protein

Human CellExp SERPINA1 / A1AT, human recombinant

MBS844123

0.01 mg

280 USD

Recombinant Protein

Human CellExp SERPINA1 / A1AT, human recombinant

[SERPINA1/A1AT]

[SerpinA1; PI; A1A; AAT; PI1; A1AT; MGC9222; PRO2275; MGC23330; alpha1AT; SPAAT]

[alpha-1-antitrypsin; Alpha-1-antitrypsin; alpha-1-antitrypsin; serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1; Alpha-1 protease inhibitor; Alpha-1-antiproteinase; Serpin A1]

[SERPINA1]

[SERPINA1; SERPINA1; PI; A1A; AAT; PI1; A1AT; PRO2275; alpha1AT; AAT; PI; SPAAT]

A1AT_HUMAN

HEK 293 cells(Glu 25 -Lys 418)

418

>=95% by SDS-PAGE gel

Lyophilized. Lyophilized from 0.22 um filtered solution in PBS. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.

Store at -20°C. After reconstitution, aliquot and store at -20°C and use within 3 months. Avoid repeated freezing and thawing cycles

SDS-PAGE; HPLC

Testing Data

Molecular Weight Note: The protein is fused with 6×His tag at the C-terminus, has a calculated MW of 45.1 kDa. The predicted N-terminus is Glu 25. DTT-reduced Protein migrates as 55-60 kDa due to glycosylation.

Reconstitution: Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 ug/ml.Do not vortex. This solution can be stored at 2-8°C for up to 1 month.For extended storage, it is recommended to store at -20°C. Endotoxin Level: <1 EU/ug by LAL method. Biological Activity: Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 in 100 ul reaction mixture containing 1.25 ng trypsin , 10 uM substrate, 50 mM Tris, 10 mM CaCl2, 0.15 M NaCl , pH 7.5.The IC50 value is approximately <4.5 nM.

Cytokines, Growth Factors & Hormones; Human cell expressed recombinant proteins Proteins and Enzymes; Human cell expressed recombinant proteins Cytokines, Growth Factors & Hormones; Cytokines & Growth Factors (A-Z)Proteins and Enzymes; Cytokines, Growth F

Background: Serpin A1 also known as Alpha-1-antitrypsin (A1AT), serum trypsin inhibitor, alpha-1 proteinase inhibitor (A1PI), AAT, which belongs to the serpin family. Most serpins inactivate enzymes by binding to them covalently, requiring very high levels to perform their function. Like all serine protease inhibitors, A1AT has a characteristic secondary structure of beta sheets and alpha helices. Serpin A1 / A1AT is 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 of SerpinA1 inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. Serpin A1 / A1AT protects tissues from enzymes of inflammatory cells, especially neutrophil elastase. Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD).

50363217

NP_000286.3

NM_000295.4

P01009

Complement And Coagulation Cascades Pathway (198880); Complement And Coagulation Cascades Pathway (83073); Complement And Coagulation Cascades Pathway (484); FOXA1 Transcription Factor Network Pathway (137979); Hemostasis Pathway (1269340); Platelet Activation, Signaling And Aggregation Pathway (1269350); Platelet Degranulation Pathway (1269367); Response To Elevated Platelet Cytosolic Ca2+ Pathway (1269365)

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]

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; Secreted, signal peptide. Chromosomal Location of Human Ortholog: 14q32.1. Cellular Component: Golgi apparatus; proteinaceous extracellular matrix; extracellular space; 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; acute-phase response; response to methanol; response to hypoxia; response to lipopolysaccharide; blood coagulation; response to estradiol stimulus. Disease: Alpha-1-antitrypsin Deficiency; Pulmonary Disease, Chronic Obstructive

0.01 mg

280 USD