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Product listing: Atg12 Antibody (Mouse Specific), UniProt ID Q9CQY1 #2011 to HMGCS2 (D3U1A) Rabbit mAb, UniProt ID P54868 #20940

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), 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 has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: 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 has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Pig

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Protein kinase D2 (PKD2) is one of three members of the protein kinase D family, including PKD1/PKCμ and PKD3/PKCν, that belong to the calcium/calmodulin superfamily of serine/threonine protein kinases (1,2). PKDs contain a conserved, carboxy-terminal catalytic domain, an amino-terminal regulatory region hallmarked by a PH domain that coordinates subcellular localization, and two zinc-finger/C1 lipid-binding domains that mediate activation of the enzyme in response to diacylglycerol (DAG) or phorbol ester (2,3). In addition to lipid-mediated activation, PKD catalytic activity can also be stimulated via phosphorylation of critical serine residues within the activation loop of the enzyme (4-8). Novel PKCs, such as PKCη and PKCε, have been shown to phosphorylate PKD1 at Ser744 and Ser748 (Ser706 and Ser710 in human PKD2), resulting in alleviation of autoinhibition of the enzyme mediated by PH domain interactions with the catalytic domain (5). Phosphorylation and activation of PKD isoforms has also been described for other upstream kinases. For example, casein kinase 2 (CK2) has been shown to phosphorylate PKD2 at Ser244, which promotes nuclear accumulation of PKD2, phosphorylation of HDAC7, and expression of Nur77 (9). Although only a handfull of PKD2 effectors have been identified, PKD2 has been implicated in regulating an array of cellular events, including cell survival, development, growth, migration, and transformation (10-14). PKD2-mediated phosphorylation of at least one known substrate, phosphatidylinositol 4-kinase type IIIβ (PI4KIIIβ), also implicates PKD2 in the formation and regulation of exocytotic transport vesicles from the trans Golgi network (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CRYAB (αB-Crystallin) is a member of the small heat shock protein (sHSP also known as HSP20) family (1). This protein was initially found to be overexpressed in the eye lens, and later also detected at high levels in heart and skeletal muscle tissues (2,3). CRYAB functions mainly as a molecular chaperone, responding to stress by binding unfolded target proteins to prevent aggregation (4,5). Research studies have shown that elevated expression of CRYAB in neurological disease and stroke patients protects tissue and cells from damage under extreme stress, leading to the investigation of CRYAB as a potential therapeutic target (6-9). Researchers also found that expression of the missense mutation of CRYAB (R120G) in the mouse model causes cardiomyopathy due to abnormal desmin aggregation (10). At the molecular level, CRYAB is involved in multiple biological processes, such as inhibiting apoptosis by binding and inhibiting caspase and proapoptotic Bax and Bcl-xS protein functions (11,12), promoting angiogenesis by binding and stabilizing VEGF for secretion (13), and regulating cytoskeletal organization through association with actin filament, intermediate filament, and cardiac titin (14-16).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

