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Merck
CN

05-1085

Anti-IRS1 Antibody, clone 4.2.2

clone 4.2.2, from mouse

别名:

insulin receptor substrate 1

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
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产品名称

Anti-IRS1 Antibody, clone 4.2.2, clone 4.2.2, from mouse

biological source

mouse

conjugate

unconjugated

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

Quality Level

Gene Information

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

Analysis Note

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.

Application

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

Biochem/physiol Actions

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

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.
~185 kDa

Immunogen

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

Other Notes

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

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.

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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


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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
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
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
Benoit Denhez et al.
Scientific reports, 10(1), 21628-21628 (2020-12-12)
Diabetic nephropathy (DN), a microvascular complication of diabetes, is the leading cause of end-stage renal disease worldwide. Multiple studies have shown that podocyte dysfunction is a central event in the progression of the disease. Beside chronic hyperglycemia, dyslipidemia can induce

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