Analytical Data
-
Gene name
SERPINA1
- Application
-
Alternative Names
SERPINA1；AAT；PI；Alpha-1-antitrypsin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P01009
-
Expression Region
25-418aa
-
AA Sequence
EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNI FFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELL RTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDT EEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEV KDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATA IFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLK SVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGA MFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
-
Molecular Weight
44 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
SERPINA1, also known as alpha-1 antitrypsin (AAT), is a serine protease inhibitor that plays a crucial role in protecting tissues from enzymatic damage caused by neutrophil elastase, particularly in the lungs. Deficiency of SERPINA1 is associated with various health issues, including chronic obstructive pulmonary disease (COPD) and liver diseases, highlighting its importance in maintaining respiratory and liver function. The recombinant protein form of SERPINA1 has gained attention as a therapeutic option to treat individuals with AAT deficiency, as it can restore deficient protein levels in the bloodstream and, consequently, provide protective effects against tissue degeneration. Research in this area has focused on the effective production, purification, and characterization of recombinant SERPINA1, as well as its potential clinical applications in treating AAT deficiency-related diseases. Recent advancements in genetic engineering and protein expression systems have facilitated the development of more efficient methods for producing high-quality recombinant SERPINA1, making it a promising candidate for therapeutic intervention. However, challenges remain in optimizing its delivery and ensuring that it maintains its functional integrity in vivo. Overall, the study of SERPINA1 recombinant protein continues to be a vibrant area of research with significant implications for improving patient outcomes in diseases associated with AAT deficiency.
