Anpep, AP-M, AP-N, Apn, Cd13, P150, mAPN, Alanyl aminopeptidase, Aminopeptidase M, Membrane protein p161, Microsomal aminopeptidase, CD13, Lap-1, Lap1, aminopeptidase N.
Greater than 95.0% as determined by SDS-PAGE.
ANPEP Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 943 amino acids (33-966 a.a.) and having a molecular mass of 107.5 kDa. ANPEPis expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Aminopeptidase N, also known as ANPEP, is an enzyme primarily located in the microvillar membrane of the small intestine and kidneys, as well as other plasma membranes. It plays a crucial role in the digestive process by breaking down peptides following their initial breakdown by gastric and pancreatic proteases. ANPEP is also involved in the modification of various peptides, including peptide hormones, neuropeptides, and chemokines. Furthermore, it contributes to angiogenesis, facilitates cholesterol crystallization, and regulates amino acid transport by interacting with and modulating the activity of the SLC6A19 transport protein.
ANPEP Mouse, produced in Sf9 Insect cells, is a single, glycosylated polypeptide chain consisting of 943 amino acids (33-966 a.a.) with a molecular weight of 107.5 kDa. This recombinant protein is expressed with a 9 amino acid His tag at the C-terminus and purified using proprietary chromatographic methods.
The ANPEP protein solution is provided at a concentration of 0.5mg/ml in a buffer consisting of PBS (pH 7.4) and 10% glycerol.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Repeated freezing and thawing of the product should be avoided.
The purity of the protein is determined to be greater than 95.0% using SDS-PAGE analysis.
The specific activity of the enzyme is measured to be greater than 4,000 pmol/min/ug. This is defined as the quantity of enzyme required to hydrolyze 1 picomole of H-AlaAMC into Alanine and AMC per minute at a pH of 7.5 and a temperature of 25°C.
Anpep, AP-M, AP-N, Apn, Cd13, P150, mAPN, Alanyl aminopeptidase, Aminopeptidase M, Membrane protein p161, Microsomal aminopeptidase, CD13, Lap-1, Lap1, aminopeptidase N.
ADPYAQEKNR NAENSATAPT LPGSTSATTA TTTPAVDESK PWNQYRLPKT LIPDSYRVIL RPYLTPNNQG LYIFQGNSTV RFTCNQTTDV IIIHSKKLNY TLKGNHRVVL RTLDGTPAPN IDKTELVERT EYLVVHLQGS LVEGRQYEMD SQFQGELADD LAGFYRSEYM EGDVKKVVAT TQMQAADARK SFPCFDEPAM KAMFNITLIY PNNLIALSNM LPKESKPYPE DPSCTMTEFH STPKMSTYLL AYIVSEFKNI SSVSANGVQI GIWARPSAID EGQGDYALNV TGPILNFFAQ HYNTSYPLPK SDQIALPDFN AGAMENWGLV TYRESSLVFD SQSSSISNKE RVVTVIAHEL AHQWFGNLVT VAWWNDLWLN EGFASYVEYL GADYAEPTWN LKDLMVLNDV YRVMAVDALA SSHPLSSPAD EIKTPDQIME LFDSITYSKG ASVIRMLSSF LTEDLFKKGL SSYLHTYQYS NTVYLDLWEH LQKAVNQQTA VQPPATVRTI MDRWILQMGF PVITVNTNTG EISQKHFLLD SKSNVTRPSE FNYIWIAPIP FLKSGQEDHY WLDVEKNQSA KFQTSSNEWI LLNINVTGYY LVNYDENNWK KLQNQLQTDL SVIPVINRAQ IIHDSFNLAS AKMIPITLAL DNTLFLVKEA EYMPWQAALS SLNYFTLMFD RSEVYGPMKR YLKKQVTPLF FYFQNRTNNW VNRPPTLMEQ YNEINAISTA CSSGLKECRD LVVELYSQWM KNPNNNTIHP NLRSTVYCNA IAFGGEEEWN FAWEQFRNAT LVNEADKLRS ALACSKDVWI LNRYLSYTLN PDYIRKQDTT STIISIASNV AGHPLVWDFV RSNWKKLFEN YGGGSFSFAN LIQGVTRRFS SEFELQQLEQ FKADNSATGF GTGTRALEQA LEKTRANIDW VKENKDAVFK WFTENSSHHH HHH
The mouse ANPEP gene encodes a protein that consists of a short cytoplasmic tail, a transmembrane region, and a large extracellular domain . The enzyme is known for its ability to cleave the fluorogenic peptide substrate, Ala-7-amido-4-methylcoumarin (Ala-AMC), with a specific activity of over 1,000 pmol/min/µg . This activity is essential for its role in peptide metabolism and various physiological processes.
The recombinant form of mouse Alanyl Aminopeptidase is produced using a mouse myeloma cell line, NS0 . This recombinant protein is often tagged with a C-terminal 10-His tag to facilitate purification and detection . The recombinant form is used in various research applications, including enzyme assays, structural studies, and functional analyses.
Recombinant Alanyl Aminopeptidase is widely used in research to study its role in: