>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
39.4 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
38 kDa, reducing conditions
Publications
Read Publications using 3770-AN in the following applications:
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 PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 400 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Annexin A1 Protein, CF
Annexin A1
annexin I (lipocortin I)
Annexin I
Annexin-1
ANX1
ANXA1
Calpactin II
calpactin-2
chromobindin-9
Lipocortin I
LPC1
LPC1annexin-1
p35
Phospholipase A2 inhibitory protein
Background
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.
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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.
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