Aminopeptidase N Antibodies

Aminopeptidase N (ANPEP)

Broad specificity aminopeptidase which plays a part in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides such as 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.

Gene Information

Human
Gene Name:	ANPEP
Uniprot:	P15144
Entrez:	290

Family

Belongs to:
peptidase M1 family

Alternative Names

alanyl (membrane) aminopeptidase; Alanyl aminopeptidase; Aminopeptidase M; Aminopeptidase N; ANPEP; AP-M; APN; AP-N; CD13 antigen; CD13; CD13APN; EC 3.4.11; EC 3.4.11.2; gp150; LAP1; Microsomal aminopeptidase; Myeloid plasma membrane glycoprotein CD13; p150; PEPN; PEPNhAPN

Molecular Weight

Mass (kDA):
109.54 kDA

Genomic Context

Human
Location:	15q26.1
Sequence:	15; NC_000015.10 (89784895..89814852, complement)

Tissue Specificity

Expressed in epithelial cells of the kidney, intestine, and respiratory tract; granulocytes, monocytes, fibroblasts, endothelial cells, cerebral pericytes at the blood- brain barrier, synaptic membranes of cells in the CNS. Also expressed in endometrial stromal cells, but not in the endometrial glandular cells. Found in the vasculature of tissues that undergo angiogenesis and in malignant gliomas and lymph node metastases from multiple tumor types but not in blood vessels of normal tissues. A soluble form has been found in plasma. It is found to be elevated in plasma and effusions of cancer patients.

Subcellular Localizations

Cell membrane; Single-pass type II membrane protein. Also found as a soluble form.

Diseases

• Malignant Neoplasms
• Neoplasms
• Hypertensive Disease
• Tumor Angiogenesis
• Adenocarcinoma
• Severe Acute Respiratory Syndrome
• Prostatic Neoplasms
• Cell Invasion
• Malignant Neoplasm Of Prostate
• Neoplasm Metastasis
• Meningeal Disorder
• Viral Meningitis
• Neoplasm Invasiveness

• Fetal Growth Retardation
• Carcinoma
• Fibrosarcoma
• Fibrosis
• Esophageal Neoplasms
• Coronavirus Infections
• Mental Disorders

Pathways

• Localization
• Angiogenesis
• Reverse Transcription
• Coagulation
• Translation
• Immune Response
• Pathogenesis

• Cholesterol Homeostasis
• Inflammatory Response

PTMs

• Disulfide bond

• Glycoprotein

• Sulfation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/ANPEP

Boster Bio - Best Uses Of The ANPEP Marker

If you're using Boster Bio, the optimization guide is an essential source. It provides answers to a variety of questions related to the use of Boster Bio, allowing you to make informed choices which will enhance the quality of your research. You can also use troubleshooting guides in order to spot and correct common mistakes. Troubleshooting guides will help you identify the variables that could be causing your results not to be as expected.

ANPEP is a membrane-associated protein

ANPEP is a membrane-associated glycoprotein which has been cloned by six different mammalian species. ANPEP is widely distributed in tissues but is concentrated in the brush boundary membrane of the tubule cells that are proximal. It has been suggested it plays a role in angiogenesis and ankephalins. It has also been implicated in tumor growth and secretion as well as angiogenesis.

It isn't clear what the function of ANPEP is in the gastric epithelium. The membrane-associated protein is found in mature ZCs. This makes it a useful surface marker to find pure ZCs in gastric epithelia. This discovery will have important implications for future research on ZCs and gastric diseases. It could also be utilized in ex vivo cell culture experiments to study changes in the gastric epithelial layer.

ANPEP expression is linked to increased bioavailability of angiogenic factors, including vascular endothelial growth factor (VEGF). ANPEP expression in mice is highest in 8-week old pups, which is the period of highest fertility. In the IW group, ANPEP expression was highest and fertility increased as they grew older. Further functional studies on ANPEP are needed.

