The Antibody was raised in rabbits by immunization with the recombinant human REG3A. The amino acid sequence of the recombinant human REG3A is 100% homologus to the amino acid sequence of the human REG3A sequence. The immunization antigen is the 18.4 kDa protein containing 149 amino acid residues- His Tag.
Sterile filtered and lyophilized from 1 mg/ml in 0.05M Phosphate buffer, 0.1M NaCl, pH-7.2.
Add 0.1 ml of deionized water and let the lyophilized pellet dissolve completely. Slight turbidity may occur after reconstitution, which does not affect activity of the antibody. In this case clarify the solution by centrifugation.
Store lyophilized antibody at –20°C. Aliquot the product after reconstitution to avoid repeated freezing/ thawing cycles and store frozen at –80°C. Reconstituted antibody can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Pancreatic regulatory molecules
Pancreatitis-associated protein (PAP) is a secretory protein not normally expressed in healthy pancreas but highly induced during acute pancreatitis. While PAP has been shown to be anti-bacterial and anti-apoptotic in vitro, its definitive biological function in vivo is not clear. Using antisepse oligonucleotides, inhibition of PAP expression significantly worsened pancreatitis in a rat model. During pancreatitis, PAP released by the pancreas could mediate lung inflammation through induction of hepatic TNFalpha expression and subsequent increase in circulating TNFalpha. PAP is activated in primary liver cancers. In normal liver, the protein is undetectable in normal mature hepatocytes and found only in some ductular cells, representing potential hepatic progenitor cells. PAP can be considered hepatic cytokine that combines mitogenic and anti-apoptotic functions regarding hepatocytes, and consequently acts as a growth factor in vivo to enhance liver regeneration. In pancreatic cancor, PAP was overexpressed in 79% (30 of 38) of pancreatic ductal adenocarcinoma, 19% (7 of 36) of chronic pancreatitis, and 29% (2 of 7) of mucinous cystadenoma. PAP was found in malignant ductular structures in pancreatic carcinomas as well as in benign proliferating ductules and acinar cells in chronic pancreatitis. Elevation of PAP in patients with pancreatic cancer is not merely explainable by concomitant pancreatitis, but seems to be due to increased PAP production by the cancer cells and is also correlated to tumour load as expressed by the UICC stages. Epithelial expression of PAP was induced under intestinal mucosal inflammation initiated by exposure to commensal bacteria or DSS as well as inflamed IBD colon. Increased serum level of PAP diagnosed ileal location in active Crohn disease with a sensitivity of 60%, a specificity of 94%, a positive predictive value of 84% and a negative predictive value of 81%. Elevated serum PAP (> 50 ng/mL ) is significantly associated with disease activity and ileal location of Crohn disease.