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Product listing: Tyrosine Hydroxylase Antibody, UniProt ID P07101 #2792 to β-Tubulin (D2N5G) Rabbit mAb, UniProt ID P07437 #15115

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms (1,2). This enzyme is required for embryonic development since TH knockout mice die before or at birth (3). Levels of transcription, translation and posttranslational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31 and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH (4-6). Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels (7-9).

$305
400 µl
This Cell Signaling Technology (CST) antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. It is useful for the immunoprecipitation of DYKDDDDK-tagged proteins. CST expects that DYKDDDDK Tag (D6W5B) Rabbit mAb (Binds to same epitope as Sigma's Anti-Flag® M2 Antibody) (Sepharose® Bead Conjugate) will display the same species cross-reactivity as the unconjugated antibody DYKDDDDK Tag (D6W5B) Rabbit mAb # 14793.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunoprecipitation

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Nucleophosmin (NPM; also known as B23, numatrin or NO38) is an abundant phosphoprotein primarily found in nucleoli. It has been implicated in several distinct cellular functions, including assembly and transport of ribosomes, cytoplasmic/nuclear trafficking, regulation of DNA polymerase α activity, centrosome duplication and molecular chaperoning activities (1,2). The NPM gene is also known for its fusion with the anaplastic lymphoma kinase (ALK) receptor tyrosine kinase. The NPM portion contributes to transformation by providing a dimerization domain, which results in activation of the fused kinase (3,4).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Dog, Human

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

Background: Tight junctions, or zonula occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Glucose homeostasis is regulated by hormones. Elevation of blood glucose levels during feeding stimulates insulin release from pancreatic β-cells through a glucose sensing pathway (1). Proinsulin, the insulin precursor molecule, is processed prior to its secretion. Insulin is composed of A-peptide and B-peptide which are joined by a disulfide bond. The center one-third of the molecule is cleaved and released as C-peptide, which has a longer half-life than insulin (2).

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

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

Background: IDH1 is one of three isocitrate dehydrogenases that catalyze the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG). These enzymes exist in two distinct subclasses that utilize either NAD or NADP+ respectively, as an electron acceptor (1). IDH1 is the NADP+-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. IDH2 and 3 are mitochondrial enzymes that also function in the Krebs cycle. IDH1 is inactivated by phosphorylation at Ser113 and contains a clasp-like domain wherein both polypeptide chains in the dimer interlock (2,3). IDH1 is expressed in a wide range of species and also in organisms that lack a complete citric acid cycle. Mutations in IDH1 have been reported in glioblastoma (4), acute myeloid leukemia (5,6), and other malignancies (7). IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway (8).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).

Phosphate Buffered Saline (PBS-1X) pH 7.2 (Sterile) is specifically formulated to be used as a buffer for reconstituting sterile cytokines or antibodies. 1X PBS contains 10 mM Na2HPO4, 10 mM NaH2PO4, 150 mM NaCl.
$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Chk2 is the mammalian orthologue of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases (1-3). The amino-terminal domain of Chk2 contains a series of seven serine or threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50, and Thr68) each followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases (4,5). After DNA damage by ionizing radiation (IR), UV irradiation, or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR (5-7). The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 at residues Thr383 and Thr387 in the activation loop of the kinase domain (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Post-transcriptional processing of RNAs such as RNA editing is an important mechanism by which diversity in RNA and protein is achieved that is not otherwise encoded by the genome (1,2). The most common form of RNA editing is the conversion of adenosine (A) into inosine (I) on double stranded RNA by the adenosine deaminase acting on RNA (ADAR) family of proteins (1-3). Since inosine base pairs with cytidine, it is interpreted as a guanosine by the splicing and translational machinery leading to alteration in the protein sequence, as well as splicing isoforms being generated (1,4-6). A-to-I editing can also influence RNA sequence recognition by RNA binding proteins and non-coding RNA, such as miRNAs, affecting subsequent RNA processing, stability, and protein expression levels (2).ADAR1 is ubiquitously expressed with two known isoforms ADAR1L (p150) and ADAR1S (p110) resulting from transcription using alternative promoters and start codons. ADAR1S is constitutively expressed in the nucleus, while ADAR1L is interferon-inducible and present in both the nucleus and the cytoplasm. The induction of ADAR1L in response to cellular stress and viral infection suggests a role for RNA editing in the innate immune response (1,7). In addition, ADAR1 is essential in mammalian development, particularly in hematopoiesis and suppression of interferon signaling to protect hematopoietic stem cells from destruction in the fetal liver and the adult bone marrow (8,9).