In Western blot analysis, cell homogenates were separated in RIPA buffer, then subjected to immunoblotting. The DC protein assay was used to measure the amount of proteins. TaKaRa's PrimeScript kit reverse-transcribed RNA. Sequence-specific primers were used to identify ANPEP, IL-1, and Integrin B. These sequences were normalized by DNAsis software.

Anpep is involved in the metabolism of angiotensin and angiotensin IV. It could play a role in regulation of Na+/K+ influx within tubule cell lines. Anpep is also connected to the RAS. Anpep is believed to regulate negatively Na+-ATPase activity within LLC-PK1 cells. In humans, it could regulate the function of ANG II.

Anpep regulates a variety of membrane-associated proteins, including the Na+–K+–ATPase in the basolateral region. Certain agents regulate multiple membrane-associated protein, such as PTH and captopril. This latter may be a therapeutic option to re-distribute Na+ within cells as it inhibits the ATPase. However, other agents affect a single transporter while regulating several membrane-associated proteins.

It is expressed in plasma and intracellular membranes.

ANPEP is a protein which is expressed on both intracellular and plasma membranes. It has been linked to cancer growth and angiogenesis, and has been implicated in bladder and proliferative cancers. A subset of significantly elevated SURFY proteins was also identified and quantified in the same study. ANPEP Fibronectin-1, ANPEP, as as glutamine-dependent proteins were all significantly increased.

The plasma membrane is a dynamic structure made up of cholesterol, lipids, and proteins that separate the cytoplasm from the external environment. These membranes can be sensitive to signals from the outside and allow the transfer of substances between cells and their environment. They also play an important function in signaling and cross-membrane transportation within the cell. The current model of plasma membrane structure was first suggested in 1972. It has been altered several times since. No matter how the membrane is structured, its fundamental structure is built on the fluid mosaic model.

PIST is a PDZ domain-containing protein that works in conjunction with MAGI-1 and harmonin. This protein regulates intracellular flow of membrane proteins. PIST is overexpressed in plasma membranes. This results in decreased expression of a variety of proteins, including CFTR and the b1 adrenergic receptors. When PIST is expressed too much, it also blocks cadherin 23 expression.

Phospholipids are one of the major components of the plasma membrane. They are arranged in bilayers that have hydrophilic and hydrophobic regions. Phospholipids have negatively charged phosphate groups and additional small groups which could be charged or polar. The heads of phosphates are hydrophilic and have a face that extends outwards within the membrane bilayer. Water has the ability to create electrostatic interactions with these lipids.

It can be used to separate mature ZCs

ANPEP is a surface marker only expressed by ZCs in gastric epithelium. ANPEP allows for the isolation of a ZC-specific population to study or ex vivo culture. ANPEP can be used to not just isolate ZCs from the gastric epithelium but as well to monitor the epithelium's metaplastic growth and maturation.

This marker is present in mature mouse and human ZCs. The use of flow cytometry has validated this marker, allowing the identification of ZCs in the culture. It has been utilized successfully in organoid culture FACS, as well as in cell-based cloning studies. To isolate ZCs follow the steps that is described in this paper. This will save you time and effort, as well as money in organoid isolation.

ANPEP is expressed on the surface of mature gastric cells. This marker is a part of the Mist1 pattern and disappears when combined with ZC reprogramming. However this marker was the sole ZC-specific marker that was not altered in SPEM. The ANPEP protein was subsequently detected on the surface of the mouse corpus gastric epithelium in the course of a 12-hour tamoxifen treatment. The mRNA levels of Anpep decreased with daily injections of tamoxifen.

The ANPEP marker is validated as a biomarker used to detect gastric zymogenic cells. It is a mRNA that is specific to the gastric epithelial lineage, which includes. pit cells that secrete mucus and acid-secreting parietal cells and digestive enzyme-secreting chief cells. All these cell types are derived directly from the same undifferentiated stomach stem cells and replenished at the age of adulthood.