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Product listing: Merlin/Ezrin/Radixin/Moesin (D1P8I) Rabbit mAb, UniProt ID P35240 #23292 to Phospho-SMAD2 (Ser465/Ser467) (E8F3R) Rabbit mAb (Alexa Fluor® 488 Conjugate), UniProt ID Q15796 #56532

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Neurofibromatosis 2 (NF2) is an autosomal dominant, inherited disorder characterized by the occurrence of vestibular schwannomas, meningiomas, and other nervous system tumors. Both the familial tumors of NF2 and equivalent sporadic tumors found in the general population are caused by inactivation of the NF2 tumor suppressor gene. Merlin (moesin, ezrin, and radixin-like protein) is the NF2 gene product, displaying striking similarity to ezrin, radixin, and moesin (ERM) proteins. Regulation of merlin (also called schwannomin) and ERM proteins involves intramolecular and intermolecular head-to-tail associations between family members (1). Merlin and ERM proteins act as linkers between the plasma membrane and the cytoskeleton, affecting cell morphology, polarity, and signal transduction (2). Merlin is phosphorylated by the Rac/Cdc42 effector p21-activated kinase (PAK) at Ser518, negatively regulating Rac (3,4).

$159
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to allophycocyanin (APC) and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Interleukin-2 (IL-2) is a T cell stimulatory cytokine best known for inducing T cell proliferation and NK cell proliferation and activation (1,2). IL-2 also promotes peripheral development of regulatory T cells (Tregs) (3,4). Conversely, IL-2 is involved in the activation-induced cell death (AICD) that is observed post T cell expansion by increasing levels of Fas on CD4+ T cells (5). The effects of IL-2 are mediated through a trimeric receptor complex consisting of IL-2Rα, IL-2Rβ, and the common gamma chain, γc (1,2). IL-2Rα binds exclusively to IL-2 with low affinity and increases the binding affinity of the whole receptor complex including IL-2Rβ and γc subunits. IL-15 also binds to IL-2Rβ (1,2). γc is used by other cytokines including IL-4, IL-7, IL-9, IL-15, and IL-21 (1,2). Binding of IL-2 initiates signaling cascades involving Jak1, Jak3, Stat5, and the PI3K/Akt pathways (1,2).

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

Application Methods: Western Blotting

Background: SET7/SET9 is a member of the SET domain-containing family, and can specifically methylate Lys4 on histone H3 (1). Like most other lysine-directed histone methyltransferases, it contains a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste and Trithorax proteins. Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Methylation of histone H3 Lys4 enhances transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (4,5). In addition, methylation of lysine 4 blocks transcriptional repression by inhibiting the binding of the NURD histone deacetylation complex to the amino-terminal tail of histone H3 and interfering with SUV39H1-mediated methylation of histone H3 Lys9 (1). SET7/SET9 is highly active on free histone H3, but only very weakly methylates H3 within nucleosomes (1). Besides histones, SET7/SET9 also methylates Lys189 of the TAF10, a member of the TFIID transcription factor complex, and Lys372 of the p53 tumor suppressor protein (6,7). Methylation of TAF10 stimulates transcription in a promoter-specific manner by increasing the affinity of TAF10 for RNA polymerase II, which may potentiate pre-initiation complex formation (6). Methylation of p53 at Lys372 increases protein stability and leads to upregulation of target genes such as p21. Thus the loss of SET7/SET9 may represent another mechanism for the inactivation of p53 in human cancers (7).

$349
100 µg
This Cell Signaling Technology antibody is conjugated to APC-Cy7® and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: F4/80 (EMR1) is a heavily glycosylated G-protein-coupled receptor and is a well-established marker for mouse macrophages (1-3). Expression of F4/80 has also been observed in microglia and subset populations of dendritic cells (4).

$249
100 µg
This Cell Signaling Technology antibody is conjugated to violetFluor™ 450 and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: Cluster of Differentiation 8 (CD8) is a disulphide-linked heterodimer consisting of the unrelated α and β subunits. Each subunit is a glycoprotein composed of a single extracellular Ig-like domain, a polypeptide linker, a transmembrane part and a short cytoplasmic tail. On T cells, CD8 is the coreceptor for the T cell receptor (TCR), and these two distinct structures recognize the Antigen–Major Histocompatibility Complex (MHC). Specifically, the Ig-like domain of CD8α interacts with the α3-domain of the MHC class I molecule. CD8 ensures specificity of the TCR–antigen interaction, prolongs the contact between the T cell and the antigen presenting cell, and the α chain recruits the tyrosine kinase Lck, which is essential for T cell activation (1).

