20% off purchase of 3 or more products* | Learn More >>

Product listing: CLIC1 (D7D6H) Rabbit mAb, UniProt ID O00299 #53424 to Coronin 1A (D6K5B) XP® Rabbit mAb, UniProt ID P31146 #92904

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Chloride intracellular channel (CLIC) proteins belong to a family of highly conserved transport proteins found as both soluble and membrane-bound forms (1). Although CLIC proteins have putative, selective chloride ion channel activity, they are structural homologs to members of the glutathione-S-transferase protein superfamily and are likewise regulated by redox status (2). CLIC proteins are distinct from other ion channels in that they are found as both soluble and integral membrane forms, and their form determines their function (3-6). Chloride intracellular channel proteins are ubiquitously expressed in numerous tissue types and are involved in diverse biological functions (1,2).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Chloride intracellular channel (CLIC) proteins belong to a family of highly conserved transport proteins found as both soluble and membrane-bound forms (1). Although CLIC proteins have putative, selective chloride ion channel activity, they are structural homologs to members of the glutathione-S-transferase protein superfamily and are likewise regulated by redox status (2). CLIC proteins are distinct from other ion channels in that they are found as both soluble and integral membrane forms, and their form determines their function (3-6). Chloride intracellular channel proteins are ubiquitously expressed in numerous tissue types and are involved in diverse biological functions (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Circadian rhythms govern many key physiological processes that fluctuate with a period of approximately 24 hours. These processes include the sleep-wake cycle, glucose, lipid and drug metabolism, heart rate, hormone secretion, renal blood flow, and body temperature, as well as basic cellular processes such as DNA repair and the timing of the cell division cycle (1,2). The mammalian circadian system consists of many individual tissue-specific clocks (peripheral clocks) that are controlled by a master circadian pacemaker residing in the suprachiasmatic nuclei (SCN) of the brain (1,2). The periodic circadian rhythm is prominently manifested by the light-dark cycle, which is sensed by the visual system and processed by the SCN. The SCN processes the light-dark information and synchronizes peripheral clocks through neural and humoral output signals (1,2).The cellular circadian clockwork consists of interwoven positive and negative regulatory loops, or limbs (1,2). The positive limb includes the CLOCK and BMAL1 proteins, two basic helix-loop-helix-PAS containing transcription factors that bind E box enhancer elements and activate transcription of their target genes. CLOCK is a histone acetyltransferase (HAT) protein, which acetylates both histone H3 and H4 (3). BMAL1 binds to CLOCK and enhances its HAT activity (3). The CLOCK/BMAL1 dimer exhibits a periodic oscillation in both nuclear/cytoplasmic localization and protein levels, both of which are regulated by phosphorylation (4,5). CLOCK/BMAL1 target genes include the Cry and Per genes, whose proteins form the negative limb of the circadian clockwork system (1,2). CRY and PER proteins (CRY1, CRY2, PER1, PER2 and PER3) form oligomers that also periodically shuttle between the nucleus and cytoplasm. When in the nucleus, CRY/PER proteins inhibit CLOCK/BMAL1-mediated transcriptional activation, thus completing the circadian transcriptional loop (1,2). In tissues, roughly six to eight percent of all genes exhibit a circadian expression pattern (1,2). This 24-hour periodicity in gene expression results from coordination of the positive and negative regulatory limbs of the cellular clockwork system, and is fine-tuned by outside signals received from the SCN.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Clusterin (CLU, apolipoprotein J) is a multifunctional glycoprotein that is expressed ubiquitously in most tissues. Clusterin functions as a secreted chaperone protein that interacts with and stabilizes stress-induced proteins to prevent their precipitation (1,2). Research studies show that clusterin plays a protective role in Alzheimer’s disease by sequestering amyloid β(1-40) peptides to form long-lived, stable complexes, which prevents amyloid fibril formation (3-5).In addition to the secreted protein, several intracellular isoforms are localized to the nucleus, mitochondria, cytoplasm, and ER. The subcellular distribution of these multiple isoforms leads to the diversity of clusterin functions. Additional studies report that clusterin is involved in membrane recycling, cell adhesion, cell proliferation, apoptosis, and tumor survival (6-9). The clusterin precursor is post-translationally cleaved into the mature clusterin α and clusterin β forms. Clusterin α and β chains create a heterodimer through formation of disulfide bonds (10).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Clusterin (CLU, apolipoprotein J) is a multifunctional glycoprotein that is expressed ubiquitously in most tissues. Clusterin functions as a secreted chaperone protein that interacts with and stabilizes stress-induced proteins to prevent their precipitation (1,2). Research studies show that clusterin plays a protective role in Alzheimer’s disease by sequestering amyloid β(1-40) peptides to form long-lived, stable complexes, which prevents amyloid fibril formation (3-5).In addition to the secreted protein, several intracellular isoforms are localized to the nucleus, mitochondria, cytoplasm, and ER. The subcellular distribution of these multiple isoforms leads to the diversity of clusterin functions. Additional studies report that clusterin is involved in membrane recycling, cell adhesion, cell proliferation, apoptosis, and tumor survival (6-9). The clusterin precursor is post-translationally cleaved into the mature clusterin α and clusterin β forms. Clusterin α and β chains create a heterodimer through formation of disulfide bonds (10).

