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Product listing: Syk (D3Z1E) XP® Rabbit mAb (Biotinylated), UniProt ID P43405 #97818 to T-bet/TBX21 (D6N8B) XP® Rabbit mAb, UniProt ID Q9UL17 #13232

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Syk (D3Z1E) XP® Rabbit mAb #13198.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Syk is a protein tyrosine kinase that plays an important role in intracellular signal transduction in hematopoietic cells (1-3). Syk interacts with immunoreceptor tyrosine-based activation motifs (ITAMs) located in the cytoplasmic domains of immune receptors (4). It couples the activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation, and phagocytosis (4). There is also evidence of a role for Syk in nonimmune cells and investigators have indicated that Syk is a potential tumor suppressor in human breast carcinomas (5). Tyr323 is a negative regulatory phosphorylation site within the SH2-kinase linker region in Syk. Phosphorylation at Tyr323 provides a direct binding site for the TKB domain of Cbl (6,7). Tyr352 of Syk is involved in the association of PLCγ1 (8). Tyr525 and Tyr526 are located in the activation loop of the Syk kinase domain; phosphorylation at Tyr525/526 of human Syk (equivalent to Tyr519/520 of mouse Syk) is essential for Syk function (9).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Pacific Blue™ fluorescent dye and tested in-house for direct flow cytometry in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated antibody Syk (D3Z1E) XP® Rabbit mAb #13198.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Syk is a protein tyrosine kinase that plays an important role in intracellular signal transduction in hematopoietic cells (1-3). Syk interacts with immunoreceptor tyrosine-based activation motifs (ITAMs) located in the cytoplasmic domains of immune receptors (4). It couples the activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation, and phagocytosis (4). There is also evidence of a role for Syk in nonimmune cells and investigators have indicated that Syk is a potential tumor suppressor in human breast carcinomas (5). Tyr323 is a negative regulatory phosphorylation site within the SH2-kinase linker region in Syk. Phosphorylation at Tyr323 provides a direct binding site for the TKB domain of Cbl (6,7). Tyr352 of Syk is involved in the association of PLCγ1 (8). Tyr525 and Tyr526 are located in the activation loop of the Syk kinase domain; phosphorylation at Tyr525/526 of human Syk (equivalent to Tyr519/520 of mouse Syk) is essential for Syk function (9).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Syk (D3Z1E) XP® Rabbit mAb #13198.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Syk is a protein tyrosine kinase that plays an important role in intracellular signal transduction in hematopoietic cells (1-3). Syk interacts with immunoreceptor tyrosine-based activation motifs (ITAMs) located in the cytoplasmic domains of immune receptors (4). It couples the activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation, and phagocytosis (4). There is also evidence of a role for Syk in nonimmune cells and investigators have indicated that Syk is a potential tumor suppressor in human breast carcinomas (5). Tyr323 is a negative regulatory phosphorylation site within the SH2-kinase linker region in Syk. Phosphorylation at Tyr323 provides a direct binding site for the TKB domain of Cbl (6,7). Tyr352 of Syk is involved in the association of PLCγ1 (8). Tyr525 and Tyr526 are located in the activation loop of the Syk kinase domain; phosphorylation at Tyr525/526 of human Syk (equivalent to Tyr519/520 of mouse Syk) is essential for Syk function (9).

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

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

Background: Syk is a protein tyrosine kinase that plays an important role in intracellular signal transduction in hematopoietic cells (1-3). Syk interacts with immunoreceptor tyrosine-based activation motifs (ITAMs) located in the cytoplasmic domains of immune receptors (4). It couples the activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation, and phagocytosis (4). There is also evidence of a role for Syk in nonimmune cells and investigators have indicated that Syk is a potential tumor suppressor in human breast carcinomas (5). Tyr323 is a negative regulatory phosphorylation site within the SH2-kinase linker region in Syk. Phosphorylation at Tyr323 provides a direct binding site for the TKB domain of Cbl (6,7). Tyr352 of Syk is involved in the association of PLCγ1 (8). Tyr525 and Tyr526 are located in the activation loop of the Syk kinase domain; phosphorylation at Tyr525/526 of human Syk (equivalent to Tyr519/520 of mouse Syk) is essential for Syk function (9).

