antibody

HUMAN ANTI HUMAN HbA1c

MBS224674

0.1 mg

440 USD

monoclonal

human

nonconjugated

AbD15783-IgG

Antibody

HUMAN ANTI HUMAN HbA1c

HbA1c

HEMOGLOBIN A1C

hemoglobin subunit beta; Hemoglobin subunit beta; hemoglobin subunit beta; beta globin chain; hemoglobin beta chain; hemoglobin, beta; Beta-globin; Hemoglobin beta chainCleaved into the following 2 chains:LVV-hemorphin-7; Spinorphin

HBB; HBB; CD113t-C; beta-globin

HBB_HUMAN

Monoclonal

IgG1

AbD15783-IgG

HuCAL

147

Clone AbD15783-IgG specifically recognizes HbA1c, hemoglobin glycated at the N-terminal valine of the hemoglobin beta chain. It does not bind to non-glycated hemoglobin. Besides binding to the normal glycated hemoglobin, clone AbD15783-IgG also recognizes the glycated hemoglobin variants HbC, HbE, HbD and to a lesser degree HbS. Elevated HbF is not detected due to the absence of the hemoglobin beta chain. The measurement of HbA1c levels is used to identify the average plasma glucose concentration. In diabetes mellitus, higher levels of HbA1c have been associated with cardiovascular disease and other diseases. Levels of more than 6.5% HbA1c (48 mmol/mol) are used as a criterion to diagnose diabetes.This antibody is also available in a Fab format.

Purified. Human IgG1 antibody selected from the HuCAL phage display library and expressed in a human cell line.This antibody is supplied as a liquid.

Total protein concentration: 0.5 mg/ml.

Store at 4 degree C or at -20 degree C if preferred. Storage in frost-free freezers is not recommended. This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use. Shelf Life: 12 months from date of despatch.

ELISA (EIA)

Perservative Stabilisers: 0.01% Thiomersal . Preparation: Purified IgG prepared by affinity chromatography on Protein A

Immunogen: The immunogens used in the generation of this antibody were: A glycated peptide, corresponding to N-terminal 9 amino acids of haemoglobin beta chain coupled to the carrier proteins BSA and TRF. Purified HbA1c. Buffer Solution: Phosphate buffered saline. Affinity: The affinity of this antibody, as a monovalent fab measured against the immunogen, was measured as KD=19 nM by real time, label-free molecular interaction analysis using HbA1c-BSA and HbA1c-TRF conjugates as immobilized antigen.The affinity of this antibody, as a monovalent fab measured against purified HbA1c, was measured as KD=58 nM by real time, label-free molecular interaction analysis using full length HbA1c as immobilized antigen. Target Species: Human

Clone AbD15783-IgG specifically recognizes HbA1c, hemoglobin glycated at the N-terminal valine of the hemoglobin beta chain. It does not bind to non-glycated hemoglobin.Besides binding to the normal glycated hemoglobin, clone AbD15783-IgG also recognizes the glycated hemoglobin variants HbC, HbE, HbD and to a lesser degree HbS. Elevated HbF is not detected due to the absence of the hemoglobin beta chain. The measurement of HbA1c levels is used to identify the average plasma glucose concentration. In diabetes mellitus, higher levels of HbA1c have been associated with cardiovascular disease and other diseases. Levels of more than 6.5% HbA1c (48 mmol/mol) are used as a criterion to diagnose diabetes.This antibody is also available in a Fab format

4504349

NP_000509.1

NM_000518.4

P68871

15,998 Da

African Trypanosomiasis Pathway (194384); African Trypanosomiasis Pathway (194323); Binding And Uptake Of Ligands By Scavenger Receptors Pathway (771599); Erythrocytes Take Up Carbon Dioxide And Release Oxygen Pathway (645347); Erythrocytes Take Up Oxygen And Release Carbon Dioxide Pathway (645348); Factors Involved In Megakaryocyte Development And Platelet Production Pathway (187196); Folate Metabolism Pathway (198833); Hemostasis Pathway (106028); 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: hemoglobin complex; extracellular region; cytosol. Molecular Function: haptoglobin binding; protein binding; peroxidase activity; hemoglobin binding; iron ion binding; heme binding; oxygen binding; oxygen transporter activity. Biological Process: receptor-mediated endocytosis; positive regulation of nitric oxide biosynthetic process; response to hydrogen peroxide; nitric oxide transport; bicarbonate transport; hydrogen peroxide catabolic process; protein heterooligomerization; oxygen transport; regulation of blood pressure; regulation of blood vessel size; blood coagulation. Disease: Fetal Hemoglobin Quantitative Trait Locus 1; Beta-thalassemia; Sickle Cell Anemia; Heinz Body Anemias; Beta-thalassemia, Dominant Inclusion Body Type; Malaria, Susceptibility To; Alpha-thalassemia

0.1 mg

440 USD