Recombinant Human Glutamyl Aminopeptidase (ENPEP) Protein (His)

Name: Recombinant Human Glutamyl Aminopeptidase (ENPEP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08278P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Glutamyl Aminopeptidase (ENPEP) Protein (His) is produced by our E.coli expression system. This is a extracellular protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q07075
Target Symbol	ENPEP
Synonyms	Aminopeptidase A; AMPE_HUMAN; AP-A; APA; bp-1; bp1; CD249; Differentiation antigen gp160; EAP; Enpep; Glutamyl aminopeptidase (aminopeptidase A); Glutamyl aminopeptidase; Gp160; Ly51
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	YFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREW
Expression Range	719-949aa
Protein Length	Extracellular Domain
Mol. Weight	31.0kDa
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	Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II.
Subcellular Location	Cell membrane; Single-pass type II membrane protein.
Protein Families	Peptidase M1 family
Database References	HGNC: 3355 OMIM: 138297 KEGG: hsa:2028 STRING: 9606.ENSP00000265162 UniGene: Hs.435765
Tissue Specificity	Expressed in choriocarcinoma cancer cell lines (at protein level). Expressed by epithelial cells of the proximal tubule cells and the glomerulus of the nephron. Also found in a variety of other tissues.

Gene Functions References

We suggest that APA enzymatic activity affects tumor initiation and cancer malignancy in a TWIST-dependent manner PMID: 28177885
The substrate Angiotensin II, the enzymes aminopeptidases-A, B, M as well as IRAP were detected in the jejunal mucosa. PMID: 26311161
This study suggests a role for GAP in the neoplastic development of renal tumours and provides additional data for considering the activity and expression of this enzyme of interest in the diagnosis and prognosis of renal neoplasms. PMID: 24885240
These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation PMID: 23888046
There was no significant alteration in plasma APA activity in the patients with Chagas disease or dilated cardiomyopathies, as compared with that in health controls PMID: 21697726
Rieger syndrome with microdeletions including only the PITX2 and ENPEP (glutamyl aminopeptidase) genes. PMID: 17850355
Data show that APA appears to be an essential enzyme in the control of blood pressure via degradation of Angiotensin II. PMID: 17990103
Data show that aminopeptidase A (APA) plays important roles in the regulation of blood pressure under both the physiological and pathological conditions. PMID: 17999179
Data show that brain aminopeptidases act upon Ang I, Ang II and Ang III in order to activate brain AT(1) receptors. PMID: 18188697
rare and common variation in ENPEP may contribute to the development of renal and hypertensive disorders and warrants further study PMID: 18206321
The presence of APA in several human brain nuclei sensitive to angiotensins and involved in blood pressure regulation suggests that APA in humans is an integral component of the brain renin angiotensin system. PMID: 18410507
A novel nonsense polymorphism in the aminopeptidase-a gene was associated with hypertension among postmenopausal women, and those with marginal calcium and vitamin D intake. PMID: 18550936
Angiotensin III and aminopeptidase A and N, related converting enzymes, contribute to cell proliferation of prostate cancer and may be implicated in cancer progression. PMID: 18677709
Over-expressed APA drastically reduces, in a calcium dependent manner, full-length-Abeta but not amyloid-beta precursor protein (APP) intracellular domain in a cell-free model of Abeta production. PMID: 19187443
The activity of glutamyl aminopeptidase was significally increased in head and neck squamous cell carcinoma tissue. PMID: 19373777

FAQs

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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.