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

Application Methods: Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

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

Application Methods: Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

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

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

Background: CNPase (2', 3’-cyclic nucleotide 3'-phosphodiesterase) catalyzes the in vitro hydrolysis of 2’, 3’-cyclic nucleotides to produce 2’-nucleotides. The in vivo molecular function and native substrate of this nucleotide phosphodiesterase remains under investigation (1). High CNPase expression is seen in oligodendrocytes and Schwann cells as CNPase accounts for roughly 4% of the total myelin protein in the central nervous system (2). CNPase binds to tubulin heterodimers and plays a role in tubulin polymerization, and oligodendrocyte process outgrowth (3). Typical myelination is seen in CNPase knock-out mice, but they suffer severe neurodegeneration from axonal loss and oligodendrocytes display abnormal paranodal loop structure prior to axonal degeneration. Paranodal loops typically contact the axolemma in axon-glial signaling; neurodegeneration in CNPase knock-out mice is a secondary consequence of impaired cell-cell communication (4).

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

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: Negative Elongation Factor (NELF) consists of four subunits: WHSC2 (NELF-A), COBRA-1 (NELF-B), TH1L (NELF-C/D), and NELF-E (1). NELF, together with DRB-sensitivity inducing factor (DSIF), inhibits RNA Polymerase II (RNAPII) elongation resulting in RNAPII promoter proximal pausing, where it waits additional signaling to resume transcription (2,3). The release of RNAPII from promoter proximal pausing is a critical regulatory point during transcription and is signaled by positive transcription elongation factor (p-TEF-b) phosphorylation of both NELF and the carboxy-terminal domain (CTD) within the largest subunit of RNAPII (3,4). WHSC2 is thought to connect the NELF complex to RNAPII machinery, while NELF-E contains an RNA binding motif that is necessary for NELF function (1,5,6). TH1L, together with COBRA-1, are integral subunits that bring WHSC2 and NELF-E together in the NELF complex (1).

