You Searched For: N-Acetyl-L-arginine

Supplier: Ambeed

Description: N-Acetyl-L-arginine dihydrate 97%

Supplier: Ambeed

Description: (2-(2,2-Diphenylethoxy)acetyl)-L-arginine 2,2,2-trifluoroacetate ≥99%

New Product

Supplier: Bachem Americas

Description: Sequence: Ac-Arg-OH

Supplier: Thermo Scientific Chemicals

Description: 5G

SDS Certificates

Supplier: Ambeed

Description: Tris(2,4,6-trimethylphenyl)phosphine 98%

New Product

Supplier: Thermo Scientific Chemicals

Description: 98% 5G

SDS Certificates

Catalog Number: (77438-234)

Supplier: Bioss

Description: Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.

New Product

Catalog Number: (76011-320)

Supplier: Prosci

Description: Similar to acetylation and phosphorylation, histone methylation at the N-terminal tail has emerged as an important role in regulating chromatin dynamics and gene activity. Histone methylation occurs on arginine and lysine residues and is catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-domain-containing methyltransferase family. Five members have been identified in the arginine methyltransferase family. About 27 are grouped into the SET-domain family, and another 17 make up the PR domain family that is related to the SET domain family. The retinoblastoma protein-interacting zinc finger geneRIZ1 is a tumor suppressor gene and a FOUNDING member of the PR domain family. RIZ1 inactivation is commonly found in many types of human cancers and occurs through loss of mRNA expression, frame shift mutation, chromosomal deletion, and missense mutation. RIZ1 is also a tumor susceptibility gene in mice. The loss of RIZ1 mRNA in human cancers was shown to associate with DNA methylation of its promoter CpG island. Methylation of the RIZ1 promoter strongly correlated with lost or decreased RIZ1 mRNA expression in breast, liver, colon, and lung cancer cell lines as well as in liver cancer tissues.

Catalog Number: (76011-368)

Supplier: Prosci

Description: Similar to acetylation and phosphorylation, histone methylation at the N-terminal tail has emerged as an important role in regulating chromatin dynamics and gene activity. Histone methylation occurs on arginine and lysine residues and is catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-domain-containing methyltransferase family. Five members have been identified in the arginine methyltransferase family. About 27 are grouped into the SET-domain family, and another 17 make up the PR domain family that is related to the SET domain family. The retinoblastoma protein-interacting zinc finger geneRIZ1 is a tumor suppressor gene and a FOUNDING member of the PR domain family. RIZ1 inactivation is commonly found in many types of human cancers and occurs through loss of mRNA expression, frame shift mutation, chromosomal deletion, and missense mutation. RIZ1 is also a tumor susceptibility gene in mice. The loss of RIZ1 mRNA in human cancers was shown to associate with DNA methylation of its promoter CpG island. Methylation of the RIZ1 promoter strongly correlated with lost or decreased RIZ1 mRNA expression in breast, liver, colon, and lung cancer cell lines as well as in liver cancer tissues.

Catalog Number: (75928-468)

Supplier: Rockland Immunochemical

Description: Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin
structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called “histone code”. Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases. Acetylation of the histone H2A variant H2A.Z is associated with the promoters of active genes. Anti-Histone H2A.Zac is ideal for research in Gene Expression, Chromatin Remodeling and Epigenetics.

Catalog Number: (103484-180)

Supplier: Affymetrix, Inc.

Description: These sequences are 100% conserved between human, mouse and rat. Suggested positive control: Hela whole cell extract, HeLa cell lysate. Diverse signal transduction pathways impinging on the N-terminal tails of histones lead to a number of post-translational modifications including acetylation, phosphorylation, poly(ADP-ribosylation), ubiquitination and methylation.   These modifications play critical roles in regulating chromatin structure and gene expression.   Histone methyltransferases (HMTases) selectively methylate evolutionarily conserved arginine or  lysine residues, primarily in the N-terminal tails of histones H3 and H4.   Set7/9 is a histone specific HMTase that methylates histone H3 lysine 4.   Set7/9 transfers methyl groups to lysine 4 of histone H3 in complex with S-adenosyl-L-methionine.   Human Set7/9 is a 336 amino acid protein.   

