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Cytokeratin (keratin) K13 Antibody (AE8) - Mouse Anti-Cytokeratin (keratin) K13, AE8 0.1ml
Cytokeratin 13 is a member of the keratin gene family The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins Most of the type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains This type I cytokeratin is paired with keratin 4 and expressed in the suprabasal layers of non-cornified stratified epithelia Mutations in this gene and keratin 4 have been associated with the autosomal dominant disorder White Sponge Nevus This antibody is specific for Cytokeratin 13 which is a marker for oesophageal type differentiation which is expressed by various internal stratified epithelia
£226.00
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
Cytokeratin (keratin) K3 (AE5) Antibody- Mouse Anti-Cytokeratin (keratin) K3, AE5
Cytokeratin 3 belongs to the intermediate filament family. It is a type II cytokeratin and is specifically expressed in the corneal epithelium. Cytokeratin 3 associates with Cytokeratin 12. Defects in Cytokeratin 3 are a cause of Meesmann corneal dystrophy.
£226.00
Cytokeratin Antibody (keratin) K1 type I (AE1) - Mouse Anti-Cytokeratin (keratin) K1 type I (AE1) 0.2ml
Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI <57) and basic (pI >60) subfamilies The acidic keratins have molecular weights of 565 55 51 50 50 48 46 45 and 40kDa The basic keratins have molecular weights of 65 - 67 64 59 58 56 and 52kDa Members of acidic and basic subfamilies are found together in pairs The composition of keratin pairs varies with cell type differentiation status and environment Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis
£226.00
Lamin B1 Antibody- Mouse Anti-Lamin B1
An important part of the nucleus is formed by nuclear lamina Nuclear lamins form a network of filaments at the nucleoplasmic site of the nuclear membrane Two main subtypes of nuclear lamins can be distinguished ie A type lamins and B type lamins The A type lamins comprise a set of three proteins arising from the same gene by alternative splicing ie lamin A lamin C and lamin Adel10 while the B-type lamins include two proteins arising from two distinct genes ie lamin B1 and lamin B2 The nuclear lamins comprise a unique subclass of the intermediate filament protein family They share a molecular domain organisation with the other intermediate filament proteins in that they are fibrous molecules that have an aminoterminal globular head a central rod of alpha helices and a carboxy terminal globular domain Many biochemical and molecular features of lamins have been studied but their functions remain still largely undetermined One of the functions ascribed to the lamina is the maintenance of the structural integrity of the nucleus Besides interactions with the nuclear membrane and other intermediate filaments lamins interact with the nuclear chromatin Eukaryotic chromatin is organised into loops which are attached to the nuclear matrix This organisation is thought to contribute to compaction of the chromatin and regulation of gene expression Lamins as part of the nuclear matrix may be involved in these processes since chromatin binding sites have been detected in both A and B type lamins
£183.00
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
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
Transportin1 (TRN) Antibody- Mouse Anti-Transportin1
Heterogeneous nuclear ribonucleoprotein hnRNPA1 is an abundant nuclear protein that plays an important role in pre-mRNA processing and mRNA export from the nucleus A1 shuttles rapidly between the nucleus and the cytoplasm and a 38-amino acid domain M9 serves as the bi-directional transport signal of A1 Recently a 90-kD protein transportin was identified as the mediator of A1 nuclear import Transportin mediates the nuclear import of additional hnRNP proteins including hnRNPF The nuclear localization of A1 is dependent on ongoing RNA polymerase II transcription
£226.00
Transportin1 (TRN) Antibody- Mouse Anti-Transportin1
Heterogeneous nuclear ribonucleoprotein hnRNPA1 is an abundant nuclear protein that plays an important role in pre-mRNA processing and mRNA export from the nucleus A1 shuttles rapidly between the nucleus and the cytoplasm and a 38-amino acid domain M9 serves as the bi-directional transport signal of A1 Recently a 90-kD protein transportin was identified as the mediator of A1 nuclear import Transportin mediates the nuclear import of additional hnRNP proteins including hnRNPF The nuclear localization of A1 is dependent on ongoing RNA polymerase II transcription
£183.00
