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Immunoprecipitation

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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
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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

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BUB1 Antibody - Mouse (monoclonal) Anti-BUB1 0.1ml
Bub1 is a kinase involved in spindle checkpoint function The kinase functions in part by phosphorylating a member of the miotic checkpoint complex and activating the spindle checkpoint Mutations in Bub1 have been associated with aneuploidy and several forms of cancer
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BUB1 Antibody - Mouse Anti-BUB1 50ul
Bub1 is a kinase involved in spindle checkpoint function The kinase functions in part by phosphorylating a member of the miotic checkpoint complex and activating the spindle checkpoint Mutations in Bub1 have been associated with aneuploidy and several forms of cancer
£183.00

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CENP-E Antibody - Mouse Anti-CENP-E 0.1ml
CENPE is a 250-300 kDa human centromere-associated kinesin-like motor protein that accumulates in G2 phase In contrast to other centromere proteins CENPE is not detected at centromeres during interphase and first appears at the centromere region of chromosomes during prometaphase CENPE function is required for the transition from metaphase to anaphase CENPE is probably one of the motors responsible for mammalian chromosome movement and/or spindle elongation
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CENP-E Antibody - Mouse Anti-CENP-E 50ul
CENPE is a 250-300 kDa human centromere-associated kinesin-like motor protein that accumulates in G2 phase In contrast to other centromere proteins CENPE is not detected at centromeres during interphase and first appears at the centromere region of chromosomes during prometaphase CENPE function is required for the transition from metaphase to anaphase CENPE is probably one of the motors responsible for mammalian chromosome movement and/or spindle elongation
£183.00

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Emerin Antibody- Rabbit 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
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EPCAM; CD326 Antibody- Rat Anti-EPCAM
Epithelial Cell Adhesion Molecule (EpCAM) is a 40 kDa cell surface antigen. This antigen has been identified independently by a number of groups, and has been known by a variety of names. Several monoclonal antibodies have been raised against EpCAM, many of which have been described as tumour specific molecules on carcinomas. EpCAM is a Type 1 transmembrane glycoprotein. It is expressed on the basolateral membrane of cells by the majority of epithelial tissues, with the exception of adult squamous epithelium and some specific epithelial cell types including hepatocytes and gastric epithelial cells. EpCAM expression has been reported to be a possible marker of early malignancy, with expression being increased in tumour cells, and de novo expression being seen in dysplastic squamous epithelium
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FMR1 (Drosophila) Antibody- Mouse (monoclonal) Anti-FMR1
Fragile X syndrome is the most common inherited form of mental retardation It is caused by loss of FMR1 gene activity due to either lack of expression or expression of a mutant form of the protein In mammals FMR1 is a member of a small protein family that consists of FMR1 FXR1 and FXR2 All three members bind RNA and contain sequence motifs that are commonly found in RNA-binding proteins including two KH domains and an RGG boxThe Drosophila genome contains a single gene homologous to the FXR family dFMR1 is subjected to transcriptional and posttranscriptional regulation during development and it homomerizes like its human counterpart dFMR1 profile of expression recapitulates that of the human FXR protein family it is highly enriched in muscles in central nervous system and in gonads In the larval brain anti-dFMR1 also recognizes mushroom bodies a centre that mediates learning and memory These features make the fly an ideal system to analyse the role of the FXR family and to identify genes in the FMRP pathway
£226.00

