Recombinant Human PAPPA2/Pappalysin 2 Protein (His Tag) | PKSH031546

Recombinant Human PAPPA2/Pappalysin 2 Protein (His Tag) | PKSH031546 | Gentaur US, UK & Europe Disrtribition

Synonyms: PAPP-A2;PAPP-E;PAPPE;PLAC3

Active Protein: N/A

Activity: A DNA sequence encoding the human PAPPA2 mature form (NP_064714.2) corresponding to amino acid (Ser 234-Cys 1396) was expressed， with a carboxy-terminal polyhistidine tag.

Protein Construction: A DNA sequence encoding the human PAPPA2 mature form (NP_064714.2) corresponding to amino acid (Ser 234-Cys 1396) was expressed， with a carboxy-terminal polyhistidine tag.

Fusion Tag: C-His

Species: Human

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 131 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: Pappalysin-2/PAPP-A2 is the second member of the pappalysin family of metzincin superfamily, of which PAPP-A is the first member. There is no homology between the prepro-peptides of PAPP-A and PAPP-A2, but 46% of the residues of mature PAPP-A are also present in mature PAPP-A2. PAPP-A specifically cleaves insulin-like growth factor-binding protein(IGFBP)-4, one of six known modulators of IGF-I and –II, whereas PAPP-A2 specifically cleaved IGFBP-5 at one site, between Ser-143 and Lys-144. In contrast to the cleavage of IGFBP-4 by PAPP-A that strictly requires the presence of IGF, the cleavage of IGFBP-5 by PAPP-A2 was IGF-independent. Recent data firmly establish PAPP-A and IGFBP-4 as an important functional pair in several systems. Because of its close relationship with PAPP-A, both structurally and functionally, PAPP-A2 is a likely candidate for IGFBP-5 proteinase in many tissues and conditioned media where IGFBP-5 proteolysis has been reported.

Research Area: Cell biology, Cardiovascular