Recombinant Human Angiopoietin-like 2 Protein, CF

When Recombinant Angiopoietin‑like Protein 2/ANGPTL2 (Catalog # 9746-AN) is coated at 2 μg/mL, Recombinant Human LILRB2/CD85d/ILT4 Fc Chimera (Catalog # 2078‑T4) binds with an ED50 of 0.02‑0.12 μg/mL.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Angiopoietin-like 2 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Angiopoietin‑like Protein 2/ANGPTL2 is coated at 2 μg/mL, Recombinant Human LILRB2/CD85d/ILT4 Fc Chimera (Catalog # 2078‑T4) binds with an ED₅₀ of 0.02‑0.12 μg/mL Measured by its ability to promote the expansion of E16 rat liver mononuclear cells in vitro, in the presence of Recombinant Mouse SCF/c‑kit Ligand (Catalog # 455-MC), Recombinant Mouse Thrombopoietin/Tpo (Catalog # 488-TO), and Recombinant Mouse Flt‑3 Ligand (Catalog # 427-FL). The ED₅₀ for this effect is 0.3-1.8 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived human Angiopoietin-like Protein 2/ANGPTL2 protein
  Gln23-His493, with a C-terminal 9-His tag
• Accession #: Q9UKU9.1
• N-terminal Sequence: No results obtained. Gln23 inferred from enzymatic pyroglutamate treatment revealing Glu24
• Structure / Form: Disulfide-linked homooligomer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >75%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
  • Bioactivity2
• Theoretical MW: 56 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 60-69 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and CHAPS with Trehalose.
• Purity: >75%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 200 μg/mL in water.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Angiopoietin-like 2 Protein, CF

• angiopoietin-like 2
• Angiopoietin-like Protein 2
• angiopoietin-related protein 2
• ANGPTL2
• ANGRP2
• ARP2HARP
• MGC8889

Background

Angiopoietin-like Protein 2 (ANGPTL2), also known as ARP2, is a secreted 56 kDa glycoprotein that contains a coiled coil domain and a fibrinogen like domain (1). ANGPTL2 is one of the eight members of the Angiopoietin like family proteins, which are structurally similar to angiopoietins (2). Mature human ANGPTL2 shares 89% sequence identity with both mouse and rat homologs. ANGPTL2 is widely expressed in many tissues, and its expression is induced by chronic, but not acute hypoxia (3). Elevated level of ANGPTL2 in the serum is also correlated with inflammation and obesity (3). ANGPTL2 has both pro and anti-angiogenic functions (1, 4). It serves as tumor suppressor in ovarian cancer (5), and also promote metastasis in various cancer types, making it potential biomarker for tumor progression (6, 7). ANGPTL2 functions as growth factor to enhance the survival of hematopoietic progenitors, mediated by its coiled-coil domain (8). Receptor of ANGPTL2 is recently identified to be LILRB2, and both the coiled-coil domain and fibrinogen like domain are required for optimal binding (9).

1. Kim, I. et al. (1999), J Biol Chem 274:26523.
2. Santulli, G. et al. (2014) Front Endocrinol 5:4.
3. Tabata, M. et al. (2009) Cell Metab 10:178.
4. Kubota, Y. et al. (2005) Proc. Natl. Acad. Sci. U.S.A. 102:13502.
5. Kikuchi, R. et al. (2008) Cancer Res 68:5067.
6. Odagiri, H. et al. (2014) Sci Signal 7:ra7.
7. Endo, M. et al. (2012) Cancer Res 72:1784.
8. Broxmeyer, H.E. et al. (2012) Blood Cells Mol Dis 48:25.
9. Deng, M. et al. (2014) Blood 124:924.

Bioinformatics

• Uniprot:
  • Q9UKU9.1()