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

Application Methods: Western Blotting

Background: Arginine methylation is a prevalent PTM found on both nuclear and cytoplasmic proteins. Arginine methylated proteins are involved in many different cellular processes, including transcriptional regulation, signal transduction, RNA metabolism, and DNA damage repair (1-3). Arginine methylation is carried out by the arginine N-methyltransferase (PRMT) family of enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (4). There are three different types of arginine methylation: asymmetric dimethylarginine (aDMA, omega-NG,NG-dimethylarginine), where two methyl groups are placed on one of the terminal nitrogen atoms of the guanidine group of arginine; symmetric dimethylarginine (sDMA, omega-NG,N’G-dimethylarginine), where one methyl group is placed on each of the two terminal guanidine nitrogens of arginine; and monomethylarginine (MMA, omega-NG-dimethylarginine), where a single methyl group is placed on one of the terminal nitrogen atoms of arginine. Each of these modifications has potentially different functional consequences. Though all PRMT proteins catalyze the formation of MMA, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce aDMA, while Type II PRMTs (PRMT5 and 7) produce sDMA. Methylated arginine residues often reside in glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (5). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within proline-glycine-methionine rich (PGM) motifs (6).

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

Application Methods: Western Blotting

Background: The nucleosome is the primary chromatin building block and consists of DNA wrapped around an octamer made of paired histone proteins H2A, H2B, H3, and H4. Chromatin remodeling plays a critical role in the regulation of various nuclear activities, including transcription. Histone proteins are targets of post-translational modification, including acetylation, phosphorylation, ubiquitination, and methylation. Modified histone residues are recognized and bound by chromatin modifiers and the transcription machinery to regulate gene expression (1-4). Protein arginine methyl transferases (PRMTs) methylate histone proteins at arginine residues to generate mono-methylated, symmetrically di-methylated, or asymmetrically di-methylated proteins. Asymmetrically di-methylated arginine residues are found on histone H3 (Arg2, 8, 17, 26 and 42), histone H4 (Arg3), and histone H2A (Arg3) proteins. Asymmetric methylation is carried out by type 1 PRMTs, which include PRMT1, PRMT2, PRMT4/CARM1, and PRMT6. These modifications are often associated with actively transcribed genes. Symmetric di-methylation of arginine residues are found on histone H3 (Arg2 and 8), Histones H4 (Arg3), and H2A (Arg3). Symmetrically di-methylated histone arginine residues are generated by type II transferases PRMT5 and PRMT7, and are often associated with transcription repression (5-9). Arginine residues can also be deiminated by a protein arginine deiminase (PADI) to form the non-coded amino acid citrulline. Conversion of arginine to citrulline prevents methylation of this residue and is thought to regulate histone arginine methylation levels (10-13).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Symplekin is necessary for 3’-end cleavage and polyadenylation of mRNAs, histone 3’-end processing and polyadenylation in the cytoplasm (1-5). It is thought to act as a scaffolding protein that brings together factors involved in mRNA 3’-end processing (1,2). Symplekin also plays a role in transcription initiation and termination by RNA polymerase II (RNAPII) through bridging the interaction between the polyadenylation machinery and RNAPII (3,6,7). In addition to its role in mRNA 3’-end processing, research studies have shown that symplekin localizes at epithelial cell tight junctions where it may help to regulate tight junction assembly, thereby maintaining the integrity of the epithelial monolayer and cell polarity (8,9).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross reactivity as the unconjugated Synapsin-1 (D12G5) XP® Rabbit mAb #5297
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse and rat tissues. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Synapsin-1 (D12G5) XP® Rabbit mAb #5297.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

