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Acetylated Lysine Antibody - Mouse Anti-Acetylated Lysine 0.1ml
CBP and p300 are large nuclear proteins that bind to many sequence-specific factors involved in cell growth and/or differentiation including c-jun and the adenoviral oncoprotein E1A The protein encoded by this gene associates with p300/CBP It has in vitro and in vivo binding activity with CBP and p300 and competes with E1A for binding sites in p300/CBP It has histone acetyl transferase activity with core histones and nucleosome core particles indicating that this protein plays a direct role in transcriptional regulation
£226.00

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Acetylated Lysine Antibody - Mouse Anti-Acetylated Lysine 50ul
CBP and p300 are large nuclear proteins that bind to many sequence-specific factors involved in cell growth and/or differentiation including c-jun and the adenoviral oncoprotein E1A The protein encoded by this gene associates with p300/CBP It has in vitro and in vivo binding activity with CBP and p300 and competes with E1A for binding sites in p300/CBP It has histone acetyl transferase activity with core histones and nucleosome core particles indicating that this protein plays a direct role in transcriptional regulation
£183.00

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Cytokeratin (keratin) K2 (AE3) Antibody- Mouse Anti-Cytokeratin (keratin) K2 (AE3)
Cytokeratins, a group of at least 29 different proteins, are characteristic of epithelial and trichocytic cells. Cytokeratins 4, 5, 6 and 8 are members of the type II neutral-to-basic subfamily. Cytokeratin peptide 4 (59 kDa) is the secondary type II keratin expressed in non cornified stratified squamous epithelia. Cytokeratin peptide 5 (58 kDa) is the primary type II keratin in stratified epithelia, while cytokeratin type 8 (52 kDa) is a major type II keratin in simple epithelia. Cytokeratin 6 (56 kDa) is a "hyperproliferation" cytokeratin expressed in tissues with natural or pathological high turnover. Cytokeratins 10, 13 and 18 are members of the type I acidic subfamily. Cytokeratin peptide 10 (56 kDa) is the secondary type I keratin expressed in cornified epithelia. Cytokeratin 13 (54 kDa) is the secondary type I keratin expressed in non-cornified stratified squamous epithelia. Cytokeratin 18 (45 kDa) is the primary type I keratin expressed in simple epithelial cells.
£226.00

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hnRNP-A2/B1 Antibody- Mouse Anti-hnRNP-A2/B1
This gene belongs to the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs) The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA) These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport While all of the hnRNPs are present in the nucleus some seem to shuttle between the nucleus and the cytoplasm The hnRNP proteins have distinct nucleic acid binding properties The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs This gene has been described to generate two alternatively spliced transcript variants which encode different isoforms
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hnRNP-A2/B1Antibody - Mouse Anti-hnRNP-A2/B1
This gene belongs to the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs) The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA) These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport While all of the hnRNPs are present in the nucleus some seem to shuttle between the nucleus and the cytoplasm The hnRNP proteins have distinct nucleic acid binding properties The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs This gene has been described to generate two alternatively spliced transcript variants which encode different isoforms
£183.00

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hnRNP-C1/C2 Antibody- Mouse Anti-hnRNP-C1/C2
The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA) These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport While all of the hnRNPs are present in the nucleus some seem to shuttle between the nucleus and the cytoplasm The hnRNP proteins have distinct nucleic acid binding properties hnRNP C1 and C2 are encoded by one gene the two alternatively spliced transcript variants have been described
£226.00

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hnRNP-C1/C2 Antibody- Mouse Anti-hnRNP-C1/C2
The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA) These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport While all of the hnRNPs are present in the nucleus some seem to shuttle between the nucleus and the cytoplasm The hnRNP proteins have distinct nucleic acid binding properties hnRNP C1 and C2 are encoded by one gene the two alternatively spliced transcript variants have been described
£183.00

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PABP Antibody- Mouse Anti-PABP
The poly(A)-binding protein (PABP) which is found complexed to the 3-prime poly(A) tail of eukaryotic mRNA is required for poly(A) shortening and translation initiation Grange et al (1987) isolated a melanoma cell cDNA encoding human PABP The predicted 633-amino acid protein contains 4 repeats of an approximately 80-amino acid unit in its N-terminal half The authors found that this repeat region is highly conserved between human and yeast PABP and is sufficient for poly(A) binding In vitro translation of the human PABP cDNA yielded a protein with an apparent molecular mass of 73 kD by SDS-PAGE Northern blot analysis indicated that PABP is expressed as a 29-kb mRNA in human melanoma cells Gorlach et al (1994) noted that each of the 4 repeats of PABP is a ribonucleoprotein (RNP) consensus sequence RNA-binding domain They determined that PABP has a pI of approximately 103 and is a very abundant stable protein Immunofluorescence studies of mammalian cells indicated that PABP is located exclusively in the cytoplasm However using both indirect immunofluorescence and tagging of PABP1 by fusion to the green fluorescent protein (GFP) Afonina et al (1998) demonstrated that PABP1 shuttles between the nucleus and cytoplasm PABP1 accumulated in the nucleus when transcription was inhibited suggesting that active transcription is required for nuclear export of PABP1
£226.00

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PABP Antibody- Mouse Anti-PABP
The poly(A)-binding protein (PABP) which is found complexed to the 3-prime poly(A) tail of eukaryotic mRNA is required for poly(A) shortening and translation initiation Grange et al (1987) isolated a melanoma cell cDNA encoding human PABP The predicted 633-amino acid protein contains 4 repeats of an approximately 80-amino acid unit in its N-terminal half The authors found that this repeat region is highly conserved between human and yeast PABP and is sufficient for poly(A) binding In vitro translation of the human PABP cDNA yielded a protein with an apparent molecular mass of 73 kD by SDS-PAGE Northern blot analysis indicated that PABP is expressed as a 29-kb mRNA in human melanoma cells Gorlach et al (1994) noted that each of the 4 repeats of PABP is a ribonucleoprotein (RNP) consensus sequence RNA-binding domain They determined that PABP has a pI of approximately 103 and is a very abundant stable protein Immunofluorescence studies of mammalian cells indicated that PABP is located exclusively in the cytoplasm However using both indirect immunofluorescence and tagging of PABP1 by fusion to the green fluorescent protein (GFP) Afonina et al (1998) demonstrated that PABP1 shuttles between the nucleus and cytoplasm PABP1 accumulated in the nucleus when transcription was inhibited suggesting that active transcription is required for nuclear export of PABP1
£183.00

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