AAT Antibody - #BF0101
| 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 |
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
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.
Cite Format: Affinity Biosciences Cat# BF0101, RRID:AB_2833711.
Fold/Unfold
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;
Immunogens
Purified recombinant fragment of human AAT expressed in E. Coli.
- P01009 A1AT_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
PTMs - P01009 As Substrate
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| T35 | Phosphorylation | Uniprot | |
| T37 | Phosphorylation | Uniprot | |
| S38 | Phosphorylation | Uniprot | |
| N70 | N-Glycosylation | Uniprot | |
| N107 | N-Glycosylation | Uniprot | |
| K159 | Acetylation | Uniprot | |
| K160 | Acetylation | Uniprot | |
| Y184 | Phosphorylation | Uniprot | |
| K198 | Acetylation | Uniprot | |
| C256 | S-Nitrosylation | Uniprot | |
| K257 | Acetylation | Uniprot | |
| S261 | Phosphorylation | Uniprot | |
| N271 | N-Glycosylation | Uniprot | |
| S307 | Phosphorylation | Uniprot | |
| S309 | Phosphorylation | Uniprot | |
| K314 | Acetylation | Uniprot | |
| S316 | Phosphorylation | Uniprot | |
| T318 | Phosphorylation | Uniprot | |
| Y321 | Phosphorylation | Uniprot | |
| S325 | Phosphorylation | Uniprot | |
| T333 | Phosphorylation | Uniprot | |
| S343 | Phosphorylation | Uniprot | |
| S383 | Phosphorylation | Uniprot | |
| T416 | Phosphorylation | Uniprot |
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.
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.
Ubiquitous. Expressed in leukocytes and plasma.
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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