Expression System	E.coli
Tag	N-6His&C-Myc
Target Protein Sequence	GHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTGVASALSSRYH
Expression Range	2-147aa
Protein Length	Full Length of Mature Protein
Mol. Weight	23.0 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.
Protein Families	Globin family
Database References	HGNC: 4832 OMIM: 142250 KEGG: hsa:3048 STRING: 9606.ENSP00000338082 UniGene: Hs.302145
Associated Diseases	Cyanosis transient neonatal (TNCY)
Tissue Specificity	Red blood cells.

Gene Functions References

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
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
The frequency of rs7482144 was determined in Colombian sickle cell anemia patients. It indicated a West African ethnic background. PMID: 26849705
In Portuguese beta-thalassemia carriers the HBG2 XmnI polymorphism is strongly associated with HbF levels. PMID: 25842369
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
Its polymorphism effects HbF, HbE, MCV and MCH levels in Thai HbE carriers. PMID: 24474642
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
Hemoglobin gamma G plays a role in modifying clinical symptoms of beta-thalassemia innorthern Thailand. PMID: 25123009
Hb F is regulated in inherited bone marrow failure syndromes by Xmn1-HBG2, as it is in the haemoglobinopathies. PMID: 23713742
Our data suggest that a temporal repression mechanism is operative in the silencing of gamma-globin gene expression PMID: 23284307
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
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
Chromatin looping between the Ggamma-globin gene and LCR HSs requires NF-E2. PMID: 21609963
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
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
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
The recently identified chromatin factor Friend of Prmt1 (FOP) is a critical modulator of gamma-globin gene expression. PMID: 20688955
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
Data suggest the G gamma-globin promoter is activated by cJun via an upstream cAMP response element. PMID: 19861239
No statistically significant difference in the frequency of positive XmnI(G)gamma polymorphism was observed between thalassemia intermedia and thalassemia major patients. PMID: 19892574
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
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
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
analysis of heme uptake from human methemoglobin by the iron-regulated surface determinants system of Staphylococcus aureus PMID: 18467329
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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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.