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Human Protein Targeting

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Peroxin-5 (PEX5) is the shuttle receptor that delivers proteins to peroxisomes (1). In the cytosol, PEX5 binds to the peroxisomal targeting signal 1 (PTS1), a short peptide sequence present at the extreme C termini of newly synthesized peroxisomal matrix proteins. The PEX5-cargo complex interacts with the peroxisomal docking/translocation machinery on the peroxisomal membrane, where the cargo is released into the organelle matrix. During this process, PEX5 is monoubiquitinated at a conserved cysteine residue, and the ubiquitin-PEX5 conjugate is released from the organelle into the cytosol, where PEX5 is deubiquitinated and ready the next round of targeting (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Sec61 translocon is a channel complex located on the endoplasmic reticulum (ER) membrane to mediate membrane protein insertion into the organelle (1). There are three components in the complex, Sec61A, Sec61B, and Sec61G (2). Sec61A is the main component of the channel on the ER membrane and directly contacts nascent synthesized polypeptide TMD (transmembrane domain) for insertion (3). Sec61G functions in stablizing the channel (3). In addition to TMD insertion, Sec61 translocon has also been shown to be involved in ER calcium leakage (4,5). Both Bip and calmodulin can inhibit this leakage by their interaction with Sec61A (6,7). Sec61B has no obvious function related to target protein ER membrane insertion, but is involved in other vesicle trafficking processes such as EGFR and Her2 trafficking from the cytosol to nucleus (8,9), Gurken trafficking from Golgi to plasma membrane (10), and copper-transporting ATPase membrane distribution (11).

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

Application Methods: Western Blotting

Background: The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways (1,2). 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ, and η that have been identified in mammals. The initially described α and δ isoforms are confirmed to be phosphorylated forms of β and ζ, respectively (3). Through their amino-terminal α helical region, 14-3-3 proteins form homo- or heterodimers that interact with a wide variety of proteins: transcription factors, metabolic enzymes, cytoskeletal proteins, kinases, phosphatases, and other signaling molecules (3,4). The interaction of 14-3-3 proteins with their targets is primarily through a phospho-Ser/Thr motif. However, binding to divergent phospho-Ser/Thr motifs, as well as phosphorylation independent interactions has been observed (4). 14-3-3 binding masks specific sequences of the target protein, and therefore, modulates target protein localization, phosphorylation state, stability, and molecular interactions (1-4). 14-3-3 proteins may also induce target protein conformational changes that modify target protein function (4,5). Distinct temporal and spatial expression patterns of 14-3-3 isoforms have been observed in development and in acute response to extracellular signals and drugs, suggesting that 14-3-3 isoforms may perform different functions despite their sequence similarities (4). Several studies suggest that 14-3-3 isoforms are differentially regulated in cancer and neurological syndromes (2,3).

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

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: SORL1, also called SorLA, is a 250 kDa type-1 membrane protein found in neurons of the central and peripheral nervous system (1). SORL1 is related to the yeast transporter Vps10p (2). While its exact function is unknown, because it shuttles between the Golgi apparatus and endolysosomal compartments, and given its structural similarity with Vps10p, it has been suggested that SORL1 acts in intracellular trafficking (3). Interestingly, SORL1 expression has been shown to be decreased in the brain of patients with Alzheimer's disease (4), and research studies have demonstrated a role for SORL1 as a neuronal sorting receptor that binds APP and regulates its trafficking and proteolytic processing, thus regulating the production of amyloid-beta peptides (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Sec61 translocon is a channel complex located on the endoplasmic reticulum (ER) membrane to mediate membrane protein insertion into the organelle (1). There are three components in the complex, Sec61A, Sec61B, and Sec61G (2). Sec61A is the main component of the channel on the ER membrane and directly contacts nascent synthesized polypeptide TMD (transmembrane domain) for insertion (3). Sec61G functions in stablizing the channel (3). In addition to TMD insertion, Sec61 translocon has also been shown to be involved in ER calcium leakage (4,5). Both Bip and calmodulin can inhibit this leakage by their interaction with Sec61A (6,7). Sec61B has no obvious function related to target protein ER membrane insertion, but is involved in other vesicle trafficking processes such as EGFR and Her2 trafficking from the cytosol to nucleus (8,9), Gurken trafficking from Golgi to plasma membrane (10), and copper-transporting ATPase membrane distribution (11).