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FMR1 (Drosophila) Antibody- Mouse Anti-FMR1 (Drosophila)
Fragile X syndrome is the most common inherited form of mental retardation It is caused by loss of FMR1 gene activity due to either lack of expression or expression of a mutant form of the protein In mammals FMR1 is a member of a small protein family that consists of FMR1 FXR1 and FXR2 All three members bind RNA and contain sequence motifs that are commonly found in RNA-binding proteins including two KH domains and an RGG boxThe Drosophila genome contains a single gene homologous to the FXR family dFMR1 is subjected to transcriptional and posttranscriptional regulation during development and it homomerizes like its human counterpart dFMR1 profile of expression recapitulates that of the human FXR protein family it is highly enriched in muscles in central nervous system and in gonads In the larval brain anti-dFMR1 also recognizes mushroom bodies a centre that mediates learning and memory These features make the fly an ideal system to analyse the role of the FXR family and to identify genes in the FMRP pathway
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FNIP1 folliculin interacting protein 1 Antibody- Rabbit Anti-FNIP1
Birt-Hogg-Dubé syndrome, a hamartoma disorder characterized by benign tumors of the hair follicle, lung cysts, and renal neoplasia, is caused by germ-line mutations in the BHD(FLCN) gene, which encodes a tumor-suppressor protein, folliculin (FLCN), with unknown function. The tumor-suppressor proteins encoded by genes responsible for several other hamartoma syndromes, LKB1, TSC1/2, and PTEN, have been shown to be involved in the mammalian target of rapamycin (mTOR) signaling pathway
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FXR2 Antibody- Mouse Anti-FXR2
FXR2 is a RNA binding protein containing two KH domains and one RCG box which is similar to FMRP and FXR1 It associates with polyribosomes predominantly with 60S large ribosomal subunits It may self-associate or interact with FMRP and FXR1 Fragile X syndrome is caused by the absence of the fragile X mental-retardation protein (FMRP) FMRP is the archetype of a class of cytoplasmic mRNA-binding proteins that includes the fragile X-related 1 and 2 proteins (FXR1 and FXR2) The fragile X-related proteins FXR1 and FXR2 contain a functional nucleolar-targeting signal equivalent to the HIV-1 regulatory proteins
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FXR2 Antibody- Mouse Anti-FXR2
FXR2 is a RNA binding protein containing two KH domains and one RCG box which is similar to FMRP and FXR1 It associates with polyribosomes predominantly with 60S large ribosomal subunits It may self-associate or interact with FMRP and FXR1 Fragile X syndrome is caused by the absence of the fragile X mental-retardation protein (FMRP) FMRP is the archetype of a class of cytoplasmic mRNA-binding proteins that includes the fragile X-related 1 and 2 proteins (FXR1 and FXR2) The fragile X-related proteins FXR1 and FXR2 contain a functional nucleolar-targeting signal equivalent to the HIV-1 regulatory proteins
£183.00

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GAD65 Antibody- Mouse Anti-GAD65
Glutamic Acid Decarboxylase (GAD) catalyzes the conversion of L glutamate to g-aminobutyric acid (GABA), the principal inhibitory neurotransmitter in the brain, and a putative paracrine signal molecule in pancreatic islets. GAD has a restricted tissue distribution. It is highly expressed in the cytoplasm of GABAergic neurons in the central nervous system (CNS) and pancreatic beta cells. It is also present in other non-neuronal tissues such as testis, oviduct and ovary. GAD is also transiently expressed in non-GABAergic cells of the embryonic and adult nervous system, suggesting its involvement in development and plasticity. GAD exists as two isoforms, GAD65 and GAD67 (molecular masses of 65 and 67 kD, respectively) that are encoded by two different genes. GAD65 is an ampiphilic, membraneanchored protein, (585 amino acid residues) and is encoded on human chromosome 10. GAD67 is a cytoplasmic protein (594 amino acid residues) and is encoded on chromosome 2. There is 64% amino acid identity between the two isoforms, with the highest diversity located at the N terminus, which in GAD65 is required for targeting the enzyme to GABA-containing secretory vesicles. The two isoforms appear to have distinct intraneuronal distribution in the brain. GAD65 has been identified as an autoantigen in insulindependent diabetes mellitus (IDDM) and stiff-man syndrome (SMS), IDDM is an autoimmune disease that results from T cell mediated destruction of pancreatic insulin-secreting beta cells. Islet-reactive T cells and antibodies primarily to GAD65 (also named beta cell autoantigen) can be detected in peripheral blood of 80% of recent-onset IDD patients and in pre-diabetic high-risk subjects before onset of clinical symptoms. This suggests that GAD may be an important marker in the early stages of the disease. Also, autoantibodies to GAD65 and GAD67 are detected in animal models of IDDM, including the non-obese diabetes (NOD) mouse. In the NOD mouse, T cell reactivity is initially restricted to the C terminal regions of GAD65, but later spreads to other parts of GAD65. Stiff-man syndrome (SMS), a rare disorder of the CNS, is characterized by progressive rigidity of the body musculature with painful spasms, due to impairment of the GABAergic neurotransmission. High-titer autoantibodies directed against GAD 65 and GABAergic neurons (nerve terminals) have been detected in the serum and cerebrospinal fluid (CSF) in 60% of patients with the syndrome. Strikingly, many of the SMS patients also developed late-onset IDDM.
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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
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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
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