protein

Recombinant Human Hemoglobin subunit beta

MBS948191

0.2 mg

460 USD

Recombinant Protein

Recombinant Human Hemoglobin subunit beta

[Hemoglobin subunit beta]

[Beta-globin, HBB]

[hemoglobin subunit beta; Hemoglobin subunit beta; hemoglobin subunit beta; hemoglobin subunit beta; Beta-globin; Hemoglobin beta chain]

[HBB]

[HBB; HBB; CD113t-C; beta-globin]

HBB_HUMAN

E.coli

[1-147]

MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWT
QRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAH
LDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAH
HFGKEFTPPVQAAYQKVVAGVANALAHKYH

>90% by SDS-PAGE

Liquid, dissolved in 20mM Tris-HCl, 500mM NaCl, pH 8.0, 50% glycerol

Aliquot and store at -20 degree C or -80 degree C. Avoid repeated freeze / thaw cycles

Calibrator or standard in ELISA and other possible application.

SDS-Page

Tag: His-SUMO-tag

Cardiovascular

HBB is encoded by the HBB gene on human chromosome 11. Mutations in the gene produce several variants of the proteins which are implicated with genetic disorders such as sickle-cell disease and beta thalassemia, as well as beneficial traits such as genetic resistance to malaria.

Nucleotide sequence analysis of coding and noncoding regions of human beta-globin mRNA.Marotta C., Forget B., Cohen-Solal M., Weissman S.M.Prog. Nucleic Acid Res. Mol. Biol. 19:165-175(1976)

4504349

NP_000509.1

NM_000518.4

P68871

31.9KD

African Trypanosomiasis Pathway (194384); African Trypanosomiasis Pathway (194323); Binding And Uptake Of Ligands By Scavenger Receptors Pathway (1269897); Erythrocytes Take Up Carbon Dioxide And Release Oxygen Pathway (1270224); Erythrocytes Take Up Oxygen And Release Carbon Dioxide Pathway (1270225); Factors Involved In Megakaryocyte Development And Platelet Production Pathway (1269377); Folate Metabolism Pathway (198833); Hemostasis Pathway (1269340); Malaria Pathway (152665); Malaria Pathway (152657)

The alpha (HBA) and beta (HBB) loci determine the structure of the 2 types of polypeptide chains in adult hemoglobin, Hb A. The normal adult hemoglobin tetramer consists of two alpha chains and two beta chains. Mutant beta globin causes sickle cell anemia. Absence of beta chain causes beta-zero-thalassemia. Reduced amounts of detectable beta globin causes beta-plus-thalassemia. The order of the genes in the beta-globin cluster is 5'-epsilon -- gamma-G -- gamma-A -- delta -- beta--3'. [provided by RefSeq, Jul 2008]

HBB: Involved in oxygen transport from the lung to the various peripheral tissues. Defects in HBB 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 HBB are the cause of beta-thalassemia (B-THAL). A form of thalassemia. Thalassemias are common monogenic diseases occurring mostly in Mediterranean and Southeast Asian populations. The hallmark of beta-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. Absence of beta chain causes beta(0)-thalassemia, while reduced amounts of detectable beta globin causes beta(+)-thalassemia. In the severe forms of beta-thalassemia, the excess alpha globin chains accumulate in the developing erythroid precursors in the marrow. Their deposition leads to a vast increase in erythroid apoptosis that in turn causes ineffective erythropoiesis and severe microcytic hypochromic anemia. Clinically, beta-thalassemia is divided into thalassemia major which is transfusion dependent, thalassemia intermedia (of intermediate severity), and thalassemia minor that is asymptomatic. Defects in HBB are the cause of sickle cell anemia (SKCA); also known as sickle cell disease. Sickle cell anemia is characterized by abnormally shaped red cells resulting in chronic anemia and periodic episodes of pain, serious infections and damage to vital organs. Normal red blood cells are round and flexible and flow easily through blood vessels, but in sickle cell anemia, the abnormal hemoglobin (called Hb S) causes red blood cells to become stiff. They are C-shaped and resembles a sickle. These stiffer red blood cells can led to microvascular occlusion thus cutting off the blood supply to nearby tissues. Defects in HBB are the cause of beta-thalassemia dominant inclusion body type (B-THALIB). An autosomal dominant form of beta thalassemia characterized by moderate anemia, lifelong jaundice, cholelithiasis and splenomegaly, marked morphologic changes in the red cells, erythroid hyperplasia of the bone marrow with increased numbers of multinucleate red cell precursors, and the presence of large inclusion bodies in the normoblasts, both in the marrow and in the peripheral blood after splenectomy. Belongs to the globin family. Protein type: Carrier. Chromosomal Location of Human Ortholog: 11p15.5. Cellular Component: cytosol; extracellular region; hemoglobin complex. Molecular Function: haptoglobin binding; heme binding; hemoglobin binding; iron ion binding; oxygen binding; oxygen transporter activity; peroxidase activity; protein binding. Biological Process: bicarbonate transport; blood coagulation; hydrogen peroxide catabolic process; nitric oxide transport; oxygen transport; positive regulation of nitric oxide biosynthetic process; protein heterooligomerization; receptor-mediated endocytosis; regulation of blood pressure; regulation of blood vessel size; response to hydrogen peroxide. Disease: Alpha-thalassemia; Beta-thalassemia; Beta-thalassemia, Dominant Inclusion Body Type; Fetal Hemoglobin Quantitative Trait Locus 1; Heinz Body Anemias; Malaria, Susceptibility To; Sickle Cell Anemia

0.2 mg

460 USD

0.5 mg

750

1 mg

1180