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

Application Methods: Western Blotting

Background: Rap1 and Rap2 belong to the Ras subfamily of small GTPases and are activated by a wide variety of stimuli through integrins, receptor tyrosine kinases (RTKs), G-protein coupled receptors (GPCR), death domain associated receptors (DD-R) and ion channels (1,2). Like other small GTPases, Rap activity is stimulated by guanine nucleotide exchange factors (GEF) and inactivated by GTPase activating proteins (GAP). A wide variety of Rap GEFs have been identified: C3G connects Rap1 with RTKs through adaptor proteins such as Crk, Epacs (or cAMP-GEFs) transmit signals from cAMP, and CD-GEFs (or CalDAG-GEFs) convey signals from either or both Ca2+ and DAG (1). Rap1 primarily regulates multiple integrin-dependent processes such as morphogenesis, cell-cell adhesion, hematopoiesis, leukocyte migration and tumor invasion (1,2). Rap1 may also regulate proliferation, differentiation and survival through downstream effectors including B-Raf, PI3K, RalGEF and phospholipases (PLCs) (1-4). Rap1 and Rap2 are not fuctionally redundant as they perform overlapping but distinct functions (5). Recent research indicates that Rap2 regulates Dsh subcellular localization and is required for Wnt signaling in early development (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: PTK7 (CCK4) is a non-active receptor tyrosine kinase originally identified in colon carcinoma cells (1). PTK7 functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization, and apoptosis to regulate embryogenesis, epithelial tissue organization, neuronal tube closure, neuronal crest formation, and axon guidance (2-5). PTK7 acts as a co-receptor in both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathways (6). In the non-canonical Wnt pathway, PTK7 activates downstream signaling by direct interaction with RACK1 and recruitment of DSH into the membrane localized receptor complex (3,6,7). PTK7 exerts an inhibitory effect on canonical Wnt pathway signal transduction through competition for frizzled receptor binding at the membrane surface (8). PTK7 gene expression is regulated by Cdx (9), while protein stability is regulated by membrane associated proteinase degradation. PTK7 is targeted for proteolytic degradation and extracellular domain shedding by the metalloproteinases MMP14 and Adam17, leading to enhanced cell proliferatiion, migration, and facilitated cancer cell invasion (10,11). PTK7 has been shown to regulate other signaling pathways by functioning as a co-receptor with membrane receptors, such as Plexin A1 and VEGFR1 (12-14).

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

Application Methods: Western Blotting

Background: Transketolase (TKT) is a homodimer in the pentose phosphate pathway (PPP) that catalyzes the interketol transfer between ketoses and aldoses (1,2). This enzyme, along with transaldolase, connects the nonoxidative branch of the PPP with glycolysis (1-3). Several regions of TKT are evolutionarily conserved from gram-negative bacteria to mammals (3). There is evidence that hypoxic (4) and non-hypoxic induction of HIF1-α (5) increases the expression of TKT. Because cancer cells rely on TKT in altered cell metabolism for nucleic acid synthesis, work has been done to develop inhibitors of TKT as novel cancer treatments (5-8).