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Product listing: APC3 (D3I1V) Rabbit mAb, UniProt ID P30260 #12530 to Keratin 19 (D7F7W) Rabbit mAb, UniProt ID P08727 #13092

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Cell proliferation in all eukaryotic cells depends strictly upon the ubiquitin ligase (E3) activity of the anaphase promoting complex/cyclosome (APC/C), whose main function is to trigger the transition of the cell cycle from metaphase to anaphase. APC/C performs its various functions by promoting the assembly of polyubiquitin chains on substrate proteins, which targets these proteins for degradation by the 26S proteasome (1,2). In humans, twelve different APC/C subunits have been identified. Like all E3 enzymes, APC/C utilizes ubiquitin residues that have been activated by E1 enzymes and then transferred to E2 enzymes. Indeed, APC/C has been shown to interact with UBE2S and UBE2C E2 enzymes, in part, via the RING-finger domain-containing subunit, APC11 (3-5). APC/C activity is also strictly dependent upon its association with multiple cofactors. For example, the related proteins, Cdc20 and Cdh1/FZR1, participate in the recognition of APC/C substrates by interacting with specific recognition elements in these substrates (6), called D-boxes (7) and KEN-boxes (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Sec61 translocon is a channel complex located on the endoplasmic reticulum (ER) membrane to mediate membrane protein insertion into the organelle (1). There are three components in the complex, Sec61A, Sec61B, and Sec61G (2). Sec61A is the main component of the channel on the ER membrane and directly contacts nascent synthesized polypeptide TMD (transmembrane domain) for insertion (3). Sec61G functions in stablizing the channel (3). In addition to TMD insertion, Sec61 translocon has also been shown to be involved in ER calcium leakage (4,5). Both Bip and calmodulin can inhibit this leakage by their interaction with Sec61A (6,7). Sec61B has no obvious function related to target protein ER membrane insertion, but is involved in other vesicle trafficking processes such as EGFR and Her2 trafficking from the cytosol to nucleus (8,9), Gurken trafficking from Golgi to plasma membrane (10), and copper-transporting ATPase membrane distribution (11).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Bim/Bod is a pro-apoptotic protein belonging to the BH3-only group of Bcl-2 family members including Bad, Bid, Bik, Hrk, and Noxa that contain a BH3 domain but lack other conserved BH1 or BH2 domains (1,2). Bim induces apoptosis by binding to and antagonizing anti-apoptotic members of the Bcl-2 family. Interactions have been observed with Bcl-2, Bcl-xL, Mcl-1, Bcl-w, Bfl-1, and BHRF-1 (1,2). Bim functions in regulating apoptosis associated with thymocyte negative selection and following growth factor withdrawal, during which Bim expression is elevated (3-6). Three major isoforms of Bim are generated by alternative splicing: BimEL, BimL, and BimS (1). The shortest form, BimS, is the most cytotoxic and is generally only transiently expressed during apoptosis. The BimEL and BimL isoforms may be sequestered to the dynein motor complex through an interaction with the dynein light chain and released from this complex during apoptosis (7). Apoptotic activity of these longer isoforms may be regulated by phosphorylation (8,9). Environmental stress triggers Bim phosphorylation by JNK and results in its dissociation from the dynein complex and increased apoptotic activity.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: G protein-coupled Receptor Kinase 6 (GRK6) is one of 7 members of the GRK serine/threonine kinase subfamily, which are known primarily for their role in desensitizing activated G protein-coupled receptors (GPCRs) (1,2). GRKs function by phosphorylating serine/threonine residues in activated GPCRs. Upon phosphorylation these residues serve as binding sites for β-arrestin proteins, inhibiting re-activation of GPCRs by blocking their re-association with G proteins (3). There is evidence that GRKs can also modulate selected non-GPCR signaling pathways (2). For example, GRK6 has been shown to modulate the Wnt signaling pathway via phosphorylation of LRP6 (4), and the insulin-like growth factor signaling pathway (5). GRK6 may also play a role in immune system function. Investigators have found GRK6 expression is typically abundant in hematopoietic tumor cell lines, and a recent research study demonstrated that GRK6 suppression was selectively lethal for a number of myeloma tumor cell lines (6).

