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Human Anti-HBB (N-terminus) Monoclonal Antibody (CBFYH-3020) (CBMAB-H1633-FY)

This product is human antibody that recognizes HBB. The antibody CBFYH-3020 can be used for immunoassay techniques such as: ELISA.
See all HBB antibodies

Summary

Host Animal
Human
Specificity
Human
Clone
CBFYH-3020
Antibody Isotype
IgG1
Application
ELISA

Basic Information

Immunogen
A glycated peptide, corresponding to N-terminal 9 amino acids of haemoglobin beta chain coupled to the carrier proteins BSA and TRF. Purified HbA1c
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
N-terminus

Target

Full Name
Hemoglobin Subunit Beta
Introduction
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'.
Entrez Gene ID
UniProt ID
Alternative Names
Hemoglobin Subunit Beta; Hemoglobin, Beta; Beta-Globin; Hemoglobin Beta Chain; Beta Globin Chain; CD113t-C
Function
Involved in oxygen transport from the lung to the various peripheral tissues.

LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.

Spinorphin:
Functions as an endogenous inhibitor of enkephalin-degrading enzymes such as DPP3, and as a selective antagonist of the P2RX3 receptor which is involved in pain signaling, these properties implicate it as a regulator of pain and inflammation.
Biological Process
Cellular oxidant detoxification Source: GOC
Hydrogen peroxide catabolic process Source: BHF-UCL
Nitric oxide transport Source: UniProtKB
Oxygen transport Source: UniProtKB
Platelet aggregation Source: UniProtKB
Positive regulation of cell death Source: BHF-UCL
Positive regulation of nitric oxide biosynthetic process Source: UniProtKB
Regulation of blood pressure Source: UniProtKB-KW
Renal absorption Source: UniProtKB
Response to hydrogen peroxide Source: BHF-UCL
Cellular Location
Cytosol; Hemoglobin complex; Blood microparticle; Extracellular exosome; Extracellular region; Extracellular space; Endocytic vesicle lumen; Ficolin-1-rich granule lumen; Haptoglobin-hemoglobin complex; Tertiary granule lumen
Involvement in disease
Heinz body anemias (HEIBAN):
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.
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.
Sickle cell anemia (SKCA):
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.
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.
PTM
Glucose reacts non-enzymatically with the N-terminus of the beta chain to form a stable ketoamine linkage. This takes place slowly and continuously throughout the 120-day life span of the red blood cell. The rate of glycation is increased in patients with diabetes mellitus.
S-nitrosylated; a nitric oxide group is first bound to Fe2+ and then transferred to Cys-94 to allow capture of O2.
Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin exposure.

Perroud, C., Porret, N., & Rovó, A. (2023). “The Long Journey of Unexplained Erythrocytosis”: Erythrocytosis due to High-Oxygen Affinity Hemoglobinopathy–Hemoglobin Variant Little Rock (HBB: c. 432C> A)–A Report of a Swiss Family and Review of the Literature. Acta Haematologica, 1-5.

Wu, Y., Li, P., Liu, L., Goodwin, A. J., Halushka, P. V., Hirose, T., ... & Fan, H. (2022). lncRNA Neat1 regulates neuronal dysfunction post-sepsis via stabilization of hemoglobin subunit beta. Molecular Therapy, 30(7), 2618-2632.

Al-Nafie, A. T., Al-Thuwaini, T. M., & Al-Shuhaib, M. B. S. (2022). A novel association between hemoglobin subunit beta gene and reproductive performance in Awassi ewes. Journal of the Saudi Society of Agricultural Sciences, 21(1), 1-7.

Melamed, D., Nov, Y., Malik, A., Yakass, M. B., Bolotin, E., Shemer, R., ... & Livnat, A. (2022). De novo mutation rates at the single-mutation resolution in a human HBB gene region associated with adaptation and genetic disease. Genome Research, 32(3), 488-498.

Zhu, J., Wang, X., Qi, R., Tan, Y., Li, C., Miao, Q., ... & Liu, G. (2021). Hemoglobin subunit beta interacts with the capsid, RdRp and VPg proteins, and antagonizes the replication of rabbit hemorrhagic disease virus. Veterinary Microbiology, 259, 109143.

Soremekun, O. S., Ezenwa, C., Isewon, I., Soliman, M., Idowu, O., Nashiru, O., & Fatumo, S. (2020). Computational and drug target analysis of functional single nucleotide polymorphisms associated with Haemoglobin Subunit Beta (HBB) gene. Computers in Biology and Medicine, 125, 104018.

Groß, R., Bauer, R., Krüger, F., Rücker-Braun, E., Olari, L. R., Ständker, L., ... & Münch, J. (2020). A placenta derived C-terminal fragment of β-hemoglobin with combined antibacterial and antiviral activity. Frontiers in microbiology, 11, 508.

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For research use only. Not intended for any clinical use.

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