$364
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 Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP® Rabbit mAb #4370.
APPLICATIONS
REACTIVITY
Bovine, D. melanogaster, Dog, Hamster, Human, Mink, Monkey, Mouse, Pig, Rat, S. cerevisiae, Zebrafish

Application Methods: Western Blotting

Background: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

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

Application Methods: Western Blotting

Background: CK2 (formerly called Casein Kinase II) is a highly conserved protein kinase with more than 300 substrates regulating cell growth, cell death, and cell survival. CK2 has been implicated in the response to UV irradiation-induced DNA damage, targeting XRCC1 (1) and BRCA1 (2) as well as regulating p53 tumor suppressor protein functions (3). Furthermore, CK2 plays a key role in NF-κB activation (4). UV irradiation stimulates CK2-mediated phosphorylation of several carboxy-terminal residues within IκBα, resulting in IκBα proteasomal degradation and the release and nuclear translocation of active NF-κB. CK2 is also dysregulated in many cancers (5) and neurodegenerative diseases such as Alzheimer's and Parkinson's diseases (6). Structurally, CK2 is a multimeric protein complex consisting of two catalytic subunits (α or α') and two regulatory β subunits (7). CK2 is distributed ubiquitously and is apparently constitutively active (7). While cell cycle-dependent Ser-Pro phosphorylation sites have been identified on CK2α and CK2β, Tyr255 phosphorylation by the Src-related kinase c-Fgr seems to have the greatest effect on CK2α activity (8,9).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated DYKDDDDK Tag (D6W5B) Rabbit mAb (Binds to same epitope as Sigma's Anti-FLAG® M2 Antibody) #14793.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: CD81 belongs to the tetraspanin family, which is characterized by four transmembrane domains, one short extracellular domain (ECL1), and one long extracellular domain (ECL2) (1-3). Tetraspanins interact with a variety of cell surface proteins and intracellular signaling molecules in specialized tetraspanin enriched microdomains (TEMs) where they mediate a range of processes including adhesion, motility, membrane organization, and signal transduction (3). CD81, like other tetraspanins, is enriched in exosomes (4). Many research studies demonstrate a role for CD81 in lymphocyte signaling (5-7). CD81 is also a well-characterized receptor for Hepatitis C Virus and facilitates the entry of the virus into target cells (8, 9).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (2,4). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mink, Mouse

Application Methods: Western Blotting

Background: The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis (1). p53 is phosphorylated at multiple sites in vivo and by several different protein kinases in vitro (2,3). DNA damage induces phosphorylation of p53 at Ser15 and Ser20 and leads to a reduced interaction between p53 and its negative regulator, the oncoprotein MDM2 (4). MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation (5,6). p53 can be phosphorylated by ATM, ATR, and DNA-PK at Ser15 and Ser37. Phosphorylation impairs the ability of MDM2 to bind p53, promoting both the accumulation and activation of p53 in response to DNA damage (4,7). Chk2 and Chk1 can phosphorylate p53 at Ser20, enhancing its tetramerization, stability, and activity (8,9). p53 is phosphorylated at Ser392 in vivo (10,11) and by CAK in vitro (11). Phosphorylation of p53 at Ser392 is increased in human tumors (12) and has been reported to influence the growth suppressor function, DNA binding, and transcriptional activation of p53 (10,13,14). p53 is phosphorylated at Ser6 and Ser9 by CK1δ and CK1ε both in vitro and in vivo (13,15). Phosphorylation of p53 at Ser46 regulates the ability of p53 to induce apoptosis (16). Acetylation of p53 is mediated by p300 and CBP acetyltransferases. Inhibition of deacetylation suppressing MDM2 from recruiting HDAC1 complex by p19 (ARF) stabilizes p53. Acetylation appears to play a positive role in the accumulation of p53 protein in stress response (17). Following DNA damage, human p53 becomes acetylated at Lys382 (Lys379 in mouse) in vivo to enhance p53-DNA binding (18). Deacetylation of p53 occurs through interaction with the SIRT1 protein, a deacetylase that may be involved in cellular aging and the DNA damage response (19).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: HER3/ErbB3 is a member of the ErbB receptor protein tyrosine kinase family, but it lacks tyrosine kinase activity. Tyrosine phosphorylation of ErbB3 depends on its association with other ErbB tyrosine kinases. Upon ligand binding, heterodimers form between ErbB3 and other ErbB proteins, and ErbB3 is phosphorylated on tyrosine residues by the activated ErbB kinase (1,2). There are at least 9 potential tyrosine phosphorylation sites in the carboxy-terminal tail of ErbB3. These sites serve as consensus binding sites for signal transducing proteins, including Src family members, Grb2, and the p85 subunit of PI3 kinase, which mediate ErbB downstream signaling (3). Both Tyr1222 and Tyr1289 of ErbB3 reside within a YXXM motif and participate in signaling to PI3K (4).Investigators have found that ErbB3 is highly expressed in many cancer cells (5) and activation of the ErbB3/PI3K pathway is correlated with malignant phenotypes of adenocarcinomas (6). Research studies have demonstrated that in tumor development, ErbB3 may function as an oncogenic unit together with other ErbB members (e.g. ErbB2 requires ErbB3 to drive breast tumor cell proliferation) (7). Thus, investigators view inhibiting interaction between ErbB3 and ErbB tyrosine kinases as a novel strategy for anti-tumor therapy.

