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Anti-HCoV-229E Spike S1 Rabbit pAb

Purified Rabbit Polyclonal Antibody

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货号 规格 价格
P104503
20µL ¥588.00
50µL ¥1080.00
100µL ¥1780.00

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Anti-HCoV-229E Spike S1 Rabbit pAb
Product NameAnti-HCoV-229E Spike S1 Rabbit pAb
DescriptionPurified Rabbit Polyclonal Antibody
Application
  • Applications Legend:
  • WB=Western Blotting
  • IHC-P=Immunohistochemistry (Paraffin)
  • IHC-F=Immunohistochemistry (Frozen)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, ELISA
DilutionWB 1:500~1:1,000
ReactivityHCoV-229E
HostRabbit
ClonalityPolyclonal
IsotypeIgG
LabelUnconjugated
ImmunogenA synthetic peptide corresponding to a sequence within amino acids 1074-1173 of coronavirus Spike S1 (NP_073551.1).
FormatAffinity purified polyclonal antibody supplied in PBS with 0.02% sodium azide and 50% glycerol, pH 7.3.
SynonymsSpike protein S1; S1 protein; Spike glycoprotein Subunit 1; S glycoprotein Subunit 1; Spike S1.
Molecular weightCalculated MW: 129 kDa; Observed MW: 160 kDa
Uniprot ID P15423
Gene ID 918758
StorageShipped on wet ice. Store at -20℃. Stable for 24 months from date of receipt. Aliquoting is unnecessary for -20℃ storage.
PrecautionsAnti-HCoV-229E Spike S1 Rabbit pAb is for research use only and not for use in diagnostic or therapeutic procedures.
Background S1 region attaches the virion to the cell membrane by interacting with host ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.

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