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

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

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Synaptophysin (SYP) is a neuronal synaptic vesicle glycoprotein that is expressed in neuroendocrine cells and neoplasms (1). Synaptophysin contains four transmembrane domains that form a hexameric channel or gap junction-like pore (2). Synaptophysin binds to the SNARE protein synaptobrevin/VAMP, which prevents the inclusion of synaptobrevin in the synaptic vesicle fusion complex and creates a pool of synaptobrevin for exocytosis when synapse activity increases (3). Synaptophysin is also responsible for targeting synaptobrevin 2/VAMP2 to synaptic vesicles, a critical component of the fusion complex (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: Synaptophysin (SYP) is a neuronal synaptic vesicle glycoprotein that is expressed in neuroendocrine cells and neoplasms (1). Synaptophysin contains four transmembrane domains that form a hexameric channel or gap junction-like pore (2). Synaptophysin binds to the SNARE protein synaptobrevin/VAMP, which prevents the inclusion of synaptobrevin in the synaptic vesicle fusion complex and creates a pool of synaptobrevin for exocytosis when synapse activity increases (3). Synaptophysin is also responsible for targeting synaptobrevin 2/VAMP2 to synaptic vesicles, a critical component of the fusion complex (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Synaptophysin (SYP) is a neuronal synaptic vesicle glycoprotein that is expressed in neuroendocrine cells and neoplasms (1). Synaptophysin contains four transmembrane domains that form a hexameric channel or gap junction-like pore (2). Synaptophysin binds to the SNARE protein synaptobrevin/VAMP, which prevents the inclusion of synaptobrevin in the synaptic vesicle fusion complex and creates a pool of synaptobrevin for exocytosis when synapse activity increases (3). Synaptophysin is also responsible for targeting synaptobrevin 2/VAMP2 to synaptic vesicles, a critical component of the fusion complex (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Synaptophysin (SYP) is a neuronal synaptic vesicle glycoprotein that is expressed in neuroendocrine cells and neoplasms (1). Synaptophysin contains four transmembrane domains that form a hexameric channel or gap junction-like pore (2). Synaptophysin binds to the SNARE protein synaptobrevin/VAMP, which prevents the inclusion of synaptobrevin in the synaptic vesicle fusion complex and creates a pool of synaptobrevin for exocytosis when synapse activity increases (3). Synaptophysin is also responsible for targeting synaptobrevin 2/VAMP2 to synaptic vesicles, a critical component of the fusion complex (4).

