FOXM1 antibody [0.T.181]
- Host / ClonalityMouse Monoclonal
- Clone Name0.T.181
- ApplicationsELISA, ICC/IF, WB
- Species reactivityHuman, Yeast
FOXM1 antibody [0.T.181] validated data
FOXM1 antibody [0.T.181]
|Full Name||forkhead box M1|
|Synonyms||Q08050, 2305, 602341, PIG29, FOXM1, HFH-11, FKHL16, INS1, INS-1, MPP-2, HFH11, MPP2, HNF3, TRIDENT, MPM2, FOXM1B, MPHOSPH2, HNF-3, INS 1, MPP 2, HNF 3, HFH 11|
|Product Description||Mouse monoclonal [0.T.181] to MPM2|
|Specificity||Recognizes a phosphorylated epitope (S/T)P found in phosphoproteins such as MAP2, HSP70, cdc25 and DNA topoisomerase IIa, most of which are phosphorylated at the onset of mitosis. The number of phosphoproteins recognized by MPM-2 varies from species to species and with the cell type.|
|Background||Progression of cells from interphase to mitosis involves alterations in cell structures and activities. The transition from G2 to M phase is induced by M phase-promoting factor, or MPF. In M phase, many proteins are phosphorylated directly by MPF or indirectly by kinases activated by MPF. These M-phase phosphoproteins (MPPs, or MPHOSPHs) permit disassembly of interphase structures and generation of M-phase enzymatic activities and structures.|
|Immunogen||Tissue / cell preparation (Mitotic human HeLa cell cytosolic lysate).|
|Species Reactivity||Human, Yeast|
|Applications||ELISA, ICC/IF, WB|
Not tested in other applications.
|ICC/IF||5 - 15 ug/ml*
*Optimal dilutions/concentrations should be determined by the researcher.
|Positive Controls||Colcemid treated HeLa cell lysate|
|Purification||Protein G purified|
|Storage Buffer||Preservative: 0.05% sodium azide Constituents: 0.1M Tris-glycine, pH 7.4, 0.15M sodium chloride, 40% glycerol|
|Storage Instruction||Keep as concentrated solution. Store at 4ºC short term. For extended storage aliquot and store at -20ºC or below. Avoid freeze-thaw cycles.|
|Notes||For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer."|
for FOXM1 antibody [0.T.181]
Why is the observed Western Blot band size different from predicted size?
The predicted M.W. is based on protein sequence analysis; however, some factors might lead to an observed band size that is different from the predicted size. The reasons might include:
1.Post-translational modification (PTM):
a. Some post-translational modifications might lead to increased protein size, including
phosphorylation, acetylation, methylation, glycosylation, sumoylation, ubiquitination,
b. Some post-translational modifications might lead to decreased protein size including
phosphatidylethanolamine conjunction (e.g. LC3-II)
c. Some proteins may be cleaved to form an active or mature form; this process will
lead to a decreased protein size (e.g. Notch activation, Caspase activation, etc.)
d. Some websites provide useful PTM information
iv.CBS data sets http://www.cbs.dtu.dk/databases/
v.CBS prediction Servers http://www.cbs.dtu.dk/services/
2.mRNA splice variants (Isoforms):
Through alternative splicing, one gene can generate different proteins with different M.W. Regulation of alternative splicing depends upon cell type, conditions, etc.
Some proteins could form dimers or multimers, increasing the M.W. This phenomenon usually can be found in reducing gel condition; however, strong interactions may still be seen with higher molecular weight proteins even in denaturing gel.
The observed size could also potentially be influenced by the protein charge
Different species likely have different protein sequence and PTM, which can lead to a different protein M.W.