$129
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to FITC and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: CD28 is a transmembrane glycoprotein expressed by T cells as well as some other hematopoietic cells (1, 2). T cell activation requires T cell receptor (TCR) recognition of antigen presented in the context of MHC molecules. CD28 acts as a T cell costimulatory receptor, and interaction of CD28 with its ligands CD80 or CD86 provides the second signal required for naïve T cell activation (3-5). Activation of naïve T cells in the absence of CD28 stimulation can result in a state of T cell anergy, or unresponsiveness (3). CD28 signals through cytoplasmic phospho-tyrosine motifs that bind several SH2 or SH3 domain-containing proteins involved in T cell activation (2). Recently, CD28 was demonstrated to be a preferred target of PD-1-mediated dephosphorylation. Consistently, CD28 expression was required for T cell proliferation following PD-1 blockade and CD28 stimulation was required for effective anti-PD-1 cancer immunotherapy in mice (6, 7). Several CD28 isoforms are produced by alternative splicing (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CYP17A1, also known as cytochrome P450C17, is a steroidogenic enzyme belonging to the P450 cytochrome superfamily of monooxygenases (1, 2). In humans, CYP17A1 expression is abundantly expressed in the adrenal cortex, where it plays a central role in the androgen synthesis pathway (2). CYP17A1 is the primary target of abiraterone, a synthetic steroid used in the treatment of castration-resistant prostate cancer (CRPC) (3, 4). Abiraterone is converted to the more active form D4A, which antagonizes androgen receptor signaling by inhibiting CYP17A1 and other steroidogenic enzymes (3, 4). This suppresses the synthesis of 5α-dihydrotestosterone (DHT), which is a driver of castration-resistant prostate cancer cell growth (3, 4).

$349
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to PerCP-Cy5.5® and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Cyclic ADP-ribose hydrolase 1 (CD38) is a transmembrane protein involved in several important biological processes, including immune response, insulin secretion, and social behavior. Originally described as a glycosylated immune cell surface marker, additional research determined that CD38 is a multifunctional enzyme that catalyzes the synthesis and hydrolysis of cyclic ADP ribose (cADPR) from NAD (1,2). Under acidic conditions, CD38 also catalyzes the synthesis of nicotinic acid adenine dinucleotide phosphate (NAADP) from NADP+. Both cADPR and NAADP act as calcium ion mobilizing messengers that target different intracellular Ca2+ stores (3-6). Since CD38 is the primary mammalian NAD+ glycohydrolase responsible for NAD+ metabolism, CD38 may be a valuable therapeutic target for treatment of metabolic diseases regulated by NAD+-dependent pathways (7,8). CD38 has also been considered a possible therapeutic target for antibody-mediated therapy for myeloma and chronic lymphocytic leukemia (9-11).

$279
100 µg
This Cell Signaling Technology antibody is conjugated to violetFluor™ 450 and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: CD24, also know as heat stable antigen HSA, is a P-selectin ligand involved in adhesion. It is a GPI-anchored glycoprotein expressed on many types of cells, including hematopoietic cells, neural cells, and epithelial cells. CD24 is widely used to delineate stages of lymphocyte development (1-3). It also binds to Siglec-10 in humans or Siglec-G in mice (4,5). CD24 is frequently used as a marker to identify and isolate cancer stem cells in various cancer types (6,7).

