Recombinant Human CNDP2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1348

Recombinant Human CNDP2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1348
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Product Overview

Tag His
Host Species Human
Accession CAC69883.1
Synonym CN2, CPGL, HEL-S-13, HsT2298, PEPA
Background Cytosolic non-specific dipeptidase, also known as CNDP dipeptidase 2, Glutamate carboxypeptidase-like protein 1, Peptidase A, CNDP2 and CN2, is a cytoplasm protein which belongs to thepeptidase M2A family. CNDP2 / CPGL is a cytosolic enzyme that can hydrolyze carnosine to yield l-histidine and beta-alanine. CNDP2 / CPGL hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Itmay be play a role as tumor suppressor in hepatocellular carcinoma (HCC) cells. Isoform1 of CNDP2 / CPGL is ubiquitously expressed with higher levels in kidney and liver (at protein level). Isoform2 of CNDP2 / CPGL is expressed in fetal tissues, it is only expressed in adult liver and placental tissues. CNDP2 / CPGL is highly expressed in the histaminergic neurons in the tuberomammillary nucleus, implying that it may supply histidine to histaminergic neurons for histamine synthesis.
Description A DNA sequence encoding the human CNDP2 (CAC69883.1) (Met 1-Asp 475) was expressed, fused with a His tag at the C-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Met 1
AA Sequence Met 1-Asp 475
Molecular Weight The secreted recombinant human CNDP2 consists of 485 a.a. and predicts a molecular mass of 54.2 kDa as estimated in SDS-PAGE under reducing conditions.
Purity >94% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 50mM Tris, 100mM NaCl, 0.5mM PMSF, pH 8.0.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Catalyzes the peptide bond hydrolysis in dipeptides, displaying a non-redundant activity toward threonyl dipeptides. Mediates threonyl dipeptide catabolism in a tissue-specific way. Has high dipeptidase activity toward cysteinylglycine, an intermediate metabolite in glutathione metabolism. Metabolizes N-lactoyl-amino acids, both through hydrolysis to form lactic acid and amino acids, as well as through their formation by reverse proteolysis. Plays a role in the regulation of cell cycle arrest and apoptosis.
Subcellular Location Cytoplasm.
Protein Families Peptidase M20A family
Database References
Tissue Specificity [Isoform 1]: Ubiquitously expressed with higher levels in kidney and liver (at protein level). Expressed in peripheral blood leukocytes. Expressed in gastric mucosa and down-regulated in gastric cancer mucosal tissues (at protein level).; [Isoform 2]: Bro

Gene Functions References

  1. The CNDP2 rs6566810 (A/A genotype) is overrepresented in endurance athletes, but only in international-level endurance athletes. Three SNPs (CNDP2 rs3764509, CNDP2-CNDP1 rs2346061, and CNDP1 rs2887) were overrepresented in power athletes compared with nonathletes. PMID: 28871847
  2. These results suggest that the zinc form of CN2 is an active enzyme, but with a different substrate specificity from that of the manganese form. PMID: 29056506
  3. To identify substrates of orphan transporter ATP-binding cassette subfamily C member 5 (ABCC5), identified a class of metabolites, N-lactoyl-amino acids, and found that a protease, cytosolic nonspecific dipeptidase 2 (CNDP2), catalyzes their formation. PMID: 25964343
  4. Expression of CN2 in clinical colon tumors and colon cancer cell lines was significantly higher than that in normal colon mucosa cell lines. Knockdown of CNDP2 can inhibit the proliferation of colon cancer in vitro and retarded carcinogenesis in vivo. PMID: 24885395
  5. Results suggest that CNDP2 acts as a functional tumor suppressor in gastric cancer via activation of the mitogen-activated protein kinase (MAPK) pathway. PMID: 24395568
  6. a key role of CNDP2 in PD neurodegeneration, by mechanisms that could involve oxidative stress, protein aggregation or inflammation. PMID: 22410244
  7. deletion of the CPGL gene is a poor prognostic marker in resected pancreatic cancer, and functional studies suggest the CPGL gene as growth suppressor gene in pancreatic cancer. PMID: 22128300
  8. Common variants in CNDP1 and CNDP2 play a role in susceptibility to kidney disease in patients with type 2 diabetes. PMID: 21573905
  9. the crystal structure of the flop-selective allosteric modulator, PEPA, bound to the binding domains of the GluA2 and GluA3 flop isoforms of AMPA receptors PMID: 20199107
  10. Our large, comprehensive study did not find an association between the D18S880 microsatellite or any other polymorphisms in the CNDP2-CNDP1 genomic region and susceptibility for diabetic nephropathy in type 1 diabetes PMID: 18753673


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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.

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