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Product listing: XPC (D1M5Y) Rabbit mAb, UniProt ID Q01831 #14768 to ZIP7/SLC39A7 (D1O3A) Rabbit mAb, UniProt ID Q92504 #33176

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Nucleotide excision repair (NER) is a process by which cells identify and repair DNA lesions resulting from chemical or radiation exposure (1). XPC forms a complex with HR23B (2) that acts as a damage sensor due to its high affinity for geometry distorting DNA lesions. This complex localizes to sites of DNA damage and recruits the remaining members of the preincision complex necessary for initiation of NER (3). XPC is one of eight NER proteins (XPA-G, XPV) where defects result in Xeroderma pigmentosum, a disease characterized by sunlight sensitivity, a predisposition to cancer of exposed tissue, and, in some instances, neurological defects (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: XPB and XPD are ATPase/helicase subunits of the TFIIH complex that are involved in nucleotide excision repair (NER) to remove lesions and photoproducts generated by UV light (1). XPB and XPD are 3’-5’ and 5’-3’ DNA helicases, respectively, that play a role in opening of the DNA damage site to facilitate repair (2,3). XPB and XPD both play an important role in maintaining genomic stability, and researchers have linked mutations of these proteins to Xeroderma Pigmentosum (XP) and Trichothiodystrophy (TTD). XP patients have abnormalities in skin pigmentation and are highly susceptible to skin cancers, while TTD patients exhibit symptoms such as brittle hair, neurological abnormalities, and mild photosensitivity (4). In addition to their role in NER, XPB and XPD are involved in transcription initiation as part of the TFIIH core complex (5). The helicase activity of XPB unwinds DNA around the transcription start site to facilitate RNA polymerase II promoter clearance and initiation of transcription (6). XPD plays a structural role linking core TFIIH components with the cdk-activating kinase (CAK) complex that phosphorylates the C-terminus of the largest subunit of RNA polymerase II, leading to transcription initiation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Western Blotting

Background: DNA repair systems operate in all living cells to manage a variety of DNA lesions. Nucleotide excision repair (NER) is implemented in cases where bulky helix-distorting lesions occur, such as those brought about by UV and certain chemicals (1). Excision Repair Cross Complementing 4 (ERCC4, XPF) forms a complex with the ERCC1 excision repair protein to create an essential 5’ endonuclease responsible for lesion excision (2). ERCC1-XPF is also required for repair of DNA interstrand crosslinks (ICLs) (3) and involved in repair of double strand breaks (4). Mutations in the corresponding XPF gene cause specific forms of xeroderma pigmentosum, Cockayne syndrome, and Fanconi anemia, while altered XPF protein levels may be associated with disease progression and response to treatment in specific human cancers (5,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: 5'-3' exoribonuclease 2 (XRN2) is a nuclear exonuclease that degrades RNA containing a 5’-monophosphate to component mononucleotides. XRN2 also plays an important role in the termination of transcription at the 3’-end of genes by displacing RNA polymerase II (RNAPII) from the DNA strand (1,2). According to the ‘torpedo’ model of transcription termination, XRN2 gains access to the 5’ phosphate of the nascent RNA during co-transcriptional polyadenylation site cleavage. XRN2 degrades RNA at a faster rate than RNAPII-mediated RNA synthesis, resulting in the eviction of RNAPII from the template (3-5). In addition, XRN2 is essential for maturation of 5.8S and 28S ribosomal RNA and small nucleolar RNA molecules (2). Several research studies suggest that XRN2 plays a role in the quality control check of RNA molecules. XRN2 co-transcriptionally degrades aberrant nuclear mRNA transcripts that result from defective 5’mRNA capping, splicing, or 3’end formation (6). XRN2 exonuclease rapidly degrades hypomodified tRNA and excess miRNA molecules, indicating that XRN2 likely regulates tRNA and miRNA quality control as well (7-9).

$269
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

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

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (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 flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated YAP (D8H1X) XP® Rabbit mAb #14074.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (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 cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated YAP (D8H1X) XP® Rabbit mAb #14074.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (9).

$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 YAP (D8H1X) XP® Rabbit mAb #14074.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (9).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated antibody YAP (D8H1X) XP® Rabbit mAb #14074.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated YAP (D8H1X) XP® Rabbit mAb #14074.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (9).

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

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

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (9).

