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RAB0444

Sigma-Aldrich

Cell-Based ELISA for detecting phospho-STAT3 (pTyr705) in cultured cell lines

96 assays

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About This Item

UNSPSC Code:
41116158
NACRES:
NA.32

usage

96 assays

species reactivity

rat, human, mouse

technique(s)

ELISA: suitable
capture ELISA: suitable

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... STAT3(6774)
mouse ... STAT3(20848)
rat ... STAT3(25125)

General description

The Cell-Based Stat3 (pTyr705) ELISA kit is a very rapid, convenient and sensitive assay kit that can monitor the activation or function of important biological pathways in cells. It can be used for measuring the relative amount of Stat3 (pTyr705) phosphorylation and screening the effects of various treatments, inhibitors (such as siRNA or chemicals), or activators in cultured human, mouse and rat cell lines.
The STAT3 (signal transducer and activator of transcription)gene is mapped to human chromosome 17q21.2. Upon phosphorylation, STAT3 translocates to nucleus from cytoplasm, where it mediates a number of biological processes. The protein structure includes the following domains : N-domain, coiled-coil domain, DNA-binding domain, linker domain, SH2 domain and transcriptional activation domain.

Immunogen

Stat3 (pTyr705) synthetic phosphopeptide

Application

For research use only. Not for use in diagnostic procedures.
Please refer to the attached General ELISA KIT Procedure (sandwich, competitive & Indirect ELISA)

Biochem/physiol Actions

Signal transducer and activator of transcription (STAT) proteins are a family of latent cytoplasmic transcription factors involved in cytokine, hormone, and growth factor signal transduction. STAT proteins mediate broadly diverse biological processes, including cell growth, differentiation, apoptosis, fetal development, transformation, inflammation, and immune response. Unlike all other members of the STAT gene family, ablation of STAT3 leads to embryonic lethality and it has been suggested that this protein might represent a primordial STAT protein. It evokes a number of distinct responses in different cells, including induction of an acute-phase response in hepatoma cells, stimulation of proliferation in B lymphocytes, activation of terminal differentiation and growth arrest in monocytes, and maintenance of the pluripotency of embryonic stem cells. Dysregulation of STAT3 signaling has been demonstrated to contribute to malignant cellular transformation. Src kinase-mediated activation of STAT3 has been shown to be essential in prostate and ovarian carcinomas. In head and neck cancers, constitutive STAT3 activity with up-regulated epidermal growth factor receptor (EGFR) signaling plays an important role in malignant proliferation. STAT3 may be a key player in the pathogenesis of diverse human cancers which makes this molecule a prime target for novel therapies.

Kit Components Also Available Separately

Product No.
Description
SDS

  • RABBLOCK5x Blocking Solution (Item F)SDS

  • RABFIX1Fixing Solution (Item D)SDS

  • RABHRP1HRP-conjugated Anti-Rabbit IgG Concentrate (Item I1)SDS

  • RABHRP2HRP-conjugated Anti-Mouse IgG Concentrate (Item I2)SDS

  • RABPLATE1Uncoated MicroplateSDS

  • RABQUENCHQuenching Solution for Cell-based ELISA Assay (Item E)SDS

  • RABSTOP1Stop SolutionSDS

  • RABTMB1TMB Substrate Reagent (Item J)SDS

  • RABWASH120X Wash Buffer Concentrate ASDS

  • RABWASH220X Wash Buffer Concentrate BSDS

See All (10)

Storage Class Code

10 - Combustible liquids


Certificates of Analysis (COA)

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The role of IL-6 and STAT3 in inflammation and cancer.
Hodge D R, et al.
European Journal of Cancer, 41(16), 2502-2512 (2005)
Targeted disruption of the mouse Stat3 gene leads to early embryonic lethality.
Takeda K, et al.
Proceedings of the National Academy of Sciences of the USA, 94(8), 3801-3804 (1997)
STATs and gene regulation.
Darnell J E
Science, 277(5332), 1630-1635 (1997)
STAT3 single-nucleotide polymorphisms and STAT3 mutations associated with hyper-IgE syndrome are not responsible for increased serum IgE serum levels in asthma families.
Wjst M, et al.
European Journal of Human Genetics, 17(3), 352-352 (2009)
Crystal structure of unphosphorylated STAT3 core fragment.
Ren Z, et al.
Biochemical and Biophysical Research Communications, 374(1), 1-5 (2008)

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