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Merck

P9498

Sigma-Aldrich

Monoclonal Anti-PIAS-x antibody produced in mouse

clone PIASX-116, purified immunoglobulin, buffered aqueous solution

Sinónimos:

Anti-Protein Inhibitor of Activator STAT

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41
conjugado:
unconjugated
application:
ARR
ELISA (i)
ICC
WB
clon:
PIASX-116, monoclonal
reactividad de especies:
human
citations:
4
técnicas:
immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL using proteasome fraction II of HeLa cells

origen biológico

mouse

conjugado

unconjugated

forma del anticuerpo

purified immunoglobulin

tipo de anticuerpo

primary antibodies

clon

PIASX-116, monoclonal

Formulario

buffered aqueous solution

mol peso

antigen ~75 kDa

reactividad de especies

human

técnicas

immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL using proteasome fraction II of HeLa cells

isotipo

IgG1

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... PIAS2(9063)

Descripción general

Monoclonal Anti-PIAS-x (mouse IgG1isotype) is derived from the PIASX-116 hybridoma produced by the fusion of mouse myeloma cells (NS1 cells) and splenocytes from BALB/c mice. Protein inhibitor of activated STAT 2 (PIAS2/PIAS-x), a small ubiquitin-like modifier (SUMO) E3 ligase contains a zinc binding motif and a highly acidic region. This gene is located on human chromosome 18q21.1.

Especificidad

Monoclonal Anti-PIAS-x recognizes human PIAS-x.

Inmunógeno

peptide corresponding to amino acids 26-40 of human PIAS-x.

Aplicación

Monoclonal Anti-PIAS-x antibody produced in mouse may be used in:
  • enzyme-linked immunosorbent assay (ELISA)
  • immunocytochemistry
  • immunoblotting

Acciones bioquímicas o fisiológicas

Protein inhibitor of activated STAT2 (PIAS2) plays a key role in SUMO modification (SUMOylation) of several host and viral proteins. PIAS-x acts as a transcriptional co-repressor of STAT4. It may participate in controlling the chromatin structure. Upregulation or suppression of this gene can control the stability of the hepatitis C virus (HCV) core, NS3 and NS5A proteins. Hence PIAS-x is considered as the restriction factor for HCV replication.

Forma física

Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.

Almacenamiento y estabilidad

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in “frost-free” freezers is also not recom-mended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Cláusula de descargo de responsabilidad

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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Protein inhibitor of activated STAT2 restricts HCV replication by modulating viral proteins degradation
Guo J, et al.
Viruses, 9(10), 285-285 (2017)
Ulf R Klein et al.
Molecular biology of the cell, 20(1), 410-418 (2008-10-24)
The ubiquitin-like SUMO system controls cellular key functions, and several lines of evidence point to a critical role of SUMO for mitotic progression. However, in mammalian cells mitotic substrates of sumoylation and the regulatory components involved are not well defined.
Search for inherited susceptibility to radiation-associated meningioma by genomewide SNP linkage disequilibrium mapping
Hosking FJ, et al.
British Journal of Cancer, 104(6), 1049-1054 (2011)
W Rozek et al.
Polish journal of veterinary sciences, 16(4), 663-669 (2013-01-01)
Changes in the level of cellular proteins in cells inoculated with equine influenza virus H7N7 and H3N8 were studied with microarray technique. H3N8 induced pro-apoptotic proteins while H7N7 induced both pro- as well as anti-apoptotic factors. The higher level of

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