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

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

Background: Synaptophysin (SYP) is a neuronal synaptic vesicle glycoprotein that is expressed in neuroendocrine cells and neoplasms (1). Synaptophysin contains four transmembrane domains that form a hexameric channel or gap junction-like pore (2). Synaptophysin binds to the SNARE protein synaptobrevin/VAMP, which prevents the inclusion of synaptobrevin in the synaptic vesicle fusion complex and creates a pool of synaptobrevin for exocytosis when synapse activity increases (3). Synaptophysin is also responsible for targeting synaptobrevin 2/VAMP2 to synaptic vesicles, a critical component of the fusion complex (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Synaptotagmin 1 (SYT1) is an integral membrane protein found in synaptic vesicles thought to play a role in vesicle trafficking and exocytosis (1). Individual SYT1 proteins are composed of an amino-terminal transmembrane region, a central linker region and a pair of carboxy-terminal C2 domains responsible for binding Ca2+ (2). The C2 domains appear to be functionally distinct, with the C2A domain responsible for regulating synaptic vesicle fusion in a calcium-dependent manner during exocytosis while the C2B domain allows for interaction between adjacent SYT1 proteins (3). Because synaptotagmin 1 binds calcium and is found in synaptic vesicles, this integral membrane protein is thought to act as a calcium sensor in fast synaptic vesicle exocytosis. Evidence suggests possible roles in vesicle-mediated endocytosis and glucose-induced insulin secretion as well (4,5). SYT1 binds several different SNARE proteins during calcium-mediated vesicle endocytosis and an association between SYT1 and the SNARE protein SNAP-25 is thought to be a key element in vesicle-mediated exocytosis (6).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Syndecan 1 (D4Y7H) Rabbit mAb #12922.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Syndecans are a family of type 1 transmembrane heparan sulphate proteoglycans comprising 4 members in mammals (SDC-1 to -4) (1) encoded by four syndecan genes. Syndecans are involved in embryonic development, tumorigenesis, and angiogenesis (2). The extracellular domain harbors attachment sites for heparan sulfate and chondroitin sulfate chains, facilitating interaction with an array of proteins including a plethora of growth factors. In addition, the hydrophobic C-terminal intracellular domain can interact with proteins containing a PDZ domain (2). These interactions place syndecans as important integrators of membrane signaling (3). Syndecans undergo proteolytic cleavage causing the release of their extracellular domain (shedding), converting the membrane-bound proteins into soluble molecular effectors (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Syndecans are a family of type 1 transmembrane heparan sulphate proteoglycans comprising 4 members in mammals (SDC-1 to -4) (1) encoded by four syndecan genes. Syndecans are involved in embryonic development, tumorigenesis, and angiogenesis (2). The extracellular domain harbors attachment sites for heparan sulfate and chondroitin sulfate chains, facilitating interaction with an array of proteins including a plethora of growth factors. In addition, the hydrophobic C-terminal intracellular domain can interact with proteins containing a PDZ domain (2). These interactions place syndecans as important integrators of membrane signaling (3). Syndecans undergo proteolytic cleavage causing the release of their extracellular domain (shedding), converting the membrane-bound proteins into soluble molecular effectors (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: SynGAP is a synaptic GTPase-activating protein selectively expressed in the brain and found at higher concentrations specifically at excitatory synapses in the mammalian forebrain. SynGAP has a PH domain, a C2 domain, and a highly conserved RasGAP domain, which negatively regulates both Ras activity and its downstream signaling pathways. SynGAP interacts with the PDZ domains of SAP102, as well as PSD95, a postsynaptic scaffolding protein that couples SynGAP to NMDA receptors (1). SynGAP is phosphorylated by Ca2+/calmodulin-dependent protein kinase II (CaMKII) at Ser765 and Ser1123, among other sites (2,3). Phosphorylation of SynGAP results in stimulation of the GTPase activity of Ras, and PSD95 dependent CaMKII phosphorylation of SynGAP increases after transient brain ischemia (1,4). SynGAP is implicated in NMDAR- and CaMKII-dependent regulation of AMPAR trafficking and plays an important role in synaptic plasticity (3,5). SynGAP is critical during neuronal development as mice lacking SynGAP protein die postnatally. Furthermore, SynGAP mutant mice have reduced long-term potentiation (LTP) and perform poorly in spatial memory tasks (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: SynGAP is a synaptic GTPase-activating protein selectively expressed in the brain and found at higher concentrations specifically at excitatory synapses in the mammalian forebrain. SynGAP has a PH domain, a C2 domain, and a highly conserved RasGAP domain, which negatively regulates both Ras activity and its downstream signaling pathways. SynGAP interacts with the PDZ domains of SAP102, as well as PSD95, a postsynaptic scaffolding protein that couples SynGAP to NMDA receptors (1). SynGAP is phosphorylated by Ca2+/calmodulin-dependent protein kinase II (CaMKII) at Ser765 and Ser1123, among other sites (2,3). Phosphorylation of SynGAP results in stimulation of the GTPase activity of Ras, and PSD95 dependent CaMKII phosphorylation of SynGAP increases after transient brain ischemia (1,4). SynGAP is implicated in NMDAR- and CaMKII-dependent regulation of AMPAR trafficking and plays an important role in synaptic plasticity (3,5). SynGAP is critical during neuronal development as mice lacking SynGAP protein die postnatally. Furthermore, SynGAP mutant mice have reduced long-term potentiation (LTP) and perform poorly in spatial memory tasks (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: SynGAP is a synaptic GTPase-activating protein selectively expressed in the brain and found at higher concentrations specifically at excitatory synapses in the mammalian forebrain. SynGAP has a PH domain, a C2 domain, and a highly conserved RasGAP domain, which negatively regulates both Ras activity and its downstream signaling pathways. SynGAP interacts with the PDZ domains of SAP102, as well as PSD95, a postsynaptic scaffolding protein that couples SynGAP to NMDA receptors (1). SynGAP is phosphorylated by Ca2+/calmodulin-dependent protein kinase II (CaMKII) at Ser765 and Ser1123, among other sites (2,3). Phosphorylation of SynGAP results in stimulation of the GTPase activity of Ras, and PSD95 dependent CaMKII phosphorylation of SynGAP increases after transient brain ischemia (1,4). SynGAP is implicated in NMDAR- and CaMKII-dependent regulation of AMPAR trafficking and plays an important role in synaptic plasticity (3,5). SynGAP is critical during neuronal development as mice lacking SynGAP protein die postnatally. Furthermore, SynGAP mutant mice have reduced long-term potentiation (LTP) and perform poorly in spatial memory tasks (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Insulin binds to and activates its receptor and initiates a signaling cascade that eventually induces the translocation of the Glut4 glucose transporter from its intracellular locations to the plasma membrane. Initiating this pathway facilitates glucose uptake in fat and skeletal muscle cells (1). Synip and Syntaxin 4 are two proteins thought to be involved in the recruitment of Glut4-containing vesicles to plasma membrane (2,3). Synip associates with Syntaxin 4 when insulin is absent. Insulin signaling triggers the dissociation of the two proteins and allows Syntaxin 4 to complex with VAMP2, which is essential for Glut4 translocation to plasma membrane (2-4). Overexpression of a dominant-negative form of Synip prevents Glut4 from translocating to plasma membrane in response to insulin stimulation (3). Synip together with Syntaxin 4, therefore, regulates Glut 4 transport to plasma membrane.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Syntaxin 1A (STX1A) is a SNARE protein involved in intracellular membrane fusion, including synaptic vesicle fusion (1). At the synapse, syntaxin 1 is located at the presynaptic plasma membrane and is therefore categorized as a t-SNARE protein (2). The amino-terminal domain of syntaxin 1 interacts with Munc18-1 and this interaction is essential for synaptic vesicle fusion (3). Although originally characterized from neural tissues, research studies have demonstrated syntaxin 1A expression in exocrine tissues such as pancreatic islets (4) where it negatively regulates insulin release (5).

