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Product listing: Pannexin-1 (D9M1C) Rabbit mAb, UniProt ID Q96RD7 #91137 to PCSK7 (D4I5G) Rabbit mAb, UniProt ID Q16549 #19346

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The pannexin family (pannexin-1, -2, and -3; PANX1-3) of gap junction proteins has homology to the invertebrate innexins and display distinct expression patterns (1). Pannexin-1 is widely expressed, with highest expression in the heart, brain, skeletal muscle, testis, and ovary (1,2). Pannexin-2 is predominately expressed in the brain (1,2) and pannexin-3 is found within the skin and connective tissues (1,3). Connexin family gap junction proteins form hemichannels that align adjacent cells, creating functional intercellular channels that are permeable to ions and small molecules. In contrast, pannexin proteins may not function as gap junction proteins since pannexins on adjacent cells may not align to form complete channels (3). These pannexin “hemichannels” may play a role in inflammation, apoptosis, and neuronal signaling by allowing permeability of ions, ATP, and potentially other small molecules into the extracellular space (4-6). Pannexin-1 can be activated by effector caspases (caspase-3 and -7), which leads to release of signal molecules that promote phagocytosis of apoptotic cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: PAR2 (F2RL1) belongs to the PAR (Protease-activated Receptor) family of G protein-coupled receptors. These membrane receptors are activated through N-terminal cleavage of the receptor by a serine protease such as thrombin, trypsin, or matrix metalloproteinases (1,2). This cleavage exposes the ‘tethered-ligand’ fragment of the receptor, which binds to a second extracellular loop of the receptor and leads to receptor activation. PAR2 is specifically activated by trypsin or trypsin-like proteases. Activated PAR2 stimulates phosphoinositide hydrolysis and calcium mobilization, interacts with β-arrestin, and eventually leads to ERK activation (3). PAR2 expression and activation are mainly associated with inflammatory diseases (3), but may also play a role in cancer development (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Poly (ADP-ribose) glycohydrolase (PARG) is an enzyme that hydrolyzes poly (ADP-ribose) (PAR) formed by members of the PAR polymerase (PARP) enzyme family. Poly (ADP)-ribosylation is a post-translational modification that is catalyzed by PARP proteins. This modification involves polymerization of ADP-ribose from NAD+ to target proteins, such as histones and transcription factors, and plays a wide range of biological roles, including the response to DNA damage and transcriptional regulation (1,2). The mammalian PARG enzyme that catalyzes the removal of this modification exists as multiple isoforms. Longer PARG isoforms (100-110 kDa) shuttle between the nucleus and cytoplasm and are responsible for most of the PARG activity. The smaller (65 kDa) isoform resides in the cytoplasm (3-5). Research studies link altered PAR metabolism to inflammatory and autoimmune diseases, as well as neuronal degeneration (6-8). PARG inhibitors that increase PAR levels may sensitize cells to cancer treatments (e.g., cisplatin) and may help in the development of cancer therapies (9).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Parkin is a protein of 465 amino acids with an amino-terminal ubiquitin domain and a carboxy-terminal RING-box (1). In the case of autosomal recessive juvenile Parkinsonism (AR-JP), deletions have been found in the gene on chromosome 6 encoding the protein Parkin (2).

$305
400 µl
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. PARP (46D11) Rabbit mAb (Sepharose® Bead Conjugate) is useful for immunoprecipitation assays. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated PARP (46D11) Rabbit mAb #9532.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation

Background: PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (2,4). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).

