|Amount :||20 µg|
|Purification :||Greater than 95.0% as determined by SDS-PAGE.|
|Content :||ANXA1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.|
|Storage condition :||Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.|
|AA sequence :||MGSSHHHHHH SSGLVPRGSH MGSMAMVSEF LKQARFLENQ EQEYVQAVKS YKGGPGSAVS PYPSFNVSSD VAALHKAIMV KGVDEATIID ILTKRTNAQR QQIKAAYLQE NGKPLDEVLR KALTGHLEEV VLAMLKTPAQ FDADELRGAM KGLGTDEDTL IEILTTRSNE QIREINRVYR EELKRDLAKD ITSDTSGDFR KALLALAKGD RCQDLSVNQD LADTDARALY EAGERRKGTD VNVFTTILTS RSFPHLRRVF QNYGKYSQHD MNKALDLELK GDIEKCLTTI VKCATSTPAF FAEKLYEAMK GAGTRHKALI RIMVSRSEID MNEIKVFYQK KYGISLCQAI LDETKGDYEK ILVALCGGN.|
|Alternative Name :||Annexin A1, Annexin I, Annexin-1, Calpactin II, Calpactin-2, Chromobindin-9, Lipocortin I, Phospholipase A2 inhibitory protein, p35.|
Sterile filtered colorless solution.
ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.
ANXA1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 369 amino acids (1-346 a.a) and having a molecular mass of 41.1kDa. ANXA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.