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>   首页   >   产品   >   一抗   >   其他   >    Histone H1 (Nuclear Marker) Antibody - With BSA and Azide   

Histone H1 (Nuclear Marker) Antibody - With BSA and Azide

Mouse Monoclonal Antibody [Clone AE-4 ]

     
  • 2 -  Histone H1 (Nuclear Marker) Antibody - With BSA and Azide AH11387
    Formalin-fixed, paraffin-embedded human Tonsil stained with Histone H1 Monoclonal Antibody (AE-4)
  • 2 -  Histone H1 (Nuclear Marker) Antibody - With BSA and Azide AH11387
    Formalin-fixed, paraffin-embedded human Ovarian Carcinoma stained with Histone H1 Monoclonal Antibody (AE-4)
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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
IHC, IF, FC
Other Accession 3005, 226117, 97358
Reactivity Human, Mouse, Rat
Host Mouse
Clonality Monoclonal
Isotype Mouse / IgG2a, kappa
Clone Names AE-4
Calculated MW 30 KDa
Additional Information
Application Note IHC~~1:100~500
IF~~1:50~200
FC~~1:10~50
StorageStore at 2 to 8°C.Antibody is stable for 24 months.
Precautions Histone H1 (Nuclear Marker) Antibody - With BSA and Azide is for research use only and not for use in diagnostic or therapeutic procedures.
Research Areas

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

BACKGROUND

Eukaryotic histones are basic and water-soluble nuclear proteins that form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.

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