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Merck

A4086

Sigma-Aldrich

Anti-ATF-2 (SS-16) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41
Konjugat:
unconjugated
application:
ARR
IP
WB CL
Klon:
polyclonal
Speziesreaktivität:
human
citations:
5
Methode(n):
immunoprecipitation (IP): 5 μg using lysates of human K562 cells
microarray: suitable
western blot (chemiluminescent): 1:250 using whole cell extract of human K562 or Jurkat cells

Biologische Quelle

rabbit

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen 65 kDa

Speziesreaktivität

human

Methode(n)

immunoprecipitation (IP): 5 μg using lysates of human K562 cells
microarray: suitable
western blot (chemiluminescent): 1:250 using whole cell extract of human K562 or Jurkat cells

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... ATF2(1386)

Allgemeine Beschreibung

ATF2 (Activating Transcription Factor 2, CRE-BP,HB-16, CREB2, TREB-7) belongs to the ATF/CREB family of basic region leucine zipper DNAbinding proteins. ATF2 regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Rabbit anti-ATF-2 (SS-16) antibody recognizes human ATF2 by immunoblotting (65kDa) and immunoprecipitation. Staining of ATF2 by immunoblotting is inhibited by the immunizing peptide.

Immunogen

synthetic peptide corresponding to amino acids 490-505 of human ATF-2.

Anwendung

Rabbit anti-ATF-2 can be used for immunoprecipitation (5μg, using lysates of human K562 cells), microarray, and chemiluminescent western blot (1:250, using whole cell extract of human K562 or Jurkat cells).

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide.

Haftungsausschluss

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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F Liu et al.
Nature, 368(6471), 520-525 (1994-04-07)
A puzzling property of the transcriptional activators encoded by several animal viruses is their ability to function promiscuously. The adenovirus E1a protein, for example, stimulates transcription of adenoviral genes as well as a wide variety of other viral and cellular
F Liu et al.
Cell, 61(7), 1217-1224 (1990-06-29)
The adenovirus E1a protein stimulates transcription of viral early genes. Recent experiments indicate that E1a contains a transcriptional activating region, which functions when directed to a promoter. Because E1a is not a sequence-specific DNA binding protein, how it targets to
X Y Li et al.
Genes & development, 10(5), 517-527 (1996-03-01)
ATF-2 is a cellular basic region-leucine zipper (bZIP) transcription factor that can mediate diverse transcriptional responses, including activation by the adenovirus Ela protein. ATF-2 contains an activation domain, required for transcriptional activity, but in the absence of an appropriate inducer
H A Abdel-Hafiz et al.
Molecular endocrinology (Baltimore, Md.), 6(12), 2079-2089 (1992-12-01)
Recent studies have detailed the ability of activating transcription factor-2 (ATF-2) to mediate adenoviral E1a stimulation of gene expression; however, an endogenous regulator for the transcriptional activity of this protein has not been described. To characterize the regulation of ATF-2
Hitomi Hasegawa et al.
PloS one, 9(12), e116048-e116048 (2014-12-30)
Activating transcription factor 2 (ATF2) and its homolog ATF7 are phosphorylated at Thr-69/Thr-71 and at Thr-51/Thr-53, respectively, by stress-activated MAPKs regulating their transcriptional functions in G1 and S phases. However, little is known about the role of ATF2 and ATF7

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