Influenza A H1N1 (A/California/07/2009) Hemagglutinin / HA Antibody, Rabbit PAb, Antigen Affinity Purified sinobiological 11085-T62

$86.00
In stock
SKU
11085-T62
Catalog No.SizePrice (USD)
11085-T62-2020 µL$88.87
11085-T62-5050 µL$147.96
11085-T62-100100 µL$251.64
11085-T62-200200 µL$355.32

General Information

Product nameInfluenza A H1N1 (A/California/07/2009) Hemagglutinin / HA Antibody, Rabbit PAb, Antigen Affinity Purified
Validated applicationsWB (FAQ Protocol), ELISA (FAQ Protocol)
Application notesIHC, FCM, IF, IP et al. applications haven't been validated. (Antibody's applications haven't been validated with corresponding virus positive samples. Optimal concentrations/dilutions should be determined by the end user.)
SpecificityInfluenza H1N1 (A/California/07/2009) Hemagglutinin / HA
ImmunogenRecombinant Influenza H1N1 (A/California/07/2009) Hemagglutinin / HA Protein (Catalog#11085-V08H)
PreparationProduced in rabbits immunized with purified, recombinant Influenza H1N1 (A/California/07/2009) Hemagglutinin / HA (Catalog#11085-V08H; ACP41953.1; Met1-Gln529). Influenza H1N1 (A/California/07/2009) Hemagglutinin / HA specific IgG was purified by Influenza H1N1 (A/California/07/2009) Hemagglutinin / HA affinity chromatography.
SourcePolyclonal Rabbit IgG
PurificationProtein A & Antigen Affinity
Formulation0.2 μm filtered solution in PBS
ConjugateUnconjugated
FormLiquid
ShippingThis antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
StorageThis antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.

Image / Experimental Information

Image 1 DescriptionAnti-HA rabbit polyclonal antibody at 1:2000 dilution. Sample:Influenza A H1N1 (A/California/07/2009) Hemagglutinin / HA Protein(Cat#11085-V08H) Lane A: 20ng Secondary Goat Anti-Rabbit IgG (H+L)/HRP at 1/10000 dilution Developed using the ECL technique. Performed under reducing conditions.
Image 1 Alt TextH1N1 Hemagglutinin/HA Western blot (WB) 35231
Image 1 URLSource image

Background Information

Full NameHemagglutinin
DescriptionThe influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
References
  1. White JM, Hoffman LR, Arevalo JH, et al. Attachment and entry of influenza virus into host cells. Pivotal roles of hemagglutinin. In Chiu W, Burnett RM, Garcea RL. Structural Biology of Viruses.1997
  2. Suzuki Y.Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses. Biol. Pharm. Bull. 2005.
  3. Senne DA, Panigrahy B, Kawaoka Y, et al. Survey of the hemagglutinin (HA) cleavage site sequence of H5 and H7 avian influenza viruses: amino acid sequence at the HA cleavage site as a marker of pathogenicity potential. Avian Dis. 1996
  4. Donald J. Benton,Influenza hemagglutinin membrane anchor,PNAS,2018

title: Complete substitution with modified nucleotides in self-amplifying RNA suppresses the interferon response and increases potency
authors: Joshua E. McGee; Jack R. Kirsch; ...; Mark W. Grinstaff
journal: Nature Biotechnology
date: 2026-01-08
pmid: 38977924
doi: 10.1038/s41587-024-02306-z
pmcid: 11707045
cited_by_count: 67
techniques: Bioprocessing; Centrifugation; Disruption; Enzyme-linked Immunosorbent Assay; Expressing; Flow Cytometry; Generated; Lysis; Membrane; Real-time Polymerase Chain Reaction; Reverse Transcription; Transferring
bioz_score: 95

title: Unveiling the Role of TMPRSS2 in the Proteolytic Activation of Pandemic and Zoonotic Influenza Viruses and Coronaviruses in Human Airway Cells.
authors: Marie Schwerdtner; Luna C Schmacke; ...; Eva Böttcher-Friebertshäuser
journal: Viruses
date: 2024-11-27
pmid: 39599912
doi: 10.3390/v16111798
cited_by_count: 2
techniques: Control; Derivative Assay; Expressing; Immunofluorescence; Infection; Plaque Assay; Plasmid Preparation; Recombinant; SDS Page; Sequencing; Staining; Titration; Western Blot
bioz_score: 95

title: Self-replicating RNA and uses thereof
authors: Joshua Edward McGee; Jack Rainier Kirsch; ...; Kexin Li
date: 2024-10-15
cited_by_count: 0
techniques: Disruption; Enzyme-linked Immunosorbent Assay; Lysis; Membrane
bioz_score: 95

title: A ferritin nanoparticle vaccine based on the hemagglutinin extracellular domain of swine influenza A (H1N1) virus elicits protective immune responses in mice and pigs.
authors: Pan Tang; Enhui Cui; ...; Huili Liu
journal: Frontiers in Immunology
date: 2024-06-05
pmid: 38835763
doi: 10.3389/fimmu.2024.1361323
cited_by_count: 7
techniques: Construct; Expressing; Infection; Purification; Recombinant; Titration
bioz_score: 95

title: ACE2 acts as a novel regulator of TMPRSS2-catalyzed proteolytic activation of influenza A virus in airway cells
authors: Miriam Ruth Heindl; Anna-Lena Rupp; ...; Eva Böttcher-Friebertshäuser
journal: Journal of virology
date: 2024-04-01
pmid: 38470058
doi: 10.1128/jvi.00102-24
pmcid: 11019950
cited_by_count: 6
techniques: Activation Assay; Activity Assay; Concentration Assay; Expressing; Incubation; Infection; Negative Control; Plaque Assay; Plasmid Preparation; Purification; Recombinant; SDS Page; Sequencing; Titration; Transfection; Virus; Western Blot
bioz_score: 95

title: Complete substitution with modified nucleotides suppresses the early interferon response and increases the potency of self-amplifying RNA
authors: McGee Joshua E.; Kirsch Jack R.; ...; Grinstaff Mark W.
journal: bioRxiv
date: 2023-09-17
cited_by_count: 0
techniques: Disruption; Enzyme-linked Immunosorbent Assay; Lysis; Membrane; Transferring
bioz_score: 95

title: Expression of TMPRSS2 is up-regulated by bacterial flagellin, LPS, and Pam3Cys in human airway cells
authors: Marie Schwerdtner; Annika Skalik; ...; Eva Böttcher-Friebertshäuser
journal: Life science alliance
date: 2023-05-19
pmid: 37208193
doi: 10.26508/lsa.202201813
pmcid: 10200810
cited_by_count: 1
techniques: Generated; Incubation; Infection; Plaque Assay; SDS Page; Software; Titration; Western Blot
bioz_score: 95

title: Pandemic influenza A (H1N1) virus causes abortive infection of primary human T cells
authors: Jiapei Yu; Hui Li; ...; Bin Cao
journal: Emerging microbes & infections
date: 2022-04-25
pmid: 35317717
doi: 10.1080/22221751.2022.2056523
pmcid: 9045768
cited_by_count: 16
techniques: Blocking Assay; Co-Culture Assay; Expressing; Immunofluorescence; Incubation; Infection; Microscopy; Sequencing; Staining; Two Tailed Test
bioz_score: 95

title: Glycan arrays for high throughput screening of viruses
authors: Chi-Huey Wong; Chung-Yi Wu; ...; An-Suei Yang
date: 2019-07-02
cited_by_count: 0
techniques: Binding Assay; Labeling; Virus
bioz_score: 95

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