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Max-like protein X (MLX), also known as transcription factor-like protein 4 (TCFL4), is a member of the Myc/Max/Mad network of transcriptional regulator proteins that share a common basic-helix-loop-helix zipper (bHLH-ZIP) motif required for dimerization and DNA-binding (1,2). MLX is ubiquitously expressed in most cell lines and functions as a binding partner for MLXIP (also known as MondoA) and MLXIPL (also known as ChREBP) (1,2). MLX/MLXIP and MLX/MLXIPL heterodimers function to regulate glucose homeostasis by sensing glucose metabolites in the cell. These heterodimeric protein complexes reside mainly in the cytoplasm and mitochondria of cells grown in low glucose, and translocate to the nucleus upon increased intracellular glucose levels to activate transcription of downstream target genes (1,2). MLX/MLXIP is required for the deregulated Myc-induced reprogramming of multiple metabolic pathways during oncogenesis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Microtubule associated proteins regulate the stability of microtubules and control processes such as cell polarity/differentiation, neurite outgrowth, cell division and organelle trafficking (1). The MARK (MAP/microtubule affinity-regulating kinases) family (MARK1-4) of serine/threonine kinases was identified based on their ability to phosphorylate microtubule-associated proteins (MAPs) including tau, MAP2 and MAP4 (2-6). MARK proteins phosphorylate MAPs within their microtubule binding domains, causing dissociation of MAPs from microtubules and increased microtubule dynamics (2-4). In the case of tau, phosphorylation has been hypothesized to contribute to the formation of neurofibrillary tangles observed in Alzheimer's disease. Overexpression of MARK leads to hyperphosphorylation of MAPs, morphological changes and cell death (4). The tumor suppressor kinase LKB1 phosphorylates MARK and the closely related AMP-kinases within their T-loops, leading to increased activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: REDD1 (REgulated in Development and DNA damage responses) expression is induced by hypoxia, cell stress, apoptosis and DNA damage. REDD1 is a transcriptional target of p53 and p63 following DNA damage, and links p63 to Ros (1). REDD1 functions as a negative regulator of mTOR in response to hypoxia in a tuberin-dependent manner (2). Depending on cell context, REDD1 can either be protecting or detrimental for cells under oxidative or ischemic stresses (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Interferon regulatory factors (IRFs) comprise a family of transcription factors that function within the Jak/Stat pathway to regulate interferon (IFN) and IFN-inducible gene expression in response to viral infection (1). IRFs play an important role in pathogen defense, autoimmunity, lymphocyte development, cell growth, and susceptibility to transformation. The IRF family includes nine members: IRF-1, IRF-2, IRF-9/ISGF3γ, IRF-3, IRF-4 (Pip/LSIRF/ICSAT), IRF-5, IRF-6, IRF-7, and IRF-8/ICSBP. All IRF proteins share homology in their amino-terminal DNA-binding domains. IRF family members regulate transcription through interactions with proteins that share similar DNA-binding motifs, such as IFN-stimulated response elements (ISRE), IFN consensus sequences (ICS), and IFN regulatory elements (IRF-E) (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Granzymes are a family of serine proteases expressed by cytotoxic T lymphocytes and natural killer (NK) cells and are key components of immune responses to pathogens and transformed cells (1). Granzymes are synthesized as zymogens and are processed into mature enzymes by cleavage of a leader sequence. They are released by exocytosis in lysosome-like granules containing perforin, a membrane pore-forming protein. Granzyme B has the strongest apoptotic activity of all the granzymes as a result of its caspase-like ability to cleave substrates at aspartic acid residues thereby activating procaspases directly and cleaving downstream caspase substrates (2,3).

