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4-Amino-1-phenylpyrrolidin-2-one+hydrochloride
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4-Amino-1-phenylpyrrolidin-2-one+hydrochloride
Catalog Number:
(10409-052)
Supplier:
Bioss
Description:
HSPC300 (hematopoietic stem cell protein 300) is also known as probable protein BRICK1 or C3orf10 (chromosome 3 open reading frame 10) and is a 75 amino acid protein that is expressed as two isoforms and localizes to both the cytoplasm and the cytoskeleton. HSPC300 is thought to regulate cytoskeletal organization and Actin polymerization. Free HSPC300 exists as homotrimers prior to its incorporation into the WAVE complex. The WAVE complex includes five proteins, one of which is HSPC300, that regulate the ARC (Arp2/3 complex) which is responsible for Actin nucleation and is Rac 1-dependent. Because HSPC300 is a highly conserved subunit of the WAVE complex across many species, it is thought to have the same or similar functions in many different organisms. In Drosophila, the WAVE/ARC pathway may affect the development of the nervous system. HSPC300 is thought to localize to axons of the central nervous system of Drosophila embryos and thus may also be involved in axonogenesis. In addition, HSPC300 is thought to be necessary for synaptic morphogenesis by motoneurons. In mice, the knockout of the WAVE complex leads to learning and memory defects, and it is therefore hypothesized that HSPC300 may also be involved in cognitive functions. Genetic depletion of HSPC300 results in cytoskeletal abnormalities and prevents cytokinesis of cells, suggesting that decreased levels of HSPC300 may be associated with tumor suppression.
Catalog Number:
(89360-918)
Supplier:
Genetex
Description:
The protein encoded by this gene is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein consists of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. This particular family member binds both acidic and basic fibroblast growth factors and is involved in limb induction. Mutations in this gene have been associated with Pfeiffer syndrome, Jackson-Weiss syndrome, Antley-Bixler syndrome, osteoglophonic dysplasia, and autosomal dominant Kallmann syndrome 2. Chromosomal aberrations involving this gene are associated with stem cell myeloproliferative disorder and stem cell leukemia lymphoma syndrome. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq]
Catalog Number:
(10409-056)
Supplier:
Bioss
Description:
HSPC300 (hematopoietic stem cell protein 300) is also known as probable protein BRICK1 or C3orf10 (chromosome 3 open reading frame 10) and is a 75 amino acid protein that is expressed as two isoforms and localizes to both the cytoplasm and the cytoskeleton. HSPC300 is thought to regulate cytoskeletal organization and Actin polymerization. Free HSPC300 exists as homotrimers prior to its incorporation into the WAVE complex. The WAVE complex includes five proteins, one of which is HSPC300, that regulate the ARC (Arp2/3 complex) which is responsible for Actin nucleation and is Rac 1-dependent. Because HSPC300 is a highly conserved subunit of the WAVE complex across many species, it is thought to have the same or similar functions in many different organisms. In Drosophila, the WAVE/ARC pathway may affect the development of the nervous system. HSPC300 is thought to localize to axons of the central nervous system of Drosophila embryos and thus may also be involved in axonogenesis. In addition, HSPC300 is thought to be necessary for synaptic morphogenesis by motoneurons. In mice, the knockout of the WAVE complex leads to learning and memory defects, and it is therefore hypothesized that HSPC300 may also be involved in cognitive functions. Genetic depletion of HSPC300 results in cytoskeletal abnormalities and prevents cytokinesis of cells, suggesting that decreased levels of HSPC300 may be associated with tumor suppression.
Catalog Number:
(10409-054)
Supplier:
Bioss
Description:
HSPC300 (hematopoietic stem cell protein 300) is also known as probable protein BRICK1 or C3orf10 (chromosome 3 open reading frame 10) and is a 75 amino acid protein that is expressed as two isoforms and localizes to both the cytoplasm and the cytoskeleton. HSPC300 is thought to regulate cytoskeletal organization and Actin polymerization. Free HSPC300 exists as homotrimers prior to its incorporation into the WAVE complex. The WAVE complex includes five proteins, one of which is HSPC300, that regulate the ARC (Arp2/3 complex) which is responsible for Actin nucleation and is Rac 1-dependent. Because HSPC300 is a highly conserved subunit of the WAVE complex across many species, it is thought to have the same or similar functions in many different organisms. In Drosophila, the WAVE/ARC pathway may affect the development of the nervous system. HSPC300 is thought to localize to axons of the central nervous system of Drosophila embryos and thus may also be involved in axonogenesis. In addition, HSPC300 is thought to be necessary for synaptic morphogenesis by motoneurons. In mice, the knockout of the WAVE complex leads to learning and memory defects, and it is therefore hypothesized that HSPC300 may also be involved in cognitive functions. Genetic depletion of HSPC300 results in cytoskeletal abnormalities and prevents cytokinesis of cells, suggesting that decreased levels of HSPC300 may be associated with tumor suppression.
