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Human Serpin A1 Protein  pdf  pdf  pdf


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Synonym

SerpinA1,PI,A1A,AAT,PI1,A1AT,MGC9222,PRO2275,MGC23330,alpha1AT,SPAAT

Source

Human Serpin A1 Protein (Human Serpin A1, His Tag) Glu 25 - Lys 418 (Accession # AAH11991) was produced in human 293 cells (HEK293) at ACROBiosystems.

Molecular Characterization

Human Serpin A1, His Tag is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 45.1 kDa. The predicted N-terminus is Glu 25. The reducing (R) protein migrates as 55-60 kDa in SDS-PAGE due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method.

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.

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Reconstitution

See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage

Avoid repeated freeze-thaw cycles.

No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C).

 

SDS-PAGE


Human Serpin A1 Protein
Human Serpin A1, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
 
 

Background

Serpin A1 is 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).

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References

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