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

Application Methods: Western Blotting

Background: The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways (1,2). 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ, and η that have been identified in mammals. The initially described α and δ isoforms are confirmed to be phosphorylated forms of β and ζ, respectively (3). Through their amino-terminal α helical region, 14-3-3 proteins form homo- or heterodimers that interact with a wide variety of proteins: transcription factors, metabolic enzymes, cytoskeletal proteins, kinases, phosphatases, and other signaling molecules (3,4). The interaction of 14-3-3 proteins with their targets is primarily through a phospho-Ser/Thr motif. However, binding to divergent phospho-Ser/Thr motifs, as well as phosphorylation independent interactions has been observed (4). 14-3-3 binding masks specific sequences of the target protein, and therefore, modulates target protein localization, phosphorylation state, stability, and molecular interactions (1-4). 14-3-3 proteins may also induce target protein conformational changes that modify target protein function (4,5). Distinct temporal and spatial expression patterns of 14-3-3 isoforms have been observed in development and in acute response to extracellular signals and drugs, suggesting that 14-3-3 isoforms may perform different functions despite their sequence similarities (4). Several studies suggest that 14-3-3 isoforms are differentially regulated in cancer and neurological syndromes (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Cofilin is an evolutionarily conserved, actin-binding protein that severs actin filaments during processes that rely on actin filament dynamics, including cytokinesis, cell migration, invasion, and neuronal development. Actin severing and filament depolymerization are regulated through the controlled cycling of cofilin between the phosphorylated and dephosphorylated forms (1). The kinases LIMK and TESK inactivate cofilin by phosphorylating it at Ser3 (2,3). The slingshot homologs (SSH1, SSH2 and SSH3) and chronophin/PDXP phosphatases remove phosphate from cofilin at Ser3, enabling cofilin binding to actin and filament depolymerization (3). LIMK and SSH1 regulate cofilin activity downstream of neuregulin signaling in Schwann cells (4).Slingshot homolog 1 (SSH1) can also dephosphorylate LIMK kinases, suppressing LIMK phosphorylation of cofilin (5). In addition, SSH1 modulates actin dynamics by stabilizing F-actin and promoting actin bundling independent of its cofilin phosphatase activity (6). SSH1 activity is regulated by phosphorylation and protein-protein interaction through various signaling pathways (1). Binding of SSH1 to F-actin stimulates its cofilin phosphatase activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), 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 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 jumonji domain-containing protein 2 (JMJD2) family, also known as the JmjC domain-containing histone demethylation protein 3 (JHDM3) family, contains four members: JMJD2A/JHDM3A, JMJD2B/JHDM3B, JMJD2C/JHDM3C, and JMJD2D/JHDM3D. In addition to the JmjC domain, these proteins also contain JmjN, PHD, and tudor domains, the latter of which has been shown to bind to methylated histone H3 at Lys4 and Lys9, and methylated histone H4 at Lys20 (4,5). JMJD2 proteins have been shown to demethylate di- and tri-methyl histone H3 at Lys9 and Lys36 and function as both activators and repressors of transcription (6-11). JMJD2A, JMJD2C, and JMJD2D function as coactivators of the androgen receptor in prostate tumor cells (7). In contrast, JMJD2A also associates with Rb and NCoR corepressor complexes and is necessary for transcriptional repression of target genes (8,9). JMJD2B antagonizes histone H3 Lys9 tri-methylation at pericentric heterochromatin (10). JMJD2C, also known as GASC1, is amplified in squamous cell carcinomas and metastatic lung carcinoma and inhibition of JMJD2C expression decreases cell proliferation (11,12). JMJD2C has also been identified as a downstream target of Oct-4 and is critical for the regulation of self-renewal in embryonic stem cells (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: SUFU (Suppressor of Fused) was identified in Drosophila as a suppressor of the Fused (Fu) kinase that is essential for Hedgehog signaling during embryonic pattern formation (1). SUFU suppresses Hedgehog signaling by regulating the localization of the transcription factors Gli and Ci (2,3). In Drosophila, SUFU may also positively regulate Hedgehog signaling depending on SUFU protein levels and Hedgehog signal intensity (4). SUFU may function as a tumor suppressor as inactivation and loss of heterozygosity of SUFU is associated with human rhabdomyosarcomas and medulloblastomas (5,6). Deletion of SUFU in mice results in embryonic lethality, while heterozygotes exhibit developmental defects characteristic of basal cell nevus syndrome. This aberrant developmental pathway is attributed to ligand-independent activation of Hedgehog signaling (7). GSK-3β binds and phosphorylates SUFU in vitro and additional information predicts that GSK-3β may positively regulate Hedgehog signaling through modification of SUFU (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Importins belong to the karyopherin family of nuclear transport proteins (1) and are divided into two subgroups: importin α and importin β. Importins mainly function in nuclear protein import and export (2,3). Importin β1 (also known as karyopherin β1, Kpnβ1, Kpnb1, or p97) plays a key role in the nuclear import process (1-3). Nuclear import via importin β1 association with adaptor importin α (also known as karyopherin α, or Kpnα) is an essential component of the classical nuclear localization signal (NLS) pathway (4). Importin α directly recognizes the NLS present in the cargo target, prompting complex formation with importin β1. The cargo:importin α:importin β1 complex is transported across the nuclear pore complex (NPC) into the nucleus, where it is dissociated by the binding of RanGTP (1-4). Nuclear import directly via importin β1 can also occur by importin β1 recognition of the cargo protein, bypassing importin α involvement. In both cases, the importin β1/target protein interaction is mediated through the binding of importin β1 HEAT repeats with the target protein sequences (either the cargo protein itself or importin α) (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: 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.

