14-3-3 beta + zeta antibody [4E2]
- Host / ClonalityMouse Monoclonal
- Clone Name4E2
- ApplicationsICC/IF, WB
- Species reactivityHuman, Mouse, Cow, Dog, Monkey, Pig, Rat, Sheep
14-3-3 beta + zeta antibody [4E2] validated data
14-3-3 beta + zeta antibody [4E2]
|Full Name||tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta polypeptide|
|Synonyms||1433, 1433 beta + zeta, GW128, 14-3-3-zeta, HS1, KCIP-1, MGC111427, YWHAA, MGC126532, MGC138156, YWHAD, KCIP 1, 14 3 3 zeta, KCIP1, 1433zeta|
|Product Description||Mouse monoclonal [4E2] to 14 - 3 - 3 beta + zeta|
|Background||14-3-3 proteins are highly conserved proteins which play a role in both signal transduction and progression through the cell cycle by binding to and regulating several different proteins. 14-3-3 proteins activate tyrosine and tryptophan hydroxylases and protein kinase C. They mediate signal transduction by binding to phosphoserine-containing proteins. There are at least 7 mammalian isoforms: alpha, beta, gamma, delta, epsilon, zeta, and eta. An eighth subtype, termed theta has been found in rat brain. The 14-3-3 proteins exists in vitro and in vivo as either homo- or heterodimers which interact via their N-terminal domains and are subject to phosphorylation by protein kinase C. 14-3-3 proteins are localized in the cytoplasm of neurons in the cerebral cortex and are axonally transported to the nerve terminals. They may be present at lower levels in various other eukaryotic tissues. Northern blot analysis has shown expression of the eta chain in cultured cell lines derived from various tumors.|
|Target||14-3-3 beta + zeta|
|Immunogen||Tissue / cell preparation (Lysed transformed human amnion cells).|
|Species Reactivity||Human, Mouse, Cow, Dog, Monkey, Pig, Rat, Sheep|
Not tested in other applications.
|Western blot||1 ug/ml*
*Optimal dilutions/concentrations should be determined by the researcher.
|Positive Controls||HeLa cell lysate|
|Purification||Protein G purified|
|Storage Buffer||Preservative: NoneConstituents: 50% Glycerol, 10mM PBS, 0.1mM PMSF. pH 7.2|
|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.|
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.
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