4-Amino-1-phenylpyrrolidin-2-one+hydrochloride
Catalog Number:
(75930-666)
Supplier:
Rockland Immunochemical
Description:
The gene for CDK2NA generates several transcripts/proteins which differ from each other in their first exons. Three of these transcripts are generated by alternative splicing (isoform 1 a.k.a p16INK4A, isoform 2 and isoform 3 a.k.a p12), two of which are known to function as inhibitors of CDK4 kinase. One other transcript that is generated from this gene contains an alternate reading frame (ARF), with the first exon located 20kb upstream of the remainder of the gene (isoform 4 a.k.a. p14ARF, p19ARF, ARF). In spite of the structural and some functional differences, all the proteins encoded by the CDKN2A gene are involved in cell cycle G1 control.
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:
(75932-532)
Supplier:
Rockland Immunochemical
Description:
Synaptogyrins comprise a family of tyrosine-phosphorylated membrane proteins with two neuronal (SYNGR1 and SYNGR3) and one ubiquitous (SYNGR2) members. SYNGR1 and -3 are synaptic vesicle proteins, residing in some cases on the same synaptic vesicle, and are thought to be involved in the regulation of neurotransmitter release. SYNGR2, by contrast, is absent from synaptic vesicles. The role and localization of a fourth synaptogyrin, SYNGR4, is unclear. SYNGR3 is predominantly expressed in brain and placenta. The exact function of SYNGR2 is unknown, but studies suggest that it may play a role in regulating membrane traffic in non-neuronal cells.
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:
(75931-996)
Supplier:
Rockland Immunochemical
Description:
Despite being first described several years ago, the roles of the Schlafen (SLFN) family of proteins remain largely unknown. The SLFN genes are preferentially expressed in lymphoid tissues and differentially regulated during thymocyte maturation. It is thought that many play roles in cell growth, hemopoietic cell differentiation, and T cell development and maturation. Most members contain at least one divergent AAA domain (AAA_4) that may play a role in ATP binding. SLFN14 is a recently identified member of the SLFN family; its role has yet to be determined.
Catalog Number:
(76008-930)
Supplier:
Prosci
Description:
This gene belongs to the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 motifs) family of zinc-dependent proteases. ADAMTS proteases are complex secreted enzymes containing a prometalloprotease domain of the reprolysin type attached to an ancillary domain with a highly conserved structure that includes at least one thrombospondin type 1 repeat. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. The product of this gene plays a major role in growth and in skin, lens, and heart development. It is also a candidate gene for autosomal recessive Weill-Marchesani syndrome.
Catalog Number:
(75930-574)
Supplier:
Rockland Immunochemical
Description:
The yeast nucleolar protein NOP7 is necessary for the maturation of 66S preribosomes and interacts with numerous other proteins. One such protein is an essential, conserved WD repeat protein, NOP seven-associated protein 1 (NSA1), that is also required for the yeast 66S ribosome assembly. NSA1 is also associated with the AAA ATPase Rix7, and release of NSA1 from a novel late nucleolar pre-60S requires the Rix7 function. NSA1 has also been found upregulated in mammalian cancer cells, suggesting it may also play a role in cell proliferation.
Supplier:
Enzo Life Sciences
Description:
The small ubiquitin-related modifier SUMO-1 belongs to the growing family of ubiquitin-related proteins involved in post-translational protein modification. It is present in all eukaryotic kingdoms and is highly conserved from yeast to humans. Whereas invertebrates have only one SUMO gene, three members of the SUMO family have been described in vertebrates, SUMO-1 and the close homologues SUMO-2 and SUMO-3 with some 50% homology between SUMO-1 and SUMO-2/3. The SUMO family members have a short N-terminal extension that is absent in ubiquitin, and the function of which is unknown and the sequence of which varies between the three family members. Unlike ubiquitin, SUMO-1 does not appear to target proteins for degradation but seems to be involved in the modulation of protein-protein interactions. Although having only 18% amino acid sequence identity with ubiquitin, the overall structure closely resembles that of ubiquitin. Whereas the two C-terminal glycine residues required for isopeptide bond formation are conserved between the two molecules, Lys48 found in ubiquitin, and required to generate ubiquitin polymers, is substituted by Gln69in SUMO-1 thereby providing an explanation of why SUMO-1 has not been observed to form polymers. An increasing number of SUMO-1 substrates are being described but three major substrates for SUMO-1 modification are RanGAP1, PML and IκBα proteins.
Catalog Number:
(76010-430)
Supplier:
Prosci
Description:
The protein encoded by this gene is a member of the TNF-receptor superfamily. This protein is one of the major receptors for the tumor necrosis factor-alpha. This receptor can activate NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor. Germline mutations of the extracellular domains of this receptor were found to be associated with the autosomal dominant periodic fever syndrome. The impaired receptor clearance is thought to be a mechanism of the disease.
Catalog Number:
(10800-540)
Supplier:
Rockland Immunochemical
Description:
Calcium/calmodulin-dependent serine protein kinase (CASK) is a conserved multi-domain scaffolding protein involved in brain development, synapse formation, and establishment of cell polarity. CASKINs (CASK interacting protein ) interact with CASK and is thought to play a role in CASK function, specifically by coupling CASK to distinct downstream effectors. CASKIN2 is a multidomain protein containing six N-terminal ankyrin repeats, one SH3 domain, and two sterile alpha motif domains followed by a long proline-rich sequence and a short conserved C-terminal domain. It is expressed ubiquitously with highest levels present in fetal and adult liver tissue.
Catalog Number:
(76079-774)
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:
(10409-040)
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:
(10409-060)
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:
(10409-062)
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:
(75930-872)
Supplier:
Rockland Immunochemical
Description:
PHLPP2 is a member of the serine/threonine phosphatase family, which are important regulators of Akt serine-threonine kinases (AKT1, AKT2, AKT3) and conventional/novel protein kinase C (PKC) isoforms. PHLPP1 and PHLPP2 have a similar domain structure and have been shown to dephosphorylate and inactivate, distinct Akt isoforms, at one of the two critical phosphorylation sites required for activation: Serine473. PHLPP2 dephosphorylates AKT1 and AKT3, whereas PHLPP1 is specific for AKT2 and AKT3. PHLPP1 promotes apoptosis and may act as a tumor suppressor. PHLPP2 associates with and is inhibited by adenylyl cyclase type 6 (AC6), thereby allowing Akt activation.
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