Rabbit polyclonal INSR antibody (A0287)

$69.00$259.00

Reactivity: Human,Mouse,Rat
Applications: WB,IHC
Conjugation: Unconjugated
Supplier: ABclonal Inc.

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Rabbit polyclonal INSR antibody (A0287)

Supplier: ABclonal Inc.

Recommended applications: WB,IHC

Recommended dilution:

WB 1:500 – 1:2000 IHC 1:50 – 1:100

Recommended protocols: check protocols

Image descriptions:

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Alternative names:

Check alternative names for the antibody

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INSR antibody,CD220 antibody,HHF5 antibody
CD220 antibody|HHF5 antibody|human insulin receptor antibody|Insr antibody|INSR_HUMAN antibody|Insulin receptor subunit beta antibody|IR 1 antibody|IR antibody|IR-1 antibody|IR1 antibody|Phospho anti-Insulin Receptor (Y1361) antibody (ab60946)

SCBT cat No: sc-57343|sc-7953|sc-57344|sc-710|sc-31366|sc-81465|sc-09|sc-135949|sc-81466|sc-711|sc-373975|sc-57342|sc-31367|sc-31369|sc-20739|sc-74506|sc-133251|sc-74505|

Name

Rabbit polyclonal INSR antibody

Catalogue No.

A0287

Reactivity

Human, Mouse, Rat

Immunogen

A synthetic peptide of human INSR

Host

Rabbit

Applications

WB, IHC

Recommended dilution

WB 1:500 – 1:2000
IHC 1:50 – 1:100

Clonality

Polyclonal

Conjugation

Unconjugated

Isotype

IgG

Molecular weight

Predicted: 152kDa/Observed: Refer to Figures

Formulation

INSR antibody was tube-contained.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Purification

INSR antibody was purified using affinity purification.

Storage

Store at -20 Celsius degree. Avoid freeze / thaw cycles.

Alternative antibody names

INSR antibody,CD220 antibody,HHF5 antibody

Database links

Human UniProt/Swiss-Prot:P06213

Protein names

INSR,CD220,HHF5

Protein function

Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosines residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K-AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). Isoform Short has a higher affinity for IGFII binding. When present in a hybrid receptor with IGF1R, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin.

Protein tissue specificity

Isoform Long and isoform Short are predominantly expressed in tissue targets of insulin metabolic effects: liver, adipose tissue and skeletal muscle but are also expressed in the peripheral nerve, kidney, pulmonary alveoli, pancreatic acini, placenta vascular endothelium, fibroblasts, monocytes, granulocytes, erythrocytes and skin. Isoform Short is preferentially expressed in fetal cells such as fetal fibroblasts, muscle, liver and kidney. Found as a hybrid receptor with IGF1R in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibroblasts, spleen and placenta (at protein level). Overexpressed in several tumors, including breast, colon, lung, ovary, and thyroid carcinomas.

Protein sequence and domain

The tetrameric insulin receptor binds insulin via non-identical regions from two alpha chains, primarily via the C-terminal region of the first INSR alpha chain. Residues from the leucine-rich N-terminus of the other INSR alpha chain also contribute to this insulin binding site. A secondary insulin-binding site is formed by residues at the junction of fibronectin type-III domain 1 and 2.Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.; Contains 3 fibronectin type-III domains.; Contains 1 protein kinase domain.

Protein post-translational modifications

After being transported from the endoplasmic reticulum to the Golgi apparatus, the single glycosylated precursor is further glycosylated and then cleaved, followed by its transport to the plasma membrane.; Autophosphorylated on tyrosine residues in response to insulin. Phosphorylation of Tyr-999 is required for binding to IRS1, SHC1 and STAT5B. Dephosphorylated by PTPRE at Tyr-999, Tyr-1185, Tyr-1189 and Tyr-1190. Dephosphorylated by PTPRF and PTPN1. Dephosphorylated by PTPN2; down-regulates insulin-induced signaling.

Protein cellular localization

Cell membrane; Single-pass type I membrane protein.

Background

Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation of Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

Research area

All research areas>Membrane Receptors>insulin R
(View all antibody categories related to Membrane Receptors)

Note

AntibodyPlus can customize INSR antibody according to your requirement, including bulk product size,etc. Please contact info@antibodyplus.com. AntibodyPlus provides antibody trial sample for your own antibody validation.

Product type

Primary antibody

Supplier

ABclonal Inc.

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