Hemoglobin Beta (HBb), Monoclonal Antibody

Hematology

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

Monoclonal

IgG1 kappa

C3

Mouse

The antibody is a mouse monoclonal antibody raised against HBb. It has been selected for its ability to recognize HBb in immunohistochemical staining and western blotting.

Antigen-specific affinity chromatography followed by Protein A affinity chromatography

Liquid; 0.01M PBS, pH7.4, containing 0.05% Proclin-300, 50% glycerol.

1mg/mL (lot specific)

Store at 4 degree C for frequent use. Aliquot and store at -20 degree C for 12 months.
Avoid repeated freeze/thaw cycles.

The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 degree C for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition.

Manufactured in an ISO 9001:2008 and ISO 13485:2003 Certified Laboratory.

Manufactured in a lab with traceable raw materials. Bulk orders can typically be prepared to the customer’s specifications, please inquire.

Small volumes of anti-HBb 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.

Western Blot (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunoprecipitation (IP)

WB: 0.5-2ug/mL; 1:500-2000
IHC: 5-20ug/mL; 1:50-200
ICC: 5-20ug/mL; 1:50-200

Figure. Western Blot: Sample: Recombinant HBb, Human

hemoglobin subunit beta

hemoglobin subunit beta

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; nitric oxide transport; response to hydrogen peroxide; oxygen transport; protein heterooligomerization; bicarbonate transport; hydrogen peroxide catabolic process; regulation of blood pressure; blood coagulation; regulation of blood vessel size

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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