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A6229

Sigma-Aldrich

Anti-AKR1C3 antibody, Mouse monoclonal

clone NP6.G6.A6, purified from hybridoma cell culture

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Synonym(s):
Anti-DD-3, Anti-DD3, Anti-HA1753
MDL number:
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

NP6.G6.A6, monoclonal

form

buffered aqueous solution

mol wt

antigen ~38 kDa

species reactivity

human

packaging

antibody small pack of 25 μL

technique(s)

immunohistochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 0.25-0.5 μg/mL using cytosolic fraction extract of A549 human lung carcinoma cell

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... AKR1C3(8644)

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This Item
A4355A2859M7194
antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

Gene Information

human ... AKR1C3(8644)

Gene Information

human ... PPP1R13B(23368)
mouse ... Ppp1r13b(21981)

Gene Information

human ... ATG5(9474)
mouse ... Atg5(11793)
rat ... Atg5(365601)

Gene Information

human ... MAP3K4(4216)
mouse ... Map3k4(26407)
rat ... Map3k4(308106)

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

species reactivity

human

species reactivity

mouse, human

species reactivity

human, mouse, rat

species reactivity

human, rat, mouse

clone

NP6.G6.A6, monoclonal

clone

LXO54.2, monoclonal

clone

ATG5-18, monoclonal

clone

MEKK4-338, monoclonal

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General description

Anti-AKR1C3 antibody, Mouse monoclonal (humanα - hydroxysteroid dehydrogenase, type 2,3; 17β- hydroxysteroid dehydrogenase, type 5) (mouse IgG1 isotype) is derived from the hybridoma NP6.G6. A6 produced by the fusion of mouse myeloma cells (SP20 cells) and splenocytes from BALB/c mice immunized with human AKR1C3 protein. Oxidoreduction of natural and foreign substrates is performed by three enzymes superfamilies, one of them being the AKRs (aldo-keto reductases) family. This family contains 114 proteins that are expressed in prokaryotes and eukaryotes and is divided into 14 subfamilies (AKR1-AKR14). The AKR1 family is the largest among the different fourteen families and contains the aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, and steroid 5 β-reductases. AKR1Cs are expressed in many tissues.

Immunogen

human AKR1C3 protein.

Application

Anti-AKR1C3 antibody, Mouse monoclonal has been used in
  • western blotting
  • immunohistochemistry
  • enzyme linked immunoassay (ELISA).

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Immunohistochemistry on human placentas were performed using monoclonal mouse anti-AKR1C3 at a dilution of 1:100 or western blot at 1:500.
Mouse monoclonal clone NP6.G6.A6 anti-AKR1C3 antibody used to tag aldo-keto reductase 1C3 for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques. It is used as a probe to determine the presence and roles of aldo-keto reductase 1C3 in the regulation of the androgen 5α-dihydrotestosterone (DHT) and 3α-diol compound levels in vivo.

Biochem/physiol Actions

In humans AKR1C3 (aldo-keto reductase family 1 member C3) including AKR1C1,2 and 4, catalyze the reduction of the androgen 5α-dihydrotestosterone (DHT) into inactive 3β or 3α-androstane diol (3α/β-Diol). AKR1C1-4 isoforms also display 3α[17β]-hydroxysteroid oxidase activity using 3α-Diol as a substrate, in vitro. In non-small cell lung carcinoma, AKR1Cs expression is dramatically increased. Due to their product profile and discrete tissue localization, they may regulate the level of active androgens, estrogens, and progestins in target tissues.

Target description

AKR1C3, aldo-keto reductase family 1, member C3 (3-α hydroxysteroid dehydrogenase, type II), encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of

Physical form

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.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3beta-hydroxysteroid dehydrogenase activity: implications for steroid hormone metabolism and action
Steckelbroeck S, et al.
The Journal of Biological Chemistry, 279(11), 10784-10795 (2004)
Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
Penning TM, et al.
The Biochemical Journal, 351(27), 1-1 (2000)
Important roles of the AKR1C2 and SRD5A1 enzymes in progesterone metabolism in endometrial cancer model cell lines
Sinreih M, et al.
Chemico-Biological Interactions, 234(1), 297-308 (2015)
The aldo-keto reductase superfamily homepage
Hyndman D, et al.
Chemico-Biological Interactions, 143-144(27), 621-631 (2003)
Julie J Loiselle et al.
Journal of environmental radioactivity, 196, 64-81 (2018-11-06)
Radon is the second leading cause of lung cancer, after tobacco smoke. While tobacco smoke-induced carcinogenesis has been studied extensively, far less is known about radon-induced carcinogenesis, particularly in relation to the influence of radon on gene expression. The objectives

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