You Searched For: N-Acetyl-L-tyrosine

Supplier: Spectrum Chemicals

Description: N-Acetyl-L-tyrosine, also known as 4-hydroxyphenylalanine, is used by cells to synthesize proteins.

Certificates

Supplier: Ambeed

Description: N-Acetyl-L-tyrosine 98%

Supplier: Thermo Scientific Chemicals

Description: 99%. 50g.

SDS Certificates

Supplier: Bachem Americas

Description: Sequence: Ac-Tyr-OH

Supplier: Thermo Scientific Chemicals

Description: N-Acetyl-L-tyrosine ethyl ester monohydrate 99%

Supplier: Ambeed

Description: N-Acetyl-L-tyrosine ethyl ester monohydrate 98%

New Product

Supplier: Thermo Scientific Chemicals

Description: 99%

SDS Certificates

Catalog Number: (TCA0087-100MG)

Supplier: TCI America

Description: CAS Number: 1027-28-7 MDL Number: MFCD00020004 Molecular Formula: C11H11I2NO4 Molecular Weight: 475.02 Purity/Analysis Method: <gt/>95.0% (T) Form: Crystal Melting point (°C): 126 Specific rotation [a]20/D: 33 deg (C=1, EtOH)

Catalog Number: (M-1080.0025BA)

Supplier: Bachem Americas

Description: Sequence: Ac-Tyr-OEt

Supplier: TCI America

Description: CAS Number: 36546-50-6
MDL Number: MFCD00149093
Molecular Formula: C13H17NO4
Molecular Weight: 251.28
Purity/Analysis Method: >98.0% (HPLC,N)
Form: Crystal
Melting point (°C): 81
Specific rotation [a]20/D: 22 deg (C=1, EtOH)

Certificates

Supplier: Ambeed

Description: (S)-2-Acetamido-3-(4-hydroxy-3,5-diiodophenyl)propanoic acid, Purity: 97%, CAS Number: 1027-28-7, Appearance: Form: Crystal - Powder / Colour: White - yellow, Storage: Keep in dark place, Sealed in dry, Store in freezer, under -20C, Size: 25G

Supplier: AFG BIOSCIENCE LLC

Description: Fmoc-L-Tyr-(β-D-Gal(Ac)4)-OH ≥95%

Supplier: AFG BIOSCIENCE LLC

Description: Fmoc-L-Tyr(β-D-Glc(Ac)4)-OH 95%

Catalog Number: (102971-626)

Supplier: Adipogen

Description: Microtubules are key elements of the eukaryotic cytoskeleton that dynamically assemble from heterodimers of alpha- and beta-tubulin. Two different mechanisms can generate microtubule diversity: the expression of different alpha- and beta-tubulin genes, referred to as tubulin isotypes, and the generation of posttranslational modifications (PTMs) on alpha- and beta-tubulin. Tubulin PTMs include the well-known acetylation or phosphorylation, and others that have so far mostly been found on tubulin, detyrosination/tyrosination, polyglutamylation and polyglycylation. These PTMs might have evolved to specifically regulate tubulin and microtubule functions. Tubulin acetylation was discovered on K40 of flagellar alpha-tubulin in Chlamydomonas reinhardtii and is generally enriched on stable microtubules in cells. It is located on the microtubule lumenal surface. As a result of its localization at the inner face of microtubules, K40 acetylation might rather affect the binding of microtubule inner proteins, a poorly characterized family of proteins. Functional experiments in cells have further suggested that K40 acetylation regulates intracellular transport by regulating the traffic of kinesin motors probably by indirect mechanisms. Acetyltransferase alpha-Tat1 (or Mec-17) specifically acetylate alpha-tubulin K40. Acetylation of tubulin by alpha-Tat1 accumulates selectively in stable, long-lived microtubules thus explaining the link between this posttranslational modication and stable microtubules in cells. However, the direct cellular function of K40 acetylation on microtubules is still unclear.

Catalog Number: (102979-944)

Supplier: Adipogen

Description: Microtubules are key elements of the eukaryotic cytoskeleton that dynamically assemble from heterodimers of alpha- and beta-tubulin. Two different mechanisms can generate microtubule diversity: the expression of different alpha- and beta-tubulin genes, referred to as tubulin isotypes, and the generation of posttranslational modifications (PTMs) on alpha- and beta-tubulin. Tubulin PTMs include the well-known acetylation or phosphorylation, and others that have so far mostly been found on tubulin, detyrosination/tyrosination, polyglutamylation and polyglycylation. These PTMs might have evolved to specifically regulate tubulin and microtubule functions. Polyglutamylation is a PTM that occurs when secondary glutamate side chains are formed on gamma-carboxyl groups of glutamate residues in a protein. Enzymes catalyzing polyglutamylation belong to the TTL-like (TTLL; Tubulin tyrosine ligase-like) family of glutamylases. Deglutamylases, the enzymes that reverse polyglutamylation, were identified within a novel family of CCPs (cytosolic carboxypeptidase). Subtle differences in polyglutamylation can be seen on diverse microtubules in different cell types. The functions of these modifications remain to be studied. However, its wide distribution strengthens the idea that it could be involved in fine-tuning a range of microtubule functions.

Catalog Number: (89357-406)

Supplier: Genetex

Description: Tubulin is the major building block of microtubules. This intracellular cylindrical filamentous structure is present in almost all eukaryotic cells. Microtubules function as structural and mobility elements in mitosis, intracellular transport, flagellar movement, and in the cytoskeleton. Tubulin is a heterodimer which consists of alpha tubulin and beta tubulin; both subunits have a molecular weight of 55 kDa and share considerable homology. The most widely studied tubulins have been isolated from vertebrate brains. The microtubules can be viewed in immunofluorescent microscopy allowing for the observation of the intracellular organization of proteins that are in the form of a supramolecular structure. Distinct classes of interphase microtubules have been described in tissue culture cells. They contain post translationally modified subunits of tubulin, detyrosinated alpha tubulin (Glutubulin) or acetylated alpha tubulin. The dynamic properties of microtubules of the Tyrtubulin type studied in living cells have suggested that they turnover and grow very rapidly in vivo with most microtubules exchanging within a half-time of approximately 10 minutes. Minor subpopulations of interphase microtubules have been found to be more stable in that they resist exchange for several hours, or that they are less sensitive to microtubule disrupting drugs. The coding portion of genes encoding alpha tubulin terminates in a tyrosine codon indicating that the primary gene product is tyrosinated (Tyr-Tu). Tubulin tyrosinylation is involved in the assembly status of tubulin. A specific tubulinyl tyrosine carboxypeptidase removes the terminal tyrosine to yield an alpha tubulin terminating in a glutamic acid residue while another enzyme modifies the alpha tubulin by addition of tyrosine to the carboxy terminus to offer a potential cycle of tyrosine addition and loss.