ArtNr |
PTM-215 |
Hersteller |
PTM Biolabs
|
Menge |
100 ul |
Kategorie |
|
Typ |
Antibody Monoclonal |
Format |
Lyophilized powder |
Applikationen |
WB |
Specific against |
Human (Homo sapiens), Mouse (Murine, Mus musculus), Rat (Rattus norvegicus) |
Host |
Mouse |
Isotype |
IgG |
Konjugat/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 |
Versandbedingung |
Raumtemperatur |
Lieferbar |
|
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 |
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Alle Produkte sind nur für Forschungszwecke bestimmt. Nicht für den menschlichen, tierärztlichen oder therapeutischen Gebrauch.