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Jarid1C / SMCX peptide
See all KDM5C / Jarid1C / SMCX products (2) ...
Synthetic peptide derived from within residues 1500 to the C-terminus of Human Jarid1C / SMCX.(Note: the amino acid sequence is proprietary)This peptide was used as an immunogen for ab34718 - Jarid1C / SMCX antibody.
1560 amino acids
Liquid
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Information available upon request.
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Epigenetics and Nuclear Signaling >> Chromatin Modifying Enzymes >> Jumonji containing proteins
Epigenetics and Nuclear Signaling >> Transcription >> Co-factors
Epigenetics and Nuclear Signaling >> Transcription >> Other factors
Epigenetics and Nuclear Signaling >> Nuclear Signaling Pathways >> Nuclear Receptors >> Co-activators/co-repressors
This peptide can be used with studies using ab34718.
Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcriptional repression of neuronal genes by recruiting histone deacetylases and REST at neuron-restrictive silencer elements.
Expressed in all tissues examined. Highest levels found in brain and skeletal muscle.
Defects in KDM5C are the cause of mental retardation syndromic X-linked JARID1C-related (MRXSJ) [MIM:300534]. MRXSJ is characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. MRXSJ patients manifest mental retardation associated with variable features such as slowly progressive spastic paraplegia, seizures, facial dysmorphism.
Belongs to the JARID1 histone demethylase family.
Contains 1 ARID domain.
Contains 1 JmjC domain.
Contains 1 JmjN domain.
Contains 2 PHD-type zinc fingers.
The first PHD-type zinc finger domain recognizes and binds H3-K9Me3.
Both the JmjC domain and the JmjN domain are required for enzymatic activity.
Nucleus.
Target information above from: UniProt accessionP41229
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
ab35501 has not yet been referenced specifically in any publications.
Publishing research using ab35501? Please let us know so that we can cite the reference in this datasheet
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