||FOR RESEARCH USE ONLY (RUO).
||Recombinant-Human alpha 1 antitrypsin-protein was developed from hek293. For use in research applications.
||Lyophilised from 0.2 Mu m filtered PBS solution, pH7.2, 5% Trehalose. Upon receipt A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers
||Spin the vial and reconstite in distilled water to a concentration not less than 0.1 mg/mL. This can then be diluted into other buffers.
||Recombinant Serpin A1 can be stored in working aliquots at 2°C-8°C for one month, or at-20°C to-70°C for 1 year. Avoid repeated freeze/thaw cycles.
||Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg (1EU/µg).
||The activity was tested by the ability to inhibit trypsin cleavage of a fluorogenic peptide substrate Mca-RPKPVE-Nval-WRKDnp-NH2, with a calculated ED50 < 4.5nM
| Tissue Specificity || Ubiquitous. Expressed in leukocytes and plasma. |
| Post Translational Modifications || N-glycosylated. Differential glycosylation produces a number of isoforms. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary. The glycan at Asn-70 is di-antennary with trace amounts of tri-antennary. Glycan at Asn-271 is exclusively di-antennary. Structure of glycans at Asn-70 and Asn-271 is Hex5HexNAc4. The structure of the antennae is Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure Man(alpha1-6)Man(alpha1-3)Man(beta1-4)GlcNAc(beta1-4)GlcNAc. Some antennae are fucosylated, which forms a Lewis-X determinant. Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418. (Microbial infection) Proteolytically processed by Staphylococcus aureus seryl, cysteinyl, and metallo-proteases. |
| Function || 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. Short peptide from AAT: Reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE). |
| Protein Name || Alpha-1-AntitrypsinAlpha-1 Protease InhibitorAlpha-1-AntiproteinaseSerpin A1 Cleaved Into - Short Peptide From AatSpaat |
| Database Links || Reactome: R-HSA-114608Reactome: R-HSA-204005Reactome: R-HSA-381426Reactome: R-HSA-5694530Reactome: R-HSA-6798695Reactome: R-HSA-8957275 |
| Cellular Localisation || SecretedEndoplasmic ReticulumThe S And Z Allele Are Not Secreted Effectively And Accumulate Intracellularly In The Endoplasmic ReticulumShort Peptide From Aat: SecretedExtracellular SpaceExtracellular Matrix |
| Alternative Protein Names || Alpha-1-Antitrypsin proteinAlpha-1 Protease Inhibitor proteinAlpha-1-Antiproteinase proteinSerpin A1 Cleaved Into - Short Peptide From Aat proteinSpaat proteinSERPINA1 proteinAAT proteinPI proteinPRO0684 proteinPRO2209 protein |
Information sourced from Uniprot.org
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