Home Cart Sign in  
Chemical Structure| 158171-14-3 Chemical Structure| 158171-14-3
Chemical Structure| 158171-14-3

*Storage: {[sel_prStorage]}

*Shipping: {[sel_prShipping]}

,{[proInfo.pro_purity]}

Fmoc-Ser(HPO3Bzl)-OH is a derivative of serine.

Synonyms: Fmoc-Ser(HPO3Bzl)-OH

4.5 *For Research Use Only !

{[proInfo.pro_purity]}
Cat. No.: {[proInfo.prAm]} Purity: {[proInfo.pro_purity]}

Change View

Size Price VIP Price

US Stock

Global Stock

In Stock
{[ item.pr_size ]} Inquiry {[ getRatePrice(item.pr_usd,item.pr_rate,item.mem_rate,item.pr_is_large_size_no_price, item.vip_usd) ]}

US Stock: ship in 0-1 business day
Global Stock: ship in 5-7 days

  • {[ item.pr_size ]}

In Stock

- +

Please Login or Create an Account to: See VIP prices and availability

US Stock: ship in 0-1 business day
Global Stock: ship in 2 weeks

  • 1-2 Day Shipping
  • High Quality
  • Technical Support
Product Citations

Product Citations

Abeywardana, Maheeshi Yapa ; Whedon, Samuel D ; Lee, Kwangwoon ; Nam, Eunju ; Dovarganes, Rafael ; Dubois-Coyne, Sarah , et al.

Abstract: Sirtuin 2 (Sirt2) is a member of the family of NAD-dependent lysine deacylases and plays important roles in regulation of the and gene expression. As a nucleocytoplasmic deacetylase, Sirt2 has been shown to target both histone and non-histone acetylated protein substrates. The central catalytic domain of Sirt2 is flanked by flexible N- and C-termini, which vary in length and composition with alternative splicing. These termini are further subject to posttranslational modifications (PTMs) including phosphorylation. Here we investigate the function of the N- and C-termini on deacetylation of nuclear substrates by Sirt2. Remarkably, we find that the C-terminus autoinhibits deacetylation, while the N-terminus enhances deacetylation of proteins and , but not nucleosomes—a chromatin model substrate. Using protein semisynthesis we characterize the effect of cell cycle-linked N-terminal phosphorylation at two major phosphorylation sites (Ser23/Ser25) and find that these further enhance protein/peptide deacetylation, with no effect on nucleosome deacetylation. Additionally, we find that VRK1, an established binding partner of both Sirt2 and nucleosomes, can stimulate deacetylation of nucleosomes by Sirt2, likely through an electrostatic mechanism. Taken together, these findings reveal multiple mechanisms regulating the activity of Sirt2, which allow for a broad range of activities across its multiple biological roles.

Purchased from AmBeed: ;

Alternative Products

Product Details of Fmoc-Ser(HP03Bzl)-OH

CAS No. :158171-14-3
Formula : C25H24NO8P
M.W : 497.43
SMILES Code : [H][C@@](COP(O)(=O)OCC1=CC=CC=C1)(NC(=O)OCC1C2=C(C=CC=C2)C2=C1C=CC=C2)C(O)=O
Synonyms :
Fmoc-Ser(HPO3Bzl)-OH
MDL No. :MFCD00797869
InChI Key :ZBPUWGDUVAAWJY-QHCPKHFHSA-N
Pubchem ID :11005563

Safety of Fmoc-Ser(HP03Bzl)-OH

GHS Pictogram:
Signal Word:Warning
Hazard Statements:H315-H319-H335
Precautionary Statements:P261-P305+P351+P338

Application In Synthesis of Fmoc-Ser(HP03Bzl)-OH

* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.

  • Downstream synthetic route of [ 158171-14-3 ]

[ 158171-14-3 ] Synthesis Path-Downstream   1~1

  • 1
  • [ 29022-11-5 ]
  • [ 68858-20-8 ]
  • [ 71989-31-6 ]
  • [ 35661-40-6 ]
  • [ 158171-14-3 ]
  • [ 146987-10-2 ]
  • C49H71N11O13PPolS [ No CAS ]
 

Historical Records

Technical Information

Categories