FHIT Antibody
Purified Rabbit Polyclonal Antibody (Pab)
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- 实验流程
- 背景知识
Application
| WB, ICC, IHC-P |
|---|---|
| Primary Accession | P49789 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 16858 Da |
| Gene ID | 2272 |
|---|---|
| Other Names | Bis(5'-adenosyl)-triphosphatase, AP3A hydrolase, AP3Aase, Diadenosine 5', 5'''-P1, P3-triphosphate hydrolase, Dinucleosidetriphosphatase, Fragile histidine triad protein, FHIT |
| Target/Specificity | KLH-conjugated synthetic peptide encompassing a sequence within the center region of human FHIT. The exact sequence is proprietary. |
| Dilution | WB~~1:1000 ICC~~N/A IHC-P~~1:50~200 |
| Format | 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50% |
| Storage | Store at -20 °C.Stable for 12 months from date of receipt |
| Name | FHIT |
|---|---|
| Function | Possesses dinucleoside triphosphate hydrolase activity (PubMed:12574506, PubMed:15182206, PubMed:8794732, PubMed:9323207, PubMed:9543008, PubMed:9576908). Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP (PubMed:12574506, PubMed:15182206, PubMed:8794732, PubMed:9323207, PubMed:9543008, PubMed:9576908). Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP (PubMed:8794732). Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate (PubMed:18694747). Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:18694747). Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'- phosphosulfate resulting in the formation of adenosine 5'- phosphoramidate (PubMed:26181368). Also catalyzes the ammonolysis of adenosine 5-phosphorofluoridate and diadenosine triphosphate (PubMed:26181368). Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5 (PubMed:18077326). Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways (PubMed:16407838). Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis (PubMed:15313915). Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake (PubMed:12574506, PubMed:19622739). Functions as a tumor suppressor (By similarity). |
| Cellular Location | Cytoplasm. Mitochondrion. Nucleus |
| Tissue Location | Low levels expressed in all tissues tested. Phospho-FHIT observed in liver and kidney, but not in brain and lung Phospho-FHIT undetected in all tested human tumor cell lines |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'- adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity. Functions as tumor suppressor.
REFERENCES
Ohta M.,et al.Cell 84:587-597(1996).
Druck T.,et al.Cancer Res. 57:504-512(1997).
Naqvi R.A.,et al.Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
Barnes L.D.,et al.Biochemistry 35:11529-11535(1996).
Gemmill R.M.,et al.Proc. Natl. Acad. Sci. U.S.A. 95:9572-9577(1998).
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