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Key Documents

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

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 165 kDa

Espèces réactives

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

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Description générale

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.

Immunogène

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

The insulin receptor substrate (IRS) proteins: at the intersection of metabolism and cancer
Shaw LM
Cell Cycle, 10(11), 1750-1756 (2011)
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)
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
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
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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