$305
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 YAP/TAZ (D24E4) Rabbit mAb #8418.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (9).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated YAP/TAZ (D24E4) Rabbit mAb #8418.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The Y-box binding protein 1 (YB1) belongs to a family of evolutionarily conserved, multifunctional Y-box proteins that bind single-stranded DNA and RNA and function as regulators of transcription, RNA metabolism, and protein synthesis (1). YB1 binds to Y-box sequences (TAACC) found in multiple gene promoters and can positively or negatively regulate transcription. YB1 activates genes associated with proliferation and cancer, such as cyclin A, cyclin B1, matrix metalloproteinase-2 (MMP-2), and the multi-drug resistance 1 (MDR1) gene (2-4). YB1 represses genes associated with cell death, including the Fas cell death-associated receptor and the p53 tumor suppressor gene (5-7). It also interacts with the RNA-splicing factor SRp30c and stabilizes interleukin-2 (IL-2) mRNA upon induction of T lymphocytes by IL-2 (8,9). The majority of YB1 protein localizes to the cytoplasm, with a minor pool found in the nucleus; however, nuclear localization appears to be critical for its role in promoting proliferation. Nuclear translocation is cell cycle regulated, with YB1 protein accumulating in the nucleus during G1/S phase (2). In addition, nuclear translocation is induced in response to extracellular stimuli such as hyperthermia and UV irradiation, or treatment of cells with thrombin, interferons, or insulin-like growth factor (IGF-I) (2,10). Treatment of the MCF7 breast cancer cell line with IGF-I results in Akt-mediated phosphorylation of YB1 at Ser102, which is required for nuclear translocation of YB1 and its ability to promote anchorage-independent growth (10). Research studies have shown that YB1 is overexpressed in many malignant tissues, including breast cancer, non-small cell lung carcinoma, ovarian adenocarcinomas, human osteosarcomas, colorectal carcinomas, and malignant melanomas. Investigators have shown that nuclear YB1 expression correlates with high levels of proliferation, drug resistance, and poor tumor prognosis (2,7,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: The Y-box binding protein 1 (YB1) belongs to a family of evolutionarily conserved, multifunctional Y-box proteins that bind single-stranded DNA and RNA and function as regulators of transcription, RNA metabolism, and protein synthesis (1). YB1 binds to Y-box sequences (TAACC) found in multiple gene promoters and can positively or negatively regulate transcription. YB1 activates genes associated with proliferation and cancer, such as cyclin A, cyclin B1, matrix metalloproteinase-2 (MMP-2), and the multi-drug resistance 1 (MDR1) gene (2-4). YB1 represses genes associated with cell death, including the Fas cell death-associated receptor and the p53 tumor suppressor gene (5-7). It also interacts with the RNA-splicing factor SRp30c and stabilizes interleukin-2 (IL-2) mRNA upon induction of T lymphocytes by IL-2 (8,9). The majority of YB1 protein localizes to the cytoplasm, with a minor pool found in the nucleus; however, nuclear localization appears to be critical for its role in promoting proliferation. Nuclear translocation is cell cycle regulated, with YB1 protein accumulating in the nucleus during G1/S phase (2). In addition, nuclear translocation is induced in response to extracellular stimuli such as hyperthermia and UV irradiation, or treatment of cells with thrombin, interferons, or insulin-like growth factor (IGF-I) (2,10). Treatment of the MCF7 breast cancer cell line with IGF-I results in Akt-mediated phosphorylation of YB1 at Ser102, which is required for nuclear translocation of YB1 and its ability to promote anchorage-independent growth (10). Research studies have shown that YB1 is overexpressed in many malignant tissues, including breast cancer, non-small cell lung carcinoma, ovarian adenocarcinomas, human osteosarcomas, colorectal carcinomas, and malignant melanomas. Investigators have shown that nuclear YB1 expression correlates with high levels of proliferation, drug resistance, and poor tumor prognosis (2,7,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The cellular oncogene c-Yes and its viral homologue v-Yes (the transforming gene of Yamaguchi 73 and Esh avian sarcoma viruses) encode a 60 kDa, cytoplasmic, membrane-associated, protein-tyrosine kinase (1). Yes belongs to the Src kinase family and is ubiquitously expressed in many tissues and cells. Like other Src family members, Yes contains several conserved functional domains such as an N-terminal myristoylation sequence for membrane targeting, SH2 and SH3 domains, a kinase domain, and a C-terminal non-catalytic domain (2). Although several lines of evidence support redundancy in signaling between Yes and other Src family kinases, there is also a growing body of evidence indicating specificity in Yes signaling (2). Yes is activated downstream of a multitude of cell surface receptors, including receptor tyrosine kinases, G protein-coupled receptors, and cytokine receptors (3). In addition, both Yes and Src kinases are activated during the cell cycle transition from G2 to M phase (3). Investigators have found that dysfunction of Yes is associated with the development of various cancers (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: YKL-40, also known as Chitinase-3-like protein 1 (CHI3L1), is a secreted glycoprotein encoded by the CHI3L1 gene (1,2). Unlike other members of the chitinase-like protein family, YKL-40 is not an active chitinase. It is produced by activated macrophages, chondrocytes, neutrophils, and synovial cells. It is a pro-inflammatory molecule that contributes to the progression of many inflammatory diseases, including fibrosis, neurodegenerative disease, breast, lung, prostate, liver, bladder, colon, and other types of cancers (3,4). Levels of YKL-40 in serum and plasma in patients with various types of tumors have been reported to predict poor prognosis, and in some clinical assays YKL-40 is being used as a predictive biomarker of cancer outcome (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: YTH domain-containing protein 1 (YTHDC1) and YTH domain-containing protein 2 (YTHDC2) both belong to a family of proteins that bind to RNA. YTHDC1 and YTHDC2 both recognize and bind to N6-methyladenosine(m6A)-containing RNAs; binding is mediated through the YTH domains (1-3). m6A is a modification that is present at internal sites of mRNAs and some non-coding RNAs and plays a role in regulating mRNA splicing, processing, and stability. YTHDC1, also known as splicing factor YT521, regulates alternative splicing by functioning as a key regulator of exon-inclusion or exon-skipping. YTHDC1 promotes exon-inclusion by recruiting pre-mRNA splicing factor SRSF3 to regions containing m6A, while repressing exon-skipping by blocking SRSF10 binding to these same regions (2). Increased expression of YTHDC1 promotes malignant endometrial carcinoma (EC) through alternative splicing of vascular endothelial growth factor A (VEGF-A), resulting in an increase in VEGF-165 isoform and increased EC cell invasion (4). YTHDC2 functions to enhance the translation efficiency of target mRNAs and may play a role in spermatogenesis (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: YTH domain-containing protein 1 (YTHDC1) and YTH domain-containing protein 2 (YTHDC2) both belong to a family of proteins that bind to RNA. YTHDC1 and YTHDC2 both recognize and bind to N6-methyladenosine(m6A)-containing RNAs; binding is mediated through the YTH domains (1-3). m6A is a modification that is present at internal sites of mRNAs and some non-coding RNAs and plays a role in regulating mRNA splicing, processing, and stability. YTHDC1, also known as splicing factor YT521, regulates alternative splicing by functioning as a key regulator of exon-inclusion or exon-skipping. YTHDC1 promotes exon-inclusion by recruiting pre-mRNA splicing factor SRSF3 to regions containing m6A, while repressing exon-skipping by blocking SRSF10 binding to these same regions (2). Increased expression of YTHDC1 promotes malignant endometrial carcinoma (EC) through alternative splicing of vascular endothelial growth factor A (VEGF-A), resulting in an increase in VEGF-165 isoform and increased EC cell invasion (4). YTHDC2 functions to enhance the translation efficiency of target mRNAs and may play a role in spermatogenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: YY1 (Yin Yang1) is a ubiquitously expressed transcription factor with fundamental roles in embryogenesis, differentiation, replication and proliferation. YY1 contains four zinc finger motifs of the Cys-Cys-His-His type and can activate different eukaryotic genes (such as CREB, c-myc, Histone H4, p53 and PARP-1) or repress different eukaryotic genes (such as α-actin, IFN-β and IFN-γ) as well as regulate some viral promoters (1). YY1 deficient embryos die approximately at the time of implantation, suggesting that YY1 has an essential role in embryonic development (2). YY1 is overexpressed in cancer cells such as prostate cancer and therefore may be considered a prognostic marker (1).

