Search results for alpha 1

Anti-Centaurin alpha 1 antibody, Abcam, AB27476

Interferon Alpha-1 (IFNA1) Antibody (Biotin), Abbexa, abx271379

Interferon Alpha-1 (IFNA1) Antibody (Biotin) is a Rabbit Polyclonal antibody conjugated to Biotin against Interferon Alpha-1 (IFNA1).

Biotin Anti-alpha 1 Antitrypsin antibody, Abcam, AB48325

Interferon Alpha-1 (IFNA1) Antibody Pair, Abbexa, abx370641

Interferon Alpha-1 (IFNA1) Antibody Pair for use in Sandwich ELISA assay development. This antibody pair contains: Component 5 × 96 tests 10 × 96 tests Capture Antibody200 µg 400 µg Biotin-Conjugated Detection Antibody 50 µg 100 µg Standard 2 µg 10 µg Please note that quantities and concentrations may change between different batches. It is recommended to use this antibody pair with abx098958 Antibody Pair Support Kit (Sandwich Method).

AMPK alpha 1 (phospho Ser496) antibody, Genetex, GTX50224

alpha 1 Catenin (phospho Ser641) antibody, Genetex, GTX50338

Sodium/Potassium ATPase alpha 1 antibody, Genetex, GTX52350

Alpha-1-antitrypsin, Human, ELISA kit, Hycult Biotech, HK387

The human alpha-1 antitripsin ELISA detects both the healthy monomeric form (M variant) and the disease associated polymeric forms (Z variants) of human alpha-1-antitrypsin with equal affinity. Alpha-1-antitrypsin is a member of the serine protease inhibitor (serpin) superfamily which are proteins known for their ability to inhibit proteases. It is the most abundant circulating protease inhibitor known. It mainly targets enzymes released by neutrophils, especially neutrophil elastase (NE) but also proteinase 3 (PR3) and Cathepsin G (CG). Serpinopathies are conformational diseases characterized by the polymerization and intracellular retention of members of the serpin superfamily. The best known is Alpha-1-antitrypsin deficiency, with the most common severe deficiency allele being the Z mutation (Glu342Lys). This severe autosomal dominant disorder causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes. Due to this accumulation of polymers in hepatocytes, blood alpha-1 trypsin levels will decrease leading to chronic uninhibited tissue breakdown. This causes the degradation especially of lung tissue which will eventually lead to pulmonary emphysema. In addition, accumulation of polymers in hepatocytes causes liver diseases such as neonatal hepatitis, cirrhosis, and hepatocellular carcinoma.

Alpha-1-antitrypsin, Human, mAb 2C1, Hycult Biotech, HM2289

The mouse monoclonal antibody clone 2C1 recognizes polymeric forms of human alpha-1-antitrypsin. Alpha-1-antitrypsin is the most abundant circulating protease inhibitor. Serpinopathies are conformational diseases characterized by the polymerization and intracellular retention of members of the serine protease inhibitor or serpin superfamily of proteins.1 The best known is a1-antitrypsin deficiency, with the most common severe deficiency allele being the Z mutation (Glu342Lys). The severe Z deficiency allele (Glu342Lys) causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes. This causes neonatal hepatitis, cirrhosis, and hepatocellular carcinoma. Clone 2C1 recognizes polymers formed by Z α1-antitrypsin in vivo. It also recognizes polymers formed by the Siiyama (Ser53Phe) and Brescia (Gly225Arg) mutants, and the novel His334Asp shutter domain mutant of a1-antitrypsin that is associated with prolonged neonatal jaundice in a 6-week-old boy. These data show that Z and shutter domain mutants form polymers with a shared epitope.

Alpha-1-antitrypsin, Human, mAb 3C11, Hycult Biotech, HM2358

Antibody clone 3C11 recognizes both the healthy monomeric form (M variant) and the disease associated polymeric forms (Z variants) of human alpha-1-antitrypsin with equal affinity. Alpha-1-antitrypsin is a member of the serine protease inhibitor (serpin) superfamily which are proteins known for their ability to inhibit proteases. It is the most abundant circulating protease inhibitor known. It mainly targets enzymes released by neutrophils, especially neutrophil elastase (NE) but also proteinase 3 (PR3) and Cathepsin G (CG). Serpinopathies are conformational diseases characterized by the polymerization and intracellular retention of members of the serpin superfamily. The best known is alpha-1 antitrypsin deficiency, with the most common severe deficiency allele being the Z mutation (Glu342Lys). This severe autosomal dominant disorder causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes. Due to this accumulation of polymers in hepatocytes, blood alpha-1 trypsin levels will decrease leading to chronic uninhibited tissue breakdown. This causes the degradation especially of lung tissue which will eventually lead to pulmonary emphysema. In addition, accumulation of polymers in hepatocytes causes liver diseases such as neonatal hepatitis, cirrhosis, and hepatocellular carcinoma.