Insulin Receptor Protein (INSR) (AA 28-748) (His tag)

Catalog No. ABIN3133026

Product Details

Target: Insulin Receptor (INSR)

Protein Type: Recombinant

Protein Characteristics: AA 28-748

Origin: Mouse

Source: Insect Cells

Purification tag / Conjugate: This Insulin Receptor protein is labelled with His tag.

Application: Western Blotting (WB), SDS-PAGE (SDS), ELISA, Crystallization (Crys)

Sequence: HLYPGEVCPG MDIRNNLTRL HELENCSVIE GHLQILLMFK TRPEDFRDLS FPKLIMITDY LLLFRVYGLE SLKDLFPNLT VIRGSRLFFN YALVIFEMVH LKELGLYNLM NITRGSVRIE KNNELCYLAT IDWSRILDSV EDNYIVLNKD DNEECGDVCP GTAKGKTNCP ATVINGQFVE RCWTHSHCQK VCPTICKSHG CTAEGLCCHK ECLGNCSEPD DPTKCVACRN FYLDGQCVET CPPPYYHFQD WRCVNFSFCQ DLHFKCRNSR KPGCHQYVIH NNKCIPECPS GYTMNSSNLM CTPCLGPCPK VCQILEGEKT IDSVTSAQEL RGCTVINGSL IINIRGGNNL AAELEANLGL IEEISGFLKI RRSYALVSLS FFRKLHLIRG ETLEIGNYSF YALDNQNLRQ LWDWSKHNLT ITQGKLFFHY NPKLCLSEIH KMEEVSGTKG RQERNDIALK TNGDQASCEN ELLKFSFIRT SFDKILLRWE PYWPPDFRDL LGFMLFYKEA PYQNVTEFDG QDACGSNSWT VVDIDPPQRS NDPKSQTPSH PGWLMRGLKP WTQYAIFVKT LVTFSDERRT YGAKSDIIYV QTDATNPSVP LDPISVSNSS SQIILKWKPP SDPNGNITHY LVYWERQAED SELFELDYCL KGLKLPSRTW SPPFESDDSQ KHNQSEYDDS ASECCSCPKT DSQILKELEE SSFRKTFEDY LHNVVFVPRP S
Sequence without tag. Tag location is at the discretion of the manufacturer. If you have a special request, please contact us.

Characteristics:

• Made in Germany - from design to production - by highly experienced protein experts.
• Mouse Insr Protein (raised in Insect Cells) purified by multi-step, protein-specific process to ensure crystallization grade.
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a made to order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

In the unlikely event that the protein cannot be expressed or purified we do not charge anything (other companies might charge you for any performed steps in the expression process for custom-made proteins, e.g. fees might apply for the expression plasmid, the first expression experiments or purification optimization).

When you order this made-to-order protein you will only pay upon receival of the correctly folded protein. With no financial risk on your end you can rest assured that our experienced protein experts will do everything to make sure that you receive the protein you ordered.

The concentration of our recombinant proteins is measured using the absorbance at 280nm. The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.

The concentration of the protein is calculated using its specific absorption coefficient. We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

Purification: Two step purification of proteins expressed in baculovirus infected SF9 insect cells:

1. In a first purification step, the protein is purified from the cleared cell lysate using three different His-tag capture materials: high yield, EDTA resistant, or DTT resistant. Eluate fractions are analyzed by SDS-PAGE.
2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.

Purity: >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Sterility: 0.22 μm filtered

Endotoxin Level: Protein is endotoxin free.

Grade: Crystallography grade

Application Details

Application Notes: In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a gurantee though.

Comment:

Protein has not been tested for activity yet. In cases in which it is highly likely that the recombinant protein with the default tag will be insoluble our protein lab may suggest a higher molecular weight tag (e.g. GST-tag) instead to increase solubility. We will discuss all possible options with you in detail to assure that you receive your protein of interest.

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: 100 mM NaCL, 20 mM Hepes, 10% glycerol. pH value is at the discretion of the manufacturer.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: Unlimited (if stored properly)

Target Details

Target: Insulin Receptor (INSR)

Alternative Name: Insr (INSR Products)

Synonyms: CD220 Protein, HHF5 Protein, 4932439J01Rik Protein, D630014A15Rik Protein, IR Protein, IR-A Protein, IR-B Protein, 18402 Protein, CG18402 Protein, DIHR Protein, DILR Protein, DIR Protein, DIRH Protein, DIRbeta Protein, DInR Protein, DInr Protein, Dir-a Protein, Dir-b Protein, Dmel\\CG18402 Protein, INR Protein, INS Protein, Inr Protein, Inr-alpha Protein, Inr-beta Protein, InsR Protein, dINR Protein, dIR Protein, dIRH Protein, dInR Protein, dInr Protein, dInsR Protein, dinr Protein, dir Protein, er10 Protein, inr Protein, insulin/insulin-like growth factor receptor Protein, l(3)05545 Protein, l(3)93Dj Protein, l(3)er10 Protein, lnR Protein, ir-A Protein, CTK-1 Protein, ir Protein, INSR Protein, NV14476 Protein, cd220 Protein, hhf5 Protein, insulin receptor Protein, Insulin-like receptor Protein, insulin receptor L homeolog Protein, INSR Protein, Insr Protein, InR Protein, LOC100122567 Protein, LOC100451802 Protein, insr.L Protein

Background: 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). When present in a hybrid receptor with IGF1R, binds IGF1 (By similarity). {ECO:0000250}.

Molecular Weight: 83.6 kDa Including tag.

UniProt: P15208

Pathways: NF-kappaB Signaling, RTK Signaling, AMPK Signaling, Carbohydrate Homeostasis, Regulation of Cell Size, Regulation of Carbohydrate Metabolic Process, Growth Factor Binding, Negative Regulation of Transporter Activity