Product Name

IMPDH2 antibody

Documents

Description

IMPDH2 Rabbit Polyclonal antibody. Positive WB detected in human heart tissue, A549 cells, human brain tissue, K-562 cells, mouse heart tissue, mouse lung tissue, rat heart tissue. Positive IP detected in K-562 cells. Positive IF detected in Hela cells. Positive IHC detected in human lung cancer tissue. Observed molecular weight by Western-blot: 56kd

Tested applications

ELISA, WB, IHC, IF, IP

Species reactivity

Human,Mouse,Rat; other species not tested.

Alternative names

IMP dehydrogenase 2 antibody; IMPD 2 antibody; IMPD2 antibody; IMPDH 2 antibody; IMPDH II antibody; IMPDH2 antibody

Isotype

Rabbit IgG

Preparation

This antibody was obtained by immunization of IMPDH2 recombinant protein (Accession Number: NM_000884). Purification method: Antigen affinity purified.

Clonality

Polyclonal

Formulation

PBS with 0.1% sodium azide and 50% glycerol pH 7.3.

Storage instructions

Store at -20℃. DO NOT ALIQUOT

Applications

Recommended Dilution:

WB: 1:500-1:5000

IP: 1:200-1:2000

IHC: 1:20-1:200

IF: 1:10-1:100

Validations

human heart tissue were subjected to SDS PAGE followed by western blot with Catalog No:111786(IMPDH2 antibody) at dilution of 1:400

IP Result of anti-IMPDH2 (IP:Catalog No:111786, 3ug; Detection:Catalog No:111786 1:800) with K-562 cells lysate 4000ug.

Immunohistochemical of paraffin-embedded human lung cancer using Catalog No:111786(IMPDH2 antibody) at dilution of 1:100 (under 10x lens)

Immunofluorescent analysis of Hela cells, using IMPDH2 antibody Catalog No:111786 at 1:25 dilution and Rhodamine-labeled goat anti-rabbit IgG (red).

Background

IMPDH2, also named as IMPD2, belongs to the IMPDH/GMPR family. It is a rate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth. It may also have a role in the development of malignancy and the growth progression of some tumors. IMPDH2 is a key enzyme in the purine nucleotide biosynthetic pathway and constitutes a pivotal biological target for immunosuppressant and antiviral drugs. (PMID:21181270) IMPDH2 is highly enriched in RR(filamentous rods and rings).

References

Carcamo WC, Satoh M, Kasahara H. Induction of cytoplasmic rods and rings structures by inhibition of the CTP and GTP synthetic pathway in mammalian cells. PloS one. 6(12):e29690. 2011.
Calise SJ, Carcamo WC, Krueger C, Yin JD, Purich DL, Chan EK. Glutamine deprivation initiates reversible assembly of mammalian rods and rings. Cellular and molecular life sciences : CMLS. 71(15):2963-73. 2014.
Kováčik L, Kereïche S, Kerïeche S. A simple Fourier filter for suppression of the missing wedge ray artefacts in single-axis electron tomographic reconstructions. Journal of structural biology. 186(1):141-52. 2014.
Keppeke GD, Satoh M, Ferraz ML, Chan EK, Andrade LE. Temporal evolution of human autoantibody response to cytoplasmic rods and rings structure during anti-HCV therapy with ribavirin and interferon-α. Immunologic research. 60(1):38-49. 2014.
Juda P, Smigová J, Kováčik L, Bártová E, Raška I. Ultrastructure of cytoplasmic and nuclear inosine-5'-monophosphate dehydrogenase 2 "rods and rings" inclusions. The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society. 62(10):739-50. 2014.
Lake JI, Tusheva OA, Graham BL, Heuckeroth RO. Hirschsprung-like disease is exacerbated by reduced de novo GMP synthesis. The Journal of clinical investigation. 123(11):4875-87. 2013.
Gunter JH, Thomas EC, Lengefeld N. Characterisation of inosine monophosphate dehydrogenase expression during retinal development: differences between variants and isoforms. The international journal of biochemistry & cell biology. 40(9):1716-28. 2008.
Keppeke GD, Andrade LE, Grieshaber SS, Chan EK. Microinjection of specific anti-IMPDH2 antibodies induces disassembly of cytoplasmic rods/rings that are primarily stationary and stable structures. Cell & bioscience. 5(1):1. 2015.

IMPDH2 antibody

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