Alpha 1 Antitrypsin Antibody [AAT/1379] | 33-599

Alpha 1 Antitrypsin Antibody [AAT/1379] | 33-599 | Gentaur UK, US & Europe Distribution

Host: Mouse

Reactivity: Human

Homology: N/A

Immunogen: A human partial recombinant protein was used as the immunogen for this Alpha 1 Antitrypsin antibody.

Research Area: Cancer, Cell Cycle, Obesity

Tested Application: WB, IHC-P, Flow, IF

Application: Western blot: 0.5-1 ug/ml
IHC (Paraffin) : 0.5-1 ug/ml
IF: 0.5-1 ug/ml
Flow Cytometry: 0.5-1ug/10e6 cells in 0.1ml
Titration of the Alpha 1 Antitrypsin antibody may be required due to differences in protocols and secondary/substrate sensitivity.

Specificiy: N/A

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: N/A

Validation: N/A

Isoform: N/A

Purification: Protein G affinity

Clonality: Monoclonal

Clone: AAT/1379

Isotype: IgG1

Conjugate: Unconjugated

Physical State: Liquid

Buffer: PBS with 0.1 mg/ml BSA and 0.05% sodium azide

Concentration: 0.2 mg/mL

Storage Condition: Aliquot and Store at 2-8˚C. Avoid freez-thaw cycles.

Alternate Name: Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Serpin A1, Short peptide from AAT, SPAAT, SERPINA1, AAT, PI

User Note: Optimal dilutions for each application to be determined by the researcher

BACKGROUND: Alpha-1 Antitrypsin or alpha1-antitrypsin (A1AT) is a protease inhibitor belonging to the serpin superfamily. It is generally known as serum trypsin inhibitor. Alpha 1-antitrypsin is also referred to as alpha-1 proteinase inhibitor (A1PI) because it inhibits a wide variety of proteases. It protects tissues from enzymes of inflammatory cells, especially neutrophil elastase, and has a reference range in blood of 1.5 - 3.5 gram/liter (in US the reference range is generally expressed as mg/dL or micromoles) , but the concentration can rise manyfold upon acute inflammation. In its absence (such as in alpha 1-antitrypsin deficiency) , neutrophil elastase is free to break down elastin, which contributes to the elasticity of the lungs, resulting in respiratory complications such as emphysema, or COPD (chronic obstructive pulmonary disease) in adults and cirrhosis in adults or children.

Like all serine protease inhibitors, A1AT has a characteristic secondary structure of beta sheets and alpha helices. Mutations in these areas can lead to non-functional proteins that can polymerise and accumulate in the liver (infantile hepatic cirrhosis) . [Wiki]