$111
20 µl
$261
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (2,4). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: PASK is a serine/threonine kinase that contains two PAS (Per-Arnt-Sim) domains (1). Its kinase activity is up-regulated by autophosphorylation of the activation loop within its catalytic domain and is inhibited in cis by one of the PAS domains (1). Studies found that the yeast homolog of PASK phosphorylates and inhibits two enzymes required for glycogen biosynthesis: UDP-glucose pyrophosphorylase and glycogen synthase, resulting in the decrease of carbohydrate storage (2). Further studies showed that increased glucose levels activate PASK activity and enhance its expression in pancreatic β-cells (3). PASK is essential for the glucose-stimulated expression of preproinsulin and Pdx1, suggesting its role in the regulation of genes involved in pancreatic β-cell functions (3). PASK was shown to be critical for glucose-stimulated insulin secretion in pancreatic β-cells (4). The absence of PASK also protects animals from obesity and insulin resistance when they are fed a high-fat diet (4). These findings suggest that PASK functions as an important metabolic sensor in various cells (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: PATL1/PAT1b is the human homolog of the evolutionarily conserved Pat1/Mrt1 protein, which was first identified in Saccharomyces cerevisiae (1,2). This protein is a critical component of the RNA decay machinery in the cytoplasmic processing bodies (P-bodies), localized foci of mRNA silencing and degradation (3). PATL1/PAT1b interacts with many key components of the RNA decay machinery. These include the 5’ decapping proteins DDX6/RCK, DCP1, DCP2, EDC4, and the LSm1–7 ring (3,4) as well as the 3’ deadenylation complex of CAF1-CCR4-NOT1 (3).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated PAX5 (D19F8) XP® Rabbit mAb #8970.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Paired box (PAX) proteins are a family of transcription factors that play important and diverse roles in animal development (1). Nine PAX proteins (PAX1-9) have been described in humans and other mammals. They are defined by the presence of an amino-terminal "paired" domain, consisting of two helix-turn-helix motifs, with DNA binding activity (2). PAX proteins are classified into four structurally distinct subgroups (I-IV) based on the absence or presence of a carboxy-terminal homeodomain and a central octapeptide region. Subgroup I (PAX1 and 9) contains the octapeptide but lacks the homeodomain; subgroup II (PAX2, 5, and 8) contains the octapeptide and a truncated homeodomain; subgroup III (PAX3 and 7) contains the octapeptide and a complete homeodomain; and subgroup IV (PAX4 and 6) contains a complete homeodomain but lacks the octapeptide region (2). PAX proteins play critically important roles in development by regulating transcriptional networks responsible for embryonic patterning and organogenesis (3); a subset of PAX proteins also maintain functional importance during postnatal development (4). Research studies have implicated genetic mutations that result in aberrant expression of PAX genes in a number of cancer subtypes (1-3), with members of subgroups II and III identified as potential mediators of tumor progression (2).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Paired box (PAX) proteins are a family of transcription factors that play important and diverse roles in animal development (1). Nine PAX proteins (PAX1-9) have been described in humans and other mammals. They are defined by the presence of an amino-terminal "paired" domain, consisting of two helix-turn-helix motifs, with DNA binding activity (2). PAX proteins are classified into four structurally distinct subgroups (I-IV) based on the absence or presence of a carboxy-terminal homeodomain and a central octapeptide region. Subgroup I (PAX1 and 9) contains the octapeptide but lacks the homeodomain; subgroup II (PAX2, 5, and 8) contains the octapeptide and a truncated homeodomain; subgroup III (PAX3 and 7) contains the octapeptide and a complete homeodomain; and subgroup IV (PAX4 and 6) contains a complete homeodomain but lacks the octapeptide region (2). PAX proteins play critically important roles in development by regulating transcriptional networks responsible for embryonic patterning and organogenesis (3); a subset of PAX proteins also maintain functional importance during postnatal development (4). Research studies have implicated genetic mutations that result in aberrant expression of PAX genes in a number of cancer subtypes (1-3), with members of subgroups II and III identified as potential mediators of tumor progression (2).