Membrane protein fraction of isolated rat glomeruli
Characteristics
Chromosomal location: 1q55 Monoclonal antibodies were produced with the help of BALB/c mice using a membrane protein fraction of isolated rat glomeruli as the immunizing antigen.
Purification
The mouse IgG1 antibody (#JG12C9C10) from hybridomas was purified from cell culture supernatant by Protein G chromatography.
Immunogen
Membrane protein fraction of isolated rat glomeruli
Clone
JG12C9C10
Isotype
IgG1
Application Notes
Optimal working dilution should be determined by the investigator.
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
Centrifuge vial prior to opening. Reconstitute in sterile water to a concentration of 0.1-1.0 mg/mL.
Buffer
PBS
Handling Advice
Centrifuge vial prior to opening.
Storage
4 °C,-20 °C
Storage Comment
The lyophilized antibody is stable for at least 2 years at -20°C. After sterile reconstitution the antibody is stable at 2-8°C for up to 6 months. Frozen aliquots are stable for at least 6 months when stored at -20°C. Addition of a carrier protein or 50% glycerol is recommended for frozen aliquots.
Expiry Date
24 months
Vlahu, Aten, de Graaff, van Veen, Everts, de Waart, Struijk, Krediet: "NEW INSIGHTS INTO THE EFFECTS OF CHRONIC KIDNEY FAILURE AND DIALYSATE EXPOSURE ON THE PERITONEUM." in: Peritoneal dialysis international : journal of the International Society for Peritoneal Dialysis, (2016) (PubMed).
Target
APP
(Aminopeptidase P (APP))
Alternative Name
Aminopeptidase P
Synonyms
AP-P antibody, CG6291 antibody, DAP-P antibody, Daminopep-p antibody, Dmel\\CG6291 antibody, aminopeptidase P antibody, Aminopeptidase P antibody, Fbal_0627 antibody, ApepP antibody
Background
X-prolyl aminopeptidase (aminopeptidase P) 1, soluble,Aminopeptidase P (AP-P, X-Pro aminopeptidase) has the unique ability to leave the N-terminal amino acid residue from peptides having proline as the penultimate amino acid residue. Biologically active peptides comprise an important and diverse class of extracellular chemical messengers that mediate a wide range of intercellular interactions. Several bioactive peptides including hormones, neuropeptides, neurotransmitters escape non-specific protease degradation by having an Xaa-Pro motif at their amino termini. Due to its cyclic nature, proline confers resistance to such peptide bonds so that aminopeptidases with broad specificity cannot act upon such peptides. There are a limited number of peptidases that act on peptide bonds involving a proline residue, such as dipeptidyl peptidase II (DPPII) and dipeptidyl peptidase W (DPPIV), and prolidase (which cleaves the Xaa-Pro bond only in dipeptides), or endopeptidases such as prolyl endopeptidase (which cleaves on the carbonyl side of proline residues within a protein or peptide). However,of these enzymes have been reported to hydrolyze Xaa-Pro bonds located at the N-terminus of peptides and proteins. Therefore, role of AP-P is crucial in this respect. AP-P activity is ubiquitous and has been found in a wide range of organisms including bacteria, yeast and vertebrates. Mammalian AP-Ps exist in membrane-bound and cytosolic forms, which represent two distinct gene products. The cytosolic (soluble) form of aminopeptidase P is found in human leukocytes and rat brain.