$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 LRRK2 (D18E12) Rabbit mAb #13046.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Parkinson’s disease (PD), the second most common neurodegenerative disease after Alzheimer’s, is a progressive movement disorder characterized by rigidity, tremors, and postural instability. The pathological hallmarks of PD are progressive loss of dopaminergic neurons in the substantia nigra of the ventral midbrain and the presence of intracellular Lewy bodies (protein aggregates of α-synuclein, ubiquitin, and other components) in surviving neurons of the brain stem (1). Research studies have shown various genes and loci are genetically linked to PD including α-synuclein/PARK1 and 4, parkin/PARK2, UCH-L1/PARK5, PINK1/PARK6, DJ-1/PARK7, LRRK2/PARK8, synphilin-1, and NR4A2 (2).Leucine-rich repeat kinase 2 (LRRK2) contains amino-terminal leucine-rich repeats (LRR), a Ras-like small GTP binding protein-like (ROC) domain, an MLK protein kinase domain, and a carboxy-terminal WD40 repeat domain. Research studies have linked at least 20 LRRK2 mutations to PD, with the G2019S mutation being the most prevalent (3). The G2019S mutation causes increased LRRK2 kinase activity, which induces a progressive reduction in neurite length that leads to progressive neurite loss and decreased neuronal survival (4). Researchers are currently testing the MLK inhibitor CEP-1347 in PD clinical trials, indicating the potential value of LRRK2 as a therapeutic target for treatment of PD (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the Janus family of tyrosine kinases (Jak1, Jak2, Jak3, and Tyk2) are activated by ligands binding to a number of associated cytokine receptors (1). Upon cytokine receptor activation, Jak proteins become autophosphorylated and phosphorylate their associated receptors to provide multiple binding sites for signaling proteins. These associated signaling proteins, such as Stats (2), Shc (3), insulin receptor substrates (4), and focal adhesion kinase (FAK) (5), typically contain SH2 or other phospho-tyrosine-binding domains.

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Interleukin-1β (IL-1β), one of the major caspase-1 targets, is a multifunctional cytokine that is involved in a host of immune and proinflammatory responses (1). It is produced primarily by activated monocytes and macrophages. It signals through various adaptor proteins and kinases that lead to activation of numerous downstream targets (2-6). Human IL-1β is synthesized as a 31 kDa precursor. To gain activity, the precursor must be cleaved by caspase-1 between Asp116 and Ala117 to yield a 17 kDa mature form (7,8). Detection of the 17 kDa mature form of IL-1β is a good indicator of caspase-1 activity.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: T cell differentiation antigen CD6 is a cell adhesion molecule expressed on immature thymocytes and mature T cells, and has also been detected on a subset of B cells and NK cells within the immune system (1-4). CD6 mediates cell-cell interactions through it’s binding partner CD166/ALCAM (2), and contributes to the formation and maturation of the immunological synapse (3,4). CD6 functions as a co-stimulatory receptor, promoting T cell activation and proliferation through the TCR/CD3 complex signaling cascade (3-6). Studies have shown CD6 can be glycosylated (7), hyperphosphorylated on serine and threonine residues (8), and phosphorylated on tyrosine residues (6,9), each of which can differentially effect the function and signaling of this molecule. CD6 also functions as a calcium-dependent pattern receptor that binds and aggregates Gram-positive and Gram-negative bacteria. In response to lipopolysaccharide, CD6 mediates activation of the inflammatory response and secretion of pro-inflammatory cytokines (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The most well characterized nuclear receptor corepressors are SMRT (silencing mediator for retinoic acid and thyroid hormone receptors) and its close paralog NCoR1 (nuclear receptor corepressor) (1,2). NCoR1 functions to transcriptionally silence various unliganded, DNA bound non-steroidal nuclear receptors by serving as a large molecular scaffold that bridges the receptors with multiple chromatin remodeling factors that repress nuclear receptor-mediated gene transcription, in part, through deacetylation of core histones surrounding target promoters. Indeed, the N-terminal portion of NCoR1 possesses multiple distinct transcriptional repression domains (RDs) reponsible for the recruitment of additional components of the corepressor complex such as HDACs, mSin3, GPS2, and TBL1/TBLR1. In between the RDs lies a pair of potent repressor motifs known as SANT motifs (SWI3, ADA2, N-CoR, and TFIIIB), which recruit HDAC3 and histones to the repressor complex in order to enhance HDAC3 activity (3). The C-terminal portion of NCoR1 contains multiple nuclear receptor interaction domains (NDs), each of which contains a conserved CoRNR box (or L/I-X-X-I/V-I) motif that allow for binding to various unliganded nuclear hormone receptors such as thyroid hormone (THR) and retinoic acid (RAR) receptors (4,5).Recent genetic studies in mice have not only corroborated the wealth of biochemical studies involving NCoR1 but have also provided significant insight regarding the function of NCoR1 in mammalian development and physiology. Although it has been observed that loss of Ncor1 does not affect early embyonic development, likely due to compensation by Smrt, embryonic lethality ultimately results during mid-gestation, largely due to defects in erythropoesis and thymopoesis (6). Another study demonstrated that the NDs of NCoR1 are critical for its ability to function in a physiological setting as a transcriptional repressor of hepatic THR and Liver X Receptor (LXR) (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: The methylation state of lysine residues in histone proteins is a major determinant for formation of active and inactive regions of the genome and is crucial for proper programming of the genome during development (1,2). Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (3). The JmjC domain can catalyze the demethylation of mono-, di-, and tri-methyl lysine residues via an oxidative reaction that requires iron and α-ketoglutarate (3). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into 7 separate families (3). The JARID (Jumonji/AT-rich interactive domain-containing protein) family contains four members: JARID1A (also RBP2 and RBBP2), JARID1B (also PLU-1), JARID1C (also SMCX) and JARID1D (also SMCY) (4). In addition to the JmJC domain, these proteins contain JmJN, BRIGHT, C5HC2 zinc-finger, and PHD domains, the latter of which binds to methylated histone H3 (Lys9) (4). All four JARID proteins demethylate di- and tri-methyl histone H3 Lys4; JARID1B also demethylates mono-methyl histone H3 Lys4 (5-7). JARID1A is a critical RB-interacting protein and is required for Polycomb-Repressive Complex 2 (PRC2)-mediated transcriptional repression during ES cell differentiation (8). A JARID1A-NUP98 gene fusion is associated with myeloid leukemia (9). JARID1B, which interacts with many proteins including c-Myc and HDAC4, may play a role in cell fate decisions by blocking terminal differentiation (10-12). JARID1B is over-expressed in many breast cancers and may act by repressing multiple tumor suppressor genes including BRCA1 and HOXA5 (13,14). JARID1C has been found in a complex with HDAC1, HDAC2, G9a and REST, which binds to and represses REST target genes in non-neuronal cells (7). JARID1C mutations are associated with X-linked mental retardation and epilepsy (15,16). JARID1D is largely uncharacterized.

