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Product listing: MCM3 (D47B6) Rabbit mAb, UniProt ID P25205 #4003 to PathScan® Sandwich ELISA Control Phospho Cell Extract II #7989

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

Application Methods: Western Blotting

Background: The minichromosome maintenance (MCM) 2-7 proteins are a family of six related proteins required for initiation and elongation of DNA replication. MCM2-7 bind together to form the heterohexameric MCM complex that is thought to act as a replicative helicase at the DNA replication fork (1-5). This complex is a key component of the pre-replication complex (pre-RC) (reviewed in 1). Cdc6 and CDT1 recruit the MCM complex to the origin recognition complex (ORC) during late mitosis/early G1 phase forming the pre-RC and licensing the DNA for replication (reviewed in 2). Licensing of the chromatin permits the DNA to replicate only once per cell cycle, thereby helping to ensure that genetic alterations and malignant cell growth do not occur (reviewed in 3). Phosphorylation of the MCM2, MCM3, MCM4, and MCM6 subunits appears to regulate MCM complex activity and the initiation of DNA synthesis (6-8). CDK1 phosphorylation of MCM3 at Ser112 during late mitosis/early G1 phase has been shown to initiate complex formation and chromatin loading in vitro (8). Phosphorylation of MCM2 at serine 139 by cdc7/dbf4 coincides with the initiation of DNA replication (9). MCM proteins are removed during DNA replication, causing chromatin to become unlicensed through inhibition of pre-RC reformation. Studies have shown that the MCM complex is involved in checkpoint control by protecting the structure of the replication fork and assisting in restarting replication by recruiting checkpoint proteins after arrest (reviewed in 3,10).

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

Application Methods: Western Blotting

Background: Ubiquitin (Ub) is a conserved polypeptide that is covalently linked to many cellular proteins through the process of ubiquitination, which targets proteins for degradation by the 26S proteasome. Three enzymatic components are involved in the protein ubiquitination cascade. Ubiquitin is first activated by forming a thioester complex with an E1 ubiquitin-activating enzyme. Activated ubiquitin is subsequently transferred to an E2 ubiquitin-carrier protein, and then from the E2 to an E3 ubiquitin ligase for final delivery to the ε-amino group of the target protein lysine residue (1-3).The ubiquitin-conjugating enzyme E2 G2 (UBE2G2, UBC7) is a ubiquitously expressed E2 enzyme and critical component of the endoplasmic reticulum-associated degradation pathway (ERAD) (4). Research studies demonstrate that UBE2G2 forms homodimers and preassembles K48-linked poly-Ub chains at its active site (5-8). The association of Ub-charged UBE2G2 molecules with the ER-resident E3 ligase AMFR (gp78) is required for Ub chain transfer and efficient removal of misfolded or aggregated proteins through the ERAD pathway (9,10).

