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Sigma-Aldrich

Anti-IRS1 Antibody, clone 4.2.2

clone 4.2.2, from mouse

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Synonym(s):
insulin receptor substrate 1
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

4.2.2, monoclonal

species reactivity

pig, canine, human, mouse, rat, monkey, bovine

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

bovine ... Irs1(538598)
dog ... Irs1(486148)
human ... IRS1(3667)
mouse ... Irs1(16367)
pig ... Irs1(100512686)
rat ... Irs1(25467)
rhesus monkey ... Irs1(707870)

General description

IRS1 (Insulin Receptor Substrate 1) transmits insulin signals via metabolic and mitogenic pathways. IRS1 is heavily phosphorylated on both serine and tyrosine residues. These phosphorylated tyrosines enable IRS to act as a docking protein that binds SH2 domains of such proteins as PI3 Kinase (phosphatidylinositol 3-kinase) and GRB2, resulting in activation. Over expression and phosphorylation of serine is associated with insulin resistance and breast cancer. Some of the more notable phosphorylation sites are Ser302 that is phosphorylated following insulin stimulation. Ser307, phosphorylated by JNK and IKK, is a key regulatory site that appears to disrupt the IRS1/IR interaction and inhibits insulin-mediated activation of the PI3 kinase and MAPK pathways, and Ser636/639 that is known to be phosphorylated by p70S6K downstream of mTOR and acts as a negative feedback loop.

Specificity

Predicted to cross-react with many other species based on 100% sequence homology with immunogen.
This antibody recognizes IRS1.

Immunogen

Synthetic peptide corresponding to amino acids 431-446 of mouse IRS1.

Application

This Anti-IRS1 Antibody, clone 4.2.2 is validated for use in WB, IP, IC for the detection of IRS1.

Quality

Evaluated by western blot on IR/IRS1 transfected CHO +/- Insulin lysate.

Western Blot Analysis:
1:1,000 dilution of this antibody was used to detect IRS1 in IRS/IR transfected CHO -/+ Calyculin A/ Okadaic Acid-treated cell lysate.

Target description

~185 kDa

Physical form

Format: Purified
Purified mouse monoclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4),150 mM NaCl with 0.05% sodium azide.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Xihong Zhang et al.
Endocrinology, 164(3) (2023-01-08)
Targeting the type I insulin-like growth factor receptor (IGF-IR) has not been successful in breast cancer. Data suggest the highly homologous insulin receptor (IR) may be an alternate growth stimulatory pathway used by cancer cells. Since both receptors phosphorylate the
Rapamycin has a biphasic effect on insulin sensitivity in C2C12 myotubes due to sequential disruption of mTORC1 and mTORC2.
Ye, L; Varamini, B; Lamming, DW; Sabatini, DM; Baur, JA
Frontiers in Genetics null
Yunxue Guo et al.
International journal of biological sciences, 8(10), 1408-1417 (2012-12-01)
Generally, most miRNAs that were up-regulated during differentiation promoted adipogenesis, but our research indicated that up-regulation of miR-145 in porcine preadipocytes did not promote but inhibit adipogenesis. In this study, miR-145 was significantly up-regulated during porcine dedifferentiated fat (DFAT) cells
Kyle D Copps et al.
The Journal of biological chemistry, 291(16), 8602-8617 (2016-02-06)
Constitutive activation of the mammalian target of rapamycin complex 1 and S6 kinase (mTORC1→ S6K) attenuates insulin-stimulated Akt activity in certain tumors in part through "feedback" phosphorylation of the upstream insulin receptor substrate 1 (IRS1). However, the significance of this
Gang Xi et al.
The Journal of biological chemistry, 292(5), 2009-2020 (2016-12-23)
Diabetes is a major risk factor for the development of atherosclerosis, but the mechanism by which hyperglycemia accelerates lesion development is not well defined. Insulin and insulin-like growth factor I (IGF-I) signal through the scaffold protein insulin receptor substrate 1

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