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GW22594

Sigma-Aldrich

Anti-DUSP12 antibody produced in chicken

affinity isolated antibody, buffered aqueous solution

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

chicken

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DUSP12(11266)

General description

DUSP12 (dual specificity phosphatase) gene is localized to human chromosome 1q21-q22. Its C-terminal contains a non-catalytic domain, which is rich in cysteine and acts as a zinc finger domain. It is an atypical DUSP member, which is recognized as a phosphatase with pro-survival attributes. It is evolutionarily conserved. Its DUSP catalytic domain is present at its N-terminal.

The previously assigned protein identifier Q5VXA8 has been merged into Q9UNI6. Full details can be found on the UniProt database.

Immunogen

Immunogen Sequence: GI # 6005956, sequence 1-340
Recombinant dual specificity phosphatase 12

Application

Anti-DUSP12 antibody produced in chicken is suitable for western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.

Biochem/physiol Actions

Dual specificity protein phosphatase 12 (DSUP12) is a novel cell survival phosphatase. DUSP12 is an evolutionary conserved phosphatase containing a unique zinc-binding domain. Its expression affects cell cycle progression. Overexpression of the gene increases cell motility and resistance to apoptosis. Overexpression also causes a significant increase in polyploidy and in the G 2/M cell population, with a subsequent decrease in the G 0/G 1 population. It promotes increased expression of the c-met proto-oncogene and collagen, and laminin receptor intergrin α 1 (itgα1), which is implicated in metastasis. DUSP12 is oncologically relevant and could be used therapeutically for targeted oncogenes. The enzyme plays a role in cell survival and ribosome biogenesis and protects cells from oxidative stress.

Physical form

Solution in phosphate buffered saline containing 0.02% sodium azide.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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Priya R Sharda et al.
The Biochemical journal, 418(2), 391-401 (2008-11-01)
hYVH1 [human orthologue of YVH1 (yeast VH1-related phosphatase)] is an atypical dual-specificity phosphatase that is widely conserved throughout evolution. Deletion studies in yeast have suggested a role for this phosphatase in regulating cell growth. However, the role of the human
M Muda et al.
The Journal of biological chemistry, 274(34), 23991-23995 (1999-08-14)
A human orthologue of the Saccharomyces cerevisiae YVH1 protein-tyrosine phosphatase is able to rescue the slow growth defect caused by the disruption of the S. cerevisiae YVH1 gene. The human YVH1 gene is located on chromosome 1q21-q22, which falls in
Anna Kozarova et al.
Cell cycle (Georgetown, Tex.), 10(10), 1669-1678 (2011-04-28)
The dual-specificity phosphatase hYVH1 (DUSP12) is an evolutionary conserved phosphatase that also contains a unique zinc-binding domain. Recent evidence suggests that this enzyme plays a role in cell survival and ribosome biogenesis. Here, we report that hYVH1 expression also affects
Christopher A Bonham et al.
The Journal of biological chemistry, 284(34), 22853-22864 (2009-07-02)
YVH1 was one of the first eukaryotic dual specificity phosphatases cloned, and orthologues poses a unique C-terminal zinc-coordinating domain in addition to a cysteine-based phosphatase domain. Our recent results revealed that human YVH1 (hYVH1) protects cells from oxidative stress. This
Erica L Cain et al.
PloS one, 6(4), e18677-e18677 (2011-05-11)
Analysis of chromosomal rearrangements within primary tumors has been influential in the identification of novel oncogenes. Identification of the "driver" gene(s) within cancer-derived amplicons is, however, hampered by the fact that most amplicons contain many gene products. Amplification of 1q21-1q23

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