protein

Hemoglobin A1C, Glycated (HbA1c, Glycohemoglobin)

MBS634425

1 mg

640 USD

Protein

Hemoglobin A1C, Glycated (HbA1c, Glycohemoglobin)

[Hemoglobin A1C, Glycated]

[hemoglobin subunit alpha; Hemoglobin subunit alpha; hemoglobin subunit alpha; alpha-globin; alpha-1 globin; alpha-1-globin; alpha one globin; hemoglobin alpha chain; hemoglobin alpha-1 chain; hemoglobin alpha 1 globin chain; hemoglobin, alpha 1; Alpha-globin; Hemoglobin alpha chain]

[HBA1; HBA1; HBH; CD31]

HBA_HUMAN

>96% (HPLC), verified by SDS-PAGE

Supplied as a liquid in buffer, pH 8.0.

1.4 mg/ml

May be stored at 4 degree C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degree C. Aliquots are stable for 6 months after receipt at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

ELISA (EL/EIA)

Other applications not tested. Optimal dilutions to be determined by the researcher.

Source: Human erythrocytes

Molecular Biology; MB-Hemoglobin

Hemoglobin is composed of one globin plus four hemes. Heme consists of protoporphyrin IX and ferrous iron. The iron content of human hemoglobin is 0.338% (w/w) which gives a minimal molecular weight of 16,520. Ultracentrifugal and osmotic pressure measurements indicate an actual molecular weight four times the minimum molecular weight. The measurement of glycated hemoglobin, Human hemoglobin A1c (HbA1c) in human blood is the most important marker for long-term assessment of the glycemic state in patients with diabetes, and goals for therapy are set at specific human Hemoglobin A1c, HbA1c target values. Glycosylated hemoglobin (HbA1c) levels are used as an indicator of blood glucose in diabetic patients. Hemoglobin A1C, Glycated (HbA1c, Glycohemoglobin) is used in enzymatic assays and is native, naturally glycated and functionally active. HbA1c has a molecular weight of 68kD and is composed of 4 subunits.

4504347

NP_000549.1

NM_000558.3

P69905

68kD

African Trypanosomiasis Pathway (194384); African Trypanosomiasis Pathway (194323); Binding And Uptake Of Ligands By Scavenger Receptors Pathway (771599); Malaria Pathway (152665); Malaria Pathway (152657); Metabolism Pathway (477135); O2/CO2 Exchange In Erythrocytes Pathway (645346); Scavenging Of Heme From Plasma Pathway (771600); Selenium Pathway (198825); Uptake Of Carbon Dioxide And Release Of Oxygen By Erythrocytes Pathway (645347)

The human alpha globin gene cluster located on chromosome 16 spans about 30 kb and includes seven loci: 5'- zeta - pseudozeta - mu - pseudoalpha-1 - alpha-2 - alpha-1 - theta - 3'. The alpha-2 (HBA2) and alpha-1 (HBA1) coding sequences are identical. These genes differ slightly over the 5' untranslated regions and the introns, but they differ significantly over the 3' untranslated regions. Two alpha chains plus two beta chains constitute HbA, which in normal adult life comprises about 97% of the total hemoglobin; alpha chains combine with delta chains to constitute HbA-2, which with HbF (fetal hemoglobin) makes up the remaining 3% of adult hemoglobin. Alpha thalassemias result from deletions of each of the alpha genes as well as deletions of both HBA2 and HBA1; some nondeletion alpha thalassemias have also been reported. [provided by RefSeq, Jul 2008]

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. Chromosomal Location of Human Ortholog: 16p13.3. Cellular Component: membrane; hemoglobin complex; extracellular region; cytosol. Molecular Function: haptoglobin binding; protein binding; peroxidase activity; iron ion binding; heme binding; oxygen binding; oxygen transporter activity. Biological Process: receptor-mediated endocytosis; response to hydrogen peroxide; hydrogen peroxide catabolic process; bicarbonate transport; oxygen transport; protein heterooligomerization. Disease: Hemoglobin H Disease; Heinz Body Anemias; Alpha-thalassemia

1 mg

640 USD