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AB219291

Recombinant Rat Neuropilin 1 protein (His tag C-Terminus)

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Recombinant Rat Neuropilin 1 protein (His tag C-Terminus) is a Rat Fragment protein, in the 22 to 855 aa range, expressed in Baculovirus infected insect cells, with >90%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.

View Alternative Names

CD304, Neuropilin-1, Vascular endothelial cell growth factor 165 receptor, Nrp1

1 Images
SDS-PAGE - Recombinant Rat Neuropilin 1 protein (His tag C-Terminus) (AB219291)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Rat Neuropilin 1 protein (His tag C-Terminus) (AB219291)

15% SDS-PAGE analysis of 3 μg ab219291.

Molecular weight : 100-150 kDa (SDS-PAGE under reducing conditions).

Key facts

Purity

>90% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Baculovirus infected insect cells

Tags

His tag C-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9QWJ9

Animal free

No

Carrier free

No

Species

Rat

Storage buffer

pH: 7.4 Constituents: PBS, 10% Glycerol (glycerin, glycerine)

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"FRSDKCGGTIKIENPGYLTSPGYPHSYHPSEKCEWLIQAPEPYQRIMINFNPHFDLEDRDCKYDYVEVIDGENEGGRLWGKFCGKIAPSPVVSSGPFLFIKFVSDYETHGAGFSIRYEIFKRGPECSQNYTAPTGVIKSPGFPEKYPNSLECTYIIFAPKMSEIILEFESFDLEQDSNPPGGVFCRYDRLEIWDGFPEVGPHIGRYCGQKTPGRIRSSSGILSMVFYTDSAIAKEGFSANYSVLQSSISEDFKCMEALGMESGEIHSDQITASSQYGTNWSVERSRLNYPENGWTPGEDSYREWIQVDLGLLRFVTAVGTQGAISKETKKKYYVKTYRVDISSNGEDWITLKEGNKAIIFQGNTNPTDVVFGVFPKPLITRFVRIKPASWETGISMRFEVYGCKITDYPCSGMLGMVSGLISDSQITASNQGDRNWMPENIRLVTSRTGWALPPSPHPYINEWLQVDLGDEKIVRGVIIQGGKHRENKVFMRKFKIAYSNNGSDWKMIMDDSKRKAKSFEGNNNYDTPELRAFTPLSTRFIRIYPERATHSGLGLRMELLGCEVEVPTAGPTTPNGNPVDECDDDQANCHSGTGDDFQLTGGTTVLATEKPTIIDSTIQSEFPTYGFNCEFGWGSHKTFCHWEHDSHAQLRWRVLTSKTGPIQDHTGDGNFIYSQADENQKGKVARLVSPVVYSQSSAHCMTFWYHMSGSHVGTLRVKLHYQKPEEYDQLVWMVVGHQGDHWKEGRVLLHKSLKLYQVIFEGEIGKGNLGGIAVDDISINNHIPQEDCAKPTDLDKKNTEIKIDETGSTPGYEEGKGDKNISRKPGNVLKTLDPLEHHHHHH","proteinLength":"Fragment","predictedMolecularWeight":"94.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":855,"aminoAcidStart":22,"nature":"Recombinant","expressionSystem":"Baculovirus infected insect cells","accessionNumber":"Q9QWJ9","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Neuropilin-1 also known as NRP1 is a transmembrane protein with a significant role in the nervous and vascular systems. It has a molecular mass of approximately 130 kDa. Neuropilin-1 expression occurs broadly in tissues including neurons endothelial cells and tumor cells. Its structure includes a large extracellular domain that binds various ligands mediating several cellular functions. Neuropilin-1 is sometimes targeted in experiments using methods like neuropilin-1 ELISA and PE immunofluorescence to study its distribution and function in different tissues.
Biological function summary

Neuropilin-1 serves as a co-receptor for both the Vascular Endothelial Growth Factor (VEGF) and Semaphorin family proteins. It plays an important role in processes such as angiogenesis axonal guidance and the immune system. Neuropilin-1 does not function alone; it forms complexes with neuropilin-2 and other receptors like Plexin and VEGFR enhancing signal transduction pathways for angiogenesis and neuronal development. This involvement allows cells to respond appropriately to their environment especially during organismal development and repair processes.

Pathways

Neuropilin-1 facilitates interactions within the VEGF and Semaphorin pathways. In the VEGF pathway Neuropilin-1 enhances binding and signaling efficiency with VEGF closely working alongside VEGFR to promote endothelial cell survival migration and new blood vessel formation. In the Semaphorin pathway Neuropilin-1 interacts with Plexins mediating neuronal pathfinding and axonal growth. These interactions highlight Neuropilin-1's adaptive capabilities in various physiological processes critical for system development.

Neuropilin-1 is linked to pathological conditions like cancer and cardiovascular diseases. Neuropilin-1 overexpression is frequently observed in tumors driving cancer progression through enhanced angiogenesis and tissue invasion closely interacting with proteins like VEGF-A. In cardiovascular disease Neuropilin-1 contributes to abnormal blood vessel formation and stability. By studying Neuropilin-1 and other biomarkers like CD304 FITC researchers aim to develop therapeutic strategies targeting its role in these diseases.
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Specifications

Form

Liquid

Additional notes

Affinity purified

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General info

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 (By similarity). 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 (By similarity). Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR (By similarity).

Sequence similarities

Belongs to the neuropilin family.

Subcellular localisation

Mitochondrion membrane

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Product protocols

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Target data

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 (By similarity). 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 (By similarity). Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR (By similarity).
See full target information Nrp1
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Assay Kits

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Proteins & Peptides

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