Item no. |
PTM-215 |
Manufacturer |
PTM Biolabs
|
Amount |
100 ul |
Category |
|
Type |
Antibody Monoclonal |
Format |
Lyophilized powder |
Applications |
WB |
Specific against |
Human (Homo sapiens), Mouse (Murine, Mus musculus), Rat (Rattus norvegicus) |
Host |
Mouse |
Isotype |
IgG |
Conjugate/Tag |
Unconjugated |
Citations |
Bing Zhou, et al. Amelioration of nonalcoholic fatty liver disease by inhibiting the deubiquitylating enzyme RPN11. Cell Metabolism, 2024. https://www.cell.com/cell-metabolism/abstract/S1550-4131(24)00285-7. |
ECLASS 10.1 |
42030590 |
ECLASS 11.0 |
42030590 |
UNSPSC |
12352203 |
Alias |
H3K14pr |
Shipping condition |
Room temperature |
Available |
|
Manufacturer - Type |
Primary Antibodies |
Manufacturer - Category |
Histone & Histone Modification Antibodies |
Manufacturer - Targets |
Histone H3 |
Shipping Temperature |
Ambient temperature |
Storage Conditions |
Store at -20°C. Avoid freeze/thaw cycles. |
Molecular Weight |
15 |
Stability |
Stable for 12 months from date of receipt/reconstitution. |
Manufacturer - Research Area |
Epigenetics |
Product description |
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Lysine propionylation (Kprop) is structurally similar to lysine acetylation, is a newly identified reversible modification controlling protein activity. Lysine propionylation is abundant in both prokaryotes and eukaryotes and has been found in wide ranges of proteins including histones and non-histone substrates, such as p53. Similar to acetylation of histone H3 at Lys12, propionylation of histone H3 at Lys14 may play a vital role in the epigenetic modulation, including chromatin remodeling and transcriptional regulation. |
Purification Method |
Protein G and immunogen affinity purified |
Formula |
PBS, Glycerol, BSA |
PTM |
Propionyl |
Modification Site |
Lys14 |
Clonality |
Monoclonal |
Background |
Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Lysine propionylation (Kprop) is structurally similar to lysine acetylation, is a newly identified reversible modification controlling protein activity. Lysine propionylation is abundant in both prokaryotes and eukaryotes and has been found in wide ranges of proteins including histones and non-histone substrates, such as p53. Similar to acetylation of histone H3 at Lys12, propionylation of histone H3 at Lys14 may play a vital role in the epigenetic modulation, including chromatin remodeling and transcriptional regulation. |
Cellular Localization |
Nucleus |
Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.
All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.