Recombinant Human Neuropilin-1 (NRP1) Protein (hFc), Active

Beta LifeScience SKU/CAT #: BLC-05808P
Greater than 95% as determined by SDS-PAGE.
Greater than 95% as determined by SDS-PAGE.
Activity Measured by its binding ability in a functional ELISA. Immobilized human VEGF165 ) at 2 μg/ml can bind human NRP1, the EC 50 is 22.68-34.55 ng/ml. Biological Activity Assay
Activity Measured by its binding ability in a functional ELISA. Immobilized human VEGF165 ) at 2 μg/ml can bind human NRP1, the EC 50 is 22.68-34.55 ng/ml. Biological Activity Assay

Recombinant Human Neuropilin-1 (NRP1) Protein (hFc), Active

Beta LifeScience SKU/CAT #: BLC-05808P
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Product Overview

Description Recombinant Human Neuropilin-1 (NRP1) Protein (hFc), Active is produced by our Mammalian cell expression system. This is a full length protein.
Purity Greater than 95% as determined by SDS-PAGE.
Endotoxin Less than 1.0 EU/ug as determined by LAL method.
Activity Measured by its binding ability in a functional ELISA. Immobilized human VEGF165 ) at 2 μg/ml can bind human NRP1, the EC 50 is 22.68-34.55 ng/ml.
Uniprotkb O14786
Target Symbol NRP1
Synonyms (Vascular endothelial cell growth factor 165 receptor)(CD304)
Species Homo sapiens (Human)
Expression System Mammalian cell
Tag C-hFc
Target Protein Sequence FRNDKCGDTIKIESPGYLTSPGYPHSYHPSEKCEWLIQAPDPYQRIMINFNPHFDLEDRDCKYDYVEVFDGENENGHFRGKFCGKIAPPPVVSSGPFLFIKFVSDYETHGAGFSIRYEIFKRGPECSQNYTTPSGVIKSPGFPEKYPNSLECTYIVFVPKMSEIILEFESFDLEPDSNPPGGMFCRYDRLEIWDGFPDVGPHIGRYCGQKTPGRIRSSSGILSMVFYTDSAIAKEGFSANYSVLQSSVSEDFKCMEALGMESGEIHSDQITASSQYSTNWSAERSRLNYPENGWTPGEDSYREWIQVDLGLLRFVTAVGTQGAISKETKKKYYVKTYKIDVSSNGEDWITIKEGNKPVLFQGNTNPTDVVVAVFPKPLITRFVRIKPATWETGISMRFEVYGCKITDYPCSGMLGMVSGLISDSQITSSNQGDRNWMPENIRLVTSRSGWALPPAPHSYINEWLQIDLGEEKIVRGIIIQGGKHRENKVFMRKFKIGYSNNGSDWKMIMDDSKRKAKSFEGNNNYDTPELRTFPALSTRFIRIYPERATHGGLGLRMELLGCEVEAPTAGPTTPNGNLVDECDDDQANCHSGTGDDFQLTGGTTVLATEKPTVIDSTIQSGIK
Expression Range 22-644aa
Protein Length Full Length of Mature Protein of Isoform 2
Mol. Weight 98.8 kDa
Research Area Cardiovascular
Form Lyophilized powder
Buffer Lyophilized from a 0.2 μm filtered PBS, 6% Trehalose, pH 7.4
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 Cell-surface receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. Mediates the chemorepulsant activity of semaphorins. Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage. It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB. Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development. Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR.; Binds VEGF-165 and may inhibit its binding to cells. May induce apoptosis by sequestering VEGF-165. May bind as well various members of the semaphorin family. Its expression has an averse effect on blood vessel number and integrity.; (Microbial infection) Acts as a host factor for human coronavirus SARS-CoV-2 infection. Recognizes and binds to CendR motif RRAR on SARS-CoV-2 spike protein S1 which enhances SARS-CoV-2 infection.
Subcellular Location [Isoform 2]: Secreted.; Mitochondrion membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein. Cytoplasm.
Protein Families Neuropilin family
Database References
Tissue Specificity [Isoform 1]: The expression of isoforms 1 and 2 does not seem to overlap. Expressed by the blood vessels of different tissues. In the developing embryo it is found predominantly in the nervous system. In adult tissues, it is highly expressed in heart and

