Athens Research & Technology;16-16-011609;Alpha 1 Antitrypsin, Human Plasma

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Synonym: α1-Proteinase inhibitor, A1PI, AAT

MW: 52,000
Extinction Coefficient: 0.433

Lyophilized from 30 mM Na phosphate, pH 6.5, with 300 mM NaCl

Storage: -20°C

Purified Native Human Alpha 1 Antitrypsin, Human Plasma
Bulk Qty Available.

An acute-phase plasma protein found at 95-350 mg per 100 ml that functions as a protease inhibitor. Clinically, its deficiency is associated with two major diseases: pulmonary emphysema and early onset/juvenile hepatic cirrhosis. It is elevated in inflammatory conditions, malignancies, liver disease and pregnancy and also after surgical trauma and use of oral contraceptives. The simultaneous quantitative determination of alpha-1-PI and ceruloplasmin permits differential diagnosis of liver afflictions.

Activity: When tested with active-site titrated porcine pancreatic trypsin using Na-Benzoyl-L-Arginine-para-Nitroanilide Hydrochloride (L-BAPNA) as substrate, it is 75-100% inhibitory.

Purity: >=95% by SDS-PAGE

Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.

Athens Research & Technology products are laboratory reagents and are not to be administered to humans or used for any drug purpose. 
For research use or for use in further manufacturing.

Product Citation: 
Sinden, Nicola J., and Robert A. Stockley. "Proteinase 3 activity in sputum from subjects with alpha-1-antitrypsin deficiency and COPD." European Respiratory Journal 41, no. 5 (2013): 1042-1050.

Borel F, Tang Q, Gernoux G, Greer C, Wang Z, et al.
Survival advantage of both human hepatocyte xenografts and genome edited hepatocytes for treatment of α-1 antitrypsin deficiency.
Molecular Therapy (2017), doi: 10.1016/j.ymthe.2017.09.020

Tang Q, Gruntman AM, Flotte TR. 
Quantification of Total Human Alpha-1 Antitrypsin by Sandwich ELISA. 
Methods Mol Biol. 2017;1639:211-216. doi: 10.1007/978-1-4939-7163-3_20.

Garratt LW, Sutanto EN, Ling KM, Looi K, et al. 
Alpha-1 Antitrypsin Mitigates the Inhibition of Airway Epithelial Cell Repair by Neutrophil Elastase.
Am J Respir Cell Mol Biol. 2016 Mar;54(3):341-9. doi: 10.1165/rcmb.2015-0074OC.

Jansen BC, Falck D, de Haan N, Hipgrave Ederveen AL, Razdorov G, Lauc G, Wuhrer M.
LaCyTools: A Targeted Liquid Chromatography-Mass Spectrometry Data Processing Package for Relative Quantitation of Glycopeptides.
J Proteome Res. 2016 Jul 1;15(7):2198-210. doi: 10.1021/acs.jproteome.6b00171. Epub 2016 Jun 17.

Sinden NJ, et al.
α-1-Antitrypsin variants and the proteinase/antiproteinase imbalance in chronic obstructive pulmonary disease.
Am J Physiol Lung Cell Mol Physiol. 2015 Jan 15;308(2):L179-90.

Ramadass M, Ghebrehiwet B, Kew RR.
Enhanced recognition of plasma proteins in a non-native state by complement C3b. A possible clearance mechanism for damaged proteins in blood.
Mol Immunol. 2015 Mar;64(1):55-62. doi: 10.1016/j.molimm.2014.10.022. Epub 2014 Nov 15.

O'Dwyer CA, et al.
The BLT1 Inhibitory Function of α-1 Antitrypsin Augmentation Therapy Disrupts Leukotriene B4 Neutrophil Signaling.
J Immunol. 2015 Oct 15;195(8):3628-41. doi: 10.4049/jimmunol.1500038. Epub 2015 Sep 14.

Ungurs MJ, Sinden NJ, Stockley RA.
Progranulin is a substrate for neutrophil-elastase and proteinase-3 in the airway and its concentration correlates with mediators of airway inflammation in COPD
Am J Physiol Lung Cell Mol Physiol. 2014 Jan 1;306(1):L80-7. doi: 10.1152/ajplung.00221.2013. Epub 2013 Nov 1.

Sinden NJ, Koura F, Stockley RA.
The significance of the F variant of alpha-1-antitrypsin and unique case report of a PiFF homozygote.
BMC Pulm Med. 2014 Aug 7;14:132. doi: 10.1186/1471-2466-14-132.

Ramadass M, Ghebrehiwet B, Smith RJ, and Kew RR.
Generation of Multiple Fluid-Phase C3b:Plasma Protein Complexes during Complement Activation: Possible Implications in C3 Glomerulopathies.
J Immunol. 2014 Feb 1;192(3):1220-30. doi: 10.4049/jimmunol.1302288. Epub 2013 Dec 23.