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

Application Methods: Western Blotting

Background: Reptin/RuvBL2 and Pontin/RuvBL1 are closely related members of the AAA+ (ATPase associated with diverse cellular activities) superfamily of proteins, and are putatively homologous to bacterial RuvB proteins that drive branch migration of Holliday junctions (1). Reptin and Pontin function together as essential components of chromatin remodeling and modification complexes, such as INO80, TIP60, SRCAP, and Uri1, which play key roles in regulating gene transcription (1,2). In their capacity as essential transcriptional co-regulators, Reptin and Pontin have both been implicated in oncogenic transformations, including those driven by c-Myc, β-catenin, and E1A (2-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: P2X purinergic receptors are ATP-gated ion channels involved in physiological processes that include inflammation, afferent sensory signaling, and sympathetic motor nerve activity. Seven different vertebrate genes (P2RX1-P2RX7) encode for individual receptor protein subunits (1). All P2X subunit proteins share similar protein domain structure, but can differ in overall protein length from 384 to 595 amino acids. Each P2X subunit is composed of amino- and carboxy-terminal intracellular domains, two transmembrane domains, and a large extracellular loop that contains ten evenly spaced cysteines and multiple glycosylation sites (2). P2X receptors are found in a variety of cell types and tissues, including central and peripheral nervous system neurons and glial cells, autonomic and sensory neurons, bone, muscle, and hematopoietic tissues (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: IRAP (also known as LNPEP) was originally described as an insulin-responsive aminopeptidase found in Glut4-containing vesicles (1). It is essentially always in the same compartments as Glut4 and has identical insulin-stimulated translocation patterns as Glut4 (2). IRAP is therefore considered to be a surrogate marker for Glut4 (2). IRAP was later found to be a critical enzyme that regulates the expression and activity of several essential hormones and regulatory proteins, including the Glut4 transporter (3,4). This membrane associated, zinc-dependent cystinyl aminopeptidase acts as both a receptor for angiotensin IV as well as the enzyme that catalyzes the synthesis of this essential hormone from its angiotensinogen precursor (5). IRAP catalyzes the hydrolysis of several peptide hormones, including oxytocin and vasopressin (4). Abnormal IRAP expression or activity is associated with several forms of cancer in humans, including renal and endometrial cancers (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: RPA70 (HSSB, REPA1, RF-A, RP-A, p70) is a component of a heterotrimeric complex, composed of 70, 32/30 and 14 kDa subunits, collectively known as RPA. RPA is a single stranded DNA binding protein, whose DNA binding activity is believed to reside entirely in the 70 kDa subunit. The complex is required for almost all aspects of cellular DNA metabolism such as DNA replication (1-3), recombination, cell cycle and DNA damage checkpoints, and all major types of DNA repair including nucleotide excision, base excision, mismatch and double-strand break repairs (4-7). In response to genotoxic stress in eukaryotic cells, RPA has been shown to associate with the Rad9/Rad1/Hus1 (9-1-1) checkpoint complex (8). RPA is hyperphosphorylated upon DNA damage or replication stress by checkpoint kinases including ataxia telangiectasia mutated (ATM), ATM and Rad3-related (ATR), and DNA-dependent protein kinase (DNA-PK) (9-11). Phosphorylation of RPA32 occurs at serines 4, 8 and 33 (11). Hyperphosphorylation may alter RPA-DNA and RPA-protein interactions. In addition to the checkpoint partners, RPA interacts with a wide variety of protein partners, including proteins required for normal replication such as RCF, PCNA and Pol α, and also proteins involved in SV40 replication, such as DNA polymerase I and SV40 large T antigen (10,12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The semaphorin family of proteins is involved in axon guidance, cell migration, angiogenesis, and immune response. Plexins and neuropilins bind with high affinity to semaphorins to mediate their functions. Semaphorins are divided into seven classes of secreted or membrane-bound proteins. Members of Class 4 semaphorins include 4A through 4G; semaphorin 4B is a membrane-associated protein (1,2). Semaphorin 4B binds to the CLCP1 receptor and regulates cell motility (3). Furthermore, semaphorin 4B, like many other semaphorins, has a PDZ domain-binding motif at the carboxy terminus that interacts with PSD95 and localizes to the post-synaptic membrane (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: SINTBAD, identified based on homology to NAP1, is an adaptor protein for TBK1 and IKKε, two related kinases that play a pivotal role in innate immune response (1). These kinases trigger the phosphorylation and subsequent activation of the transcription factor IRF-3, resulting in gene regulation required for immune responses (2). The precise mechanism by which SINTBAD activates TBK1 and IKKε is still unclear. Expression of a central region of SINTBAD termed a TBD (TBK binding domain) can function as a dominant negative protein and interfere with IRF-3 activation. SINTBAD and NAP1 can also bind to NDP52, a protein that associates with poly-ubiquitinated proteins, such as those produced on the surfaces of bacteria, and can trigger autophagy (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Structural maintenance of chromosomes 2 (SMC2) and 4 (SMC4) proteins are subunits of the condensin complex, which enables chromosome condensation and maintains the compaction of chromosomes as they separate to opposite poles during anaphase (1-3). In addition to regulating chromosome condensation, condensin is a general regulator of chromosome architecture and may function to regulate gene expression and DNA repair. SMC proteins contain a hallmark bipartite ATPase domain of the ABC ATPase superfamily, which consists of an N-terminal Walker A motif nucleotide-binding domain and C-terminal Walker B motif catalytic domain that interact to form a functional ATPase (1-3). The two ATPase domains are connected by two coiled coil domains separated by a central hinge region that facilitates protein-protein interactions between partnering SMC proteins. In the case of the condensin complex, SMC2 and SMC4 interact to form a functional ATPase required for chromatin condensation; however, the mechanism by which this ATPase activity regulates chromsome architecture is still being determined. In addition to SMC proteins, condensin contains three auxiliary subunits, which function to regulate condensin ATPase activity. Higher eukaryotes contain two distinct condensin complexes (condensin I and II), both of which contain SMC2 and SMC4 (1-3). Condensin I also contains the auxiliary subunits CAP-D2, CAP-G and CAP-H, while condensin II contains the related auxiliary proteins CAP-D3, CAP-G2 and CAP-H2. The two condensin complexes show different localization patterns during the cell cycle and on chromosomes and both are required for successful mitosis, suggesting distinct functions for each complex (1-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. During neurotransmission, glutamate is released from vesicles of the pre-synaptic cell, and glutamate receptors (e.g. NMDA Receptor, AMPA Receptor) bind glutamate for activation at the opposing post-synaptic cell. Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels. In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion. Five EAATs (EAAT1-5) are characterized: EAAT2 (GLT-1) is primarily expressed in astrocytes but is also expressed in neurons of the retina and during fetal development (1). Homozygous EAAT2 knockout mice have spontaneous, lethal seizures and an increased predisposition to acute cortical injury (2). PKC phosphorylates Ser113 of EAAT2 and coincides with glutamate transport (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ron is a member of the Met protooncogene family of receptor tyrosine kinases, which also includes Stk, c-Met, and c-Sea. The functional Ron is a heterodimer composed of a 40 kDa α chain and a 150 kDa β chain. Ron is initially synthesized in the cells as a single-chain, pro-Ron precursor that is cleaved into the two active chains. The α chain is completely extracellular, whereas the β chain traverses the cell membrane and contains the intracellular tyrosine kinase and regulatory elements (1,2). Ron mediates multiple signaling cascades that involve cell motility, adhesion, proliferation, and apoptosis. The signaling pathways activated downstream of Ron include the ras/mitogen-activated protein kinase (MAPK), phosphatidyl inositol-3 kinase (PI3K)/Akt, and focal adhesion kinase (FAK) pathways. Ron activation can also significantly increase c-Src activity, a signaling intermediate involved in cell cycle progression, motility, angiogenesis and survival (3,4). The function of Ron has been shown to be important for embryological development as well as implicated in the progression and metastasis of tumors (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses (1-4). TLRs recognize conserved motifs found in various pathogens and mediate defense responses (5-7). Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes (4). The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the Toll/Interleukin-1 receptor (TIR) domain (1). Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (TRIF), and Toll-receptor-associated molecule (TRAM) (8-10). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK (8,11-14). Activation of IKK leads to the degradation of IκB, which normally maintains NF-κB in an inactive state by sequestering it in the cytoplasm.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) is an essential step in the formation of thymine nucleotides (1,2, reviewed in 3). This process is catalyzed by thymidylate synthase (TS or TYMS), a homodimer composed of two 30 kDa subunits. TS is an intracellular enzyme that provides the sole de novo source of thymidylate, making it a required enzyme in DNA biosynthesis with activity highest in proliferating cells (1). Being the exclusive source of dTMP, investigators have concluded that TS is also an important target for anticancer agents such as 5-fluorouracil (5-FU) (1-5). 5-FU acts as a TS inhibitor and is active against solid tumors such as colon, breast, head, and neck. Research studies have demonstrated that patients with metastases expressing lower levels of TS have a higher response rate to treatment with 5-FU than patients with tumors that have increased levels of TS (5). Researchers continue to investigate TS expression in different types of cancers (6-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: In Drosophila, lethal giant larvae (lgl), discs large (dlg), and scribble (scrib) act as tumor suppressor genes. Their loss of function in flies causes neoplastic overgrowth of larval brain tissue and imaginal epithelial cells hallmarked by disruption of the cytoskeletal network and cellular polarity (1,2). The human homolog of the Drosophila lgl protein, lethal giant larvae protein homolog 1(LLGL1), is a cytoskeletal protein implicated in regulating cellular organization, migration, and cell polarity (3). As in Drosophila, decreased expression of LLGL1 correlates with an increased incidence of cellular overgrowth and malignant transformation (4-6). In mammalian epithelial cells, LLGL1 redistributes from the cytoplasm to regions of cell-cell contact, allowing the establishment and maintainence of a polarized morphology (7). LLGL1 also plays a role in the formation of epithelial junctions via its direct interactions with PAR6 and aPKC, the latter of which has been shown to phosphorylate LLGL1 at Ser663, thus restricting its localization to the basolateral region of the cell (8). LLGL1 may also play an additional, unrealized role in cellular development and differentiation as indicated by the fact that Drosophila lgl has been implicated in controlling self-renewal and differentiation of progenitor cells (9). Recent studies in mice have suggested that a mammalian LLGL1 homolog that does not have tumor suppressor-like acitvity, LLGL2, is required for proper polarized invasion of trophoblasts and efficient branching morphogenesis during placental development (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: MutT Homolog 1 (MTH1), an oxidized purine nucleoside triphosphatase, hydrolyzes potentially mutagenic oxidized nucleotide triphosphates, preventing their accumulation in nucleotide pools and their incorporation into DNA and RNA (1). In addition to its function in sanitizing the cell’s nucleotide pool, MTH1 has been shown to have anti-proliferative effects in RAS-transformed tumors (2). Researchers have shown that, while not essential in normal cells, MTH1 is required for cancer cell survival due to increased oxidative damage, and that inhibition of MTH1 activity suppresses cancer growth (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The CXXC finger protein 1 (CXXC1, CGBP, CFP1) is a key subunit of the human SET1 histone methyltransferase complex (1,2) that methylates histone H3 at Lys4 to create a mark of transcriptionally active promoters (3,4). CXXC1 is enriched at CpG islands where it selectively binds non-methylated CpG motifs to provide a link between global H3K4 methylation and CpG islands (5). Research studies have revealed a role for CXXC1 in the maintenance of cytosine methylation through direct interaction with DNMT1 (6-9). The epigenetic functions of CXXC1 are critical for normal embryonic development. Targeted deletion of the murine Cxxc1 gene results in early embryonic lethality while Cxxc1-null embryonic stem (ES) cells exhibit increased apoptosis and fail to undergo differentiation in vitro following withdrawal of leukemia inhibitory factor LIF (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: High mobility group (HMG) proteins are a superfamily of abundant and ubiquitous nuclear proteins that bind DNA without sequence specificity and induce structural changes to the chromatin fiber to regulate access to the underlying DNA. The HMGN family of proteins, which includes five members (HMGN1-5), is characterized by the presence of several conserved protein domains: a positively charged domain, a nucleosome binding domain, and an acidic C-terminal chromatin-unfolding domain (1,2). HMGN proteins function in transcriptional regulation and are recruited to gene promoters by transcription factors, such as estrogen receptor α (ERα), serum responsive factor (SRF), and PITX2, where they can facilitate either gene activation or repression (3-5). HMGN proteins bind specifically to nucleosomal DNA and reduce compaction of the chromatin fiber, in part by competing with linker histone H1 for nucleosome binding (6). In addition, HMGN proteins act to modulate local levels of post-translational histone modifications, decreasing phosphorylation of histone H3 at Ser10 and histone H2A at Ser1 and increasing acetylation of histone H3 at Lys14 (7-9). HMGN proteins can also modulate the activity of several chromatin-remodeling factors and restrict nucleosome mobility (10).