Gene Functions References

  1. HLA-G, NRP1, and PD-1, may be involved in the immune response in psoriatic patients PMID: 29790686
  2. miR-320/NRP-1 axis contributes to the growth and metastasis of cholangiocarcinoma cells. PMID: 28618167
  3. we demonstrated that HS3ST3B enhances the proliferation and survival of breast cancer MDA-MB-231 cells, via a mechanism that is dependent on Nrp1. PMID: 30360368
  4. The serum NRP1 was significantly associated with AFP, gamma-GT, Alb, bile acid, ALT, AST, ALP and pre-Alb. NRP1 is a novel tumor marker in HCC. PMID: 29966621
  5. lnc00152 was aberrantly overexpressed in colorectal tumors and cancer cells and that lnc00152 was modulated by miRNA206. lnc00152 overexpression promoted epithelial-mesenchymal transition and increased neuropilin1 expression in the colorectal cancer cells. PMID: 29956750
  6. the results presented herein indicate that NRP1 exerts tumor suppressive effects in NB, at least in part by regulating the expression of beta1 integrin PMID: 29750423
  7. NRP1 may be important in the etiology of menstrual migraine. PMID: 29671086
  8. clinical samples from apical periodontitis patients were obtained to analyse the expression of Sema3A/Nrp1. These results indicated that the bone destruction level expanded from days 7 to 35 PMID: 29457037
  9. Study demonstrated that NRP1+ cells possess tumor-initiating cells (TIC) properties, including the preferential expression of stemness markers, higher clonogenic and self-renewal potential, and increased cell migration capacity. These findings support an important role for NRP1 in the biology of lung cancer TICs. PMID: 29138851
  10. Authors demonstrated that when VEGFR2 was inhibited, NRP-1 appeared to regulate RAD51 expression through the VEGFR2-independent ABL-1 pathway, consequently regulating radiation sensitivity. In addition, the combined inhibition of VEGFR2 and NRP-1 appears to sensitize cancer cells to radiation. PMID: 29777301
  11. NRP1, as a promoter of odontoblast differentiation, regulates dental pulp stem cells via the classical Wnt/beta-catenin pathway. PMID: 28910136
  12. The new observation that shows strong NP-1 immunoreactivity of these particles, and decreased NP1 expression in syncytiotrophoblast of preeclampsia (PET) placentas in comparison to the control group, may imply a role of NP-1 in PET. PMID: 26937865
  13. rs2228638 of NRP1 may have a role in tetralogy of Fallot risk in European and Chinese Han populations PMID: 29432830
  14. Data show that neuropilin 1 (NRP1) binds extracellular AGO2 (carrying miRNA or not), and internalizes AGO2/miRNA complexes. PMID: 27486976
  15. Data suggest neuropilin-1 (NRP-1) as a therapeutic target to reduce tumor fibrosis and pancreatic ductal adenocarcinoma (PDAC) progression. PMID: 27542226
  16. Results suggest that targeting the transmembrane domains (TMD) of neuropilin-1 (NRP1) in breast cancer is a potent new strategy to fight against breast cancer and related metastasis. PMID: 27351129
  17. By blocking neuropilin-1 receptor (NRP-1) in tumor-bearing mice, luciferase activity in tumors delivered by HK polyplexes was reduced by 96%, whereas activity in normal tissues was minimally reduced. PMID: 27257039
  18. High NRP1 expression is associated with metastasis in triple-negative breast cancer. PMID: 26967387
  19. Overexpression of Neuropilin 1 incresed in breast cancer stem cells formation and breast cancer stem cells-induced tube formation and knockdown of Neuropilin 1 reduced CSCs-related traits. PMID: 29179185
  20. Nrp1 mediates the migratory behavior of mesangial cells. PMID: 28835419
  21. this study identified the NRP1 cytoplasmic domain as essential for acute vascular hyperpermeability induced by different NRP1 ligands: a ligand- blocking antibody against NRP1 and a CendR peptide. PMID: 27117252
  22. Data indicate that miR-206 inhibits neuropilin-1 (NRP1) and SMAD2 gene expression by directly binding to their 3'-UTRs. PMID: 27014911
  23. Results show that Nrp1 plays a critical role in balancing responsiveness to VEGF-A versus TGFbeta to regulate glioblastoma growth, progression, and recurrence after anti-vascular therapy. PMID: 28938007
  24. Data provide evidence that NRP1 functions to enhance the metastatic potential of prostate tumors. PMID: 28092670
  25. NRP1 is an important niche component PMID: 27676403
  26. our data suggest a novel molecular mechanism by which tMUC1 may modulate NRP1-dependent VEGFR signaling in PDA cells. PMID: 26804176