$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 Cofilin (D3F9) XP® Rabbit mAb #5175.
APPLICATIONS
REACTIVITY
Dog, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Cofilin and actin-depolymerization factor (ADF) are members of a family of essential conserved small actin-binding proteins that play pivotal roles in cytokinesis, endocytosis, embryonic development, stress response, and tissue regeneration (1). In response to stimuli, cofilin promotes the regeneration of actin filaments by severing preexisting filaments (2). The severing activity of cofilin is inhibited by LIMK or TESK phosphorylation at Ser3 of cofilin (3-5). Phosphorylation at Ser3 also regulates cofilin translocation from the nucleus to the cytoplasm (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Cofilin and actin-depolymerization factor (ADF) are members of a family of essential conserved small actin-binding proteins that play pivotal roles in cytokinesis, endocytosis, embryonic development, stress response, and tissue regeneration (1). In response to stimuli, cofilin promotes the regeneration of actin filaments by severing preexisting filaments (2). The severing activity of cofilin is inhibited by LIMK or TESK phosphorylation at Ser3 of cofilin (3-5). Phosphorylation at Ser3 also regulates cofilin translocation from the nucleus to the cytoplasm (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The nuclear protein coilin (COIL) is found in eukaryotic nucleoplasm and serves a marker for sub-organelles known as Cajal bodies (1,2). Cajal bodies (CB) are nuclear structures that are home to various RNA-processing complexes, including those responsible for pre-mRNA splicing, processing of rRNA and histone pre-mRNA, and telomere maintenance (1-3). The presence of coilin protein is essential for CB formation, and the protein plays a role in maintaining Cajal body structural integrity (4,5). Research studies indicate that coilin binds RNA, including telomerase RNA (hTR), pre-rRNA, and U2 snRNA, in addition to DNA (5). Additional research indicates that coilin protein may exhibit specific RNase activity towards hTR and U2 snRNA transcripts, and that this activity may be regulated through phosphorylation of coilin (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Type 1 collagen is the most abundant collagen in many human tissues, including bone, skin, and tendons. It is a trimeric complex comprised of two molecules of COL1A1 (alpha-1 type 1 collagen) and one molecule of COL1A2 (alpha-2 type 1 collagen) (1-3). The expression levels of COL1A1 are regulated by multiple mechanisms, including mRNA stability, translation, and posttranslational modification (3-5). Overexpression of COL1A1 has been positively associated with tissue fibrosis disorders, including systemic sclerosis (6), while loss-of-function mutations in the COL1A1 gene are a major causative factor for osteogenesis imperfecta (brittle bone disease) (7). Notably, COL1A1 expression levels have also been associated with tumor development in gastric, lung, thyroid, and breast cancers. Research studies suggest that upregulation of COL1A1 can generate a modified extracellular matrix environment that promotes cancer cell survival, proliferation, metastasis, and invasion (8-11).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Type 1 collagen is the most abundant collagen in many human tissues, including bone, skin, and tendons. It is a trimeric complex comprised of two molecules of COL1A1 (alpha-1 type 1 collagen) and one molecule of COL1A2 (alpha-2 type 1 collagen) (1-3). The expression levels of COL1A1 are regulated by multiple mechanisms, including mRNA stability, translation, and posttranslational modification (3-5). Overexpression of COL1A1 has been positively associated with tissue fibrosis disorders, including systemic sclerosis (6), while loss-of-function mutations in the COL1A1 gene are a major causative factor for osteogenesis imperfecta (brittle bone disease) (7). Notably, COL1A1 expression levels have also been associated with tumor development in gastric, lung, thyroid, and breast cancers. Research studies suggest that upregulation of COL1A1 can generate a modified extracellular matrix environment that promotes cancer cell survival, proliferation, metastasis, and invasion (8-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Complexins are small soluble proteins composed of a central α-helical-structured domain surrounded by amino- and carboxy-terminal unstructured domains (1). These cytosolic proteins bind to t-SNAREs with low affinity and to assembled SNARE complexes with high affinity (1,2). Two isoforms, complexin-1 and complexin-2, are expressed in neuronal cells (3) where they regulate evoked and spontaneous exocytosis (4,5). Altered complexin expression resulting from RNAi-mediated knockdown (6) or gene invalidation (7) leads to alteration in spontaneous fusion events and neurotransmitter release, which reflects functions at both inhibitory and stimulatory synapses.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Complexins are small soluble proteins composed of a central α-helical-structured domain surrounded by amino- and carboxy-terminal unstructured domains (1). These cytosolic proteins bind to t-SNAREs with low affinity and to assembled SNARE complexes with high affinity (1,2). Two isoforms, complexin-1 and complexin-2, are expressed in neuronal cells (3) where they regulate evoked and spontaneous exocytosis (4,5). Altered complexin expression resulting from RNAi-mediated knockdown (6) or gene invalidation (7) leads to alteration in spontaneous fusion events and neurotransmitter release, which reflects functions at both inhibitory and stimulatory synapses.