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: Paired box (PAX) proteins are a family of transcription factors that play important and diverse roles in animal development (1). Nine PAX proteins (PAX1-9) have been described in humans and other mammals. They are defined by the presence of an amino-terminal "paired" domain, consisting of two helix-turn-helix motifs, with DNA binding activity (2). PAX proteins are classified into four structurally distinct subgroups (I-IV) based on the absence or presence of a carboxy-terminal homeodomain and a central octapeptide region. Subgroup I (PAX1 and 9) contains the octapeptide but lacks the homeodomain; subgroup II (PAX2, 5, and 8) contains the octapeptide and a truncated homeodomain; subgroup III (PAX3 and 7) contains the octapeptide and a complete homeodomain; and subgroup IV (PAX4 and 6) contains a complete homeodomain but lacks the octapeptide region (2). PAX proteins play critically important roles in development by regulating transcriptional networks responsible for embryonic patterning and organogenesis (3); a subset of PAX proteins also maintain functional importance during postnatal development (4). Research studies have implicated genetic mutations that result in aberrant expression of PAX genes in a number of cancer subtypes (1-3), with members of subgroups II and III identified as potential mediators of tumor progression (2).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Paired box (PAX) proteins are a family of transcription factors that play important and diverse roles in animal development (1). Nine PAX proteins (PAX1-9) have been described in humans and other mammals. They are defined by the presence of an amino-terminal "paired" domain, consisting of two helix-turn-helix motifs, with DNA binding activity (2). PAX proteins are classified into four structurally distinct subgroups (I-IV) based on the absence or presence of a carboxy-terminal homeodomain and a central octapeptide region. Subgroup I (PAX1 and 9) contains the octapeptide but lacks the homeodomain; subgroup II (PAX2, 5, and 8) contains the octapeptide and a truncated homeodomain; subgroup III (PAX3 and 7) contains the octapeptide and a complete homeodomain; and subgroup IV (PAX4 and 6) contains a complete homeodomain but lacks the octapeptide region (2). PAX proteins play critically important roles in development by regulating transcriptional networks responsible for embryonic patterning and organogenesis (3); a subset of PAX proteins also maintain functional importance during postnatal development (4). Research studies have implicated genetic mutations that result in aberrant expression of PAX genes in a number of cancer subtypes (1-3), with members of subgroups II and III identified as potential mediators of tumor progression (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Paired box (PAX) proteins are a family of transcription factors that play important and diverse roles in animal development (1). Nine PAX proteins (PAX1-9) have been described in humans and other mammals. They are defined by the presence of an amino-terminal "paired" domain, consisting of two helix-turn-helix motifs, with DNA binding activity (2). PAX proteins are classified into four structurally distinct subgroups (I-IV) based on the absence or presence of a carboxy-terminal homeodomain and a central octapeptide region. Subgroup I (PAX1 and 9) contains the octapeptide but lacks the homeodomain; subgroup II (PAX2, 5, and 8) contains the octapeptide and a truncated homeodomain; subgroup III (PAX3 and 7) contains the octapeptide and a complete homeodomain; and subgroup IV (PAX4 and 6) contains a complete homeodomain but lacks the octapeptide region (2). PAX proteins play critically important roles in development by regulating transcriptional networks responsible for embryonic patterning and organogenesis (3); a subset of PAX proteins also maintain functional importance during postnatal development (4). Research studies have implicated genetic mutations that result in aberrant expression of PAX genes in a number of cancer subtypes (1-3), with members of subgroups II and III identified as potential mediators of tumor progression (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Paired box (PAX) proteins are a family of transcription factors that play important and diverse roles in animal development (1). Nine PAX proteins (PAX1-9) have been described in humans and other mammals. They are defined by the presence of an amino-terminal "paired" domain, consisting of two helix-turn-helix motifs, with DNA binding activity (2). PAX proteins are classified into four structurally distinct subgroups (I-IV) based on the absence or presence of a carboxy-terminal homeodomain and a central octapeptide region. Subgroup I (PAX1 and 9) contains the octapeptide but lacks the homeodomain; subgroup II (PAX2, 5, and 8) contains the octapeptide and a truncated homeodomain; subgroup III (PAX3 and 7) contains the octapeptide and a complete homeodomain; and subgroup IV (PAX4 and 6) contains a complete homeodomain but lacks the octapeptide region (2). PAX proteins play critically important roles in development by regulating transcriptional networks responsible for embryonic patterning and organogenesis (3); a subset of PAX proteins also maintain functional importance during postnatal development (4). Research studies have implicated genetic mutations that result in