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated S100A9 (D3U8M) Rabbit mAb (Rodent Specific) #73425.
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Flow Cytometry

Background: S100A8 and S100A9 are calcium-binding proteins that form a noncovalent heterodimer present in monocytes, neutrophils, macrophages, and some epithelial cells (1, 2). S100A8 and S100A9 are secreted by a tubulin-dependent mechanism during inflammatory conditions and have antimicrobial and chemotactic functions (3-5). Extracellular S100A8/S100A9 also induces an inflammatory response in endothelial cells, including induction of proinflammatory chemokines and adhesion molecules and increased vascular permeability (6). S100A8/S100A9 induces and recruits myeloid-derived suppressor cells (MDSC) in tumor-bearing mice (7). MDSC produce additional S100A8/S100A9 themselves, resulting in a positive feedback mechanism that sustains MDSC accumulation (7). S100A8/S100A9 is also highly expressed in psoriatic skin, where it directly upregulates transcription of complement protein C3, which contributes to disease (8). In addition, tumor-infiltrating myeloid cells induce expression of S100A8 and S100A9 in cancer cells, which increases invasiveness and metastasis (9).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated FoxM1 (D3F2B) Rabbit mAb #20459.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Forkhead box M1 (FoxM1) is a forkhead box family transcription factor that regulates a number of genes throughout the cell cycle to help control DNA replication, mitosis, and cell proliferation. FoxM1 expression increases during G1 and S and reaches maximum levels in G2/M (1-3). Nuclear translocation occurs just before entry into G2/M and is associated with FoxM1 phosphorylation (4). Phosphorylation of FoxM1 by MAPK (Ser331, Ser704), Cyclin/Cdk (Ser4, Ser35, Thr600, Thr611, Thr620, Thr627, Ser638), Plk1 (Ser715, Ser724), and Chk2 (Ser376) stabilizes and activates FoxM1 (4-8). Forkhead box M1 is expressed in all embryonic tissues but is restricted to proliferating tissues in adults (9). Research studies show that FoxM1 expression is negatively regulated by p53 (10,11). Upregulation of FoxM1 is associated with many human cancers, including prostate, breast, lung, ovary, colon, pancreas, stomach, bladder, liver, and kidney, and may be associated with p53 mutations in some tumors (11,12). As a result, FoxM1 inhibitors have become a topic of interest for potential cancer therapy (13).

