Anti-Insulin Receptor antibody [Fab 83-7] (ab245688)
Key features and details
- Rabbit monoclonal [Fab 83-7] to Insulin Receptor
- Suitable for: ICC/IF
- Reacts with: Human
- Isotype: IgG
Overview
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Product name
Anti-Insulin Receptor antibody [Fab 83-7]
See all Insulin Receptor primary antibodies -
Description
Rabbit monoclonal [Fab 83-7] to Insulin Receptor -
Host species
Rabbit -
Tested applications
Suitable for: ICC/IFmore details -
Species reactivity
Reacts with: Human -
Immunogen
Full length native protein (purified) corresponding to Insulin Receptor. IM-9 lymphocytes followed by purified insulin receptor
Database link: P06213 -
Epitope
This antibody recognizes an epitope within the cysteine rich region (amino acids 140-301) of the extracellular domain of the human insulin receptor alpha. -
Positive control
- ICC/IF: MCF7 cells.
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General notes
The Life Science industry has been in the grips of a reproducibility crisis for a number of years. Abcam is leading the way in addressing this with our range of recombinant monoclonal antibodies and knockout edited cell lines for gold-standard validation. Please check that this product meets your needs before purchasing.
If you have any questions, special requirements or concerns, please send us an inquiry and/or contact our Support team ahead of purchase. Recommended alternatives for this product can be found below, along with publications, customer reviews and Q&As
Properties
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Form
Liquid -
Storage instructions
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle. -
Storage buffer
Preservative: 0.02% Proclin 300
Constituent: 99% PBS -
Concentration information loading...
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Purity
Protein A purified -
Clonality
Monoclonal -
Clone number
Fab 83-7 -
Isotype
IgG -
Light chain type
kappa -
Research areas
Associated products
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Compatible Secondaries
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Recombinant Protein
Applications
The Abpromise guarantee
Our Abpromise guarantee covers the use of ab245688 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application | Abreviews | Notes |
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ICC/IF |
Use a concentration of 10 µg/ml.
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Notes |
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ICC/IF
Use a concentration of 10 µg/ml. |
Target
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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. -
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. -
Involvement in disease
Rabson-Mendenhall syndrome
Leprechaunism
Diabetes mellitus, non-insulin-dependent
Familial hyperinsulinemic hypoglycemia 5
Insulin-resistant diabetes mellitus with acanthosis nigricans type A -
Sequence similarities
Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.
Contains 3 fibronectin type-III domains.
Contains 1 protein kinase domain. -
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. -
Post-translational
modificationsAfter 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. -
Cellular localization
Cell membrane. - Information by UniProt
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Database links
- Entrez Gene: 3643 Human
- Omim: 147670 Human
- SwissProt: P06213 Human
- Unigene: 465744 Human
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Alternative names
- CD220 antibody
- HHF5 antibody
- human insulin receptor antibody
see all
Images
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Immunocytochemical analysis of paraformaldehyde fixed MCF7 (Human breast adenocarcinoma cell line) cells on a poly-L-lysine coated coverslip, permeabalized with 0.15% Triton using ab245688 at 10 µg/ml for 1 hour at RT, followed by Alexa Fluor® 488 conjugated Goat anti-rabbit secondary antibody at 1 µg/ml (green). The nuclear stain is DAPI (DAPI).
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab245688 has not yet been referenced specifically in any publications.