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Apolipoprotein E4 Antibody ; Mouse Anti-Apolipoprotein E4
Apolipoprotein E, a main apoprotein of the chylomicron, binds to a specific receptor on liver cells and peripheral cells and is essential for the normal catabolism of triglyceride-rich lipoprotein constituents.ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer's disease. Defects in apolipoprotein E result in familial dysbetalipoproteinemia, or type III hyperlipoproteinemia (HLP III), in which increased levels of plasma cholesterol and triglycerides are the consequence of impaired clearance of chylomicron and VLDL remnants
£226.00
EAPP Antibody ; Mouse Anti-EAPP
Transcription activator that binds DNA cooperatively with dp proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F-1 binds preferentially RB1 protein, in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent apoptosis
£226.00
Emerin Antibody - Goat Anti-Emerin
Emerin is a serine rich nuclear membrane protein and a member of the nuclear lamina associated protein family. It mediates membrane anchorage to the cytoskeleton. Dreifuss-Emery muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the emerin gene
£226.00
Gemin 3 Antibody- Mouse Anti-Gemin 3
The survival of motor neurons (SMN) gene is the disease gene of spinal muscular atrophy (SMA) a common motor neuron degenerative disease The SMN protein is part of a complex containing several proteins of which one SIP1 (SMN interacting protein 1) has been characterized so far The SMN complex is found in both the cytoplasm and in the nucleus where it is concentrated in bodies called gems In the cytoplasm SMN and SIP1 interact with the Sm core proteins of spliceosomal small nuclear ribonucleoproteins (snRNPs) and they play a critical role in snRNP assembly In the nucleus SMN is required for pre-mRNA splicing likely by serving in the regeneration of snRNPs A DEAD box putative RNA helicase named Gemin 3 which is another component of the SMN complex has been identified Gemin 3 interacts directly with SMN as well as with SmB SmD2 and SmD3 Immunolocalization studies using mAbs to Gemin 3 show that it colocalizes with SMN in gems Gemin 3 binds SMN via its unique COOH-terminal domain and SMN mutations found in some SMA patients strongly reduce this interaction The presence of a DEAD box motif in Gemin 3 suggests that it may provide the catalytic activity that plays a critical role in the function of the SMN complex on RNPs
£226.00
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
Gemin3 Antibody- Mouse Anti-Gemin3
The survival of motor neurons (SMN) gene is the disease gene of spinal muscular atrophy (SMA) a common motor neuron degenerative disease The SMN protein is part of a complex containing several proteins of which one SIP1 (SMN interacting protein 1) has been characterized so far The SMN complex is found in both the cytoplasm and in the nucleus where it is concentrated in bodies called gems In the cytoplasm SMN and SIP1 interact with the Sm core proteins of spliceosomal small nuclear ribonucleoproteins (snRNPs) and they play a critical role in snRNP assembly In the nucleus SMN is required for pre-mRNA splicing likely by serving in the regeneration of snRNPs A DEAD box putative RNA helicase named Gemin 3 which is another component of the SMN complex has been identified Gemin 3 interacts directly with SMN as well as with SmB SmD2 and SmD3 Immunolocalization studies using mAbs to Gemin 3 show that it colocalizes with SMN in gems Gemin 3 binds SMN via its unique COOH-terminal domain and SMN mutations found in some SMA patients strongly reduce this interaction The presence of a DEAD box motif in Gemin 3 suggests that it may provide the catalytic activity that plays a critical role in the function of the SMN complex on RNPs
£183.00
Lamin A/C mutant R453W Antibody ; Mouse Anti-Lamin A/C mutant R453W