aberrant expression of PAX genes in a number of cancer subtypes (1-3), with members of subgroups II and III identified as potential mediators of tumor progression (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Paxillin is a multidomain protein that localizes primarily to focal adhesion sites in the extracellular matrix (1). Paxillin is one of the key components of integrin signaling, and tyrosine phosphorylation of paxillin is required for integrin-mediated cytoskeletal reorganization (2). Paxillin is phosphorylated by another focal adhesion component, focal adhesion kinase (FAK), at Tyr118 (3,4). Phospho-Paxillin (Tyr118) may provide a docking site for recruitment of other signaling molecules to focal adhesions. It has been shown that the SH2 domain of Crk binds to the phosphorylated Tyr118 of paxillin (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Double stranded DNA breaks (DSBs) are the most toxic of DNA lesions. They occur in response to genotoxic stress, and they are also an obligate intermediate in the V(D)J recombination events in the immune system. In mammalian cells, the most prominent mechanism by which cells deal with DSBs is known as NHEJ (non-homologous end-joining), and involves a core group of proteins that includes Ku, DNA-PK, XRCC4, and XLF (1).PAXX, (PAralog of XRCC4 and XLF, also known as C9orf142 or XLS), is a more recently identified component of the NHEJ machinery whose crystal structure resembles that of XRCC4 (2). PAXX directly interacts with Ku, and promotes accumulation of Ku at DSBs (2,3). Depletion of PAXX impairs cellular DSB repair (2-4,5). Paxx -/- mice develop normally with mild radiosensitivity, but a Paxx/Xlf double knockout is embryonic lethal in mice, indicating synthetic lethality between Paxx and Xlf (6). Paxx/Xlf double knockout have increased apopotosis in post-mitotic motor neurons, as well as impaired development of the adaptive immune system (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Nicotinamide phosphoribosyltransferase (NAMPT; also known as Pre-B cell-enhancing factor PBEF) catalyzes the synthesis of nicotinamide mononucleotide (NMN) from nicotinamide and 5-phosphoribosylpyrophosphate (PRPP), the rate-limiting step in the NAD biosynthesis pathway starting from nicotinamide (1,2). NAD biosynthesis mediated by NAMPT plays a critical role in glucose-stimulated insulin secretion in pancreatic beta cells (3). Both NAMPT inhibitors and activators have been sought for clinical applications (4,5). NAMPT has intra- and extracellular forms (iNAMPT and eNAMPT), and deacetylation of iNAMPT by SIRT1 promotes eNAMPT secretion through a nonclassical secretory pathway (3,6). eNAMPT, independent of its enzymatic activity, can induce epithelial-to-mesenchymal transition in mammary epithelial cells and promote monocyte differentiation into a tumor-supporting M2 macrophage (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Nicotinamide phosphoribosyltransferase (NAMPT; also known as Pre-B cell-enhancing factor PBEF) catalyzes the synthesis of nicotinamide mononucleotide (NMN) from nicotinamide and 5-phosphoribosylpyrophosphate (PRPP), the rate-limiting step in the NAD biosynthesis pathway starting from nicotinamide (1,2). NAD biosynthesis mediated by NAMPT plays a critical role in glucose-stimulated insulin secretion in pancreatic beta cells (3). Both NAMPT inhibitors and activators have been sought for clinical applications (4,5). NAMPT has intra- and extracellular forms (iNAMPT and eNAMPT), and deacetylation of iNAMPT by SIRT1 promotes eNAMPT secretion through a nonclassical secretory pathway (3,6). eNAMPT, independent of its enzymatic activity, can induce epithelial-to-mesenchymal transition in mammary epithelial cells and promote monocyte differentiation into a tumor-supporting M2 macrophage (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: ATP-dependent chromatin remodeling complexes play an essential role in the regulation of various nuclear processes, such as gene expression, DNA replication, and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits with a single molecule of the ATPase catalytic subunit BRM or BRG1, but not both. The activities of these two subunits drive the disruption of histone-DNA contacts that lead to changes in accessibility of crucial regulatory elements within chromatin (2-5). The BRM/BRG1 containing SWI/SNF complexes are recruited to target promoters by transcription factors, such as nuclear receptors, p53, RB, and BRCA1 to regulate gene activation, cell growth, the cell cycle, and differentiation processes (1,6-9).PBRM1/BAF180 is a unique member of the SWI/SNF complex PBAF, which binds to kinetochores in mitotic chromatin (10,11). PBAF is involved in nuclear receptor-mediated transcription and retinoic acid driven gene activation (12, 13). PBRM1/BAF180 has been shown to be a potent tumor suppressor, as it is the second-most mutated gene in renal carcinomas (14). Mutations of PBRM1/BAF180 have also been shown to be involved in breast cancer, and low expression relates to poorer prognosis (15,16)

