产品: | AAT 抗体 |
货号: | BF0101 |
描述: | Mouse monoclonal antibody to AAT |
应用: | WB ELISA |
反应: | Human, Mouse |
分子量: | 47kDa; 47kD(Calculated). |
蛋白号: | P01009 |
RRID: | AB_2833711 |
产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
引用格式: Affinity Biosciences Cat# BF0101, RRID:AB_2833711.
展开/折叠
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;
抗原和靶标
Purified recombinant fragment of human AAT expressed in E. Coli.
- P01009 A1AT_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
翻译修饰 - P01009 作为底物
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 |
研究背景
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.
研究领域
· Organismal Systems > Immune system > Complement and coagulation cascades. (View pathway)
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