Nuclear lamins are intermediate filament proteins that are the major structural component of the nuclear lamina on the inner surface of the nuclear envelope. Lamin A and Lamin C are splice variants of the Lamin A gene. Lamin A/C (CDCD1, LMN1, EMD2) expression is a hallmark of embryonic stem cell differentiation. In addition to adding structural integrity to the nucleus, lamins contribute to the makeup of the nuclear matrix. Lamins also help organize interphase chromatin through interactions with several chromatin proteins, including histones and Lap2, such that alteration in lamin organization (laminopathy) results in disruption of DNA replication, transcription and RNA processing. The R453W mutation is one of the most common causes of autosomal dominant Emery-Dreifuss muscular dystrophy (EDMD)
£226.00
Nup53 Antibody- Rabbit Anti-Nup53
Nup53 encodes a recently identified nuclear pore protein. Transport of macromolecules between the nucleus and the cytoplasm of eukaryotic cells occurs through the nuclear pore complex (NPC), a large macromolecular complex that spans the nuclear envelope. The yeast NPC shares several features with the vertebrate NPC, despite being smaller and less elaborate. Nup53p forms a complex with two other nucleoporins, Nup170p and Asm4p. The complex is found on both the nuclear and cytoplasmic faces of the NPC, and associates with Pse1p, a member of a protein family implicated in nuclear protein import, via direct interaction between Nup53p and Pse1p. Nup53p is structurally similar to Asm4p, and similar proteins sequences are found in several eukaryotes including human and other multicellular species. Nup53p is not essential; deletion of Nup53 and ASM4 causes slow growth and altered subcellular distribution of Pse1p. In a nup53 pse1 double mutant, NLS-containing proteins are mislocalized to the cytoplasm
£226.00
OVCA1 Antibody- Rabbit Anti-OVCA1
Chromosome 17 is a hotspot for chromosomal aberrations in breast and ovarian cancer. Candidate oncogenes and tumor suppressors located on this chromosome include OVCA1 and OVCA2, p53, BRCA1, HER2/neu and others. OVCA1 and 2 map to a highly conserved region on human chromosome 17p13.3 that is deleted in 80% of ovarian cancers and shows frequent loss of heterozygosity in breast cancers . OVCA1 is induced by BRCA1 and is closely linked to p53, a well-known tumor suppressor gene. The close linkage of OVCA1 and p53 suggests that coordinated loss of the two genes may lead to ovarian, breast and other tumor types
£226.00
OVCA1 Antibody- Rabbit Anti-OVCA1
Chromosome 17 is a hotspot for chromosomal aberrations in breast and ovarian cancer. Candidate oncogenes and tumor suppressors located on this chromosome include OVCA1 and OVCA2, p53, BRCA1, HER2/neu and others. OVCA1 and 2 map to a highly conserved region on human chromosome 17p13.3 that is deleted in 80% of ovarian cancers and shows frequent loss of heterozygosity in breast cancers . OVCA1 is induced by BRCA1 and is closely linked to p53, a well-known tumor suppressor gene. The close linkage of OVCA1 and p53 suggests that coordinated loss of the two genes may lead to ovarian, breast and other tumor types
£183.00
OVCA2 Antibody- Rabbit Anti-OVCA2
Chromosome 17 is a hotspot for chromosomal aberrations in breast and ovarian cancer. Candidate oncogenes and tumor suppressors located on this chromosome include OVCA1 and OVCA2, p53, BRCA1, HER2/neu and others. OVCA1 and 2 map to a highly conserved region on human chromosome 17p13.3 that is deleted in 80% of ovarian cancers and shows frequent loss of heterozygosity in breast cancers . OVCA1 is induced by BRCA1 and is closely linked to p53, a well-known tumor suppressor gene. The close linkage of OVCA1 and p53 suggests that coordinated loss of the two genes may lead to ovarian, breast and other tumor types
£226.00
Progerin Antibody ; Mouse Anti-Progerin
Progerin is a 614 amino acid protein involved in Hutchinson-Gilford progeria syndrome. Progerin is most often generated by a point mutation (C1824T) in the LMNA gene that codes for lamin A and C. This mutation activates a cryptic splice site and gives rise to a form of lamin A with a 50-amino acids internal deletion within the carboxyl-terminal domain of the protein. Approximately 80% of Hutchinson-Gilford progeria syndrome cases carry a single copy of the most common mutation, a silent point mutation, G608G (GGC > GGT), within exon 11 of LMNA gene
£226.00