Catalog Number:
(10749-156)
Supplier:
Prosci
Description:
PUMA Monoclonal Antibody: Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible pro-apoptotic gene was identified recently and designated PUMA (for p53 upregulated modulator of apoptosis) and bbc3 (for Bcl-2 binding component 3) in human and mouse. PUMA/bbc3 is one of the pro-apoptotic Bcl-2 family members including Bax and Noxa, which are also transcriptional targets of p53. The PUMA gene encodes two BH3 domain-containing proteins termed PUMAalpha and PUMAbeta ;. PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome c release and apoptosis in response to p53. PUMA may be a direct mediator of p53-induced apoptosis.
Catalog Number:
(10749-134)
Supplier:
Prosci
Description:
Apaf-1 Monoclonal Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. The mammalian homologous of the key cell death gene CED-4 in C. elegans was identified recently from human and mouse and designated Apaf1 for apoptosis protease-activating factor 1. Apaf1 binds to cytochrome c (Apaf2) and caspase-9 (Apaf3), which leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Apaf1 can also associate with caspase-4 and caspase-8. Apaf1 transcript is ubiquitously expressed in human tissues.
Catalog Number:
(10749-152)
Supplier:
Prosci
Description:
PUMA Monoclonal Antibody: Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible pro-apoptotic gene was identified recently and designated PUMA (for p53 upregulated modulator of apoptosis) and bbc3 (for Bcl-2 binding component 3) in human and mouse. PUMA/bbc3 is one of the pro-apoptotic Bcl-2 family members including Bax and Noxa, which are also transcriptional targets of p53. The PUMA gene encodes two BH3 domain-containing proteins termed PUMAalpha and PUMAbeta ;. PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome c release and apoptosis in response to p53. PUMA may be a direct mediator of p53-induced apoptosis.
Catalog Number:
(89415-412)
Supplier:
Prosci
Description:
Toso Antibody: Apoptosis is an important process by which normal tissue homeostasis and function are maintained. One of the major signals that regulate this process is mediated by the activation of the Fas receptor by its ligand. This leads to the formation of a Fas-associated death domain (FADD)- containing death-inducing signaling complex and the activation of caspase-8, which in turn activates downstream effector caspases, such as caspase-3 and -7. Recent experiments have shown that overexpression of Toso, a novel regulator of Fas-induced apoptosis in lymphoid cells, in Jurkat cells as well as transgenic mice render these cells resistant to Fas-induced apoptosis but not to TRAIL-induced apoptosis. Furthermore, Toso was found to associate with FADD, suggesting that Toso functions by disrupting the formation of the death-inducing signaling complex.
Catalog Number:
(89415-490)
Supplier:
Prosci
Description:
MCG10 Antibody: MCG10 is a member of the KH-domain RNA-binding protein family. Proteins of this family also referred to as alpha-CPs, bind to RNA with specificity for C-rich pyrimidine regions. Alpha-CPs play important roles in post-transcriptional activities and have different cellular distributions. MCG10 is induced by p53 and DNA damage via two p53-responsive promoter elements. Its overexpression in transfected cells results in the suppression of cell proliferation by inducing apoptosis and cell cycle arrest in G2-M. Decreased expression of one isoform of MCG10 has been observed in many forms of lung cancer, leading to speculation that MCG10 can act as a tumor suppressor. Multiple alternatively spliced isoforms of MCG10 have been identified.
Catalog Number:
(89416-064)
Supplier:
Prosci
Description:
MD-1 Antibody: Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The signaling of these TLRs is kept under tight control by the expression of endogenous inhibiting proteins such as RP105, a recently identified homolog of TLR4. This protein, in association with MD-1, interacts with and inhibits the TLR4/MD-2 signaling pathway. While MD-2 can directly bind to LPS, one of the activating molecules of TLR4, the function of MD-1 is less well-known. It has been suggested however, that the RP105/MD-1 complex influences antibody production mediated by both TLR4/MD-2 and TLR2 receptor complexes.
Catalog Number:
(10749-164)
Supplier:
Prosci
Description:
EndoG Monoclonal Antibody: The fragmentation of nuclear DNA is a hallmark of apoptotic cell death. The activities of caspase and nuclease are involved in the DNA fragmentation. Caspase-activated deoxyribonuclease (CAD), also termed DNA fragmentation factor (DFF40), is one such nuclease, and is capable of inducing DNA fragmentation and chromatin condensation after cleavage by caspase-3 of its inhibitor ICAD/DFF45. Caspase and CAD independent DNA fragmentation also exists. Recent studies demonstrated that another nuclease, endonuclease G (EndoG), is specifically activated by apoptotic stimuli and is able to induce nucleosomal fragmentation of DNA independently of caspase and DFF/CAD. EndoG is a mitochondrion-specific nuclease that translocates to the nucleus and cleaves chromatin DNA during apoptosis. The homologue of mammalian EndoG is the first mitochondrial protein identified to be involved in apoptosis in <i>C. elegans</i>. EndoG also cleaves DNA in vitro.
Catalog Number:
(89415-298)
Supplier:
Prosci
Description:
Caspase-9 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf-3. Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation. Caspase-9 is also activated by granzyme B and CPP32. Activated caspase-9 cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Caspase-9 play a central role in cell death induced by a wide variety of apoptosis activators including TNF alpha , TRAIL, anti-CD-95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues.
