Recombinant Human NFkB p100 / p52 protein (ab125611)

Overview

  • Product nameRecombinant Human NFkB p100 / p52 protein
  • Protein lengthFull length protein

Description

  • NatureRecombinant
  • SourceBaculovirus infected Sf9 cells
  • Amino Acid Sequence
    • AccessionQ00653
    • SpeciesHuman
    • Molecular weight84 kDa including tags
    • Amino acids1 to 454

Associated products

Specifications

Our Abpromise guarantee covers the use of ab125611 in the following tested applications.

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

  • Applications

    Western blot

    SDS-PAGE

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 7.50
    Constituents: 0.31% Glutathione, 0.002% PMSF, 0.005% DTT, 0.79% Tris HCl, 0.003% EDTA, 25% Glycerol, 0.88% Sodium chloride

General Info

  • Alternative names
    • CVID10
    • DNA binding factor KBF2
    • DNA-binding factor KBF2
    • H2TF1
    • Lymphocyte translocation chromosome 10
    • Lymphocyte translocation chromosome 10 protein
    • Lyt 10
    • Lyt10
    • NF kB2
    • NFKB2
    • NFKB2_HUMAN
    • Nuclear factor NF kappa B p100 subunit
    • Nuclear factor NF kappa B p52 subunit
    • Nuclear factor NF-kappa-B p52 subunit
    • Nuclear factor of kappa light chain gene enhancer in B cells 2
    • Nuclear factor of kappa light polypeptide gene enhancer in B cells 2
    • Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2
    • Oncogene Lyt 10
    • Oncogene Lyt-10
    • p105
    • p49/p100
    see all
  • FunctionNF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65.
  • Involvement in diseaseNote=A chromosomal aberration involving NFKB2 is found in a case of B-cell non Hodgkin lymphoma (B-NHL). Translocation t(10;14)(q24;q32) with IGHA1. The resulting oncogene is also called Lyt-10C alpha variant.
    Note=A chromosomal aberration involving NFKB2 is found in a cutaneous T-cell leukemia (C-TCL) cell line. This rearrangement produces the p80HT gene which encodes for a truncated 80 kDa protein (p80HT).
    Note=In B-cell leukemia (B-CLL) cell line, LB40 and EB308, can be found after heterogeneous chromosomal aberrations, such as internal deletions.
  • Sequence similaritiesContains 7 ANK repeats.
    Contains 1 death domain.
    Contains 1 RHD (Rel-like) domain.
  • DomainThe C-terminus of p100 might be involved in cytoplasmic retention, inhibition of DNA-binding by p52 homodimers, and/or transcription activation.
    The glycine-rich region (GRR) appears to be a critical element in the generation of p52.
  • Post-translational
    modifications
    While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p52 making it an acceptable substrate for the proteasome. This process is known as cotranslational processing. The processed form is active and the unprocessed form acts as an inhibitor (I kappa B-like), being able to form cytosolic complexes with NF-kappa B, trapping it in the cytoplasm. Complete folding of the region downstream of the GRR repeat precludes processing.
    Subsequent to MAP3K14-dependent serine phosphorylation, p100 polyubiquitination occurs then triggering its proteasome-dependent processing.
    Constitutive processing is tightly suppressed by its C-terminal processing inhibitory domain, named PID, which contains the death domain.
  • Cellular localizationNucleus. Cytoplasm. Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor.
  • Information by UniProt

Recombinant Human NFkB p100 / p52 protein images

  • SDS-PAGE analysis of ab125611.

References for Recombinant Human NFkB p100 / p52 protein (ab125611)

ab125611 has not yet been referenced specifically in any publications.

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