• Mouse TUBa4A (Tubulin Alpha 4A) Sandwich ELISA Kit (STJE0012862)

Mouse TUBa4A (Tubulin Alpha 4A) Sandwich ELISA Kit (STJE0012862)

SKU:
STJE0012862

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Applications: ELISA
Reactivity: Mouse
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Sensitivity: 0.114ng/mL
Detection Limit: 0.312-20ng/mL
Short Description: This TUBa4A Sandwich ELISA Kit is an in-vitro enzyme-linked immunosorbent assay for the measurement of samples in mouse cell culture supernatant, serum and plasma (EDTA, citrate, heparin).
Storage Instruction: Store the unopened kit in the fridge at 2-8°C for up to 6 months. Once opened store individual kit contents according to components table provided with the kit.
Assay Time: 4.5 hrs
Gene Symbol: Tuba4a
Gene ID: 22145
Uniprot ID: TBA4A_MOUSE
Sample Type: tissue homogenates, cell lysates or other biological fluids.
Tissue Specificity
Post Translational Modifications Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility. Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Glutamylation is also involved in cilia motility. Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly. Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. Although this tubulin does not encode a C-terminal tyrosine, a C-terminal tyrosine can be added post-translationally by the tubulin tyrosine ligase (TTL). It can then undergo a detyrosination cycle by the tubulin tyrosine carboxypeptidase (KIAA0895L/MATCAP).
Function Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Protein Name Tubulin Alpha-4a Chain
Alpha-Tubulin 4
Alpha-Tubulin Isotype M-Alpha-4
Tubulin Alpha-4 Chain
Database Links Reactome: R-MMU-114608
Reactome: -MMU-190840
Reactome: -MMU-2132295
Reactome: -MMU-2467813
Reactome: -MMU-2500257
Reactome: -MMU-2565942
Reactome: -MMU-3371497
Reactome: -MMU-380259
Reactome: -MMU-380270
Reactome: -MMU-380284
Reactome: -MMU-380320
Reactome: -MMU-437239
Reactome: -MMU-5610787
Reactome: -MMU-5617833
Reactome: -MMU-5620912
Reactome: -MMU-5620924
Reactome: -MMU-5626467
Reactome: -MMU-5663220
Reactome: -MMU-6807878
Reactome: -MMU-6811434
Reactome: -MMU-6811436
Reactome: -MMU-68877
Reactome: -MMU-8852276
Reactome: -MMU-8854518
Reactome: -MMU-8955332
Reactome: -MMU-9646399
Reactome: -MMU-9648025
Reactome: -MMU-9668328
Reactome: -MMU-983189
Cellular Localisation Cytoplasm
Cytoskeleton
Alternative ELISA Names Tubulin Alpha-4a Chain ELISA kit
Alpha-Tubulin 4 ELISA kit
Alpha-Tubulin Isotype M-Alpha-4 ELISA kit
Tubulin Alpha-4 Chain ELISA kit
Tuba4a ELISA kit
Tuba4 ELISA kit
output

Information sourced from Uniprot.org

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