DATASHEET
Host:
Rabbit
Target Protein:
Acinus Ser1180
Specificity:
The phosphorylation on Ser1180 is homologous to the phosphorylation at Ser1179 in mouse.
Modification Site:
Ser1180
Clonality:
Polyclonal
Isotype:
IgG
Entrez Gene:
22985
Swiss Prot:
Q9UKV3
Source:
KLH conjugated synthetic phosphopeptide derived from human Acinus around the phosphorylation site of Ser1180.
Purification:
Purified by Protein A.
Storage Buffer:
Aqueous buffered solution containing 0.01M TBS (pH 7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
Storage:
Store at -20°C for 12 months.
Background:
Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells.
Conjugation:
Biotin
Excitation/ Emission:
N/A
Size:
100ul
Concentration:
1ug/ul
Applications:
WB(1:300-5000)
IHC-P(1:200-400)
IHC-F(1:100-500)
148
Human
Mouse
Predicted Cross Reactive Species:
Rat
Dog
Cow
Pig
Horse
For research use only. Not intended for diagnostic or therapeutic use.