Recombinant Human Annexin A1 Protein, CF Summary
Met1-Asn346, with a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 400 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: Annexin A1
The Annexins comprise a family of proteins that are involved in many aspects of cellular membrane dynamics and the regulation of membrane‑associated proteins. They are characterized by multiple repeats of 60‑70 amino acids (aa) which assemble into a curved disc‑like domain that binds to membrane phospholipids in a calcium‑dependent manner (1). Human Annexin A1 (ANXA1), also known as Lipocortin 1, Calpactin II, Lipomodulin, and Chromobindin 9, contains four annexin repeats and shares approximately 88% aa sequence identity with mouse and rat Annexin A1 (2). Annexin A1 is found in the cytoplasm, on the cell surface, and in the extracellular fluid (3). The full length 37 kDa protein is susceptible to intracellular and extracellular proteolytic cleavages which generate various N‑terminal peptides and a truncated C‑terminal portion (3‑6). In addition to its membrane activities, Annexin A1 is a major effector of glucocorticoid‑induced immune suppression and growth arrest (7, 8). It associates with S100A11, and this complex inhibits Phospholipase A2 and the production of inflammatory eicosanoids (2, 4). Annexin A1 is released by apoptotic cells and also during neutrophil adhesion to vascular endothelial cells (3, 9). It binds the FPRL1/ALX receptor on neutrophils, while the cleaved N‑terminal aa 2‑26 peptide additionally binds FPR (10, 11). These interactions inhibit leukocyte activation and extravasation to sites of inflammation (3, 9, 10, 12). In contrast, the 33 kDa molecule (generated by the removal of aa 2‑26) promotes activation of vascular endothelial cells and neutrophil transendothelial migration (6). Annexin A1 phosphorylation at multiple locations is important for the regulation of its cleavage, membrane interactions, and ability to suppress ACTH production in the pituitary (4, 13, 14). Annexin A1 additionally regulates adaptive immune responses by enhancing T cell activation and promoting a Th1 bias (15). It can exert both positive and negative effects on epithelial‑mesenchymal transition and tumor metastasis (16‑18).
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- Hayhoe, R.P. et al. (2006) Blood 107:2123.
- Gastardelo, T.S. et al. (2009) Am. J. Pathol. 174:177.
- Dorovkov, M.V. et al. (2011) Biochemistry 50:2187.
- McArthur, S. et al. (2009) FASEB J. 23:4000.
- D’Acquisto, F. et al. (2007) Blood 109:1095.
- Yi, M. and J.E. Schnitzer (2009) Proc. Natl. Acad. Sci. 106:17886.
- Maschler, S. et al. (2010) EMBO Mol. Med. 2:401.
- de Graauw, M. et al. (2010) Proc. Natl. Acad. Sci. 107:6340.
Citations for Recombinant Human Annexin A1 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 4
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Inhibitory role of Annexin A1 in pathological bone resorption and therapeutic implications in periprosthetic osteolysis
Authors: H Alhasan, MA Terkawi, G Matsumae, T Ebata, Y Tian, T Shimizu, Y Nishida, S Yokota, F Garcia-Mar, M M Abd Elwa, D Takahashi, MA Younis, H Harashima, K Kadoya, N Iwasaki
Sample Types: Whole Cells
Proteomic analysis of the host-pathogen interface in experimental cholera
Authors: A Zoued, H Zhang, T Zhang, RT Giorgio, CJ Kuehl, B Fakoya, B Sit, MK Waldor
Nature Chemical Biology, 2021;17(11):1199-1208.
Annexin A1-dependent tethering promotes extracellular vesicle aggregation revealed with single-extracellular vesicle analysis
Authors: MA Rogers, F Buffolo, F Schlotter, SK Atkins, LH Lee, A Halu, MC Blaser, E Tsolaki, H Higashi, K Luther, G Daaboul, CVC Bouten, SC Body, SA Singh, S Bertazzo, P Libby, M Aikawa, E Aikawa
Science Advances, 2020;6(38):.
Sample Types: Whole Cells
Human Melanoma-Derived Extracellular Vesicles Regulate Dendritic Cell Maturation
Authors: RLG Maus, JW Jakub, WK Nevala, TA Christense, K Noble-Orcu, Z Sachs, TJ Hieken, SN Markovic
Front Immunol, 2017;8(0):358.
Sample Types: Whole Cells
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