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Catalog Number: (89416-004)
Supplier: Prosci
Description: LSD1 Antibody: Histone modifications mediate changes in gene expression by altering chromatin structure or by serving as a platform to recruit other proteins. LSD1 is a recently discovered amine oxidase that catalyzes the lysine-specific demethylation of histone proteins via an FAD-dependent oxidative reaction. Methylation on histone H3-K9 is thought to play an important role in heterochromatin formation, while methylation on arginine and some lysine residues (such as H3-K4) is associated with active transcription. LSD1 associates with various proteins, including HDAC1/2, CoREST, and BHC80, that act to regulate LSD1 activity in vivo, and in a histone H3-K4-specific methylase complex that is involved in transcriptional regulation. Experiments have shown that CoREST, a SANT domain-containing corepressor acts to enhance LSD1 activity, while BHC80, a PHD domain-containing protein, inhibits CoREST/LSD1 activity in vitro. LSD1-mediated histone demethylation thus may have significant effects on gene expression.


Catalog Number: (10748-556)
Supplier: Prosci
Description: LSD1 Antibody: Histone modifications mediate changes in gene expression by altering chromatin structure or by serving as a platform to recruit other proteins. LSD1 is a recently discovered amine oxidase that catalyzes the lysine-specific demethylation of histone proteins via an FAD-dependent oxidative reaction. Methylation on histone H3-K9 is thought to play an important role in heterochromatin formation, while methylation on arginine and some lysine residues (such as H3-K4) is associated with active transcription. LSD1 associates with various proteins, including HDAC1/2, CoREST, and BHC80, that act to regulate LSD1 activity in vivo, and in a histone H3-K4-specific methylase complex that is involved in transcriptional regulation. Experiments have shown that CoREST, a SANT domain-containing corepressor acts to enhance LSD1 activity, while BHC80, a PHD domain-containing protein, inhibits CoREST/LSD1 activity in vitro. LSD1-mediated histone demethylation thus may have significant effects on gene expression.


Catalog Number: (103009-046)
Supplier: Anaspec Inc
Description: This peptide is histone H4 (1-25) with acetylation at Lys12. It is biotinylated through a C-terminal GSGSK linker. Lys12 acetylation is necessary for the methylation of Lys9 of histone H3 in the formation of heterochromatin. Provided at >95% peptide purity, this peptide was dissolved in distilled water at 1 mg/ml and re-lyophilized to powder form.
Sequence:SGRGKGGKGLG-K(Ac)-GGAKRHRKVLRDN-GSGSK(Biotin)
MW:3274.8 Da
% peak area by HPLC:95
Storage condition:-20° C


Catalog Number: (10751-406)
Supplier: Prosci
Description: UHRF1BP1 Antibody: The Ubiquitin-like containing PHD and RING finger domains 1-binding protein 1 (UHRF1BP1), also known as ICBP90, is a transcription and cell cycle regulator. It specifically binds to the histone H3 N-terminal tail when methylated on K9 by two functional domains, a PHD finger that defines the binding specificity and an SRA (SET- and RING-associated) domain that promotes binding activity. UHRF1BP1 is required for proper heterochromatin formation in mammalian cells. Furthermore, UHRF1BP1 is thought to be a pivotal target for the ERK1/2 signaling pathway to control the proliferation of Jurkat T cells.


Catalog Number: (77440-708)
Supplier: Bioss
Description: Ubiquitin ligase that mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1), in response to DNA damage. Protects cells exposed to DNA-damaging agents. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me). Involved in the recruitment of 53BP1/TP53BP1 to sites of DNA damage by mediating H4K91ub1 formation. In concert with PARP9, plays a role in PARP1-dependent DNA damage repair. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites.


Catalog Number: (10082-134)
Supplier: Proteintech
Description: Four-and-a-half LIM domains 1 (FHL1), a member of the FHL protein family, which composed of FHL 1, 2, 3, 4 and ACT (activator of CREM), and characterized by an N-terminal half LIM domain followed by four complete LIM domains. FHL1 may contribute to sarcomere synthesis, assembly and biomechanical stress sensing. FHL1 is also a methylation-silenced tumor-suppressor gene on chromosome X in gastrointestinal cancers, which contributes to the formation of an epigenetic field for cancerization. FHL1(10991-1-AP) is highly expressed in skeletal muscle and to a lesser extent in heart, placenta, ovary, prostate, testis, small intestine, colon and spleen. This is a rabbit polyantibody raised against full length of human FHL1.


Catalog Number: (10495-554)
Supplier: Bioss
Description: Leucine-rich repeats (LRRs) are 20-29 amino acid motifs that mediate protein-protein interactions. The primary function of these motifs is to provide a versatile structural framework for the formation of these protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutation in the genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 3B (LRRC3B), also designated LRP15, is a 259 amino acid protein that contains 3 LRR repeats. The gene encoding LRRC3B is a tumor suppressor gene that is regulated by DNA methylation. Decreased expression of LRRC3B has been shown in colorectal cancer and gastric cancer, making LRRC3B a candidate marker for those cancers.


Catalog Number: (10090-920)
Supplier: Proteintech
Description: Retinoblastoma-like protein 1, also named RBL1, p107, is a member of E1A-binding proteins, which contains a A/B pocket, or pRb. Via this structure, RBL1 can bind to viral oncoproteins and other perteins containing LXCXE motif. It regulates cell proliferation via phosphorylation-sensitive interactions with E2F transcription factors and other proteins. Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression.(uniprot). It has been reported there are two transcirpts variants of RBL1, which encode a 119-kd protein and a 68-kd protein.


