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Neuropilin-1 Recombinant Rabbit mAb

Neuropilin-1 Recombinant Rabbit mAb

     
  • 1 - Neuropilin-1 Recombinant Rabbit mAb AP94009
    Sample:
    Lane 1: Mouse Heart Lysates
    Lane 2: Mouse Spinal cord Lysates
    Lane 3: Rat Kidney Lysates


    Primary: Anti-Neuropilin-1 (AP94009) at 1/1000 dilution
    Secondary: IRDye800CW Goat Anti-Rabbit IgG at 1/20000 dilution
    Predicted band size: 103kDa
    Observed band size: 130kDa
  • 14 - Neuropilin-1 Recombinant Rabbit mAb AP94009
    Paraformaldehyde-fixed, paraffin embedded (human pancreatic cancer); Antigen retrieval by boiling in sodium citrate buffer (pH6.0) for 15min; Block endogenous peroxidase by 3% hydrogen peroxide for 20 minutes; Blocking buffer (normal goat serum) at 37°C for 30min; Antibody incubation with (Neuropilin-1 ) Monoclonal Antibody, Unconjugated (AP94009) at 1:200 overnight at 4°C, followed by operating according to SP Kit(Rabbit) (sp-0023) instructionsand DAB staining.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, IHC-F, IF
Primary Accession O14786
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Recombinant
Calculated MW 103134 Da
Physical State Liquid
Immunogen KLH conjugated synthetic peptide derived from human Neuropilin-1
Purity affinity purified by Protein A
Buffer 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
SUBCELLULAR LOCATION Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted.
SIMILARITY Belongs to the neuropilin family. Contains 2 CUB domains. Contains 2 F5/8 type C domains. Contains 1 MAM domain.
SUBUNIT Homodimer, and heterodimer with NRP2. Interacts with FER. Binds PLXNB1.
Important Note This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
Background Descriptions This gene encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Neuropilins contain a large N-terminal extracellular domain, made up of complement-binding, coagulation factor V/VIII, and meprin domains. These proteins also contains a short membrane-spanning domain and a small cytoplasmic domain. Neuropilins bind many ligands and various types of co-receptors; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. Several alternatively spliced transcript variants that encode different protein isoforms have been described for this gene. [provided by RefSeq, Oct 2011]
Additional Information
Gene ID 8829
Other Names Neuropilin-1, Vascular endothelial cell growth factor 165 receptor, CD304, NRP1 (HGNC:8004), NRP, VEGF165R
Target/Specificity The expression of isoforms 1 and 2 does not seem to overlap. Isoform 1 is 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 placenta; moderately in lung, liver, skeletal muscle, kidney and pancreas; and low in adult brain. Isoform 2 is found in liver hepatocytes, kidney distal and proximal tubules.
Dilution WB=1:500-2000,IHC-P=1:50-200,IHC-F=1:50-200,IF=1:50-200
StorageStore at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
Protein Information
Name NRP1 (HGNC:8004)
Synonyms NRP, VEGF165R
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 (PubMed:10688880, PubMed:9288753, PubMed:9529250). Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage (PubMed:19805273). It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB (PubMed:10688880, PubMed:19805273, PubMed:9288753, PubMed:9529250). 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 (PubMed:30623799).
Cellular Location [Isoform 2]: Secreted
Tissue Location [Isoform 1]: The expression of isoforms 1 and 2 does not seem to overlap. Expressed in olfactory epithelium (at protein level) (PubMed:33082293). Expressed in fibroblasts (at protein level) (PubMed:36213313). 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 placenta; moderately in lung, liver, skeletal muscle, kidney and pancreas; and low in adult brain (PubMed:10688880, PubMed:9529250). Expressed in the central nervous system, including olfactory related regions such as the olfactory tubercles and paraolfactory gyri (PubMed:33082293)
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

This gene encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Neuropilins contain a large N-terminal extracellular domain, made up of complement-binding, coagulation factor V/VIII, and meprin domains. These proteins also contains a short membrane-spanning domain and a small cytoplasmic domain. Neuropilins bind many ligands and various types of co-receptors; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. Several alternatively spliced transcript variants that encode different protein isoforms have been described for this gene. [provided by RefSeq, Oct 2011]

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