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

Application Methods: Western Blotting

Background: CDC37 is an important component of the HSP90 chaperone complex (1,2). It was initially identified for its involvement in cell-cycle progression and was later found to have a much broader role as a chaperone for a wide variety of kinases and other proteins (1-3). CDC37 protein has an amino-terminal kinase binding domain followed by a central HSP90 binding domain. It recruits and stabilizes kinases in the HSP90 complex by protecting the newly synthesized kinase peptide chain from degradation and promoting the next step of protein maturation (4,5). CDC37 also suppresses the ATPase activity of HSP90, thereby leading to conformational changes in the complex that preclude target kinase loading (6). CDC37 has been proposed as a therapeutic target because of its important role in multiple kinase pathways involved in proliferation and cancer cell survival, including Raf, Akt, Src, and ErbB2 pathways (7,8).

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

Application Methods: Western Blotting

Background: CDC37 is an important component of the HSP90 chaperone complex (1,2). It was initially identified for its involvement in cell-cycle progression and was later found to have a much broader role as a chaperone for a wide variety of kinases and other proteins (1-3). CDC37 protein has an amino-terminal kinase binding domain followed by a central HSP90 binding domain. It recruits and stabilizes kinases in the HSP90 complex by protecting the newly synthesized kinase peptide chain from degradation and promoting the next step of protein maturation (4,5). CDC37 also suppresses the ATPase activity of HSP90, thereby leading to conformational changes in the complex that preclude target kinase loading (6). CDC37 has been proposed as a therapeutic target because of its important role in multiple kinase pathways involved in proliferation and cancer cell survival, including Raf, Akt, Src, and ErbB2 pathways (7,8).

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

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

Background: CDC37 is an important component of the HSP90 chaperone complex (1,2). It was initially identified for its involvement in cell-cycle progression and was later found to have a much broader role as a chaperone for a wide variety of kinases and other proteins (1-3). CDC37 protein has an amino-terminal kinase binding domain followed by a central HSP90 binding domain. It recruits and stabilizes kinases in the HSP90 complex by protecting the newly synthesized kinase peptide chain from degradation and promoting the next step of protein maturation (4,5). CDC37 also suppresses the ATPase activity of HSP90, thereby leading to conformational changes in the complex that preclude target kinase loading (6). CDC37 has been proposed as a therapeutic target because of its important role in multiple kinase pathways involved in proliferation and cancer cell survival, including Raf, Akt, Src, and ErbB2 pathways (7,8).

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

Application Methods: Western Blotting

Background: The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways (1,2). 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ, and η that have been identified in mammals. The initially described α and δ isoforms are confirmed to be phosphorylated forms of β and ζ, respectively (3). Through their amino-terminal α helical region, 14-3-3 proteins form homo- or heterodimers that interact with a wide variety of proteins: transcription factors, metabolic enzymes, cytoskeletal proteins, kinases, phosphatases, and other signaling molecules (3,4). The interaction of 14-3-3 proteins with their targets is primarily through a phospho-Ser/Thr motif. However, binding to divergent phospho-Ser/Thr motifs, as well as phosphorylation independent interactions has been observed (4). 14-3-3 binding masks specific sequences of the target protein, and therefore, modulates target protein localization, phosphorylation state, stability, and molecular interactions (1-4). 14-3-3 proteins may also induce target protein conformational changes that modify target protein function (4,5). Distinct temporal and spatial expression patterns of 14-3-3 isoforms have been observed in development and in acute response to extracellular signals and drugs, suggesting that 14-3-3 isoforms may perform different functions despite their sequence similarities (4). Several studies suggest that 14-3-3 isoforms are differentially regulated in cancer and neurological syndromes (2,3).

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

Application Methods: Western Blotting

Background: Ribosomal protein L11 (RPL11) is a nucleolar protein and component of the 60S ribosomal subunit. Research studies have shown that RPL11 plays a critical role in eukaryotic ribosome biogenesis (1). It has also been suggested that extraribosomal RPL11 functions in an RP-MDM2-p53 network in which RPL11 acts as a sensor of nucleolar stresses that perturb ribosome biogenesis (2). Indeed, RPL11 contributes to enhanced p53 stability and transcriptional activity in response to nucleolar stress and impaired ribosome biogenesis by binding and inhibiting the ubiquitin ligase activity of MDM2 (2-9). In addition to regulating p53 activity, research studies have also shown that RPL11 can inhibit cell cycle progression and ribosome biogenesis in response to nucleolar stress through repression of c-Myc transcriptional activity as well as its mRNA translation (10-12). Mutations in the RPL11 gene have been found in patients with Diamond-Blackfan anemia (13).

