Anti-phospho-IGF-1R (Tyr1161/Tyr1165/Tyr1166) Antibody

There are two kinds of IGF receptors based on their relative affinities for IGF-1 versus IGF-2. The IGF-1 receptor (IGF-1R) prefers IGF-1 over IGF-2 and weakly binds insulin. IGF-1 receptor is a disulfide-linked heterotetrameric transmembrane protein consisting of two alpha (130 kDa) and two beta (95 kDa) subunits. Both the alpha and beta subunits are encoded within a single receptor precursor cDNA. The IGF-1 receptor is therefore similar in structure to the insulin receptor. The proreceptor polypeptide is proteolytically cleaved and disulfide-linked to yield the mature heterotetrameric receptor. The IGF-1 receptor is highly expressed in all cell types and tissues and is highly overexpressed in most malignant tissues where it functions as an anti-apoptotic agent by mediating signaling pathways that enhance cell survival.

This antibody recognizes IGF-1R phosphorylated at Tyr1161/Tyr1165/Tyr1166. Please note that some sources list the phsophorylation sites as Tyr1131/Tyr1135/Tyr1136. The difference in the amino acid sequence is due to a 30 amino acid signal chain that is removed due to protein processing.

Epitope: Phosphorylated Tyr1161/Tyr1165/Tyr1166.

KLH-conjugated linear peptide corresponding to human IGF-1R phosphorylated at Tyr1161/Tyr1165/Tyr1166.

Anti-phospho-IGF-1R (Tyr1161/Tyr1165/Tyr1166) Antibody is an antibody against phospho-IGF-1R (Tyr1161/Tyr1165/Tyr1166) for use in WB, Cell Function Assay.

Research Category
Epigenetics & Nuclear Function

Signaling

Research Sub Category
Insulin/Energy Signaling

Insulin/Energy Signaling

Western Blot Peptide Inhibition Analysis: A representative lot detected IGF-1R in IGF1 treated HEK293 cell lysate.

Evaluated by Western Blot in IGF1treated HEK293 cell lysate.

Western Blot Analysis: A 1:200 dilution of this antibody detected IGF-1R in IGF1 treated HEK293 cell lysate.

~95 kDa observed. IGF-1R can be cleaved into an Insulin-like growth factor 1 receptor alpha (aa 31-736) and beta (aa 741-1367) chain. Both chains are known to contain multiple potential glycosylation sites. Distinct beta-subunits are present in hybrid insulin-like-growth-factor-1 receptors in the central nervous system. (Moss, A.M., et al. (1993). Biochem J. 294( Pt 3):685-692.)

Affinity purified

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

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

Control
IGF1 untreated and treated HEK293 cell lysate

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