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Western Blotting

Background: ATP-dependent chromatin remodeling complexes play an essential role in the regulation of various nuclear processes, such as gene expression, DNA replication, and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits with a single molecule of the ATPase catalytic subunit BRM or BRG1, but not both. The activities of these two subunits drive the disruption of histone-DNA contacts that lead to changes in accessibility of crucial regulatory elements within chromatin (2-5). The BRM/BRG1 containing SWI/SNF complexes are recruited to target promoters by transcription factors, such as nuclear receptors, p53, RB, and BRCA1 to regulate gene activation, cell growth, the cell cycle, and differentiation processes (1,6-9).PBRM1/BAF180 is a unique member of the SWI/SNF complex PBAF, which binds to kinetochores in mitotic chromatin (10,11). PBAF is involved in nuclear receptor-mediated transcription and retinoic acid driven gene activation (12, 13). PBRM1/BAF180 has been shown to be a potent tumor suppressor, as it is the second-most mutated gene in renal carcinomas (14). Mutations of PBRM1/BAF180 have also been shown to be involved in breast cancer, and low expression relates to poorer prognosis (15,16)

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The proprotein convertases (PCs) are enzymes that activate precursor proteins through proteolytic cleavage within the secretory pathway. PCs comprise several enzymes that are basic amino acid-specific proteinases (furin, PC1/3, PC2, PC4, PACE4, PC5/6, and PC7), as well as nonbasic amino acid convertases (S1P and PC9) (1). PCs have a common structure that includes an N-terminal signal peptide for secretory pathway targeting; a pro-domain that is thought to act as an intramolecular chaperone; a catalytic domain containing the active site; a P-domain that contributes to the overall folding of the enzyme by regulating stability, calcium-, and pH-dependence; and a C-terminal domain that interacts with the membrane (2). PCs act in a tissue- and substrate-specific fashion to generate an array of bioactive peptides and proteins from precursors, both in the brain and the periphery (3).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: p300/CBP-associated factor (PCAF), also known as lysine acetyl-transferase 2B (KAT2B), is a transcriptional adaptor protein and histone acetyl-transferase (HAT) that functions as the catalytic subunit of the PCAF transcriptional co-activator complex (1). PCAF is 73% homologous to GCN5L2, another HAT protein found in similar complexes (1,2). Like GCN5L2, PCAF acetylates histone H3 on Lys14 and histone H4 on Lys8, both of which contribute to gene activation by modulating chromatin structure and recruiting additional co-activator proteins that contain acetyl-lysine binding bromo-domains (3). PCAF also acetylates non-histone proteins including transcriptional activators (p53, E2F1, MyoD), general transcription factors (TFIIEβ and TFIIF) and architectural DNA binding proteins (HMGA1 and HMG17) (4-10). Acetylation of these proteins regulates their nuclear localization, protein stability, DNA binding, and co-activator association.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Phosphoenolpyruvate carboxykinase 1 (PCK1, PEPCK1 or PEPCK-C) is a cytosolic enzyme responsible for the conversion of oxaloacetate to phosphoenolpyruvate (1). PCK1 is involved in controlling the rate-limiting step of gluconeogenesis in the liver, which generates glucose from non-carbohydrate substrates such as lactate and glycerol (2). The deacetylase SirT1 stimulates transcription of PCK1 and glucose-6-phosphatase to activate gluconeogenesis (3). Depending on nutritional state, Stat3 can inhibit PCK1 and glucose-6-phosphatase expression and suppress gluconeogenesis (4). Relatively high glucose concentration can result in acetylation of PCK1 by P300 acetyltransferase, promoting an interaction between PCK1 and the E3 ligase UBR5 that leads to the PCK1 destabilization (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: PCK2 (PEPCK2 or PEPCK-M) encodes an isoform of phosphoenolpyruvate carboxykinase (PEPCK) that is found in the mitochondria of renal and hepatic tissues (1). PEPCK is involved in gluconeogenesis, the process of generating glucose from non-carbohydrate substrates such as lactate and glycerol (2). PEPCK catalyzes the reaction whereby oxaloacetate becomes phosphoenolpyruvate, a rate limiting step in the metabolic process (2). The predominant function of PCK2 is to process the lactate that is continually produced by red blood cells in the liver and kidney (1).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Proliferating cell nuclear antigen (PCNA) is a member of the DNA sliding clamp family of proteins that assist in DNA replication (1). Crystal structure data suggests that a PCNA homotrimer ring can encircle and slide along the DNA double helix (2). Multiple proteins involved in DNA replication, DNA repair, and cell cycle control bind to PCNA rather than directly associating with DNA, thus facilitating fast processing of DNA (reviewed in 3). PCNA protein expression is a well-accepted marker of proliferation.

