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Merck
CN

07-848-I

Anti-phospho-IRS1 Antibody (Tyr941)

from rabbit, purified by affinity chromatography

别名:

Insulin receptor substrate 1, Tyr941 phosphorylated, IRS-1, Tyr941 phosphorylated

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eCl@ss:
32160702
UNSPSC Code:
12352203
Clone:
polyclonal
Species reactivity:
human
Application:
WB
Citations:
2
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biological source

rabbit

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

ambient

target post-translational modification

phosphorylation (pTyr941)

Quality Level

Gene Information

human ... IRS1(3667)

General description

Insulin receptor substrate 1 (UniProt P35568; also known as IRS-1) is encoded by the IRS1 gene (Gene ID 3667) in human. The insulin receptor substrates (IRS-1, IRS-2, IRS-3, and IRS-4) are adaptor proteins involved in modulating cell growth, metabolism, survival, and differentiation by transducing receptor signaling to multiple downstream effectors. IRS family proteins contain a conserved N-terminal pleckstrin homology (PH) domain (a.a. 12-115 of human IRS-1), a phosphotyrosine-binding (PTB) domain (a.a. 160-264 of human IRS-1), and multiple tyrosine phosphorylation sites in the C-terminal region, including Tyr612, Tyr896, Tyr941, Tyr1158, and Tyr1220. The PTB domain meidates the interaction of IRS-1, -2 and -3 with IR juxtamembrane NPXYp motif, facilitating subsequent receptor-mediated IRS tyrosine phosphorylation. Upon phosphorylation, IRS proteins serve as binding sites for Src homology 2 (SH2) domain-containing proteins, such as SHP-2 and PI 3-kinase. Functions of IRS proteins are largely dependent on the phosphorylations of specific tyrosine residues, which in turn are subject to negative regulation by phosphatase activity. In addition, IRS proteins can be phosphorylated by serine/threonine kinases, such as PI-3 kinase, Akt/PKB, GSK-3, mTOR, and PKC, and increased Ser/Thr phosphorylation reduces their binding to IR and tyrosine phosphorylation. Inhibition of PI 3-kinase enhances insulin-stimulated IRS-1 Tyr612/Tyr941 phosphorylation (p85-binding sites) and increases IRS-1 association with PI 3-kinase p85 subunit.
~165 kDa observed. 131.6 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Immunogen

KLH-conjugated phosphopeptide corresponding to human IRS1 target region sequence containing phosphorylated Tyr941.

Application

Detect IRS1 Tyr941 phosphorylation using this rabbit polyclonal Anti-phospho-IRS1 (Tyr941) antibody, Cat. No. 07-848-I, validated for use in Western Blotting.
Research Category
Signaling

Biochem/physiol Actions

This polyclonal antibody detected a ~165 kDa target band in lysates from serum-starved HEK293 cells only after, but not before, insulin stimulation. Target region sequence is not 100% conserved among human, mouse, and rat species.

Physical form

Affinity purified.
Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Evaluated by Western Blotting in HEK293 cell lysate.

Western Blotting Analysis: A 1:200 dilution of this antibody detected IRS1 Tyr941 phosphorylation induction in 10 µg of lysate from serum-starved HEK293 cells following insulin treatment.

Other Notes

Concentration: Please refer to lot specific datasheet.
Replaces: 07-848

Disclaimer

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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存储类别

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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Giorgia Maroni et al.
Scientific reports, 7(1), 15573-15573 (2017-11-16)
Transcriptional regulators are crucial in adipocyte differentiation. We now show that the homeodomain-containing transcription factor Prep1 is a repressor of adipogenic differentiation since its down-regulation (DR) in both ex vivo bone marrow-derived mesenchymal stromal cells (MSC) and in vitro 3T3-L1
Max Brown et al.
Molecular biology of the cell, 31(23), 2597-2629 (2020-09-03)
Accumulation of unfolded proteins in the endoplasmic reticulum (ER) causes ER stress and activates a signaling network known as the unfolded protein response (UPR). Here we characterize how ER stress and the UPR inhibit insulin signaling. We find that ER

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