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Human Serpin A1 Protein, His Tag

Human Serpin A1 Protein, His Tag

Item no.	SE1-H5226-1mg
Manufacturer	ACROBiosystems
Amount	500 ug x 2
Quantity options	500 ug x 2 50 ug
Category	Peptides & Proteins Recombinant Proteins
Type	Proteins Recombinant
Format	Solid
Specific against	Human (Homo sapiens)
Host	HEK293
Conjugate/Tag	Unconjugated
Purity	95%
Citations	(1) Tanaka N., et al., 1991, Jpn. J. Cancer Res. 82:693-700. (2) Niemann M.A., et al., 1992, Matrix 12:233-241. (3) Gettins PG., 2002, Chem Rev 102 (12): 4751-804.
NCBI	AAH11991
ECLASS 10.1	32160409
ECLASS 11.0	32160409
UNSPSC	12352202
Alias	SerpinA1,PI,A1A,AAT,PI1,A1AT,MGC9222,PRO2275,MGC23330,alpha1AT,SPAAT
Shipping Condition	Room temperature
Available
Manufacturer - Category	Protein
Manufacturer - Conjugate / Tag	C-6xHis, Unconjugated
Shipping Temperature	RT
Storage Conditions	-20°C
Molecular Weight	45.4 kDa
Manufacturer - Format	Powder
Description	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).
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).
Molecule	Serpin A1
Exp Region	Glu 25 - Lys 418
Characteristics	This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 45.4 kDa. The protein migrates as 50-60 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.
Endotoxin	1.0 EU per μg
Buffer	PBS, pH7.4
Stability	● -20°C to -70°C for 12 months in lyophilized state ● -70°C for 3 months under sterile conditions after reconstitution._x000D_For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Protectant	trehalose

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

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SE1-H5226-1mg-datasheet.pdf

SE1-H5226-1mg-safety-datasheet.pdf