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

Application Methods: Western Blotting

Background: Flotillins belong to a family of lipid raft-associated integral membrane proteins that carry an evolutionarily conserved domain called the prohibitin homology domain (PHB) (1). Flotillin members are ubiquitously expressed and located in noncaveolar microdomains (lipid rafts) on the plasma membrane where they support signal transduction and regulate lipid raft motility and localization (2-5). Two flotillin members have been described, flotillin-1 and flotillin-2. In addition to its colocalization with lipid rafts on the plasma membrane, flotillin-1 also has been found in compartments of the endocytic and autophagosomal pathways, such as recycling/late endosomes, the Golgi complex, and the nucleus (6,7). Flotillin-2 is mainly localized to the plasma membrane and is prevalent in cell-cell contact sites. However, overexpressed flotillin-2 has also been found in the late endosome (4,8,9). Both flotillin-1 and flotillin-2 are commonly used as lipid raft-associated markers.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Endogenous cannabinoids have been implicated in addictive behaviors and drug abuse (1). Fatty-acid amide hydrolase 1 (FAAH1) is a plasma membrane-bound hydrolase that converts oleamide to oleic acid (2). This hydrolase also converts the cannabinoid anandamide, the endogenous ligand for the CB1 cannabinoid receptor, to arachidonic acid, suggesting a role in fatty-acid amide inactivation (2). Mice lacking FAAH1 have significantly higher levels of anandamide in the brain and show decreased sensitivity to pain, further indicating a role for FAAH1 in the regulation of endocannabinoid signaling in vivo (3). FAAH1 null mice also demonstrate an increased preference for alcohol and an increased voluntary uptake of alcohol as compared to wild-type mice, indicating a role of FAAH1 in modulating addictive behaviors (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Fatty acid binding proteins (FABPs) are cytoplasmic lipid chaperones that bind fatty acids and lipids for transport to various cellular components (1,2). Research studies demonstrate differential FABP expression in several types of tumors and their normal-cell counterparts (3). Fatty acid binding protein 3 (FABP3) is predominantly expressed in heart, skeletal muscle, brain, and mammary gland (4). FABP3 may play a role in supplying energy to the heart and other tissues (5). The release of FABP3 from the heart upon infarction is used as a serum marker for myocardial stress and cardiotoxicity (6). Additional studies suggest that FABP3 is a potential tumor suppressor in breast cancer (7).

