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R3653

Sigma-Aldrich

Anti-Radixin antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti-DFNB24
MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~80 kDa

species reactivity

mouse, rat, human

technique(s)

immunoprecipitation (IP): 10-20 μg using RIPA extract (250 μg) of rat liver
indirect immunofluorescence: 10-20 μg/mL using cultured human HeLa cells
western blot: 1-2 μg/mL using whole extract of cultured HeLa cells
western blot: 1-2 μg/mL using whole extract of cultured mouse NIH3T3 cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... RDX(5962)
mouse ... Rdx(19684)
rat ... Rdx(315655)

General description

RDX (radixin) belongs to the ERM (ezrin-radixin-moesin) family. It is present in several normal cells, neoplastic cells, epithelial and lymphoid cells. It is located on chromosome 11. In mouse, RDX is found in the hair cell stereocilia of inner ear.

Immunogen

synthetic peptide corresponding to amino acid residues 400-409 of human radixin with an N-terminal added tripeptide, conjugated to KLH. The corresponding sequence is identical in mouse, rat, and pig and differs by two amino acids in chicken.

Application

Anti-Radixin antibody produced in rabbit has been used in
  • immunoblotting
  • immunoprecipitation
  • immunofluorescence staining of cultured cells

Biochem/physiol Actions

In human, knockdown of radixin (RDX) represses the development of glioblastoma cell in vitro and in vivo. It participates in cell motility, invasion and tumor progression. It acts as a membrane-cytoskeletal linker in cell surface structures that are abundant with actin. It is necessary for the arrangement of cortical cytoskeleton. RDX mutation can lead to DFNB24 hearing loss in human.
Radixin is the dominant ezrin-radixin-moesin (ERM) protein in liver bile canaliculi where it is considered to have a critical role in bile conjugated-bilirubin secretion by influencing the cellular localization of the multidrug resistance protein 2 (MRP2). Resting normal human blood cells lack detectable radixin. Radixin is found in classical NK cells. Radixin has closed and open forms corresponding to the inactive and active forms as cross-linkers between actin filaments. It may be phosphorylated and it plays an important role in the activation of the Rho family members by recruiting their positive and negative regulators.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 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.

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

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Radixin knockdown by RNA interference suppresses human glioblastoma cell growth in vitro and in vivo
Qin JJ, et al.
Asian Pacific Journal of Cancer Prevention, 15(22), 9805-9812 (2014)
Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes.
Kikuchi S, et al.
Nature Genetics, 31(3), 320-320 (2002)
Lixin Zhu et al.
American journal of physiology. Gastrointestinal and liver physiology, 296(2), G185-G195 (2008-12-17)
ERM (ezrin, radixin, and moesin) proteins play critical roles in epithelial and endothelial cell polarity, among other functions. In gastric glands, ezrin is mainly expressed in acid-secreting parietal cells, but not in mucous neck cells or zymogenic chief cells. In
Richard J Goodyear et al.
The Journal of comparative neurology, 522(14), 3281-3294 (2014-04-05)
Early postnatal mouse cochlear cultures were treated with a small panel of kinase inhibitors to elucidate the mechanisms underlying the maintenance of hair-bundle structure in the developing inner ear. At low concentrations (1-10 nM), staurosporine causes the collapse and loss
A novel splice site mutation in the RDX gene causes DFNB24 hearing loss in an Iranian family
Shearer AE, et al.
American Journal of Medical Genetics. Part A, 149A(3), 555-558 (2009)

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