Recombinant Mouse Anpep protein, His & T7-tagged
Cat.No. : | Anpep-1455M |
Product Overview : | Recombinant Mouse Anpep aa. (Tyr720~Phe961 (Accession # P97449)) fused with N-terminal His & T7 tag was produced in E. coli cells. |
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Source : | E. coli |
Species : | Mouse |
Tag : | His & T7 |
Form : | Freeze-dried powder |
Molecular Mass : | 27kDa as determined by SDS-PAGE reducing conditions. |
Protein length : | Tyr720~Phe961 (Accession # P97449) |
Endotoxin : | <1.0EU per 1µg (determined by the LAL method). |
Purity : | >95% |
Characteristic : | The isoelectric point is 8.6. |
Applications : | SDS-PAGE; WB; ELISA; IP. |
Stability : | The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37°C for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition. |
Storage : | Avoid repeated freeze/thaw cycles. Store at 2-8°C for one month. Aliquot and store at -80°C for 12 months. |
Storage buffer : | Supplied as lyophilized form in PBS, pH7.4, containing 5% sucrose, 0.01% sarcosyl. |
Reconstitution : | Reconstitute in sterile PBS, pH7.2-pH7.4. |
SDS-PAGE: |
Gene Name : | Anpep alanyl (membrane) aminopeptidase [ Mus musculus (house mouse) ] |
Official Symbol : | Anpep |
Synonyms : | Apn; AP-M; AP-N; Cd13; P150; alanyl aminopeptidase; aminopeptidase M; aminopeptidase N/CD13; membrane protein p161; microsomal aminopeptidase; aminopeptidase N |
Gene ID : | 16790 |
mRNA Refseq : | NM_008486.2 |
Protein Refseq : | NP_032512.2 |
UniProt ID : | P97449 |
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◆ Native Protein | ||
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◆ Lysates | ||
ANPEP-3090HCL | Recombinant Human ANPEP cell lysate | +Inquiry |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (13)
Ask a questionANPEP protein expression has been investigated as a potential diagnostic and prognostic marker in certain diseases. For example, increased ANPEP expression has been observed in certain cancers, such as colorectal cancer, and may serve as a biomarker for disease progression or response to treatment. However, further research is still needed to establish its clinical significance.
Yes, various genetic variations and mutations have been identified in the ANPEP gene. Some of these variations may influence ANPEP protein expression, activity, or function, and have been associated with certain diseases or conditions. For example, certain genetic variants of ANPEP have been linked to an increased risk of developing inflammatory bowel diseases.
There are currently no specific drugs or therapies that directly target ANPEP protein. However, the knowledge about the involvement of ANPEP in certain diseases, such as viral infections and IBD, may help guide the development of potential therapies. For example, research is ongoing to develop antiviral drugs that can inhibit the interaction between ANPEP and viral particles.
Yes, ANPEP protein has been implicated in various diseases. For example, it has been linked to viral infections, such as human coronavirus infections, as the ANPEP protein acts as a receptor for the virus to enter host cells. ANPEP has also been associated with inflammatory bowel diseases (IBD) and renal diseases, where its expression and activity levels may be altered.
Several compounds have been identified as inhibitors or activators of ANPEP protein. For example, amastatin and bestatin are known inhibitors that can block the enzymatic activity of ANPEP. These inhibitors have been used in research to investigate the function of ANPEP and its role in various physiological and pathological processes. On the other hand, activators of ANPEP are less well-studied, and more research is needed to identify specific compounds that can modulate ANPEP activity.
ANPEP protein is not expressed in all tissues of the body. Its expression is generally highest in tissues and organs that have high metabolic activity, such as the kidneys, small intestine, and lung. ANPEP is also found in other tissues, including the liver, brain, spleen, and immune cells.
The ANPEP protein is synthesized through a process called translation. The ANPEP gene is transcribed into messenger RNA (mRNA) in the cell nucleus. The mRNA is then exported to the cytoplasm, where it serves as a template for the synthesis of ANPEP protein. Ribosomes, along with transfer RNA (tRNA) molecules carrying specific amino acids, bind to the mRNA and catalyze the assembly of amino acids in the correct sequence to form the ANPEP protein.
ANPEP protein expression has been investigated as a potential diagnostic marker in various diseases. For example, increased ANPEP expression has been observed in certain cancers and may serve as a biomarker for disease detection, prognosis, or response to treatment. Additionally, ANPEP expression in the kidneys has been evaluated as a marker for kidney function. However, further research and validation are required before ANPEP can be routinely used for diagnostic purposes.
While there are currently no approved therapies specifically targeting ANPEP protein, it is being investigated as a potential therapeutic target for certain diseases. For example, in cancer research, ANPEP is being explored as a target for antibody-based therapies, such as antibody-drug conjugates or immunotoxins, to selectively deliver cytotoxic agents to ANPEP-expressing cancer cells. Additionally, targeting ANPEP may have potential in the treatment of viral infections by developing drugs that block the interaction between ANPEP and viral particles. However, more studies and clinical trials are needed to validate the efficacy and safety of such approaches.
ANPEP protein is primarily localized on the surface of cells, particularly on the apical membrane of epithelial cells lining the intestines and the proximal tubules of the kidneys. It is also found on the surface of immune cells, such as T cells and neutrophils.
Yes, ANPEP protein is expressed in various tissues and organs throughout the body, although its levels and functions may vary. It can be found in the lungs, liver, spleen, brain, reproductive organs, and immune cells like T cells and neutrophils.
Yes, genetic mutations and polymorphisms in the ANPEP gene have been identified and associated with certain diseases or physiological traits. For example, specific mutations in the ANPEP gene have been linked to familial renal glucosuria, a rare inherited disorder characterized by excess glucose in the urine. In addition, certain polymorphisms in the ANPEP gene have been associated with an increased risk of developing certain types of cancers, such as colorectal cancer and breast cancer. However, more research is needed to fully understand the functional consequences of these genetic variants and their impact on ANPEP protein function.
ANPEP protein, expressed on the surface of immune cells, plays a role in immune responses by mediating the adhesion and migration of cells. It interacts with other immune cells and mediates the binding of immune cells to endothelial cells, which is essential for immune cell trafficking and immune responses. ANPEP also aids in the regulation of inflammatory processes.
Customer Reviews (5)
Write a reviewThe knowledgeable and responsive support team offers valuable assistance and expertise, making troubleshooting and problem-solving much more efficient.
Its purity and functionality have been extensively tested, ensuring reliable and reproducible results in my research.
One notable advantage of using the ANPEP protein is the outstanding technical support provided by its manufacturer.
By using the ANPEP protein in my experiments, I am confident in obtaining accurate and dependable data.
the ANPEP protein not only fulfills my experimental requirements but is also backed by excellent technical support, which guarantees a smooth and successful research experience.
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