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Catechol-O-methyltransferase (COMT) is an intracellular enzyme that catalyzes the O-methylation and inactivation of catecholamine neurotransmitters and hormones, including dopamine, epinephrine, and norepinephrine (1). Two distinct COMT proteins are generated from separate promoters in cells, including a 28 kDa, membrane-bound protein (mb-COMT), and a soluble protein (s-COMT) of 24 kDa (2,3). The soluble s-COMT is the predominant form of COMT found in peripheral organs, while the mb-COMT protein is more abundant in the central nervous system (4,5).In addition to inactivating endogenous catecholamines, COMT can also inhibit catechol-based drugs used to treat a number of disorders, including Parkinson's disease and schizophrenia. Research studies using COMT inhibitors indicate that these reagents can prolong the bioavailability of psychoactive drugs such as levodopa by preventing O-methylation and subsequent degradation (6). A Val158Met polymorphism in the corresponding COMT gene reduces COMT enzymatic activity and leads to increased cortical dopamine levels (7). Several research studies suggest that this reduced COMT activity is associated with a large number of mental disorders, including schizophrenia, bipolar disorder, attention deficit hyperactivity disorder, obsessive-compulsive disorder, and anorexia nervosa (reviewed in 8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Myelinated axons contain un-myelinated gaps called nodes of Ranvier. These regularly spaced gaps are critical for the proper propagation and rapid conduction of nerve impulses in the central and peripheral nervous system (1). The structure and organization of the nodes of Ranvier is dictated by interaction between the axon and glial cells (2). Voltage-gated sodium channels concentrated at the nodes and potassium channels clustered at the paranodes are responsible for propagation of the action potentials (3,4). Other proteins that contribute to the architecture and function of the nodes of Ranvier include βIV spectrin (5), ankyrin-G (6), and the L1 cell adhesion molecules, neurofascin and NrCAM (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Cool/Pix proteins comprise a family of guanine nucleotide exchange factors (GEFs) localized to focal adhesions. The family consists of two isoforms, cool2/αPix and cool1/βPix, the latter having two splice variants that vary in their carboxy termini (1). Cool2/αPix, like other GEFs, has a DH (Dbl homology) domain, which allows binding of small GTPases and GDP/GTP exchange, and a PH (Pleckstrin homology) domain (2).X-chromosomal genes mutated in nonspecific mental retardation (MRX) comprise a family of genes, including the gene encoding Cool2/αPix, thought to be involved in mental retardation (3,4).Cool2/αPix interacts with β-parvin/affixin, a protein involved in integrin signaling (5), and may act downstream of integrin-linked kinase (ILK) to regulate actin reorganization and cell spreading (6).When Cool2αPix exists as a dimer, it functions as a Rac-specific GEF, whereas the monomeric protein acts as a GEF for both Rac and Cdc42. Regulation of Cool2/αPix dimerization, and therefore its specificity, occurs at least in part through p21 activated kinase (PAK) in response to extracellular signaling (7). Further, binding of Cdc42 enhances the Rac GEF activity of the Cool2/αPix dimer. Activated Rac in turn inhibits Cool2/αPix Rac GEF activity (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The COP9 Signalosome (CSN) is a ubiquitously expressed multiprotein complex that is involved in a vast array of cellular and developmental processes, which is thought to be attributed to its control over the ubiquitin-proteasome pathway. Typically, the CSN is composed of eight highly conserved subunits (CSN1-CSN8), each of which is homologous to one of the eight subunits that form the lid of the 26S proteasome particle, suggesting that these complexes have a common evolutionary ancestor (1). CSN was first identified in Arabidopsis thaliana mutants with a light-grown seedling phenotype when grown in the dark (2-4). The subsequent cloning of the constitutive morphogenesis 9 (cop9) mutant from Arabidopsis thaliana was soon followed by the biochemical purification of the COP9-containing multiprotein complex (4). It is now widely accepted that the CSN directly interacts with cullin-RING ligase (CRL) families of ubiquitin E3 complexes, and that CSN is required for their proper function (5). In addition, CSN may also regulate protein homeostasis through its association with protein kinases and deubiquitinating enzymes. Collectively, these activities position the CSN as a pivotal regulator of the DNA-damage response, cell-cycle control, and gene expression (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The REST corepressor 1 (CoREST, RCOR1) was first identified as a repressor element 1-silencing transcription factor (REST) corepressor (1,2). The CoREST protein is encoded by the RCOR1 gene and is part of a large, multi-subunit repressor complex that includes the histone demethylase LSD1 and histone deacetylases (HDAC) 1 and 2 (1,3-5). CoREST binds the carboxy-terminal domain of REST and is recruited to repress neuronal gene transcription in non-neuronal and neural stem cells (1,6,7). The REST corepressor is essential for repressor complex-nucleosome interaction, the subsequent deacetylation of histone amino-terminal tails by HDAC1/2, and the LSD1 methylation of histone H3 at Lys4 (8-10). The targeting of CoREST to genes that are not repressed by REST suggests a role apart from neural cell fate regulation. These include growth factor independent (Gfi) target genes during erythroid differentiation, targets of carboxy-terminal binding protein (CtBP), and heat shock and pro-inflammatory response genes (11-15).

