Hemoglobin, Polyclonal Antibody

Hgb; Haemoglobin; Hemoglobin (Hb), Goat Polyclonal anti-Human Antibody - Liquid

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Goat

Affinity Purified

Liquid

AB Concentration: >= 1.0 mg/mL (lot specific)

2-8 degree C

Small volumes of anti-Hb antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MyBioSource producer and supplier of goat anti-human HEMOGLOBIN POLYCLONAL ANTIBODY protein can be custom filled in any quantity to meet your research and bulk requirements. Polyclonal Goat Anti-human hemoglobin antibody used in elisa tests and medical research.

Polyclonal Antibody Goat anti-human hemoglobin purification: Goats were immunized with human hemoglobin in Freund's adjuvant. After multiple immunizations the goats were bled, serum collected and the anti- human hemoglobin immunoaffinity purified off an antigen containing immunoabsorbant.

Our Polyclonal Antibody Goat anti-human hemoglobin purification forms a single precipitin band with human ***** hemoglobin A1, A2, F and S, by immunoelectrophoresis.

Western Blots 1:1,000-1:5,000 ELISA capture: 5 ug/mL

Inquire on our custom polyclonal antibody production. We can host from any species and cross link to your requirements. Custom Polyclonal antibody concentrations available.

Antibodies; Polyclonal; Hemoglobin (hb); Polyclonal Antibody

ELISA (EIA), Blotting

15,998 Da

hemoglobin, beta

hemoglobin subunit beta; beta globin chain; hemoglobin beta chain

Hemoglobin subunit beta

HBB_HUMAN

The alpha (HBA) and beta (HBB) loci determine the structure of the 2 types of polypeptide chains in ***** hemoglobin, Hb A. The normal ***** 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 ***** 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; oxygen transport; protein heterooligomerization; 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

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