  27. Our findings identify aberrant active integrin b1-driven Src-Akt hyperactivation as a primary resistance mechanism to cetuximab in PDAC cells and offer an effective therapeutic strategy to overcome this resistance using an EGFR and NRP1 dual targeting antibody PMID: 27797376
  28. VEGF-A acts via interaction with NRP-1 to trigger intracellular events leading to ECS cell survival and formation of aggressive, invasive and highly vascularized tumors. PMID: 26804163
  29. These data identify a new molecular mechanism of brain microvascular endothelial inflammatory response through NRP1-IFNgamma crosstalk. PMID: 27591257
  30. This study indicates that capsaicin application results in significant loss of epidermal NRP-1 receptor expression, whereas diabetic subjects presenting small fiber neuropathy show full epidermal NRP-1 expression in contrast to the basal expression pattern seen in healthy controls PMID: 27598321
  31. Study show that a high percentage of intratumoral NRP1(+) Tregs correlates with poor prognosis in melanoma and head and neck squamous cell carcinoma. PMID: 28552348
  32. Study revels the structural description of the neuropilin-1 ectopic region by reporting the crystal structure of its MAM domain. The domain adopts a jellyroll fold that is stabilized by a Ca2+ ion while forming a molecular surface that is distinct from its structural homologs. PMID: 27720589
  33. Data suggest that neuropilin-1 (NRP1) functions as a receptor for neutrophil elastase (NE), mediates uptake/absorption of NE, and facilitates cross-presentation of PR1 (a peptide fragment of NE) in breast cancer cells. PMID: 28468826
  34. This report is the first study characterizing the specific functions of NRP1-Delta7, a glycosaminoglycan-defective neuropilin-1 splice variant that displays anti-tumorigenic properties in vitro and in vivo. PMID: 27798666
  35. this study shows that NRP1 can act as a co-receptor for PDGF-D-PDGFRbeta signaling and is possibly implicated in intercellular communication in the vascular wall PMID: 28254885
  36. This review provides a general overview of current knowledge of the signalling pathways that are modulated by NRP1, with particular focus on neuronal and vascular roles in the brain and retina. PMID: 26923176
  37. Curcumin-loaded nanoliposomes linked to homing peptides for integrin targeting and neuropilin-1-mediated internalization reduced viability of breast cancer cells. PMID: 27937055
  38. Upregulated expression of NRP1 is associated with glioma. PMID: 27481513
  39. Studies suggest that the activation of NRP-1 by PlGF directly contributes to tumour aggressiveness and to melanoma escape from anti-VEGF-A therapies. PMID: 26846845
  40. REVIEW: Nrp1 functions in the vasculature is critical for the development of targeted therapeutics for cancer and vascular diseases such as atherosclerosis and retinopathies. PMID: 26849476
  41. High Expression of Neuropilin-1 Associates with Hepatocellular Carcinoma. PMID: 26563279
  42. Increased NRP-1 expression is associated with metastatic endometrial and lung cancers. PMID: 26701889
  43. miR-152 suppression in NSCLC cells might promote neuropilin-1 mediated cancer metastasis. PMID: 26823738
  44. NRP-1 was found to be overexpressed in gastric cancer (GC) tissues, and its expression correlates with the clinical staging, tumor differentiation and pathological types of gastric cancer. PMID: 26795388
  45. NRP1 was targeted by miR130a and miR130b at the binding site of chromosome 10: 334668643466870, which was involved in the axon guidance signaling pathway. PMID: 26573160
  46. Semaphorin-3a, neuropilin-1 and plexin-A1 are axonal guidance molecules that have been recently implicated in regulating bone metabolism. PMID: 26602825
  47. neuropilin-1 is regulated in the oral epithelium and is selectively up-regulated during epithelial dysplasia PMID: 26877262
  48. NRP1 over-expression in miR-365 expressing cells could rescue invasion and growth defects of miR-365. In addition, miR-365 expression inversely correlated with NRP1 protein levels in malignant melanoma PMID: 26406949
  49. Data show that binding of pleiotrophin (PTN) to neuropilin-1 (NRP-1) stimulated the internalization and recycling of NRP-1 at the cell surface. PMID: 26408254
  50. Study found significant down-regulation of placental NRP-1 expression in fetal growth restriction pregnancies complicated with absent end-diastolic flow in the umbilical artery. PMID: 26409917

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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.

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