$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 Coronin 1A (D6K5B) XP® Rabbit mAb #92904.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: The coronin family of actin-binding proteins regulates a variety of cellular functions, including migration, phagocytosis, and cytokinesis. Coronin 1A is highly expressed in lymphocytes, and is required for appropriate immune regulation in mice and humans. Researchers are investigating coronin 1A as a potential therapeutic target for autoimmune diseases and lymphoid cancers (1,2). Coronin 1A affects bone resorption through its regulation of lysosome fusion and secretion of cathepsin K in osteoclasts (3). In the nervous system, coronin 1A has been shown to regulate GPCR signaling and neurite outgrowth (4,5).

$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 Coronin 1A (D6K5B) XP® Rabbit mAb #92904.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: The coronin family of actin-binding proteins regulates a variety of cellular functions, including migration, phagocytosis, and cytokinesis. Coronin 1A is highly expressed in lymphocytes, and is required for appropriate immune regulation in mice and humans. Researchers are investigating coronin 1A as a potential therapeutic target for autoimmune diseases and lymphoid cancers (1,2). Coronin 1A affects bone resorption through its regulation of lysosome fusion and secretion of cathepsin K in osteoclasts (3). In the nervous system, coronin 1A has been shown to regulate GPCR signaling and neurite outgrowth (4,5).

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Coronin 1A (D6K5B) XP® Rabbit mAb #92904.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: The coronin family of actin-binding proteins regulates a variety of cellular functions, including migration, phagocytosis, and cytokinesis. Coronin 1A is highly expressed in lymphocytes, and is required for appropriate immune regulation in mice and humans. Researchers are investigating coronin 1A as a potential therapeutic target for autoimmune diseases and lymphoid cancers (1,2). Coronin 1A affects bone resorption through its regulation of lysosome fusion and secretion of cathepsin K in osteoclasts (3). In the nervous system, coronin 1A has been shown to regulate GPCR signaling and neurite outgrowth (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The coronin family of actin-binding proteins regulates a variety of cellular functions, including migration, phagocytosis, and cytokinesis. Coronin 1A is highly expressed in lymphocytes, and is required for appropriate immune regulation in mice and humans. Researchers are investigating coronin 1A as a potential therapeutic target for autoimmune diseases and lymphoid cancers (1,2). Coronin 1A affects bone resorption through its regulation of lysosome fusion and secretion of cathepsin K in osteoclasts (3). In the nervous system, coronin 1A has been shown to regulate GPCR signaling and neurite outgrowth (4,5).