Recombinant Pig Aminopeptidase N (ANPEP), partial

Code CSB-YP001827PI
MSDS
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Source Yeast
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Code CSB-EP001827PI-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP001827PI
MSDS
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Source Baculovirus
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Code CSB-MP001827PI
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
ANPEPAminopeptidase N; AP-N; pAPN; EC 3.4.11.2; Alanyl aminopeptidase; Aminopeptidase M; AP-M; Microsomal aminopeptidase; gp130; CD antigen CD13
Species
Sus scrofa (Pig)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.
Description

The recombinant pig Aminopeptidase N (ANPEP) can be produced in multiple expression systems, including yeast, in vivo biotinylation in E. coli, baculovirus, and mammalian cells. The gene encoding the partial pig ANPEP protein is cloned into an expression vector, which is transformed into the expression system. If needed, any tag could be added to the target gene. The cells are cultured under conditions that promote protein expression. After sufficient growth is achieved, the cells are lysed to release the recombinant ANPEP protein, which is subjected to affinity chromatography purification. The purity of the protein is confirmed using SDS-PAGE, reaching up to 85%.

ANPEP, also known as CD13, is a type II membrane glycoprotein belonging to the family of membrane-bound metalloproteases. It is expressed in various cells, including porcine enterocytes [1]. ANPEP has been identified as an endocytotic F4 receptor in pigs, enhancing the intestinal mucosal immune response [2]. This transmembrane metalloprotease is highly expressed in immune cells, activated endothelial cells, certain epithelial cells, and fibroblasts at sites of inflammation [3]. ANPEP plays a crucial role in protein and peptide degradation, cell invasion, migration, and angiogenesis [4]. It cleaves N-terminal neutral amino acids from peptides and proteins [5]. ANPEP is overexpressed in several tumor cell malignancies, where it mediates the intracellular hydrolysis of compounds like Mel-flufen [6].

ANPEP has been studied in viral infections, with some coronaviruses, including transmissible gastroenteritis virus (TGEV), utilizing it as a receptor for cell entry [7]. Research has demonstrated that ANPEP has the potential as a biomarker and therapeutic target in diseases like gallbladder carcinoma and atherosclerosis [4][8].

Furthermore, ANPEP has been linked to various physiological processes, such as impaired angiogenesis in mice lacking ANPEP [9] and delayed mammary gland development in mice deficient in ANPEP [10]. The enzyme's multifaceted functions extend to its involvement in cancer dissemination, making it a target for anti-cancer agents [11].