Catalog Number:
(10409-058)
Supplier:
Bioss
Description:
HSPC300 (hematopoietic stem cell protein 300) is also known as probable protein BRICK1 or C3orf10 (chromosome 3 open reading frame 10) and is a 75 amino acid protein that is expressed as two isoforms and localizes to both the cytoplasm and the cytoskeleton. HSPC300 is thought to regulate cytoskeletal organization and Actin polymerization. Free HSPC300 exists as homotrimers prior to its incorporation into the WAVE complex. The WAVE complex includes five proteins, one of which is HSPC300, that regulate the ARC (Arp2/3 complex) which is responsible for Actin nucleation and is Rac 1-dependent. Because HSPC300 is a highly conserved subunit of the WAVE complex across many species, it is thought to have the same or similar functions in many different organisms. In Drosophila, the WAVE/ARC pathway may affect the development of the nervous system. HSPC300 is thought to localize to axons of the central nervous system of Drosophila embryos and thus may also be involved in axonogenesis. In addition, HSPC300 is thought to be necessary for synaptic morphogenesis by motoneurons. In mice, the knockout of the WAVE complex leads to learning and memory defects, and it is therefore hypothesized that HSPC300 may also be involved in cognitive functions. Genetic depletion of HSPC300 results in cytoskeletal abnormalities and prevents cytokinesis of cells, suggesting that decreased levels of HSPC300 may be associated with tumor suppression.
Catalog Number:
(10072-798)
Supplier:
Prosci
Description:
Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of Vaspin predicts the presence of three β-sheets, nine α-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible ("suicidal”) serine-protease inhibitors, characterized by having more than 30% sequence homology with α1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In human, the serpins represent approximately 2% of total serum proteins, of which 70% is α1- antitrypsin. Vaspin exhibits 40.2% sequence identity with α-1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. Administration of Vaspin to obese mice improved glucose tolerance and insulin sensitivity, reflected by normalized blood glucose levels. It also led to the reversal of altered expression of diabetes-relevant adipocytokines including leptin, adiponectin, resistin, and TNF-α. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the diabetic/obesity metabolic syndrome. Recombinant human Vaspin is a 45.2 kDa protein containing 395 amino-acid residues.
Supplier:
Enzo Life Sciences
Description:
P62, also known as Sequestosome I, is a 62kDa, 440 amino acid protein, initially identified as a ligand of the SH2 domain of p56lck, now known to be expressed in many tissues. In addition to TRAF6, PEST and zinc finger motifs, p62 has a C-terminal ubiquitin binding association (UBA) domain with an affinity for multi-ubiquitin chains, and it is considered to serve as a scaffold protein, capable of binding to multiple signalling molecules and uniting receptor-mediated signalling events with ubiquitinylation. Elevated levels of p62 have been reported in breast tumours and in alcoholic liver disease where p62 has been shown to be involved in the formation of Mallory bodies. Several mutations in the p62 UBA domain have been identified and the etiology of Paget’s disease of bone has been linked to one such mutation. Kuusisto and colleagues have demonstrated that p62 is also present in elevated levels in the hallmark inclusions found in various neurodegenerative conditions, including tauopathies (Alzheimer’s disease, Picks disease, and frontotemporal dementia) and synucleinopathies (Parkinson’s disease, dementia with Lewy body disease and multiple system atrophy). In recent years ubiquitin immunostaining has been used to provide adjunct information for neuropathological diagnosis, but it is becoming evident that p62 may be an even more reliable marker of neurodegenerative disease inclusion detection than tau, alpha-synuclein or ubiquitin immunostaining.
Catalog Number:
(10264-054)
Supplier:
Bioss
Description:
Cerebral cavernous malformation (CCM) is an autosomal dominant or sporadic neurovascular disease marked by vascular anomalies located mostly in the central nervous system that can cause stroke, seizures, cerebral hemorrhages, headaches and focal neurologic deficits. CCM is caused by mutations in one of three genes: CCM1, CCM2 or CCM3. CCM1 encodes the protein KRIT1, CCM2 encodes the protein Malcavernin and CCM3 shares its name with the protein it encodes. Malcavernin, also designated cerebral cavernous malformations 2 protein, is a scffolding protein for MEK kinase-3. Like KRIT1, Malcavernin is expresed in a variety of human organs including the arterial vascular endothelium, pyramidal neurons, astrocytes and their foot processes. In addition, Malcavernin is expressed in various epithelial cells that are required for the formation of the blood-organ barrier. Malcavernin is localized to the cytoplasm but is known to shuttle to and from the nucleus. Due to its lack of a nuclear export signal or nuclear localization signal, it is believed that Malcavernin accomplishes this shuttling via an attachment to KRIT1, which contains a nuclear localization signal. Two isoforms exist for Malcavernin. Isoform 1 represents the full length protein while isoform 2 contains an alternative four amino acid sequence rather than the first 10 residues of isoform 1.
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is still displayed and you need assistance, please call us at 1-800-932-5000.
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