α1 Antitrypsin Antibody [L14P15]

Application: Reactivity: Human

Usage Information

Dilution
WB1:5000 IP1:20 IHC1:400 IF1:50

Application
WB, IP, IHC, IF

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
46 kDa 51 kDa,55 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Positive Control	Human fetal liver tissue; Human liver tissue; Human heart tissue; Human kidney tissue; Human hepatocellular carcinoma tissue; Human spleen tissue; K562 cells; HepG2 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
α1 Antitrypsin Antibody [L14P15] detects endogenous levels of total α1 Antitrypsin protein.

Clone
L14P15

Synonym(s)
AAT; PI; PRO0684; PRO2209; SERPINA1; Alpha-1-antitrypsin; Alpha-1 protease inhibitor; Alpha-1-antiproteinase; Serpin A1

Background
Alpha-1 Antitrypsin (A1AT) belongs to the serpin superfamily of protease inhibitors predominantly synthesized in hepatocytes and secreted into plasma at 1-2 g/L concentrations. Mature A1AT spans 394 amino acids forming a glycoprotein with three β-sheets (A-C), nine α-helices, and a mobile reactive center loop (RCL, residues 357-394) where Met358-Met359 serves as the neutrophil elastase (NE) P1-P1' cleavage site exposed at the protein apex. N-linked glycans at Asn107, Asn206, and Asn271 stabilize the metastable native fold, with sheet A expansion capacity enabling inhibitory mechanism. NE attacks the RCL scissile bond, forming an acyl-enzyme intermediate that translocates the protease 70 Å into sheet A, distorting its catalytic triad via full loop insertion and steric occlusion. This suicide inhibition neutralizes excess NE from activated neutrophils during inflammation, preserving elastin, collagen, and proteoglycans in lungs, vasculature, and connective tissues against proteolytic destruction. A1AT also inhibits proteinase 3, cathepsin G, and kallikrein, balancing coagulation via thrombomodulin interactions while suppressing ADAM-17 to sustain anti-inflammatory cytokine shedding. Augmentation therapy replenishes plasma levels >11 μM to restore protease-antiprotease equilibrium in deficient patients. SERPINA1 mutations like Z (Glu366Lys, Glu342Lys) or S (Glu264Val) destabilize sheet A via aberrant RCL insertion, causing hepatocyte retention, polymerization, and toxic gain-of-function cirrhosis alongside unopposed NE-driven emphysema. Pi*ZZ homozygotes retain 85-90% intracellularly, dropping plasma to 10-15% normal and accelerating COPD via airspace destruction. Polymers trigger IL-6/STAT3 inflammation independent of protease trapping, while M variants confer cardiovascular protection. A1AT mitigates ischemia-reperfusion injury through caspase inhibition and NF-κB suppression, extending graft viability. Deficiency exacerbates ANCA vasculitis and type 1 diabetes via unchecked proteinase 3 activity.

Background

Alpha-1 Antitrypsin (A1AT) belongs to the serpin superfamily of protease inhibitors predominantly synthesized in hepatocytes and secreted into plasma at 1-2 g/L concentrations. Mature A1AT spans 394 amino acids forming a glycoprotein with three β-sheets (A-C), nine α-helices, and a mobile reactive center loop (RCL, residues 357-394) where Met358-Met359 serves as the neutrophil elastase (NE) P1-P1' cleavage site exposed at the protein apex. N-linked glycans at Asn107, Asn206, and Asn271 stabilize the metastable native fold, with sheet A expansion capacity enabling inhibitory mechanism. NE attacks the RCL scissile bond, forming an acyl-enzyme intermediate that translocates the protease 70 Å into sheet A, distorting its catalytic triad via full loop insertion and steric occlusion. This suicide inhibition neutralizes excess NE from activated neutrophils during inflammation, preserving elastin, collagen, and proteoglycans in lungs, vasculature, and connective tissues against proteolytic destruction. A1AT also inhibits proteinase 3, cathepsin G, and kallikrein, balancing coagulation via thrombomodulin interactions while suppressing ADAM-17 to sustain anti-inflammatory cytokine shedding. Augmentation therapy replenishes plasma levels >11 μM to restore protease-antiprotease equilibrium in deficient patients. SERPINA1 mutations like Z (Glu366Lys, Glu342Lys) or S (Glu264Val) destabilize sheet A via aberrant RCL insertion, causing hepatocyte retention, polymerization, and toxic gain-of-function cirrhosis alongside unopposed NE-driven emphysema. Pi*ZZ homozygotes retain 85-90% intracellularly, dropping plasma to 10-15% normal and accelerating COPD via airspace destruction. Polymers trigger IL-6/STAT3 inflammation independent of protease trapping, while M variants confer cardiovascular protection. A1AT mitigates ischemia-reperfusion injury through caspase inhibition and NF-κB suppression, extending graft viability. Deficiency exacerbates ANCA vasculitis and type 1 diabetes via unchecked proteinase 3 activity.

References
https://pubmed.ncbi.nlm.nih.gov/2669992/ https://pubmed.ncbi.nlm.nih.gov/27564663/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%