|
|
APPL1 Antibody - Rabbit Anti-APPL1 50ul
The protein encoded by this gene has been shown to be involved in the regulation of cell proliferation and in the crosstalk between the adiponectin signalling and insulin signalling pathways The encoded protein binds many other proteins including RAB5A DCC AKT2 PIK3CA adiponectin receptors and proteins of the NuRD/MeCP1 complex This protein is found associated with endosomal membranes but can be released by EGF and translocated to the nucleus
£226.00
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
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
HEF 1/Cas-L (NEDD9)Antibody - Mouse Anti-HEF-1/Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£226.00
HEF-1/Cas-L (NEDD9) Antibody- Mouse Anti-HEF-1/Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£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 Antibody - Mouse Anti-Lamin A
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 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
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
Lamin C Antibody- Rabbit Anti-Lamin C
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
£226.00
LAP2a Antibody- Rabbit Anti-LAP2a
Lamins are type V intermediate filament proteins and are grouped into constitutively expressed B-type lamins and developmentally regulated A- type lamins Lamin-binding proteins in the nuclear lamina and the nuclear interior include several protein families and/or types of proteins in higher eu karyotes such as the inner nuclear membrane proteins lamin B receptor emerin and MANI three isoforms of lamina-associated polypeptide 1 (LAP 1) and several isoforms of LAP 2 Up to six LAP 2 isoforms derive from a single gene by alternative splicing in mammals and various isoforms have been described in Xenopus The best characterized LAP2 isoforms are the inner nuclear membrane protein LAP 2 beta and the nucleoplasmic protein LAP 2 alpha which are identical in their N-terminal 187-amino acid constant region but differ in their C termini While LAP 2 beta binds to B-type lamins at the nuclear periphery and was suggested to regulate nuclear lamina growth LAP 2 alpha specifically interacts with A-type lamins within the nuclear interior as part of a detergent/salt-resistant nucleoskeletal structure
£226.00