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PCNA (D3H8P) XP® Rabbit mAb #13110.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry)

Background: Proliferating cell nuclear antigen (PCNA) is a member of the DNA sliding clamp family of proteins that assist in DNA replication (1). Crystal structure data suggests that a PCNA homotrimer ring can encircle and slide along the DNA double helix (2). Multiple proteins involved in DNA replication, DNA repair, and cell cycle control bind to PCNA rather than directly associating with DNA, thus facilitating fast processing of DNA (reviewed in 3). PCNA protein expression is a well-accepted marker of proliferation.

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PCNA (D3H8P) XP® Rabbit mAb #13110.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Proliferating cell nuclear antigen (PCNA) is a member of the DNA sliding clamp family of proteins that assist in DNA replication (1). Crystal structure data suggests that a PCNA homotrimer ring can encircle and slide along the DNA double helix (2). Multiple proteins involved in DNA replication, DNA repair, and cell cycle control bind to PCNA rather than directly associating with DNA, thus facilitating fast processing of DNA (reviewed in 3). PCNA protein expression is a well-accepted marker of proliferation.

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated PCNA (PC10) Mouse mAb #2586.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Proliferating cell nuclear antigen (PCNA) is a member of the DNA sliding clamp family of proteins that assist in DNA replication (1). Crystal structure data suggests that a PCNA homotrimer ring can encircle and slide along the DNA double helix (2). Multiple proteins involved in DNA replication, DNA repair, and cell cycle control bind to PCNA rather than directly associating with DNA, thus facilitating fast processing of DNA (reviewed in 3). PCNA protein expression is a well-accepted marker of proliferation.

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Proliferating cell nuclear antigen (PCNA) is a member of the DNA sliding clamp family of proteins that assist in DNA replication (1). Crystal structure data suggests that a PCNA homotrimer ring can encircle and slide along the DNA double helix (2). Multiple proteins involved in DNA replication, DNA repair, and cell cycle control bind to PCNA rather than directly associating with DNA, thus facilitating fast processing of DNA (reviewed in 3). PCNA protein expression is a well-accepted marker of proliferation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: PCSK7 (PC7) is a member of the subtilisin-like proprotein convertase family (1,2). Like other members of the family, the protein cleaves precursors at basic amino acids within the motif Arg/Lys-Xn-Arg (cleavage site) (n=2 or 4). PC7 was reported to be localized in the trans-golgi network and at the cell surface membrane, as well as in membrane internalized recycling vesicles (2,3). One function of PCSK7 is its critical role in growth factors processing, for example proEGF to EGF, proVEGF-C to VEGF-C, and BDNF neuropeptide maturation. PCSK7 is also involved in transferrin receptor shedding to regulate ion homeostasis (7,8) and MHC class I stability to regulate antigen presentation in the immunoresponse process (9).