产品名称
Anti-BAF (BANF1) Antibody, serum, from rabbit
biological source
rabbit
conjugate
unconjugated
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
rat, mouse, human
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... BANF1(8815)
Analysis Note
Evaluated by Western Blot in HeLa cell lysate.
Western Blot Analysis: A 1:1,000 dilution of this antibody detected BAF in 10 µg of HeLa cell lysate.
Western Blot Analysis: A 1:1,000 dilution of this antibody detected BAF in 10 µg of HeLa cell lysate.
Application
Use Anti-BAF (BANF1) Antibody (Rabbit Polyclonal Antibody) validated in WB to detect BAF (BANF1) also known as 53 kDa BRG1-associated factor A.
Western Blot Analysis: A 1:1,000 dilution from a previous lot detected BAF in C2C12, Hek293, HeLa, HepG2, Huvec, Jurkat, L6, NIH/3T3, PC12, PC3, and RAW264.7 cell lysates.
Biochem/physiol Actions
This antibody recognizes BAF (BANF1).
General description
Barrier-to-auto integration factor (BAF or BANF1) plays fundamental roles in nuclear assembly, chromatin organization, gene expression and development. BAF may potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. BAF contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging. BAF is exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. BAF is found in both the nucleus and cytoplasm and is significantly enriched at the nuclear inner membrane, diffused throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase.
~10 kDa
Immunogen
KLH-conjugated linear peptide corresponding to human BAF (BANF1).
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存储类别
10 - Combustible liquids
wgk
WGK 1
Chih-Cheng Yang et al.
F1000Research, 3, 115-115 (2014-09-02)
NKX3.1 is a homeobox transcription factor whose function as a prostate tumor suppressor remains insufficiently understood because neither the transcriptional program governed by NKX3.1, nor its interacting proteins have been fully revealed. Using affinity purification and mass spectrometry, we have
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