B9277
Monoclonal Anti-Band 3 antibody produced in mouse
clone BIII-136, ascites fluid
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About This Item
Productos recomendados
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
BIII-136, monoclonal
contains
15 mM sodium azide
species reactivity
human
technique(s)
immunoprecipitation (IP): suitable using human erythrocytes
indirect immunofluorescence: suitable using methanol-fixed human erythrocytes
western blot: 1:5,000 using human erythrocytes
isotype
IgG2a
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... SLC4A1(6521)
General description
Band 3 is a hydrophobic protein, it exists in erythrocytes as a dimer and tetramer and has a strong tendency to aggregate because of oxidative stress.
Band 3 is an anion exchanger that is abundantly found in erythrocyte membranes. This integral membrane anion exchanger protein regulates mechanical stability and ion homeostasis across the red blood cell membrane. Genetic alterations in Band 3 have been associated with familial distal renal tubular acidosis
Monoclonal Anti-Band 3 antibody detects Band 3 protein (90-100 kD) and several lower molecular mass peptides migrating in SDS-PAGE gels in the regions of 60, 40 and 20 kD. The product specifically binds to the cytoplasmic amino-terminal protein of band 3 (the epitope is approx. 20 kD from the N-terminal end). As the epitope is not located at the erythrocyte surface, the antibody product does not agglutinate red blood cells. Furthermore, its cell surface binding cannot be detected by an indirect agglutination assay. The antibody does not localize Band 3 from horse, bovine, pig, guinea pig, dog or mouse erythrocytes, nor does it localize Band 3 from nonerythroid human fibroblast extract.
Monoclonal Anti-Band 3 antibody detects Band 3 protein (90-100 kD) and several lower molecular mass peptides migrating in SDS-PAGE gels in the regions of 60, 40 and 20 kD. The product specifically binds to the cytoplasmic amino-terminal protein of band 3 (the epitope is approx. 20 kD from the N-terminal end). As the epitope is not located at the erythrocyte surface, the antibody product does not agglutinate red blood cells. Furthermore, its cell surface binding cannot be detected by an indirect agglutination assay. The antibody does not localize Band 3 from horse, bovine, pig, guinea pig, dog or mouse erythrocytes, nor does it localize Band 3 from nonerythroid human fibroblast extract.
Specificity
The antibody recognizes an epitope located in the cytoplasmic N-terminus of the band 3 molecule/proteins (90-100kDa).
Immunogen
Glycophorin B from human erythrocytes.
Application
Monoclonal Anti-Band 3 antibody can be used for western blot, immunoprecipitation and indirect immunofluorescence using human erythrocytes.
Monoclonal Anti-Human Band 3 has been used in immunoblotting. It may also be used in the study of red cell structures and functions and to study the fragmentation of the cytoplasmic domain of band 3 protein in vivo and in vitro.
Monoclonal anti-Band 3 antibodies can be used in ELISA and immunoprecipitation. It may also be used for immunofluorescent staining.
Biochem/physiol Actions
Band 3, a 90-100kD protein is the major integral protein of human erythrocytes responsible for anion exchange. It also regulates the intracellular pH. Monoclonal anti-Band 3 antibody is useful in in vivo and in vitro study of fragmentation of cytoplasmic domain of band 3 protein. It may also be used for immunoblot analysis. Monoclonal Anti-Human Band 3 antibody reacts specifically with cytoplasmic N-terminal band 3 proteins (90-100kD).
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
L J Bruce et al.
Biochemistry and cell biology = Biochimie et biologie cellulaire, 76(5), 723-728 (1999-06-03)
In distal renal tubular acidosis (dRTA) the tubular secretion of hydrogen ion in the distal nephron is impaired, leading to the development of metabolic acidosis, frequently accompanied by hypokalemia, nephrocalcinosis, and metabolic bone disease. The condition can be familial, when
Mohammad Al-Ansari et al.
BMC hematology, 15, 17-17 (2015-12-22)
Glucose-6-phosphate dehydrogenase (G6PD) deficiency is associated with erythrocyte sensitivity to oxidative damage and hemolytic crises. In β-thalassemia major, where hemoglobin instability imposes oxidative stress, erythrocytes show reduced hENT1 nucleoside transporter expression and decreased nucleoside uptake. This study investigated hENT1 expression
Daan Vorselen et al.
Nature communications, 9(1), 4960-4960 (2018-11-25)
Extracellular vesicles (EVs) are widely studied regarding their role in cell-to-cell communication and disease, as well as for applications as biomarkers or drug delivery vehicles. EVs contain membrane and intraluminal proteins, affecting their structure and thereby likely their functioning. Here
Antonella Pantaleo et al.
Oxidative medicine and cellular longevity, 2016, 6051093-6051093 (2016-04-02)
In erythrocytes, the regulation of the redox sensitive Tyr phosphorylation of band 3 and its functions are still partially defined. A role of band 3 oxidation in regulating its own phosphorylation has been previously suggested. The current study provides evidences
Gabriella Donà et al.
International journal of molecular sciences, 21(11) (2020-06-11)
Bicarbonate uptake is one of the early steps of capacitation, but the identification of proteins regulating anion fluxes remains elusive. The aim of this study is to investigate the role of sperm solute carrier 4 (SLC4) A1 (spAE1) in the
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