References:
[1] V. Melkebeek, K. Rasschaert, P. Bellot, K. Tilleman, H. Favoreel, D. Deforceet al., Targeting aminopeptidase n, a newly identified receptor for f4ac fimbriae, enhances the intestinal mucosal immune response, Mucosal Immunology, vol. 5, no. 6, p. 635-645, 2012. https://doi.org/10.1038/mi.2012.37
[2] T. Goetstouwers, M. Poucke, V. Nguyen, V. Melkebeek, A. Coddens, D. Deforceet al., F4-related mutation and expression analysis of the aminopeptidase n gene in pigs1, Journal of Animal Science, vol. 92, no. 5, p. 1866-1873, 2014. https://doi.org/10.2527/jas.2013-7307
[3] M. Ghosh and L. Shapiro, Cd13 regulation of membrane recycling: implications for cancer dissemination, Molecular & Cellular Oncology, vol. 6, no. 6, p. e1648024, 2019. https://doi.org/10.1080/23723556.2019.1648024
[4] R. Priya, V. Jain, J. Akhtar, G. Chauhan, P. Sakhuja, S. Goyalet al., Plasma-derived candidate biomarkers for detection of gallbladder carcinoma, Scientific Reports, vol. 11, no. 1, 2021. https://doi.org/10.1038/s41598-021-02923-7
[5] A. Kido, S. Krueger, C. Haeckel, & A. Roessner, Untitled, Clinical & Experimental Metastasis, vol. 20, no. 7, p. 585-592, 2003. https://doi.org/10.1023/a:1027383729767
[6] D. Chauhan, A. Ray, K. Viktorsson, J. Spira, C. Paba‐Prada, N. Munshiet al., in vitro and in vivo antitumor activity of a novel alkylating agent, melphalan-flufenamide, against multiple myeloma cells, Clinical Cancer Research, vol. 19, no. 11, p. 3019-3031, 2013. https://doi.org/10.1158/1078-0432.ccr-12-3752
[7] W. Li, R. Luo, Q. He, F. Kuppeveld, P. Rottier, & B. Bosch, Aminopeptidase n is not required for porcine epidemic diarrhea virus cell entry, Virus Research, vol. 235, p. 6-13, 2017. https://doi.org/10.1016/j.virusres.2017.03.018
[8] Y. Li, Q. Jia, H. Cao, P. He, X. Shen, Y. Huanget al., Effect of bushen jiangzhi recipe on atherosclerosis in apoe−/- mice by regulating the expression of anpep via mmu_circrna_22187, Evidence-Based Complementary and Alternative Medicine, vol. 2021, p. 1-10, 2021. https://doi.org/10.1155/2021/4738264
[9] R. Rangel, Y. Sun, L. Guzman-Rojas, M. Ozawa, J. Sun, R. Giordanoet al., Impaired angiogenesis in aminopeptidase n-null mice, Proceedings of the National Academy of Sciences, vol. 104, no. 11, p. 4588-4593, 2007. https://doi.org/10.1073/pnas.0611653104
[10] A. Kolb, D. Sorrell, C. Lassnig, S. Lillico, A. Carlisle, C. Neilet al., Mammary gland development is delayed in mice deficient for aminopeptidase n, Transgenic Research, vol. 22, no. 2, p. 425-434, 2012. https://doi.org/10.1007/s11248-012-9654-7
[11] S. Amin, N. Adhikari, & T. Jha, Design of aminopeptidase n inhibitors as anti-cancer agents, Journal of Medicinal Chemistry, vol. 61, no. 15, p. 6468-6490, 2018. https://doi.org/10.1021/acs.jmedchem.7b00782

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Target Background

Function
Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization. It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity.; (Microbial infection) In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.
Gene References into Functions
  1. Genetic ablation of APN expression had no effect on infectability by porcine epidemic diarrhea virus, demonstrating that APN is not essential for porcine epidemic diarrhea virus cell entry. PMID: 28363778
  2. pAPN is not a functional receptor for porcine epidemic diarrhea virus, but promotes the infection of PEDV through its protease activity. PMID: 27449937
  3. The C-terminal domain of the S1 domain of porcine epidemic diarrhea virus is bound to swine pAPN. PMID: 26907329
  4. Data indicate that fluorogenic substrates can be successfully used to identify aminopeptidase N and to measure their activity in cell lysates. PMID: 26449746
  5. SPC subdomain of APN plays a key role in cell entry of PEDV and its expression permits PEDV growth PMID: 26044794
  6. Porcine epidemic diarrhea virus recognizes protein receptor aminopeptidase N from pig and human and sugar coreceptor N-acetylneuraminic acid. PMID: 25787280
  7. These data demonstrate that pAPN, the cellular receptor for porcine epidemic diarrhea virus, mediates polarized virus infection. PMID: 25681796
  8. It was concluded that the difference in F4 binding to ANPEP is due to modifications in its carbohydrate moieties. PMID: 24663207
  9. The region aa 673-722 of the C subunit of porcine aminopeptidase N is indicated to play a key role in swine transmissible gastroenteritis virus binding. PMID: 22083718
  10. The binding ability of four truncated porcine aminopeptidase N proteins to transmissible gastroenteritis virus (TGEV), a porcine coronavirus, was analyzed by ELISA and immunoblotting. PMID: 20643168
  11. Aminoeptidase N is the major for cell entry system of porcine epidemic diarrhea virus infection. PMID: 20074871
  12. results demonstrate that aminopeptidase N reduces basolateral Na(+)-K(+)-ATPase levels via ANG IV/AGTRIV signaling. This novel pathway may be important in renal adaptation to high salt PMID: 17634404

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Subcellular Location
Cell membrane; Single-pass type II membrane protein.
Protein Families
Peptidase M1 family
Database Links
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