$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 DJ-1 (D29E5) XP® Rabbit mAb #5933.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Parkinson's disease (PD) is characterized by the presence of Lewy bodies (intracellular inclusions) and by the loss of dopaminergic neurons. Research studies have shown that mutations in α-synuclein, Parkin, and DJ-1 are linked to PD (1). α-synuclein is a major component of the aggregates found in Lewy bodies. Parkin is involved in protein degradation through the ubiquitin-proteasome pathway, and investigators have shown that mutations in Parkin cause early onset of PD (1). Loss-of-function mutations in DJ-1 cause early onset of PD, but DJ-1 is associated with multiple functions: it cooperates with Ras to increase cell transformation, it positively regulates transcription of the androgen receptor, and it may function as an indicator of oxidative stress (2-5). Dopamine D2 receptor-mediated functions are greatly impaired in DJ-1 (-/-) mice, resulting in reduced long-term depression (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Myelin proteolipid protein (PLP1) corresponds to the majority of myelin proteins in the CNS, providing support to axons and modulating the axonal growth (1). DM20 is the result of the alternative splicing of the plp1 gene, which is linked to oligodendrocyte differentiation and survival. The imbalance of PLP1/DM20, is linked to Pelizaeus-Merzbacher disese (2,3), including mitochonmdrial damage (4). In addition, PLP1, but not DM20, can enter the mitochondria and participate in the metabolism of cells (5, 6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: TNFRSF9 is a member of the tumor necrosis factor receptor superfamily (1, 2). It is also called 4-1BB or CD137 (1, 2). 4-1BB/CD137/TNFRSF9 is expressed in activated CD4+ and CD8+ T cells, natural killer cells and dendritic cells (2-5). The ligand 4-1BBL/CD137L/TNFSF9 on antigen presenting cells binds to 4-1BB/CD137/TNFRSF9 and costimulates the activation of T cells (5). The binding of agonistic antibodies to 4-1BB/CD137/TNFRSF9 also leads to costimulation for T cell activation (5). Studies have shown the effectiveness of targeting 4-1BB/CD137/TNFRSF9 by its agonistic antibodies in cancer immunotherapy (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Double FYVE-containing protein 1 (DFCP1; gene name ZFYVE1), which was identified from a human bone marrow library, contains two carboxyl terminal FYVE domains that function as binding sites for phosphatidylinositol 3-phosphate (PI3P) (1). PI3P generated predominantly by the class III PI3-kinase VPS34 plays a key role in membrane trafficking as well as autophagy (2,3). DFCP1 is primarily localized to the Golgi and endoplasmic reticulum (ER) (4,5). However, during autophagy DFCP1 re-localizes to subdomains of the ER, the omegasome, which become the sites for autophagosome formation (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation, but it has also been associated with a number of physiological processes including development, differentiation, neurodegenerative diseases, infection, and cancer (3). Autophagy marker Light Chain 3 (LC3) was originally identified as a subunit of microtubule-associated proteins 1A and 1B (termed MAP1LC3) (4) and subsequently found to contain similarity to the yeast protein Apg8/Aut7/Cvt5 critical for autophagy (5). Three human LC3 isoforms (LC3A, LC3B, and LC3C) undergo post-translational modifications during autophagy (6-9). Cleavage of LC3 at the carboxy terminus immediately following synthesis yields the cytosolic LC3-I form. During autophagy, LC3-I is converted to LC3-II through lipidation by a ubiquitin-like system involving Atg7 and Atg3 that allows for LC3 to become associated with autophagic vesicles (6-10). The presence of LC3 in autophagosomes and the conversion of LC3 to the lower migrating form, LC3-II, have been used as indicators of autophagy (11).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Notch signaling is activated upon engagement of the Notch receptor with its ligands, the DSL (Delta, Serrate, Lag2) proteins of single-pass type I membrane proteins. The DSL proteins contain multiple EGF-like repeats and a DSL domain that is required for binding to Notch (1,2). Five DSL proteins have been identified in mammals: Jagged1, Jagged2, Delta-like (DLL) 1, 3 and 4 (3). Ligand binding to the Notch receptor results in two sequential proteolytic cleavages of the receptor by the ADAM protease and the γ-secretase complex. The intracellular domain of Notch is released and then translocates to the nucleus where it activates transcription. Notch ligands may also be processed in a way similar to Notch, suggesting a bi-directional signaling through receptor-ligand interactions (4-6).