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

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

Background: The mTORC1 kinase complex is a critical regulator of cell growth (1,2). Its activity is modulated by energy levels, growth factors, and amino acids via signaling through Akt, MAPK, and AMPK pathways (3,4). Recent studies found that the four related GTPases, RagA, RagB, RagC, and RagD, interact with raptor within the mTORC1 complex (1,2). These interactions are both necessary and sufficient for mTORC1 activation in response to amino acid signals (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Mammalian long-chain acyl-CoA synthetase (ACSL) catalyzes the ligation of the fatty acid to CoA to form fatty acyl-CoA in a two-step reaction (1). Five isoforms of ACSL have been identified (1). These isoforms have different substrate preferences and subcellular localizations (1). Overexpression of ACSL1 results in changes to fatty acid metabolism in rat primary hepatocytes (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

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

Background: The CRISPR associated protein 9 (Cas9) is an RNA-guided DNA nuclease and part of the Streptococcus pyogenes CRISPR antiviral immunity system that provides adaptive immunity against extra chromosomal genetic material (1). The CRISPR antiviral mechanism of action involves three steps: (i), acquisition of foreign DNA by host bacterium; (ii), synthesis and maturation of CRISPR RNA (crRNA) followed by the formation of RNA-Cas nuclease protein complexes; and (iii), target interference through recognition of foreign DNA by the complex and its cleavage by Cas nuclease activity (2). The type II CRISPR/Cas antiviral immunity system provides a powerful tool for precise genome editing and has potential for specific gene regulation and therapeutic applications (3). The Cas9 protein and a guide RNA consisting of a fusion between a crRNA and a trans-activating crRNA (tracrRNA) must be introduced or expressed in a cell. A 20-nucleotide sequence at the 5' end of the guide RNA directs Cas9 to a specific DNA target site. As a result, Cas9 can be "programmed" to cut various DNA sites both in vitro and in cells and organisms. CRISPR/Cas9 genome editing tools have been used in many organisms, including mouse and human cells (4,5). Research studies demonstrate that CRISPR can be used to generate mutant alleles or reporter genes in rodents and primate embryonic stem cells (6-8).

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

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

Background: Metastasis suppressor 1 (MTSS1) is a multi-functional scaffold protein that was initially discovered using a differential display technique that identified proteins missing from bladder cancer cell lines (1,2). MTSS1 (also known as Missing in Metastasis or MIM) is a cytoskeletal remodeling protein that contains a C-terminal WH2 actin-binding motif (1,3). Presence of an IMD (IRSp53/MIM homology) domain allows MTSS1 to induce F-actin bundling and filopodia formation in cells (4). MTSS1 binds to and activates Rac, a protein known to promote the formation of filopodia and lamellipodia (5). The receptor tyrosine phosphatase δ (PTPRD) is associated with MTSS1 and is required for MTSS1-dependent cytoskeletal change (6,7). MTSS1 is a SHH responsive gene that can help regulate GLI-dependent transcriptional activity (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Importins belong to the karyopherin family of nuclear transport proteins and are divided into two subgroups: importin alpha and importin beta. Importins function mainly in the import and export of nuclear proteins (1,2). KPNA2 (karyopherin alpha 2), a member of the importin alpha family, contains an N-terminal importin beta binding (IBB) motif followed by a hydrophobic region consisting of 10 armadillo repeats that function in binding to the nuclear localization signal (NLS) sites of cargo proteins (3-5). A trimeric complex (importin beta/KPNA2/cargo protein) forms, translocates into the nucleus, and then dissociates upon binding of RanGTP to importin beta. The dissociated importin alpha is recycled back to the cytoplasm with the help of export factor CAS (6,7). KPNA2 can differentially regulate target localization by binding to different cargo proteins, either actively transporting them to the nucleus (such as oct3/4) or retaining them in the cytoplasm by formation of incompetent complexes (such as oct6/brn2) (8). Research studies indicate that KPNA2 promotes cell proliferation and tumorigenesis. Research studies have also shown that up-regulation of KPNA2 is associated with cancer progression. Therefore, it has become a focus of biomarker research (9-13).

