Recombinant Rat Aminopeptidase N (ANPEP) Protein (His-SUMO)

Name: Recombinant Rat Aminopeptidase N (ANPEP) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09500P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Rattus norvegicus (Rat) Anpep.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Rat Aminopeptidase N (ANPEP) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P15684
Target Symbol	ANPEP
Synonyms	AnpepAminopeptidase N; AP-N; rAPN; EC 3.4.11.2; Alanyl aminopeptidase; Aminopeptidase M; AP-M; Kidney Zn peptidase; KZP; Microsomal aminopeptidase; CD antigen CD13
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	YAQEKNRNAENSAIAPTLPGSTSATTSTTNPAIDESKPWNQYRLPKTLIPDSYQVTLRPYLTPNEQGLYIFKGSSTVRFTCNETTNVIIIHSKKLNYTNKGNHRVALRALGDTPAPNIDTTELVERTEYLVVHLQGSLVKGHQYEMDSEFQGELADDLAGFYRSEYMEGGNKKVVATTQMQAADARKSFPCFDEPAMKASFNITLIHPNNLTALSNMLPKDSRTLQEDPSWNVTEFHPTPKMSTYLLAYIVSEFKYVEAVSPNRVQIRIWARPSAIDEGHGDYALQVTGPILNFFAQHYNTAYPLEKSDQIALPDFNAGAMENWGLVTYRESALVFDPQSSSISNKERVVTVIAHELAHQWFGNLVTVDWWNDLWLNEGFASYVEFLGADYAEPTWNLKDLIVLNDVYRVMAVDALASSHPLSSPANEVNTPAQISELFDSITY
Expression Range	33-476aa
Protein Length	Partial
Mol. Weight	65.8kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity.
Subcellular Location	Cell membrane; Single-pass type II membrane protein.
Protein Families	Peptidase M1 family
Database References	KEGG: rno:81641 STRING: 10116.ENSRNOP00000020002 UniGene: Rn.11132
Tissue Specificity	Widely distributed throughout the CNS. Particularly abundant in kidney and intestinal microvilli, also detected in lung and liver. Weakly expressed in heart and aorta.

Gene Functions References

Data indicate that fluorogenic substrates can be successfully used to identify aminopeptidase N and to measure their activity in cell lysates. PMID: 26449746
the LAP1 gene (TOR1AIP1) undergoes alternative splicing to originate three LAP1 isoforms (LAP1A, B and C). PMID: 25461922
the anti-oxidant potential of APN in oxidative stress-associated cardiovascular diseases, such as hypertension-induced HF-preserved EF. PMID: 23894332
This study demonistrated that aminopeptidase N were up-regulated ipsilaterally from 6 h to 7 days post ischemia PMID: 22373413
Results suggest that the upregulation of serotonergic activity may be related to a lowered brain dipeptidyl peptidase III, alanyl- and arginyl aminopeptidase activity which may influence the cleavage of their substrates. PMID: 18547641
hypothalamic CD13 plays a role in the regulation of energy metabolism not by means of puromycin-insensitive membrane-bound neutral aminopeptidase enzyme activity. PMID: 20851150
The present study clearly demonstrated that the activities of AlaAP and CysAP in the hippocampus were associated with lateralization in normal rats. PMID: 20096929
We therefore hypothesize that the effect of angiotensin IV on dopamine release in the striatum is mediated via activation of IRAP and/or AP-N, possibly acting as receptors for angiotensin IV. PMID: 17169335
a possible association of the Anpep gene with hypertension in Dahl rat and raise the prospect that increased Anpep may play a mechanistic role in adaptation to high salt. PMID: 17242304
These results demonstrate that expression of neprilysin and aminopeptidase N can be regulated when peptide neurons are activated and, that regulation is enzyme-, region-, and stage-specific. PMID: 17952634

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.