Product: AAT Antibody
Catalog: BF0101
Description: Mouse monoclonal antibody to AAT
Application: WB ELISA
Reactivity: Human, Mouse
Mol.Wt.: 47kDa; 47kD(Calculated).
Uniprot: P01009
RRID: AB_2833711

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Product Info

ELISA 1:10000, WB 1:500-1:2000
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Monoclonal [AFB1687]
AAT antibody detects endogenous levels of total AAT.
Cite Format: Affinity Biosciences Cat# BF0101, RRID:AB_2833711.
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


A1A; A1AT; A1AT_HUMAN; AAT; Alpha 1 antiproteinase; Alpha 1 antitrypsin; Alpha 1 antitrypsin null; Alpha 1 protease inhibitor; Alpha-1 protease inhibitor; Alpha-1-antiproteinase; alpha1 proteinase inhibitor; Alpha1AT; Dom1; PI; PI1; PRO2275; Serine (or cysteine) proteinase inhibitor clade A member 1; Serine protease inhibitor 1-1; Serine protease inhibitor A1a; Serpin A1; Serpin A1a; Serpin peptidase inhibitor clade A member 1; Serpina1; Short peptide from AAT; SPAAT; Spi1-1;



Purified recombinant fragment of human AAT expressed in E. Coli.

P01009 A1AT_HUMAN:

Ubiquitous. Expressed in leukocytes and plasma.

AAT, also known as SERPINA1; serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1. It is secreted and is a serine protease inhibitor whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Severe Serpin A1 deficiency leads to several clinical complications such as pulmonary emphysema, juvenile hepatisis, cirrhosis and hepatocellular carcinoma.

PTMs - P01009 As Substrate

Site PTM Type Enzyme
T35 Phosphorylation
T37 Phosphorylation
S38 Phosphorylation
N70 N-Glycosylation
N107 N-Glycosylation
K159 Acetylation
K160 Acetylation
Y184 Phosphorylation
K198 Acetylation
C256 S-Nitrosylation
K257 Acetylation
S261 Phosphorylation
N271 N-Glycosylation
S307 Phosphorylation
S309 Phosphorylation
K314 Acetylation
S316 Phosphorylation
T318 Phosphorylation
Y321 Phosphorylation
S325 Phosphorylation
T333 Phosphorylation
S343 Phosphorylation
S383 Phosphorylation
T416 Phosphorylation

Research Backgrounds


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.

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).


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.

Subcellular Location:

Secreted. Endoplasmic reticulum.
Note: The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum.

Secreted>Extracellular space>Extracellular matrix.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Ubiquitous. Expressed in leukocytes and plasma.

Subunit Structure:

The variants S and Z interact with CANX AND PDIA3.


The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.

Belongs to the serpin family.

Research Fields

· Organismal Systems > Immune system > Complement and coagulation cascades.   (View pathway)

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