The HSP/Chaperone Sampler Kit provides an economical means to investigate protein folding within the cell. The kit contains enough primary and secondary antibodies to perform two Western blot experiments with each antibody.
$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Transglutaminase 2 (TGM2) is a calcium-dependent enzyme that cross-links both cytosolic and extracellular matrix proteins by catalyzing the formation of bonds between lysine and glutamine residues (1). This bifunctional enzyme also has intrinsic GTPase activity, and it has been suggested that regulation of the transamidase activity might be regulated through a G-protein coupled receptor-signaling pathway (2). In cross-linking peptides, TGM2 helps to regulate cytoskeletal structure, cell migration, apoptosis and cell-matrix adhesion. In addition, the enzyme plays an important role in wound healing and the immune response (3). TGM2 has exhibited kinase activity in vitro, with insulin-like growth factor-binding protein-3 (IGFBP-3) as one possible substrate (4). This widely expressed protein is localized to the cytosol and nucleus, but has also been isolated from the cell surface and extracellular matrix (reviewed in 5). Because of its interaction with a number of different substrates, and its role in the response to injury, TGM2 has been associated with the pathology of a number of human disorders. It has long been recognized as the major autoantigen in celiac disease (6); altered TGM2 expression or activity may be associated with Alzheimer disease, Huntington disease, arteriosclerosis, diabetes, and numerous forms of cancer (reviewed in 7).

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

Application Methods: Western Blotting

Background: Paxillin is a multidomain protein that localizes primarily to focal adhesion sites in the extracellular matrix (1). Paxillin is one of the key components of integrin signaling, and tyrosine phosphorylation of paxillin is required for integrin-mediated cytoskeletal reorganization (2). Paxillin is phosphorylated by another focal adhesion component, focal adhesion kinase (FAK), at Tyr118 (3,4). Phospho-Paxillin (Tyr118) may provide a docking site for recruitment of other signaling molecules to focal adhesions. It has been shown that the SH2 domain of Crk binds to the phosphorylated Tyr118 of paxillin (5).

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

Application Methods: Western Blotting

Background: Rac and Cdc42 are members of the Rho-GTPase family. In mammals, Rac exists as three isoforms, Rac1, Rac2 and Rac3, which are highly similar in sequence. Rac1 and Cdc42, the most widely studied of this group, are ubiquitously expressed. Rac2 is expressed in cells of hematopoietic origin, and Rac3, while highly expressed in brain, is also found in many other tissues. Rac and Cdc42 play key signaling roles in cytoskeletal reorganization, membrane trafficking, transcriptional regulation, cell growth and development (1). GTP binding stimulates the activity of Rac/Cdc42, and the hydrolysis of GTP to GDP through the protein's intrinsic GTPase activity, rendering it inactive. GTP hydrolysis is aided by GTPase activating proteins (GAPs), while exchange of GDP for GTP is facilitated by guanine nucleotide exchange factors (GEFs). Another level of regulation is achieved through the binding of RhoGDI, a guanine nucleotide dissociation inhibitor, which retains Rho family GTPases, including Rac and Cdc42, in their inactive GDP-bound state (2,3).