Catalog Number: (10353-856)
Supplier: Bioss
Description: Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fibre is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. Covalent modifications of the canonical core histones, including acetylation, phosphorylation, methylation, and monoubiquitination are used to mark nucleosomes to create chromatin domains with a range of functions. The information encoded by histone modifications can contribute to the formation and/or maintenance of transcriptionally active and inactive chromatin in response to various signalling pathways.


Catalog Number: (10353-832)
Supplier: Bioss
Description: Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fibre is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. Covalent modifications of the canonical core histones, including acetylation, phosphorylation, methylation, and monoubiquitination are used to mark nucleosomes to create chromatin domains with a range of functions. The information encoded by histone modifications can contribute to the formation and/or maintenance of transcriptionally active and inactive chromatin in response to various signalling pathways.


Catalog Number: (10495-558)
Supplier: Bioss
Description: Leucine-rich repeats (LRRs) are 20-29 amino acid motifs that mediate protein-protein interactions. The primary function of these motifs is to provide a versatile structural framework for the formation of these protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutation in the genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 3B (LRRC3B), also designated LRP15, is a 259 amino acid protein that contains 3 LRR repeats. The gene encoding LRRC3B is a tumor suppressor gene that is regulated by DNA methylation. Decreased expression of LRRC3B has been shown in colorectal cancer and gastric cancer, making LRRC3B a candidate marker for those cancers.


Catalog Number: (10481-124)
Supplier: Bioss
Description: The Dumpy-30 (DPY-30) protein was first described in C. elegans, in which it is involved in dosage compensation of sex chromosomes. Conserved from yeast to humans, the DPY-30 family is involved in gene expression and chromatin modification, specifically histone methylation. DPY-30 and closely related proteins contain a short motif that is related to the dimerization motif in the regulatory subunit of protein kinase A (PKA), which consists of two ?helices that form a four-helix bundle during dimerization. As a member of the DPY-30 family, DYDC1 (DPY30 domain-containing protein 1), also known as DPY30D1 and RSD9, is a 177 amino acid protein that binds to Endophilin III and plays a crucial role during acrosome biogenesis. DYDC1 is specifically expressed in brain and testis and accumulates in the acrosome area during spermatogenesis. Knockdown of DYDC1 mRNA results in disruption of acrosome formation and spermatid differentiation.


Catalog Number: (10481-128)
Supplier: Bioss
Description: The Dumpy-30 (DPY-30) protein was first described in C. elegans, in which it is involved in dosage compensation of sex chromosomes. Conserved from yeast to humans, the DPY-30 family is involved in gene expression and chromatin modification, specifically histone methylation. DPY-30 and closely related proteins contain a short motif that is related to the dimerization motif in the regulatory subunit of protein kinase A (PKA), which consists of two ?helices that form a four-helix bundle during dimerization. As a member of the DPY-30 family, DYDC1 (DPY30 domain-containing protein 1), also known as DPY30D1 and RSD9, is a 177 amino acid protein that binds to Endophilin III and plays a crucial role during acrosome biogenesis. DYDC1 is specifically expressed in brain and testis and accumulates in the acrosome area during spermatogenesis. Knockdown of DYDC1 mRNA results in disruption of acrosome formation and spermatid differentiation.


Catalog Number: (76108-476)
Supplier: Bioss
Description: The Dumpy-30 (DPY-30) protein was first described in C. elegans, in which it is involved in dosage compensation of sex chromosomes. Conserved from yeast to humans, the DPY-30 family is involved in gene expression and chromatin modification, specifically histone methylation. DPY-30 and closely related proteins contain a short motif that is related to the dimerization motif in the regulatory subunit of protein kinase A (PKA), which consists of two ?helices that form a four-helix bundle during dimerization. As a member of the DPY-30 family, DYDC1 (DPY30 domain-containing protein 1), also known as DPY30D1 and RSD9, is a 177 amino acid protein that binds to Endophilin III and plays a crucial role during acrosome biogenesis. DYDC1 is specifically expressed in brain and testis and accumulates in the acrosome area during spermatogenesis. Knockdown of DYDC1 mRNA results in disruption of acrosome formation and spermatid differentiation.


Catalog Number: (89416-006)
Supplier: Prosci
Description: LSD1 Antibody: Histone modifications mediate changes in gene expression by altering chromatin structure or by serving as a platform to recruit other proteins. LSD1 is a recently discovered amine oxidase that catalyzes the lysine-specific demethylation of histone proteins via an FAD-dependent oxidative reaction. Methylation on histone H3-K9 is thought to play an important role in heterochromatin formation, while methylation on arginine and some lysine residues (such as H3-K4) is associated with active transcription. LSD1 associates with various proteins, including HDAC1/2, CoREST, and BHC80, that act to regulate LSD1 activity in vivo, and in a histone H3-K4-specific methylase complex that is involved in transcriptional regulation. Experiments have shown that CoREST, a SANT domain-containing corepressor acts to enhance LSD1 activity, while BHC80, a PHD domain-containing protein, inhibits CoREST/LSD1 activity in vitro. LSD1-mediated histone demethylation thus may have significant effects on gene expression.


Catalog Number: (10070-898)
Supplier: Prosci
Description: Key regulator of entry into cell division that acts as a tumor suppressor. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.


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