Hemoglobin subunit alpha Recombinant Protein | Hba recombinant protein

Recombinant Mouse Hemoglobin subunit alpha

Cat. Num. AAA1264434

• Gene Names: Hba-a1; Hba; Hba1; Hbat1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Hemoglobin subunit alpha; Recombinant Mouse Hemoglobin subunit alpha; Alpha-globin; Hemoglobin alpha chain; Hba recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 2-142aa; Full Length
• Sequence: VLSGEDKSNIKAAWGKIGGHGAEYGAEALERMFASFPTTKTYFPHFDVSHGSAQVKGHGKKVADALASAAGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLASHHPADFTPAVHASLDKFLASVSTVLTSKYR
• Sequence Length: 142

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for Hba recombinant protein

Involved in oxygen transport from the lung to the various peripheral tissues.

References

The complete sequence of a chromosomal mouse alpha-globin gene reveals elements conserved throughout vertebrate evolution.Nishioka Y., Leder P.Cell 18:875-882(1979) Hemoglobins of mice sequence and possible ambiguity at one position of the alpha chain.Popp R.A.J. Mol. Biol. 27:9-16(1967) Lubec G., Klug S., Kang S.U.Submitted (APR-2007) to UniProtKB Comparison of cloned mouse alpha- and beta-globin genes conservation of intervening sequence locations and extragenic homology.Leder A., Miller H.I., Hamer D.H., Seidman J.G., Norman B., Sullivan M., Leder P.Proc. Natl. Acad. Sci. U.S.A. 75:6187-6191(1978) Characterization and kinetics of synthesis of 15S beta-globin RNA, a putative precursor of beta-globin mRNA.Curtis P.J., Mantei N., Weissmann C.Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978) SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.Mol. Cell 50:919-930(2013) Studies on the mouse hemoglobin loci. 8. A fourth alpha-chain phenotype.Popp R.A.J. Hered. 60:126-133(1969) Popp R.A.(In) Altman P.A., Katz D.D. (eds.) ;Inbred and genetically defined strains of laboratory animals, pp.105-105, Federation of American Societies for Experimental Biology, Bethesda (1979) The primary structure of genetic variants of mouse hemoglobin.Popp R.A., Bailiff E.G., Skow L.C., Whitney J.B. IIIBiochem. Genet. 20:199-208(1982)

NCBI and Uniprot Product Information

• NCBI GI #: 122441
• NCBI GeneID: 15122
• UniProt Accession #: P01942
• Molecular Weight: 17 kDa
• NCBI Official Full Name: Hemoglobin subunit alpha
• NCBI Official Synonym Full Names: hemoglobin alpha, adult chain 1
• NCBI Official Symbol: Hba-a1
• NCBI Official Synonym Symbols: Hba; Hba1; Hbat1
• NCBI Protein Information: hemoglobin subunit alpha
• UniProt Protein Name: Hemoglobin subunit alpha
• Protein Family: Hemoglobin
• UniProt Gene Name: Hba
• UniProt Synonym Gene Names: Hba-a1
• UniProt Entry Name: HBA_MOUSE

Uniprot Description

HBA1: Involved in oxygen transport from the lung to the various peripheral tissues. Defects in HBA1 may be a cause of Heinz body anemias (HEIBAN). This is a form of non-spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency. Defects in HBA1 are the cause of alpha-thalassemia (A- THAL). The thalassemias are the most common monogenic diseases and occur mostly in Mediterranean and Southeast Asian populations. The hallmark of alpha-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. The level of alpha chain production can range from none to very nearly normal levels. Deletion of both copies of each of the two alpha-globin genes causes alpha(0)-thalassemia, also known as homozygous alpha thalassemia. Due to the complete absence of alpha chains, the predominant fetal hemoglobin is a tetramer of gamma-chains (Bart hemoglobin) that has essentially no oxygen carrying capacity. This causes oxygen starvation in the fetal tissues leading to prenatal lethality or early neonatal death. The loss of three alpha genes results in high levels of a tetramer of four beta chains (hemoglobin H), causing a severe and life-threatening anemia known as hemoglobin H disease. Untreated, most patients die in childhood or early adolescence. The loss of two alpha genes results in mild alpha-thalassemia, also known as heterozygous alpha-thalassemia. Affected individuals have small red cells and a mild anemia (microcytosis). If three of the four alpha-globin genes are functional, individuals are completely asymptomatic. Some rare forms of alpha-thalassemia are due to point mutations (non- deletional alpha-thalassemia). The thalassemic phenotype is due to unstable globin alpha chains that are rapidly catabolized prior to formation of the alpha-beta heterotetramers. Alpha(0)-thalassemia is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non- immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders. Defects in HBA1 are the cause of hemoglobin H disease (HBH). HBH is a form of alpha-thalassemia due to the loss of three alpha genes. This results in high levels of a tetramer of four beta chains (hemoglobin H), causing a severe and life-threatening anemia. Untreated, most patients die in childhood or early adolescence. Belongs to the globin family.

Protein type: Carrier

Cellular Component: hemoglobin complex; membrane

Molecular Function: haptoglobin binding; heme binding; organic acid binding; oxygen binding; peroxidase activity

Biological Process: erythrocyte development; in utero embryonic development