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Merck
CN

ABE551

Anti-E3 ubiquitin-protein ligase UHRF1 Antibody

from rabbit, purified by affinity chromatography

别名:

E3 ubiquitin-protein ligase UHRF1, Inverted CCAAT box-binding protein of 90 kDa, Nuclear protein 95, Nuclear zinc finger protein Np95, HuNp95, hNp95, RING finger protein 106, Transcription factor ICBP90, Ubiquitin-like PHD and RING finger domain-containi

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IHC, WB
Citations:
1
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biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human

species reactivity (predicted by homology)

primate (based on 100% sequence homology), bovine (based on 100% sequence homology), porcine (based on 100% sequence homology), feline (based on 100% sequence homology), horse (based on 100% sequence homology), canine (based on 100% sequence homology)

technique(s)

immunohistochemistry: suitable, western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

Gene Information

bovine ... Uhrf1(530411)
dog ... Uhrf1(611463)
human ... UHRF1(29128)
pig ... Uhrf1(100511003)

General description

Ubiquitin-like with PHD and ring finger domains 1 (UHRF1), also known as ICBP90 or Np95, is a multifunctional nuclear protein that may be an important mediator of heterochromatin formation which is indicative of gene repression. UHRF1 contains a set and RING-finger-associated domain that detects hemi-methylated cytosine residues leading to the recruitment of DNMT1 to these residues during the S phase. UHRF1 thereby facilitates the transfer of methylation status to newly synthesized DNA molecules. UHRF1 may also interact with histones and HDAC1 via its PHD domain to promote modifications of histone residues which contribute to heterochromatin formation. UHRF1 may also directly modify histone H3 by ubiquitination. In addition, UHRF1 may contribute to the DNA-repair process though associations with PCNA. Several studies have suggested that overexpression of UHRF1 may contribute to the development of many cancers.
~97 kDa observed

Immunogen

KLH-conjugated linear peptide corresponding to a region near the C-terminus of human E3 ubiquitin-protein ligase UHRF1.

Application

Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected E3 ubiquitin-protein ligase UHRF1 in human breast cancer tissue.
Detect UHRF1 using this rabbit polyclonal antibody, Anti-E3 ubiquitin-protein ligase UHRF1 Antibody validated for use in western blotting & IHC.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Chromatin Biology

Physical form

Affinity purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Evaluated by Western Blotting in HEK293 cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected E3 ubiquitin-protein ligase UHRF1 in 10 µg of HEK293 cell lysate.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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存储类别

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Lingyu Qiu et al.
Nucleic acids research, 51(17), 9166-9182 (2023-07-28)
Histone deacetylase 6 (HDAC6) mediates DNA damage signaling by regulating the mismatch repair and nucleotide excision repair pathways. Whether HDAC6 also mediates DNA double-strand break (DSB) repair is unclear. Here, we report that HDAC6 negatively regulates DSB repair in an

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