Anti-TPPP antibody [R06-8I4] (STJA0034964)

SPECIFICATIONS
ClonalityMonoclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
ImmunogenA synthetic peptide of human Tubulin Polymerization Promoting Protein
STJA0034964
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General Information

Short DescriptionRabbit monoclonal anti-TPPP for use in WB, IHC-F, IHC-P, ICC and IF in Human, Mouse and Rat samples. Datasheet included with dilution recommendations, and related reagents.
ApplicationsWB/IHC-F/IHC-P/ICC/IF
HostRabbit
ReactivityHuman/Mouse/Rat
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityMonoclonal
Clone IDR06-8I4
IsotypeIgG
ConjugationUnconjugated
Concentration0.3 mg/mL
PurificationAffinity Purified
Dilution RangeWB 1:500-1:1000
IHC 1:50-1:100
IF 1:50-1:200
Formulation50mM Tris-Glycine (pH 7.4) , 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
Storage InstructionStore at 4°C short term. Aliquot and store at-20°C long term. Avoid freeze/thaw cycles.

Target Information

Gene SymbolTPPP
Gene ID11076
Uniprot IDTPPP_HUMAN
ImmunogenA synthetic peptide of human Tubulin Polymerization Promoting Protein

Additional Info

Tissue Specificity Widely expressed.
Post Translational Modifications Phosphorylated by LIMK1 on serine residues.phosphorylation may alter the tubulin polymerization activity. Phosphorylation by LIMK2, but not LIMK1, regulates astral microtubule organization at early stage of mitosis. Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase. Phosphorylation by CDK1 inhibits the microtubule polymerizing activity. Degraded by the proteasome.zinc-binding inhibits degradation by the proteasome.
Function Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath. Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath. Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes. Shows magnesium-dependent GTPase activity.the role of the GTPase activity is unclear. In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network. Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6. Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility. Plays a role in cell proliferation by regulating the G1/S-phase transition. Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis.this process is regulated by phosphorylation by LIMK2.
Protein Name Tubulin Polymerization-Promoting Protein
Tppp
25 Kda Brain-Specific Protein
Tppp/P25
P24
P25-Alpha
Database Links
Cellular Localisation Golgi Outpost
Cytoplasm
Cytoskeleton
Microtubule Organizing Center
Nucleus
Spindle
Specifically Localizes To The Postsynaptic Golgi Apparatus Region
Also Named Golgi Outpost
Which Shapes Dendrite Morphology By Functioning As Sites Of Acentrosomal Microtubule Nucleation
Mainly Localizes To The Cytoskeleton
Also Found In The Nucleus
However
Nuclear Localization Is Unclear And Requires Additional Evidences
Localizes To Glial Lewy Bodies In The Brains Of Individuals With Synucleinopathies
During Mitosis
Colocalizes With Limk2 At The Mitotic Spindle
Alternative Antibody Names Anti-Tubulin Polymerization-Promoting Protein antibody
Anti-Tppp antibody
Anti-25 Kda Brain-Specific Protein antibody
Anti-Tppp/P25 antibody
Anti-P24 antibody
Anti-P25-Alpha antibody
Anti-TPPP antibody
Anti-TPPP1 antibody

Information sourced from Uniprot.org

Citations

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