Inherited genetic disorders are caused by mutagenic changes in an organism’s gene profile in e.g. Fragile X syndrome caused by a mutation of the FMR1 gene. The FMRP protein expressed is thought to be implicated in neuronal development e.g. Axons and synaptic formation the overall development and connectivity of the neural network and has major impacts on the ability to learn utilise memory functions.
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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
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
£226.00
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
£226.00
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
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.
£226.00
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
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
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 A/C - Mouse Anti-Lamin A/C
Nuclear Lamins form a network of intermediate-type 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 Adel 10 while the B-type Lamins include two proteins arising from two distinct genes ie Lamin B1 and Lamin B2 Recent evidence has revealed that mutations in A-type Lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A-type Lamins coincides with cell differentiation and as A-type Lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A-type Lamins
£183.00
Lamin A/C Antibody- Mouse Anti-Lamin A/C
Nuclear Lamins form a network of intermediate-type 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 Adel 10 while the B-type Lamins include two proteins arising from two distinct genes ie Lamin B1 and Lamin B2 Recent evidence has revealed that mutations in A-type Lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A-type Lamins coincides with cell differentiation and as A-type Lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A-type Lamins
£226.00
Lamin A/C Antibody- Mouse Anti-Lamin A/C
Nuclear Lamins form a network of intermediate-type 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 Adel 10 while the B-type Lamins include two proteins arising from two distinct genes ie Lamin B1 and Lamin B2 Recent evidence has revealed that mutations in A-type Lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A-type Lamins coincides with cell differentiation and as A-type Lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A-type Lamins
£226.00
Lamin A/C Antibody- Mouse Anti-Lamin A/C
Nuclear Lamins form a network of intermediate-type 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 Adel 10 while the B-type Lamins include two proteins arising from two distinct genes ie Lamin B1 and Lamin B2 Recent evidence has revealed that mutations in A-type Lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A-type Lamins coincides with cell differentiation and as A-type Lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A-type Lamins
£183.00
Lamin A/C Antibody- Mouse Anti-Lamin A/C
Nuclear Lamins form a network of intermediate-type 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 Adel 10 while the B-type Lamins include two proteins arising from two distinct genes ie Lamin B1 and Lamin B2 Recent evidence has revealed that mutations in A-type Lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A-type Lamins coincides with cell differentiation and as A-type Lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A-type Lamins
£183.00
Lamin A/C Antibody- Mouse Anti-Lamin A/C
Nuclear Lamins form a network of intermediate-type 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 Adel 10 while the B-type Lamins include two proteins arising from two distinct genes ie Lamin B1 and Lamin B2 Recent evidence has revealed that mutations in A-type Lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A-type Lamins coincides with cell differentiation and as A-type Lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A-type Lamins
£226.00
MCPH1 (BRIT1) Antibody- Mouse Anti-MCPH1 (BRIT1)
This gene encodes a DNA damage response protein. The encoded protein may play a role in G2/M checkpoint arrest via maintenance of inhibitory phosphorylation of cyclin-dependent kinase 1. Mutations in this gene have been associated with primary autosomal recessive microcephaly 1 and premature chromosome condensation syndrome
MCPH1 looks like it might be a useful prognostic indicator in breast cancer associated with BRCA1 inactivation
£226.00