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

Application Methods: Western Blotting

Background: CDC37 is an important component of the HSP90 chaperone complex (1,2). It was initially identified for its involvement in cell-cycle progression and was later found to have a much broader role as a chaperone for a wide variety of kinases and other proteins (1-3). CDC37 protein has an amino-terminal kinase binding domain followed by a central HSP90 binding domain. It recruits and stabilizes kinases in the HSP90 complex by protecting the newly synthesized kinase peptide chain from degradation and promoting the next step of protein maturation (4,5). CDC37 also suppresses the ATPase activity of HSP90, thereby leading to conformational changes in the complex that preclude target kinase loading (6). CDC37 has been proposed as a therapeutic target because of its important role in multiple kinase pathways involved in proliferation and cancer cell survival, including Raf, Akt, Src, and ErbB2 pathways (7,8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: CDC37 is an important component of the HSP90 chaperone complex (1,2). It was initially identified for its involvement in cell-cycle progression and was later found to have a much broader role as a chaperone for a wide variety of kinases and other proteins (1-3). CDC37 protein has an amino-terminal kinase binding domain followed by a central HSP90 binding domain. It recruits and stabilizes kinases in the HSP90 complex by protecting the newly synthesized kinase peptide chain from degradation and promoting the next step of protein maturation (4,5). CDC37 also suppresses the ATPase activity of HSP90, thereby leading to conformational changes in the complex that preclude target kinase loading (6). CDC37 has been proposed as a therapeutic target because of its important role in multiple kinase pathways involved in proliferation and cancer cell survival, including Raf, Akt, Src, and ErbB2 pathways (7,8).

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

Application Methods: Western Blotting

Background: Ribosomal protein L5 (RPL5) is one of several proteins that comprise the 60S ribosomal subunit. RPL5 binds 5S rRNA and the nucleolar RPL11 protein to form the 5S ribonucleoprotein particle (RNP) that is incorporated into the large 60S ribosomal subunit (1). An RP-MDM2-p53 protein complex that contains ribosomal proteins RPL5, RPL11, and RPL23 acts as a nucleolar stress sensor that binds and inhibits MDM2 ubiquitin ligase activity and enhances p53-mediated transcriptional activity (2,3). RPL5 cooperates with RPL11 to influence ribosome biogenesis through regulating expression of the transcription factor c-Myc, which acts as the master regulator of ribosome biogenesis (4). Mutations in the corresponding RPL5 gene are associated with Diamond-Blackfan anemia, which is a form of red blood cell aplasia, and some cases of pediatric T-cell acute lymphoblastic leukemia (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Ribosomal protein L5 (RPL5) is one of several proteins that comprise the 60S ribosomal subunit. RPL5 binds 5S rRNA and the nucleolar RPL11 protein to form the 5S ribonucleoprotein particle (RNP) that is incorporated into the large 60S ribosomal subunit (1). An RP-MDM2-p53 protein complex that contains ribosomal proteins RPL5, RPL11, and RPL23 acts as a nucleolar stress sensor that binds and inhibits MDM2 ubiquitin ligase activity and enhances p53-mediated transcriptional activity (2,3). RPL5 cooperates with RPL11 to influence ribosome biogenesis through regulating expression of the transcription factor c-Myc, which acts as the master regulator of ribosome biogenesis (4). Mutations in the corresponding RPL5 gene are associated with Diamond-Blackfan anemia, which is a form of red blood cell aplasia, and some cases of pediatric T-cell acute lymphoblastic leukemia (5,6).

$320
100 µg
This peptide is used to block Phospho-S6 Ribosomal Protein (Ser235/236) Antibody #2211 reactivity.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

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

Application Methods: Western Blotting

Background: Ribosomal protein L26 (RPL26) is a component of the 60S ribosomal subunit and is involved in translation (1,2). It was shown that RPL26 increases the translation of p53 mRNA by binding to its 5' untranslated region (UTR) after DNA damage. Studies found that overexpression of RPL26 enhances the binding of p53 mRNA to the ribosomes and increases p53 translation. Overexpression of RPL26 also induces cell-cycle arrest at G1 phase and increases radiation-stimulated apoptosis (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Ribosomal protein L13a (RPL13a, 60S ribosomal protein L13a) is a member of the L13 ribosomal protein family and a structural component of the 60S ribosomal subunit (1). RPL13a appears to play an important role in transcript-specific translational silencing. Interferon-γ induces the phosphorylation of RPL13a and triggers the release of this protein from the 60S ribosomal subunit (2). Free RPL13a protein binds to the GAIT (interferon-γ-activated inhibitor of translation) complex at the 3'-UTR of ceruloplasmin (Cp) mRNA to repress Cp expression (2). RPL13a bound to the GAIT complex interacts with eIF4G, which prevents the recruitment of 43S ribosomal subunit and results in transcript-specific translation suppression (3).

$364
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluorescence of human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-S6 Ribosomal Protein (Ser235/236) (D57.2.2E) XP® Rabbit mAb #4858.
APPLICATIONS
REACTIVITY
Human, Mink, Monkey, Mouse, Rat, S. cerevisiae

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$327
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 and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-S6 Ribosomal Protein (Ser235/236) (2F9) Rabbit mAb #4856.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$307
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).