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

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

Background: Syntaxin 6 is a ubiquitously expressed S25C family member of the SNARE proteins (1,2). The protein has an amino-terminal H1 domain followed by an H2 SNARE domain and a carboxy-terminal membrane anchor (3). Syntaxin 6 protein is localized to the trans-Golgi and within endosomes and regulates membrane trafficking by partnering with a variety of other SNARE proteins (3-5). Depending on cell type and SNARE parter, syntaxin 6 is involved in the regulation of GLUT4 trafficking, neutrophil exocytosis and granule secretion (6-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Synoviolin-1 (SYVN1/HRD1) is a RING-type E3 ubiquitin-protein ligase and major component of the endoplasmic reticulum (ER) quality control system that is involved in the ubiquitin-dependent degradation of misfolded proteins (1). SYVN1 is a multispanning ER membrane protein whose expression is upregulated at the protein level under conditions that promote ER stress (1-4). Research studies have shown that SYVN1 is an anti-apoptotic factor that is implicated in the pathogenesis of arthropathy by promoting synovial hyperplasia (5). Furthermore, gene-targeting studies have demonstrated that SYVN1 expression is indispensable for embryogenesis (6).

$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 T-bet/TBX21 (D6N8B) XP® Rabbit mAb #13232.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: The T-box gene family consists of transcription factors characterized by a related DNA-binding domain (T-box) of approximately 200 amino acids (1,2). The T-box genes exhibit diverse temporal and spatial patterns in the developing embryo. Studies have demonstrated members of this family play crucial roles during embryogenesis in a wide range of organisms by regulating cell fate decisions to establish the early body plan and to regulate later processes underlying organogenesis (3-5). Mutations in T-box genes are associated with many developmental defects (6). Recent studies also indicate potential roles in cancer by members of T-box family (7-9).

$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 cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated T-bet/TBX21 (D6N8B) XP® Rabbit mAb #13232.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: The T-box gene family consists of transcription factors characterized by a related DNA-binding domain (T-box) of approximately 200 amino acids (1,2). The T-box genes exhibit diverse temporal and spatial patterns in the developing embryo. Studies have demonstrated members of this family play crucial roles during embryogenesis in a wide range of organisms by regulating cell fate decisions to establish the early body plan and to regulate later processes underlying organogenesis (3-5). Mutations in T-box genes are associated with many developmental defects (6). Recent studies also indicate potential roles in cancer by members of T-box family (7-9).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The T-box gene family consists of transcription factors characterized by a related DNA-binding domain (T-box) of approximately 200 amino acids (1,2). The T-box genes exhibit diverse temporal and spatial patterns in the developing embryo. Studies have demonstrated members of this family play crucial roles during embryogenesis in a wide range of organisms by regulating cell fate decisions to establish the early body plan and to regulate later processes underlying organogenesis (3-5). Mutations in T-box genes are associated with many developmental defects (6). Recent studies also indicate potential roles in cancer by members of T-box family (7-9).