Recombinant
RabMAb

Recombinant Anti-Fibrillarin antibody [EPR10823(B)] - Nucleolar Marker (HRP) (ab196980)

Overview

  • Product name

    Anti-Fibrillarin antibody [EPR10823(B)] - Nucleolar Marker (HRP)
    See all Fibrillarin primary antibodies
  • Description

    Rabbit monoclonal [EPR10823(B)] to Fibrillarin - Nucleolar Marker (HRP)
  • Host species

    Rabbit
  • Conjugation

    HRP
  • Tested applications

    Suitable for: WBmore details
  • Species reactivity

    Reacts with: Human
    Predicted to work with: Mouse, Rat
  • Immunogen

    Synthetic peptide corresponding to residues in Human Fibrillarin was used as an immunogen (UniProt ID: P22087). (The amino acid sequence is considered to be commercially sensitive).

  • Positive control

    • WB: HEK293, HeLa, HepG2 and MOLT4 whole cell lysates.
  • General notes

    Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMab® patents.

    This product is a recombinant rabbit monoclonal antibody.

Properties

Applications

Our Abpromise guarantee covers the use of ab196980 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/5000. Detects a band of approximately 33 kDa (predicted molecular weight: 33 kDa).

Target

  • Function

    S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (PubMed:24352239).
  • Sequence similarities

    Belongs to the methyltransferase superfamily. Fibrillarin family.
  • Post-translational
    modifications

    By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA).
  • Cellular localization

    Nucleus, nucleolus. Fibrillar region of the nucleolus.
  • Information by UniProt
  • Database links

  • Alternative names

    • 34 kD nucleolar scleroderma antigen antibody
    • 34 kDa nucleolar scleroderma antigen antibody
    • Fbl antibody
    • FBRL_HUMAN antibody
    • FIB antibody
    • FIB1 antibody
    • FLRN antibody
    • Histone-glutamine methyltransferase antibody
    • Nop1p antibody
    • RNA U3 small nucleolar interacting protein 1 antibody
    • RNU3IP1 antibody
    • rRNA 2' O methyltransferase fibrillarin antibody
    • rRNA 2'-O-methyltransferase fibrillarin antibody
    see all

Images

  • All lanes : Anti-Fibrillarin antibody [EPR10823(B)] - Nucleolar Marker (HRP) (ab196980) at 1/5000 dilution

    Lane 1 : HEK293 (Human) Whole Cell Lysate (ab52256)
    Lane 2 : HeLa whole cell lysate (ab150035)
    Lane 3 : HepG2 (Human hepatocellular liver carcinoma cell line) Whole Cell Lysate
    Lane 4 : MOLT4 (Human acute lymphoblastic leukemia cell line) Whole Cell Lysate

    Lysates/proteins at 10 µg per lane.

    Developed using the ECL technique.

    Performed under reducing conditions.

    Predicted band size: 33 kDa
    Observed band size: 33 kDa


    Exposure time: 8 minutes


    This blot was produced using a 4-12% Bis-tris gel under the MOPS buffer system. The gel was run at 200V for 50 minutes before being transferred onto a Nitrocellulose membrane at 30V for 70 minutes. The membrane was then blocked for an hour using 3% milk before being incubated with ab196980 overnight at 4°C. Antibody binding was visualised using ECL development solution ab133406.

References

ab196980 has not yet been referenced specifically in any publications.

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