Product Name: Alpha 1 Antitrypsin Antibody [AAT/1379]
Species Reactivity: Human
Tested Applications: Flow, IF, IHC-P, WB
Applications: Western blot: 0.5-1 ug/mlIHC (Paraffin): 0.5-1 ug/mlIF: 0.5-1 ug/ml Flow Cytometry: 0.5-1ug/10e6 cells in 0.1mlTitration of the Alpha 1 Antitrypsin antibody may be required due to differences in protocols and secondary/substrate sensitivity.
User Note: Optimal dilutions for each application to be determined by the researcher
Predicted Molecular Weight:
Immunogen: A human partial recombinant protein was used as the immunogen for this Alpha 1 Antitrypsin antibody.
Host Species: Mouse
Purification: Protein G affinity
Physical State: Liquid
CAS NO.: 114311-32-9
Product: Imazamox
Buffer: PBS with 0.1 mg/ml BSA and 0.05% sodium azide
Concentration: 0.2 mg/mL
Storage Conditions: Aliquot and Store at -20C. Avoid freez-thaw cycles.
Clonality: Monoclonal
Conjugate: Unconjugated
Alternate Names: Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Serpin A1, Short peptide from AAT, SPAAT, SERPINA1, AAT, PI
Accession NO.:
Protein Ino:
Official Symbol: SERPINA1
Geneid: 5265
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]
PubMed ID:http://aac.asm.org/content/52/9/3202.abstract