Catalog Number: (75928-466)

Supplier: Rockland Immunochemical

Description: Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called “histone code”. Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases. Acetylation of the histone H2A variant H2A.Z is associated with the promoters of active genes. Anti-H2A.Zac Antibody is ideal for research in Chromatin Remodeling and Epigenetics.

Catalog Number: (76011-370)

Supplier: Prosci

Description: Histone methyltransferases (HMTases) selectively methylate evolutionarily conserved arginine or lysine residues, primarily in the N-terminal tails of histones H3 and H4. Signal transduction pathways affecting the N-terminal tails of histones lead to a number of post-translational modifications including acetylation, phosphorylation, poly(ADP-ribosylation), ubiquitination and methylation. These modifications play critical roles in regulating chromatin structure and gene expression. Set7/9 is a histone specific HMTase that methylates histone H3 lysine 4. Set7/9 transfers methyl groups to lysine 4 of histone H3 in complex with S-adenosyl-L-methionine. In yeast, H4-K20 methylation does not have any apparent role in the regulation of gene expression or heterochromatin function; rather it appears to play a role in DNA damage response. Loss of Set9 activity or mutation of H4-K20 markedly impairs yeast cell survival after genotoxic challenge and compromises the ability of cells to maintain checkpoint mediated cell cycle arrest. Genetic experiments link Set9 to Crb2, a homolog of the mammalian checkpoint protein 53BP1, and the enzyme is required for Crb2 localization to sites of DNA damage.

Supplier: Adipogen

Description: Potent, competitive and reversible cysteine, serine and threonine protease inhibitor. Inhibits calpain, kallikrein, trypsin, plasmin, papain and cathepsin B. Does not inhibit pepsin, elastase, renin, cathepsins A and D, thrombin or alpha-chymotrypsin. Used to protect against hearing loss caused by acoustic overstimulation or the ototoxic antibiotic gentamicin. Shown to inhibit activation-induced programmed cell death. Antioxidant and anti-inflammatory agent. Widely used as a protein purification tool to prevent proteases present in tissue samples from degrading the protein of interest.

Catalog Number: (102468-496)

Supplier: Affymetrix, Inc.

Description: 5 to 10^8 cells/test. Protocols: We recommend using Protocol A: Two-step protocol: intracellular (cytoplasmic) proteins or Protocol C: Two-step protocol: Fixation/Methanol. Protocol B: One-step protocol: intracellular (nuclear) proteins cannot be used. All Protocols can be found in the ""Staining intracellular Antigens for Flow Cytometry Protocol"" located in the Best Protocols Section under the Resources tab online. eFluor®® 660 is a replacement for Alexa Fluor® 647. eFluor®® 660 emits at 659 nm and is excited with the red laser (633 nm). Please make sure that your instrument is capable of detecting this fluorochome. Excitation: 633-647 nm; Emission: 668 nm; Laser: Red Laser Histone H3 is one of the DNA-binding proteins found in the chromatin of all eukaryotic cells. H3 along with four core histone proteins binds to DNA forming the structure of the nucleosome. Histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Post tranlationally, histones are modified in a variety of ways to either directly change the chromatin structure or allow for the binding of specific transcription factors. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.

Catalog Number: (102468-498)

Supplier: Affymetrix, Inc.

Description: 5 to 10^8 cells/test. Protocols: We recommend using Protocol A: Two-step protocol: intracellular (cytoplasmic) proteins or Protocol C: Two-step protocol: Fixation/Methanol. Protocol B: One-step protocol: intracellular (nuclear) proteins cannot be used. All Protocols can be found in the ""Staining intracellular Antigens for Flow Cytometry Protocol"" located in the Best Protocols Section under the Resources tab online. eFluor®® 660 is a replacement for Alexa Fluor® 647. eFluor®® 660 emits at 659 nm and is excited with the red laser (633 nm). Please make sure that your instrument is capable of detecting this fluorochome. Excitation: 633-647 nm; Emission: 668 nm; Laser: Red Laser Histone H3 is one of the DNA-binding proteins found in the chromatin of all eukaryotic cells. H3 along with four core histone proteins binds to DNA forming the structure of the nucleosome. Histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Post tranlationally, histones are modified in a variety of ways to either directly change the chromatin structure or allow for the binding of specific transcription factors. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.