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

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

Background: α-Actinin belongs to the spectrin family of cytoskeletal proteins. It was first recognized as an actin cross-linking protein, forming an antiparallel homodimer with an actin binding head at the amino terminus of each monomer. The α-actinin protein interacts with a large number of proteins involved in signaling to the cytoskeleton, including those involved in cellular adhesion, migration, and immune cell targeting (1). The interaction of α-actinin with intercellular adhesion molecule-5 (ICAM-5) helps to promote neurite outgrowth (2). In osteoblasts, interaction of α-actinin with integrins stabilizes focal adhesions and may protect cells from apoptosis (3). The cytoskeletal α-actinin isoforms 1 and 4 (ACTN1, ACTN4) are non-muscle proteins that are present in stress fibers, sites of adhesion and intercellular contacts, filopodia, and lamellipodia. The muscle isoforms 2 and 3 (ACTN2, ACTN3) localize to the Z-discs of striated muscle and to dense bodies and plaques in smooth muscle (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: ETS-2 is a member of the E26 Transformation-specific Sequence (ETS) transcription factor family, members of which bind to a core GGAA/T DNA sequence in the promoter region of target genes to activate gene expression (1). ETS-2 activates expression of a wide variety of target genes, including MMPs, TERT, TCR, uPA, and oncogenic miRNAs (2-4). It's activity has been shown to be important for cell growth and differentiation, bone formation, autoimmune disease, and cancer progression (5-7). Phosphorylation by MAP kinase at Thr72 upregulates the function of ETS-2, suggesting that therapeutic strategies targeting ETS-2 may provide an alternative to MEK inhibitor therapy (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: B cell linker protein (BLNK), also known as SLP-65 or BASH, is an adaptor molecule that plays key roles in B cell activation and B cell antigen receptor (BCR) engagement. BLNK acts at the interface between BCR-associated Syk and downstream signaling cascades (1,2). BLNK has multiple SH2 binding motifs (YXXP) at its amino terminus and an SH2 domain at its carboxy terminus. After BCR ligation, BLNK is phosphorylated by Syk at multiple YXXP motifs including Tyr72, Tyr84, Tyr96, and Tyr178 (1). These phosphorylated motifs provide docking sites for signaling molecules, such as BTK, PLCγ, and Vav. These signaling molecules bind to BLNK through their SH2 domains and together activate downstream signaling pathways (3,4). Through its SH2 domain, BLNK can also interact with tyrosine-phosphorylated targets, such as HPK1, thereby recruiting them to the BCR complex for signaling (5).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: MLANA, also known as MART-1, is a member of a melanocyte lineage-specific family of proteins. It is expressed in melanocytes, retinal pigment epithelium, and melanoma cells. Its function is not entirely understood, but it is believed to be involved in the stability of GPR143, as well as the stability, trafficking, and processing of PMEL; both proteins are involved in the formation of stage II melanosomes (1). In melanosomes, MLANA is specifically located in the trans-Golgi network, however conformational changes to the protein or a sub-population of the protein causes it to localize back to the ER and small endosomal vesicles (2). In the context of melanoma cells, the conformational change is thought to be caused by aberrant exposure of epitopes, which are recognized by cytolytic T-lymphocytes (3). MLANA may be useful as a marker of metastatic melanoma (4). MHC-II restricted phospho-MLANA peptides, which are recognized by CD4 cells, are being investigated as potential candidates for cancer immunotherapy (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CXCR4 is a chemokine receptor that belongs to the G protein-coupled receptor family. It is activated by a small cytokine, CXCL12, also known as stromal cell derived factor 1 (SDF-1) (1). The main function of CXCR4 is the mediation of the homing of progenitor cells in the bone marrow and their recruitment to sites of injury (2). More recently, CXCR4 has been studied, as a potential therapeutic target, in the context of autoimmune diseases (3) as well as cancer, as the receptor is involved in the regulation of migration, proliferation, and survival of cancer cells (4).

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Smad2 (Ser465/Ser467) (E8F3R) Rabbit mAb #18338.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).