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

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

Background: YY1 (Yin Yang1) is a ubiquitously expressed transcription factor with fundamental roles in embryogenesis, differentiation, replication and proliferation. YY1 contains four zinc finger motifs of the Cys-Cys-His-His type and can activate different eukaryotic genes (such as CREB, c-myc, Histone H4, p53 and PARP-1) or repress different eukaryotic genes (such as α-actin, IFN-β and IFN-γ) as well as regulate some viral promoters (1). YY1 deficient embryos die approximately at the time of implantation, suggesting that YY1 has an essential role in embryonic development (2). YY1 is overexpressed in cancer cells such as prostate cancer and therefore may be considered a prognostic marker (1).

$305
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 of human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$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.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Zap-70 (D1C10E) XP® Rabbit mAb #3165.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

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

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

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The ZFX (X-linked zinc finger protein) gene is expressed from the inactive X chromosome and is structurally similar to its homologue on the Y chromosome, ZFY (1). Transcripts of ZFX and ZFY encode proteins composed of a highly acidic amino-terminal domain and a carboxy-terminal zinc-finger motif that is commonly associated with nucleic acid-binding proteins (2). Both ZFY and ZFX are probable transcriptional activators and may function in sex determination (3). Multiple alternatively spliced transcript variants of ZFX, encoding different isoforms, have been identified and may be functionally distinct (2). Conditional gene targeting studies in mouse have suggested ZFX is also required for self-renewal of embryonic and hematopoietic stem cells (4). ZFX has also been suggested to play a role in proliferation and expansion of B cells, and could contribute to lymphocyte homeostasis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The solute carrier family 39 (zinc transporter) member 7 (SLC39A7, ZIP7) is an ER and Golgi membrane protein that regulates cellular zinc homeostasis by controlling release of zinc from these organelles to the cytoplasm (1,2). Zinc release mediated by ZIP7 results in activation of protein kinases that are involved in cell proliferation and migration (3,4). The protein kinase CK2 phosphorylates and activates ZIP7 in response to extracellular signals, such as growth factor stimulation (4,5). Increased expression of ZIP7 is observed in breast cancer tissues (6). Research studies indicate that ZIP7 is responsible for activation of multiple tyrosine kinases in aggressive, tamoxifen-resistant breast cancer (7,8).