Napsin A Aspartic Peptidase (NAPSA) (C-Term) Peptide

Details for Product No. ABIN699718, Supplier: Log in to see
Protein Name
  • KAP
  • Kdap
  • NAP1
  • NAPA
  • pronapsin
  • AV014846
  • Nap1
  • napsin A aspartic peptidase
  • NCK-associated protein 1
  • RIKEN cDNA 5830415F09 gene
  • Napsa
  • Nckap1
  • 5830415F09Rik
Protein Region
Peptide Type
Blocking Peptide (BP)
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Specificity The synthetic peptide sequence used to generate the antibody AP13772b was selected from the C-term region of NAPSA. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Background The activation peptides of aspartic proteinases plays role as inhibitors of the active site. These peptide segments, or pro-parts, are deemed important for correct folding, targeting, and control of the activation of aspartic proteinase zymogens. The pronapsin A gene is expressed predominantly in lung and kidney. Its translation product is predicted to be a fully functional, glycosylated aspartic proteinase precursor containing an RGD motif and an additional 18 residues at its C-terminus. [provided by RefSeq].
Restrictions For Research Use only
Storage 4
Storage Comment Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles
Expiry Date 6 months
Background publications Bishop, Sharma, Illei: "Napsin A and thyroid transcription factor-1 expression in carcinomas of the lung, breast, pancreas, colon, kidney, thyroid, and malignant mesothelioma." in: Human pathology, Vol. 41, Issue 1, pp. 20-5, 2009 (PubMed).

Innocenti, Zucconi, Disanza, Frittoli, Areces, Steffen, Stradal, Di Fiore, Carlier, Scita: "Abi1 is essential for the formation and activation of a WAVE2 signalling complex." in: Nature cell biology, Vol. 6, Issue 4, pp. 319-27, 2004 (PubMed).

Brasch, Ochs, Kahne, Guttentag, Schauer-Vukasinovic, Derrick, Johnen, Kapp, Muller, Richter, Giller, Hawgood, Buhling: "Involvement of napsin A in the C- and N-terminal processing of surfactant protein B in type-II pneumocytes of the human lung." in: The Journal of biological chemistry, Vol. 278, Issue 49, pp. 49006-14, 2003 (PubMed).