This sampler kit provides an economical means of evaluating key members of the Hedgehog signaling pathway. The kit contains enough primary and secondary antibody to perform two western miniblot experiments.
$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

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

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

Background: Wiskott-Aldrich syndrome proteins (WASPs) mediate actin dynamics by activating the Arp2/3 actin nucleation complex in response to activated Rho family GTPases. In mammals, five WASP family members have been described. Hematopoietic WASP and ubiquitously expressed N-WASP are autoinhibited in unstimulated cells. Upon stimulation they are activated by cdc42, which relieves the autoinhibition in conjunction with phosphatidyl inositol 4,5-bisphosphate. Three WAVE (Wasf, SCAR) family proteins are similar in sequence to WASP and N-WASP but lack the WASP/N-WASP autoinhibition domains and are indirectly activated by Rac (reviewed in 1). Both WASP and WAVE functions appear to be essential, as knockout of either N-WASP or Scar-2 in mice results in cardiac and neuronal defects and embryonic lethality (2,3). Loss of WASP results in immune system defects and fewer immune cells (4). WAVE-2 (WASF2) is widely distributed, while WAVE-1 and WAVE-3 are strongly expressed in brain (5). WAVE-3 may act as a tumor suppressor in neuroblastoma, a childhood disease of the sympathetic nervous system (6). Increased expression of WAVE-3 is seen in breast cancer, and studies in breast adenocarcinoma cells indicate that WAVE-3 regulates breast cancer progression, invasion and metastasis through the p38 mitogen-activated protein kinase (MAPK) pathway (7,8).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Guinea Pig, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Vasodilator-stimulated phosphoprotein (VASP) was originally characterized as a substrate of both cGMP- and cAMP-dependent kinases (PKG and PKA, or cGPK and cAPK, respectively) (1). It is now believed that VASP belongs to the Ena/VASP family of adaptor proteins linking the cytoskeletal system to the signal transduction pathways and that it functions in cytoskeletal organization, fibroblast migration, platelet activation and axon guidance (2,3). Three phosphorylation sites, Ser157, Ser239, and Thr278, have been identified. Ser239 is the major PKG phosphorylation site while Ser157 is the major PKA phosphorylation site (4). Evidence suggests that VASP phosphorylation reduces its association with actin and has a negative effect on actin polymerization (5). Phosphorylation at Ser239 of VASP is a useful marker for monitoring PKG activation and signaling (6,7).

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

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

Background: The estrogen-related receptor (ERR) subfamily of orphan nuclear receptors include three protein receptors, ERRα/NR3B1, ERRβ/NR3B2, and ERRγ/NR3B3, that have yet to be associated with natural ligands. PGC-1 coactivators regulate ERR transcription activation ability and receptor-induced transcription of genes involved in lipid metabolism, glucose metabolism, and mitochondrial biogenesis (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: FIP200 (FAK family kinase-interacting protein of 200 kDa) was identified in a two-hybrid screen with the tyrosine kinase Pyk2 and can inhibit Pyk2 kinase activity as well as related family members (1). FIP200 was later independently identified in a multi-drug resistance screen and named RB1CC1 (RB1-inducible coiled-coil 1) due to its induction by cytotoxic stress and RB1 expression regulation (2). FIP200 function has been linked to apoptosis, cell cycle progression, cell growth, and migration (reviewed in 3). FIP200 has also recently been shown to interact with ULK1 and is required for autophagosome formation (4). FIP200 is part of an ULK1 complex along with Atg13 that is regulated by mTOR and is required for starvation induced autophagy (5-7).

The Src Antibody Sampler kit provides an economical means of evaluating total Src protein levels and its phosphorylation status. The kit contains enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

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

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

Background: The cytoskeleton consists of three types of cytosolic fibers: microtubules, microfilaments (actin filaments), and intermediate filaments. Globular tubulin subunits comprise the microtubule building block, with α/β-tubulin heterodimers forming the tubulin subunit common to all eukaryotic cells. γ-tubulin is required to nucleate polymerization of tubulin subunits to form microtubule polymers. Many cell movements are mediated by microtubule action, including the beating of cilia and flagella, cytoplasmic transport of membrane vesicles, chromosome alignment during meiosis/mitosis, and nerve-cell axon migration. These movements result from competitive microtubule polymerization and depolymerization or through the actions of microtubule motor proteins (1).