SerpinA1 active protein

SerpinA1 Protein, Human, Recombinant (His Tag)

Cat. Num. AAA8120178

• Gene Names: SERPINA1; PI; A1A; AAT; PI1; A1AT; PRO2275; alpha1AT
• Purity: >95% as determined by SDS-PAGE
• Synonyms: SerpinA1; SerpinA1 Protein; Human; Recombinant (His Tag); Human SerpinA1/A1AT Protein (His Tag); A1A Protein; A1AT Protein; AAT Protein; alpha1AT Protein; MGC23330 Protein; MGC9222 Protein; PI Protein; PI1 Protein; PRO2275 Protein; serpin peptidase inhibitor; clade A (alpha-1 antiproteinase; antitrypsin); member 1; SerpinA1 active protein

• Host: HEK293 Cells
• Purity/Purification: >95% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Met1-Lys418

• Species: Human
• Endotoxin: <1.0EU per ug of the protein as determined by the LAL method
• Predicted N Terminal: Glu 25
• Tag: C-His
• Protein Construction: A DNA sequence encoding the human SerpinA1 (NP_000286.3) pre-protein (Met 1-Lys 418) was expressed with a C-terminal polyhistidine tag.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Activity: Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2. The IC50 value is <3.0nM, as measured in 100uL reaction mixture containing 1.25 ng trypsin, 10uM substrate, 50 mM Tris, 10 mM CaCl2, 0.15 M NaCl, pH7.5.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

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Related Product Information for SerpinA1 active protein

Background: SerpinA1, also known as Alpha-1 antitrypsin (AAT), is a prototype member of the Serpin superfamily of the serine protease inhibitors. This serine protease inhibitor blocks the protease, neutrophil elastase. Alpha-1 antitrypsin is mainly produced in the liver and acts as an antiprotease. Its principal function is to inactivate neutrophil elastase, preventing tissue damage. SerpinA1 (alpha1-antitrypsin), an acute phase protein and the classical neutrophil elastase inhibitor, is localized within lipid rafts in primary human monocytes in vitro. Its association with monocytes is inhibited by cholesterol depleting/efflux-stimulating agents (nystatin, filipin, MbetaCD (methyl-beta-cyclodextrin) and oxidized low-density lipoprotein (oxLDL) and conversely, enhanced by free cholesterol. Furthermore, SerpinA1/monocyte association per se depletes lipid raft cholesterol as characterized by the activation of extracellular signal-regulated kinase 2, formation of cytosolic lipid droplets, and complete inhibition of oxLDL uptake by monocytes. Previous population studies have suggested that heterozygote status for the AAT gene (SerpinA1) is a risk factor for chronic rhinosinusitis with nasal polyposis (CRSwNP). Alpha-1 antitrypsin deficiency is a recently identified genetic disease that occurs almost as frequently as cystic fibrosis. It is caused by various mutations in the SerpinA1 gene, and has numerous clinical implications. Alpha-1 antitrypsin deficiency is an inherited disease affecting the lung and liver. In the liver, alpha-1 antitrypsin deficiency may manifest as benign neonatal hepatitis syndrome; a small percentage of adults develop liver fibrosis, with progression to cirrhosis and hepatocellular carcinoma. Its most important physiologic functions are the protection of pulmonary tissue from aggressive proteolytic enzymes and regulation of pulmonary immune processes.

References

Khnlein T, et al. (2008) Alpha-1 antitrypsin deficiency: pathogenesis, clinical presentation, diagnosis, and treatment. Am J Med. 121(1): 3-9.Camelier AA, et al. (2008) Alpha-1 antitrypsin deficiency: diagnosis and treatment. J Bras Pneumol. 34(7): 514-27.Subramaniyam D, et al. (2010) Cholesterol rich lipid raft microdomains are gateway for acute phase protein, SERPINA1. Int J Biochem Cell Biol. 42(9): 1562-70.Kilty SJ, et al. (2010) Polymorphisms in the SERPINA1 (Alpha-1-Antitrypsin) gene are associated with severe chronic rhinosinusitis unresponsive to medical therapy. Am J Rhinol Allergy. 24(1): e4-9.

NCBI and Uniprot Product Information

• NCBI GI #: 50363217
• NCBI GeneID: 5265
• NCBI Accession #: NP_000286.3
• NCBI GenBank Nucleotide #: NM_000295.4
• UniProt Accession #: P01009; Q0PVP5; Q13672; Q53XB8; Q5U0M1; Q7M4R2; Q86U18; Q86U19; Q96BF9; Q96ES1; A6PX14; B2RDQ8
• Molecular Weight: 52,000
• NCBI Official Full Name: alpha-1-antitrypsin
• NCBI Official Synonym Full Names: serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1
• NCBI Official Symbol: SERPINA1
• NCBI Official Synonym Symbols: PI; A1A; AAT; PI1; A1AT; PRO2275; alpha1AT
• NCBI Protein Information: alpha-1-antitrypsin; serpin A1; alpha-1-antiproteinase; alpha-1-antitrypsin null; alpha-1 protease inhibitor; protease inhibitor 1 (anti-elastase), alpha-1-antitrypsin; serine (or cysteine) proteinase inhibitor, clade A, member 1
• UniProt Protein Name: Alpha-1-antitrypsin
• Protein Family: Alpha-1-antitrypsin
• UniProt Gene Name: SERPINA1
• UniProt Synonym Gene Names: AAT; PI; SPAAT
• UniProt Entry Name: A1AT_HUMAN

NCBI Description

The protein encoded by this gene is secreted and is a serine protease inhibitor whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Defects in this gene can cause emphysema or liver disease. Several transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

SERPINA1: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD). A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age. Belongs to the serpin family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Inhibitor; Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 14q32.1

Cellular Component: Golgi apparatus; extracellular space; proteinaceous extracellular matrix; endoplasmic reticulum; extracellular region

Molecular Function: serine-type endopeptidase inhibitor activity; identical protein binding; protein binding; protease binding; glycoprotein binding

Biological Process: platelet activation; response to chromate; platelet degranulation; response to triglyceride; response to cytokine stimulus; response to lead ion; response to hypoxia; response to methanol; acute-phase response; response to lipopolysaccharide; blood coagulation; response to estradiol stimulus

Disease: Alpha-1-antitrypsin Deficiency; Pulmonary Disease, Chronic Obstructive