$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, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: SET and MYND domain-containing protein 2 (SMYD2), also known as lysine methyltransferase protein 3C (KMT3C), is a member of the SMYD family of protein methyltransferases (1). All five members of this family (SMYD1, SMYD2, SMYD3, SMYD4, and SMYD5) contain a conserved catalytic SET domain, originally identified in Drosophila Su[var]3-9, Enhancer of zeste, and Trithorax proteins. This domain is split by the MYN domain/zinc finger motif believed to facilitate protein-protein interactions (1). SMYD2 localizes to both the cytoplasm and nucleus, and is highly expressed in the adult mouse heart, brain, liver, kidney, thymus, and ovary, as well as in the developing mouse embryo (1). SMYD2 functions to repress transcription by interacting with the Sin3A repressor complex and methylating Lys36 of histone H3 (1). SMYD2 also interacts with HSP90α and methylates Lys4 of histone H3, a mark associated with transcriptional activation (2). In addition to histones as methyl substrates, SMYD2 methylates p53 at Lys370 to repress p53-mediated transcriptional activation and apoptosis (3,4).

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

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

Background: The methylation state of lysine residues in histone proteins is a major determinant of the formation of active and inactive regions of the genome and is crucial for the 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 of several proteins has been shown to 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 seven separate families (3). The JMJD1 (Jumonji domain-containing protein 1) family, also known as JHDM2 (JmjC domain-containing histone demethylation protein 2) family, contains four members: hairless (HR), JMJD1A/JHDM2A, JMJD1B/JHDM2B, and JMJD1C/JHDM2C. Hairless is expressed in the skin and brain and acts as a co-repressor of the thyroid hormone receptor (4-6). Mutations in the hairless gene cause alopecia in both mice and humans (4,5). JMJD1A is expressed in meiotic and post-meiotic male germ cells, contributes to androgen receptor-mediated gene regulation, and is required for spermatogenesis (7-9). It has also been identified as a downstream target of OCT4 and STAT3 and is critical for the regulation of self-renewal in embryonic stem cells (10,11). JMJD1B is a more widely expressed family member and is frequently deleted in myeloid leukemia (12). JMJD1C (also known as TRIP8) is a co-factor of both the androgen and thyroid receptors and has a potential link to autism (13-15). Members of the JMJD1/JHDM2 family have been shown to demethylate mono-methyl and di-methyl histone H3 (Lys9) (3,8).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Mouse, Rat, Zebrafish

Application Methods: Western Blotting

Background: The highly conserved receptor for activated C kinase 1 (RACK1), homologous to the β subunit of heterotrimeric G-proteins, was originally identified through its binding of active PKCβII and other classical PKC isoforms (1). RACK1 is a scaffold protein that recruits PKC and a wide range of other proteins to specific subcellular locations, promoting the formation of multiprotein complexes to induce and integrate various signaling pathways (reviewed in 2). One example of this is its enhancement of PKC-dependent JNK activation (3). RACK1 protein also resides in the eukaryotic ribosome, suggesting the possibility that RACK1 participates in the assembly of signaling complexes that regulate translation as well (reviewed in 4). RACK1 binds the SH2 domain of Src, and phosphorylation of RACK1 by Src occurs at Tyr228 after PKC activation (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Two related serine/threonine kinases, UNC-51-like kinase 1 and 2 (ULK1, ULK2), were discovered as mammalian homologs of the C. elegans gene UNC-51 in which mutants exhibited abnormal axonal extension and growth (1-4). Both proteins are widely expressed and contain an amino-terminal kinase domain followed by a central proline/serine rich domain and a highly conserved carboxy-terminal domain. The roles of ULK1 and ULK2 in axon growth have been linked to studies showing that the kinases are localized to neuronal growth cones and are involved in endocytosis of critical growth factors, such as NGF (5). Yeast two-hybrid studies found ULK1/2 associated with modulators of the endocytic pathway, SynGAP and syntenin (6). Structural similarity of ULK1/2 has also been recognized with the yeast autophagy protein Atg1/Apg1 (7). Knockdown experiments using siRNA demonstrated that ULK1 is essential for autophagy (8), a catabolic process for the degradation of bulk cytoplasmic contents (9,10). It appears that Atg1/ULK1 can act as a convergence point for multiple signals that control autophagy (11), and can bind to several autophagy-related (Atg) proteins, regulating phosphorylation states and protein trafficking (12-16).

Jurkat cells are treated with 100 nM calyculin A and 1 mM pervanadate to inhibit multiple serine/threonine and tyrosine phosphatases, respectively and upregulate protein phosphorylation. Treated Jurkat cells were lysed in 1X cell lysis buffer and lysates were lyophilized.