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Merck

SAB4200722

Sigma-Aldrich

Anti-Band 3 antibody, Mouse monoclonal

clone BIII-136, purified from hybridoma cell culture

Sinónimos:

AE 1, Anion exchange protein 1, Anion exchanger 1, Band 3 anion transport protein, Solute carrier family 4 member 1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

Quality Level

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

BIII-136, monoclonal

form

buffered aqueous solution

species reactivity

human

concentration

~1 mg/mL

technique(s)

immunoblotting: 2-4 μg/mL (human erythrocytes ghosts extract)
immunoprecipitation (IP): suitable

isotype

IgG2a

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SLC4A1(6521)

General description

Anti-Band 3 antibody, Mouse monoclonal (mouse IgG2a isotype) is derived from the BIII-136 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mouse immunized with glycophorin B purified from human erythrocytes.

Application

Anti-Band 3 antibody, Mouse monoclonal may be used in immunoblotting and immunoprecipitation.

Biochem/physiol Actions

As a response to an oxidative stress, Band 3 protein forms clusters and clear damaged and aged RBCs from circulation. Enhanced band 3 protein clustering is implicated in RBC disorders such as hemolytic anemia, glucose-6-phosphate dehydrogenase (G6PD) deficiency, malaria and sickle-cell disease.

Physical form

Glycophorin B purified from human erythrocytes
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Akihiro Moriyama et al.
Scientific reports, 5, 17427-17427 (2015-12-01)
Membrane proteins interact with membrane lipids for their structural stability and proper function. However, lipid-protein interactions are poorly understood at a molecular level especially in the live cell membrane, due to current limitations in methodology. Here, we report that amphiphilic
Kodjo Ayi et al.
Blood, 104(10), 3364-3371 (2004-07-29)
High frequency of erythrocyte (red blood cell [RBC]) genetic disorders such as sickle cell trait, thalassemia trait, homozygous hemoglobin C (Hb-C), and glucose-6-phosphate dehydrogenase (G6PD) deficiency in regions with high incidence of Plasmodium falciparum malaria and case-control studies support the
Changes in band 3 structure as determinants of erythrocyte integrity during storage and survival after transfusion.
Giel J C G M Bosman et al.
Blood transfusion = Trasfusione del sangue, 8 Suppl 3, s48-s52 (2010-07-08)
Changes in band 3 structure as determinants of erythrocyte integrity during storage and survival after transfusion
Bosman G, et al.
Blood Transfusion = Trasfusione del Sangue, 8(Suppl 3), s48-s48 (2010)
J R Pawloski et al.
Nature, 409(6820), 622-626 (2001-02-24)
Previous studies support a model in which the physiological O2 gradient is transduced by haemoglobin into the coordinate release from red blood cells of O2 and nitric oxide (NO)-derived vasoactivity to optimize oxygen delivery in the arterial periphery. But whereas

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