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I7153

Sigma-Aldrich

Anti-Insulin Receptor Substrate 1 (IRS-1) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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About This Item

MDL number:
MFCD01633547
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 165 kDa

species reactivity

human, mouse, rat

technique(s)

immunoprecipitation (IP): 4 μg using 0.5 mg of a 3T3/A31 RIPA lysate
western blot: 0.5-2 μg/mL using RIPA lysates of 3T3/A31 mouse fibroblasts

UniProt accession no.

P35568

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... IRS1(3667)
mouse ... Irs1(16367)
rat ... Irs1(25467)

General description

Insulin receptor substrate 1 (IRS1) gene is mapped to human chromosome 2q36.3. The gene encodes a 185 kDa protein and is ubiquitously expressed. Irs1 belongs to the group of cytoplasmic adaptor proteins.

Immunogen

C-terminal 14 amino acid residues of rat liver insulin receptor substrate 1.

Application

Anti-Insulin Receptor Substrate 1 (IRS-1) antibody can be used in immunoprecipitation using 0.5 mg of a 3T3/A31 RIPA lysate.

Biochem/physiol Actions

Insulin receptor substrate 1 (IRS-1) is phosphorylated on multiple tyrosine residues. It plays a crucial role in transmitting signals from the insulin and insulin-like growth factor-1 (IGF-1) receptors to intracellular pathways. Over expression of IRS-1can leads to mammary tumorigenesis and metastasis. Anti-Insulin Receptor Substrate 1 (IRS-1) antibody can be used in western blotting using RIPA lysates of 3T3/A31 mouse fibroblasts. Rabbit anti-Insulin Receptor Substrate 1 (IRS-1) antibody reacts specifically with insulin receptor substrate 1 (165 kD). The product has shown species cross reactivity with rat, mouse and human IRS-1.

Physical form

Solution in 0.1 M Tris-glycine, pH 7.4, containing 0.15 M NaCl, and 0.05% sodium azide.

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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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Common variants in and near IRS1 and subclinical cardiovascular disease in the Framingham Heart Study
Lim S, et al.
Atherosclerosis, 229(1), 149-154 (2013)
The insulin receptor substrate (IRS) proteins: at the intersection of metabolism and cancer
Shaw LM
Cell Cycle, 10(11), 1750-1756 (2011)
S R Keller et al.
Molecular reproduction and development, 35(4), 346-351 (1993-08-01)
The insulin and insulin-like growth factor-I (IGF-I) receptors are tyrosine kinases. Consequently, an approach to investigating signaling pathways from these receptors is to characterize proteins rapidly phosphorylated on tyrosine in response to insulin and IGF-I. In many cell types the
Robert K Dearth et al.
Molecular and cellular biology, 26(24), 9302-9314 (2006-10-13)
Insulin receptor substrates (IRSs) are signaling adaptors that play a major role in the metabolic and mitogenic actions of insulin and insulin-like growth factors. Reports have recently noted increased levels, or activity, of IRSs in many human cancers, and some
Judit Mohás-Cseh et al.
Biomedicines, 10(5) (2022-05-29)
A link between oxidative stress and insulin resistance has been suggested. Hydroxyl free radicals are known to be able to convert phenylalanine (Phe) into the non-physiological tyrosine isoforms ortho- and meta-tyrosine (o-Tyr, m-Tyr). The aim of our study was to

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