KDM4C / GASC1 / JMJD2C Antibody - #DF13567
| Product: | KDM4C / GASC1 / JMJD2C Antibody |
| Catalog: | DF13567 |
| Description: | Rabbit polyclonal antibody to KDM4C / GASC1 / JMJD2C |
| Application: | WB |
| Reactivity: | Human, Mouse, Rat |
| Mol.Wt.: | 119kDa, 200 kDa; 120kD(Calculated). |
| Uniprot: | Q9H3R0 |
| RRID: | AB_2846586 |
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Protocols
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# DF13567, RRID:AB_2846586.
Fold/Unfold
bA146B14.1; GASC 1 protein; GASC-1 protein; GASC1; Gene amplified in squamous cell carcinoma 1 protein; JHDM3C; JmjC domain containing histone demethylation protein 3C; JmjC domain-containing histone demethylation protein 3C; JMJD2C; Jumonji domain containing 2C; Jumonji domain containing protein 2C; Jumonji domain-containing protein 2C; Kdm4c; KDM4C_HUMAN; Lysine (K) specific demethylase 4C; Lysine demethylase 4C; Lysine-specific demethylase 4C; TDRD14C; Tudor domain containing 14C;
Immunogens
A synthesized peptide derived from human KDM4C / GASC1 / JMJD2C, corresponding to a region within the internal amino acids.
- Q9H3R0 KDM4C_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MEVAEVESPLNPSCKIMTFRPSMEEFREFNKYLAYMESKGAHRAGLAKVIPPKEWKPRQCYDDIDNLLIPAPIQQMVTGQSGLFTQYNIQKKAMTVKEFRQLANSGKYCTPRYLDYEDLERKYWKNLTFVAPIYGADINGSIYDEGVDEWNIARLNTVLDVVEEECGISIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAQGFFPSSSQGCDAFLRHKMTLISPSVLKKYGIPFDKITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATVRWIDYGKVAKLCTCRKDMVKISMDIFVRKFQPDRYQLWKQGKDIYTIDHTKPTPASTPEVKAWLQRRRKVRKASRSFQCARSTSKRPKADEEEEVSDEVDGAEVPNPDSVTDDLKVSEKSEAAVKLRNTEASSEEESSASRMQVEQNLSDHIKLSGNSCLSTSVTEDIKTEDDKAYAYRSVPSISSEADDSIPLSSGYEKPEKSDPSELSWPKSPESCSSVAESNGVLTEGEESDVESHGNGLEPGEIPAVPSGERNSFKVPSIAEGENKTSKSWRHPLSRPPARSPMTLVKQQAPSDEELPEVLSIEEEVEETESWAKPLIHLWQTKSPNFAAEQEYNATVARMKPHCAICTLLMPYHKPDSSNEENDARWETKLDEVVTSEGKTKPLIPEMCFIYSEENIEYSPPNAFLEEDGTSLLISCAKCCVRVHASCYGIPSHEICDGWLCARCKRNAWTAECCLCNLRGGALKQTKNNKWAHVMCAVAVPEVRFTNVPERTQIDVGRIPLQRLKLKCIFCRHRVKRVSGACIQCSYGRCPASFHVTCAHAAGVLMEPDDWPYVVNITCFRHKVNPNVKSKACEKVISVGQTVITKHRNTRYYSCRVMAVTSQTFYEVMFDDGSFSRDTFPEDIVSRDCLKLGPPAEGEVVQVKWPDGKLYGAKYFGSNIAHMYQVEFEDGSQIAMKREDIYTLDEELPKRVKARFSTASDMRFEDTFYGADIIQGERKRQRVLSSRFKNEYVADPVYRTFLKSSFQKKCQKRQ
Research Backgrounds
Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.
Nucleus.
Overexpressed in several esophageal squamous cell carcinomas (ESCs).
The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails (By similarity).
Belongs to the JHDM3 histone demethylase family.
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