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Recombinant Human IGF1 Receptor Protein

Recombinant Human IGF1 Receptor Protein (RMPP-00230055)

Cat. No.: RMPP-00230055

Category: Recombinant Protein

Research Area: Immunology

INQUIRY 100 μg Customer Size

Product Features

Source HEK 293 cells
Purity > 95% SDS-PAGE. >90% as determined by SEC-HPLC.
Nature Recombinant
Endotoxin Level < 1.000 Eu/µg
Animal Free No
Tags Fc tag C-Terminus
Form Lyophilized
Applications ELISA; HPLC; SDS-PAGE
Key Features Expression system: HEK 293 cells; Purity: > 95% SDS-PAGE; Endotoxin level: < 1.000 Eu/µg; Active: Yes; Tags: Fc tag C-Terminus; Suitable for: ELISA; HPLC, SDS-PAGE

Protein Information

UniProt ID P16070
Molecular Weight 49 kDa including tags
Sequence QIDLNITCRF AGVFHVEKNG RYSISRTEAA
DLCKAFNSTL PTMAQMEKAL SIGFETCRYG FIEGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN ASAPPEEDCT SVTDLPNAFD GPITITIVNR DGTRYVQKGE YRTNPEDIYP SNPTDDDVSS GSSSERSSTS GGYIFYTFST VHPIPDEDSP WITDSTDRIPP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK
Sequence Similarities Contains 1 Link domain.
Protein Length Protein fragment
Cellular Localization Membrane.
Tissue Specificity Isoform 10 (epithelial isoform) is expressed by cells of epithelium and highly expressed by carcinomas. Expression is repressed in neuroblastoma cells.
Domain The lectin-like LINK domain is responsible for hyaluronan binding.
Function Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.
Post-translational Modifications Proteolytically cleaved in the extracellular matrix by specific proteinases (possibly MMPs) in several cell lines and tumors.N-glycosylated.O-glycosylated; contains more-or-less-sulfated chondroitin sulfate glycans, whose number may affect the accessibility of specific proteinases to their cleavage site(s).Phosphorylated; activation of PKC results in the dephosphorylation of Ser-706 (constitutive phosphorylation site), and the phosphorylation of Ser-672.

Storage & Shipping

Shipping and Storage Shipped at 4°C. Store at -80°C. Avoid freeze / thaw cycle.
pH: 7.4Constituents: 0.61% Tris, Glycine, Trehalose, L-Arginine, Sodium chlorideLyophilized from 0.22 µm filtered solution
This product is an active protein and may elicit a biological response in vivo, handle with caution.

For research use only. Not for clinical use.