|
|
ALY Antibody - Mouse Anti-ALY 0.1ml
The protein encoded by this gene is a heat stable nuclear protein and functions as a molecular chaperone It is thought to regulate dimerization DNA binding and transcriptional activity of basic region-leucine zipper (bZIP) proteins
£226.00
ALY Antibody - Mouse Anti-ALY 50ul
The protein encoded by this gene is a heat stable nuclear protein and functions as a molecular chaperone It is thought to regulate dimerization DNA binding and transcriptional activity of basic region-leucine zipper (bZIP) proteins
£183.00
Gemin1/SMN Antibody- Mouse Anti-SMN
This gene is part of a 500 kb inverted duplication on chromosome 5q13 This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region The telomeric and centromeric copies of this gene are nearly identical and encode the same protein However mutations in this gene the telomeric copy are associated with spinal muscular atrophy mutations in the centromeric copy do not lead to disease The centromeric copy may be a modifier of disease caused by mutation in the telomeric copy The critical sequence difference between the two genes is a single nucleotide in exon 7 which is thought to be an exon splice enhancer It is thought that gene conversion events may involve the two genes leading to varying copy numbers of each gene The protein encoded by this gene localizes to both the cytoplasm and the nucleus Within the nucleus the protein localizes to subnuclear bodies called gems which are found near coiled bodies containing high concentrations of small ribonucleoproteins (snRNPs) This protein forms heteromeric complexes with proteins such as SIP1 and GEMIN 4 and also interacts with several proteins known to be involved in the biogenesis of snRNPs such as hnRNP U protein and the small nucleolar RNA binding protein Two transcript variants are produced by this gene
£226.00
Gemin2 Antibody- Mouse Anti-Gemin2
Involved in biogenesis of spliceosomal snRNPs forms complex with Survival of Motor Neurons (SMN) protein interacts tightly with spliceosomal proteins and spliceosomal snRNAs U1 and U5
£226.00
Gemin2 Antibody- Mouse Anti-Gemin2
Involved in biogenesis of spliceosomal snRNPs forms complex with Survival of Motor Neurons (SMN) protein interacts tightly with spliceosomal proteins and spliceosomal snRNAs U1 and U5
£183.00
gp210 (N-terminal) Antibody- Rabbit Anti-gp210 (N-terminal)
The nuclear pore complex is a massive structure that extends across the nuclear envelope forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells GP210 is a membrane-spanning glycoprotein that is a major component of the nuclear pore complex it is an evolutionarily conserved and has early roles in nuclear pore formation and mediates pore dilation with its tail-binding partners
£226.00
hnRNP-F/H Antibody- Mouse Anti-hnRNP-F/H
The hnRNPs belong to a subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins 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
£183.00
hnRNP-F/HAntibody - Mouse Anti-hnRNP-F/H
The hnRNPs belong to a subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins 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
£226.00
hnRNP-K/J Antibody- Mouse (monoclonal) Anti-hnRNP-K/J
Particulate complex of heterogeneous nuclear RNA (hnRNA) is a heterogeneous mixture of RNA molecules of high Mr with a rapid turnover rate that occurs in cell nuclei during protein synthesis with proteins which are cell specific and heterogeneous The protein component may play a role in the processing of the hnRNA to mRNA
£226.00
hnRNP-K/J Antibody- Mouse Anti-hnRNP-K/J
Particulate complex of heterogeneous nuclear RNA (hnRNA) is a heterogeneous mixture of RNA molecules of high Mr with a rapid turnover rate that occurs in cell nuclei during protein synthesis with proteins which are cell specific and heterogeneous The protein component may play a role in the processing of the hnRNA to mRNA
£183.00
hnRNP-Q Antibody- Mouse Anti-hnRNP-Q
Spinal muscular atrophy (SMA) is a common neurodegenerative disease caused by deletion or loss-of-function mutations of the survival of motor neurons (SMN) protein SMN is complexed with several proteins including Gemin2 Gemin3 and Gemin4 and plays important roles in small nuclear ribonucleoprotein (snRNP) biogenesis and in pre-mRNA splicing The hnRNP Q proteins interact with SMN they are required for efficient pre-mRNA splicing in vitro The hnRNP Q proteins may provide a molecular link between the SMN complex and splicing
£226.00
hnRNP-Q Antibody- Mouse Anti-hnRNP-Q
Spinal muscular atrophy (SMA) is a common neurodegenerative disease caused by deletion or loss-of-function mutations of the survival of motor neurons (SMN) protein SMN is complexed with several proteins including Gemin2 Gemin3 and Gemin4 and plays important roles in small nuclear ribonucleoprotein (snRNP) biogenesis and in pre-mRNA splicing The hnRNP Q proteins interact with SMN they are required for efficient pre-mRNA splicing in vitro The hnRNP Q proteins may provide a molecular link between the SMN complex and splicing
£183.00
Lamin B2 Antibody- Mouse Anti-Lamin B2
An important part of the cell 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 a-helices and a carboxyterminal 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
Nup153 Antibody- Sheep Anti-Nup153
Nuclear pore complexes are extremely elaborate structures that mediate the regulated movement of macromolecules between the nucleus and cytoplasm These complexes are composed of at least 100 different polypeptide subunits many of which belong to the nucleoporin family Nucleoporins are pore complex specific glycoproteins characterized by cytoplasmically oriented O linked N acetylglucosamine residues and numerous repeats of the pentapeptide sequence XFXFG Nup153 has three distinct domains a N terminal region within which a pore targeting domain has been identified a central region containing multiple zinc finger motifs and a C terminal region containing multiple XFXFG repeats Nup153 is a possible DNA binding subunit of the nuclear pore complex (NPC) The repeat containing domain may be involved in anchoring components of the pore complex to the pore membrane
£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
£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