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

Application Methods: Chromatin IP, Western Blotting

Background: Suppressor of Ty-16 (SPT16) and structure-specific recognition protein-1 (SSRP1) are subunits of the facilitates chromatin transcription (FACT) complex that is essential for transcription elongation (1,2). FACT facilitates RNA polymerase-dependent transcription of chromatin templates by destabilizing the nucleosomes within the open reading frames of active genes (3-5). FACT destabilizes the nucleosomes, which would otherwise act as barriers to RNA polymerase transcription activity, by disrupting histone-histone and histone-DNA contacts that lead to the eviction of the histone H2A-H2B dimer (2,3,6). FACT may also function as a histone chaperone to reassemble nucleosomes after RNA polymerase passage (7). In addition to transcription, FACT activity has been shown to have a role in DNA replication in yeast and in DNA repair by contributing to the activation of p53 by CK2 and by facilitating histone H2AX-H2B exchange upon DNA damage (8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: MAP kinases are inactivated by dual-specificity protein phosphatases (DUSPs) that differ in their substrate specificity, tissue distribution, inducibility by extracellular stimuli, and cellular localization. DUSPs, also known as MAPK phosphatases (MKP), specifically dephosphorylate both threonine and tyrosine residues in MAPK P-loops and have been shown to play important roles in regulating the function of the MAPK family (1,2). At least 13 members of the family (DUSP1-10, DUSP14, DUSP16, and DUSP22) display unique substrate specificities for various MAP kinases (3). MAPK phosphatases typically contain an amino-terminal rhodanese-fold responsible for DUSP docking to MAPK family members and a carboxy-terminal catalytic domain (4). These phosphatases can play important roles in development, immune system function, stress responses, and metabolic homeostasis (5). In addition, research studies have implicated DUSPs in the development of cancer and the response of cancer cells to chemotherapy (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in vesicle transport and membrane fusion by pairing of vesicular SNAREs (v-SNAREs) with cognate target SNAREs (t-SNAREs) (reviewed in 1,2). Vesicle associated membrane protein 8 (VAMP8), also known as endobrevin, is a v-SNARE originally found preferentially localized to early endosomes (3). VAMP8 knockout mice did not show abnormal endosomal vesicular trafficking, perhaps having a redundant role with other VAMP family members (4). Instead, research studies have shown that VAMP8 is widely expressed in exocrine tissues and has a critical role in the exocytosis pathways of a variety of cells (4-9). In addition, lysosome localized VAMP8 has been shown to play a role in autophagosome/lysosome fusion during antimicrobial (xenophagy) and canonical starvation induced autophagy (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The SHANK family proteins, also known as proline-rich synapse-associated proteins, consist of SHANK1, SHANK2, and SHANK3. SHANK proteins act as scaffolds at the neuronal post-synaptic density (PSD) (1), where they play a critical role in PSD assembly of excitatory synapses during development (2). While recruitment of SHANK proteins to the synapse is independent of their interaction with Homer (3), proper synaptic targeting of SHANK1 is mediated by interactions between its PDZ domain and PSD proteins (4). At the synapse, SHANK proteins interact with NMDA receptors and metabotropic glutamate receptor complexes (5). Research studies have proposed the involvement of SHANK proteins in autism and neurodegenerative diseases (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (HMGCS2) generates hydroxymethylglutaryl-CoA (HMG-CoA) from acetyl-CoA and acetoacetyl-CoA, a rate-limiting step in ketogenesis (1). Starvation or a high-fat and low-carbohydrate diet increases the levels of hepatic FGF21, which in turn up-regulates HMGCS2 expression (2). Furthermore, mTORC1 inhibition was shown to be required for the increase of HMGCS2 expression mediated by PPARα in response to fasting (3). In addition, studies on mice lacking HMGCS2 suggest that ketogenesis plays a role in the prevention of diet-induced fatty liver injury and hyperglycemia (4).