Recombinant Human XPNPEP1 Protein (C-6His)

Name: Recombinant Human XPNPEP1 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1274NP
Availability: InStock

BL-1274NP: Greater than 85% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Xaa-Pro Aminopeptidase 1 is produced by our E.coli expression system and the target gene encoding Pro2-His623 is expressed with a 6His tag at the C-terminus.
Accession	Q9NQW7
Synonym	Xaa-Pro Aminopeptidase 1; Aminoacylproline Aminopeptidase; Cytosolic Aminopeptidase P; Soluble Aminopeptidase P; sAmp; X-Pro Aminopeptidase 1; X-Prolyl Aminopeptidase 1 Soluble; XPNPEP1; XPNPEPL; XPNPEPL1
Gene Background	X-Prolyl Aminopeptidase (XPNPEP1) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-Prolyl Aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. X-Prolyl Aminopeptidase is a member of the M24 family of metalloproteases, which also contains methionine aminopeptidases, X-Pro dipeptidase, aminopeptidase P2, aminopeptidase P homolog, proliferation-associated protein 1, and suppressor of Ty homolog or chromatin-specific transcription elongation factor large subunit. It is a soluble enzyme, in contrast to the GPI-anchored Aminopeptidase P2 encoded by XPNPEP2. Deficiency of X-Prolyl Aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine. Human Aminopeptidase P1 is widely expressed. The amino acid sequence of human X-Prolyl Aminopeptidase is 99%, 97%, 95%, 74% and 73% identical to that of canine, bovine, mouse/rat, Xenopus and zebrafish, respectively.
Molecular Mass	70.6 KDa
Apmol Mass	69-85 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM PB, 8% Sucrose, 100mM NaCl, 10% Glycerol, 0.05% Tween80, 0.02% Tween20, pH 7.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 85% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro.
Subcellular Location	Cytoplasm.
Protein Families	Peptidase M24B family
Database References	HGNC: 12822 OMIM: 602443 KEGG: hsa:7511 STRING: 9606.ENSP00000421566 UniGene: Hs.390623
Tissue Specificity	Expressed in all tissues tested, including pancreas, heart, muscle, kidney, liver, lung and brain. Highest levels in pancreas.

Gene Functions References

Alanine replacement of Arg535 destabilizes the AMPP dimer and guanidine hydrochloride restores the native monomer-dimer equilibrium. It is proposed that Arg535 plays an important role in AMMP catalysis and in stabilization of the catalytically active dimeric state PMID: 29351301
These data suggest that progesterone-induced increases in AP-P may contribute to the development of oral contraceptive pill-induced hypertension in susceptible Women. PMID: 19126663

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.