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

Application Methods: Western Blotting

Background: Rab11a, Rab11b and Rab25 are members of the Rab11 family of small Ras-like GTPases. Rab11 (isoforms Rab11a and Rab11b) functions as a key regulator in the recycling of perinuclear, plasma membrane and Golgi compartment endosomes (1,2). Despite some overlap, distinct differences exist between Rab11a and Rab11b in both their cellular distribution and functional roles. Rab11a is ubiquitously expressed while Rab11b is found mainly in the heart and brain (3,4). Like other Rab proteins, Rab11 exerts its function via interactions with Rab11 family interacting proteins (FIPs). While there are three distinct classes of FIPs, all appear to share a conserved carboxy-terminal Rab-binding domain that allows Rab-FIP protein interaction. When bound together, these proteins are thought to regulate membrane-associated protein sorting (5,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: TAK1 is a mitogen-activated protein kinase kinase kinase activated by TGF-β and various pro-inflammatory signals (1,2). In vivo, TAK1 activation requires its association with TAK1 binding protein 1 (TAB1), which triggers TAK1 autophosphorylation at Thr184 and Thr187 (3,4). The TAB2 adaptor protein links TAK1 with TRAF6 to mediate TAK1 activation following IL-1 stimulation (5). Once activated, TAK1 phosphorylates the MAPK kinases MKK4 and MKK3/6, which activate JNK and p38 MAPK, respectively. TAK1 and TRAF6 also activate the NF-κB pathway by phosphorylating the NF-κB inducing kinase (NIK) to trigger subsequent activation of IKK (2,6). In addition to TAK1, TAB1 interacts with and activates p38α MAPK (7). Targeted disruption of the TAB1 gene in mice causes a drastic reduction in TAK1 activity and leads to embryonic lethality (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The p21-activated kinase (PAK) family of serine/threonine kinases is engaged in multiple cellular processes, including cytoskeletal reorganization, MAPK signaling, apoptotic signaling, control of phagocyte NADPH oxidase, and growth factor-induced neurite outgrowth (1,2). Several mechanisms that induce PAK activity have been reported. Binding of Rac/Cdc42 to the CRIB (or PBD) domain near the amino terminus of PAK causes autophosphorylation and conformational changes in PAK (1). Phosphorylation of PAK1 at Thr423 by PDK induces activation of PAK1 (3). Several autophosphorylation sites have been identified, including Ser199 and Ser204 of PAK1 and Ser192 and Ser197 of PAK2 (4,5). Because the autophosphorylation sites are located in the amino-terminal inhibitory domain, it has been hypothesized that modification in this region prevents the kinase from reverting to an inactive conformation (6). Research indicates that phosphorylation at Ser144 of PAK1 or Ser139 of PAK3 (located in the kinase inhibitory domain) affects kinase activity (7). Phosphorylation at Ser21 of PAK1 or Ser20 of PAK2 regulates binding with the adaptor protein Nck (8). PAK4, PAK5, and PAK6 have lower sequence similarity with PAK1-3 in the amino-terminal regulatory region (9). Phosphorylation at Ser474 of PAK4, a site analogous to Thr423 of PAK1, may play a pivotal role in regulating the activity and function of PAK4 (10).

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

Application Methods: Western Blotting

Background: Chromodomain-helicase-DNA-binding domain (CHD) proteins have been identified in a variety of organisms (1,2). This family of proteins, which consists of nine members, has been divided into three separate subfamilies: subfamily I (CHD1 and CHD2), subfamily II (CHD3 and CHD4), and subfamily III (CHD5, CHD6, CHD7, CHD8, and CHD9). All of the CHD proteins contain two tandem N-terminal chromodomains, a SWI/SNF-related ATPase domain, and a C-terminal DNA binding domain (1,2). The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes the energy from ATP hydrolysis to modify chromatin structure. CHD1 is a euchromatic protein that associates with the promoters of active genes, and is required for the maintenance of open chromatin and pluripotency in embryonic stem cells (3-6). The two chromodomains of CHD1 facilitate its recruitment to active genes by binding to methyl-lysine 4 of histone H3, a mark associated with transcriptional activation (4-6). Yeast CHD1 is a component of the SAGA and SLIK histone acetyltransferase complexes, and is believed to link histone methylation with histone acetylation during transcriptional activation (6). The CHD2 protein is not well characterized; however, mouse knockout studies suggest important functions in development and tumor suppression. Homozygous CHD2 knockout mice exhibit delayed growth and perinatal lethality (7). Heterozygous knockout mice show increased mortality and gross organ abnormalities, in addition to increased extramedullary hematopoiesis and susceptibility to lymphomas (7,8). CHD2 mutant cells are defective in hematopoietic stem cell differentiation and exhibit aberrant DNA damage responses (8).

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

Application Methods: Western Blotting

Background: The cohesin complex consists of a heterodimer between SMC1 (SMC1A or B) and SMC3, bound by additional RAD21 and STAG proteins (STAG1, 2, or 3) (1,2). These proteins form a ring-like structure that mediates the cohesion of two sister chromatids after DNA replication in S phase (1,2). RAD21 and STAG2 are phosphorylated by Polo-like kinase (PLK) during prophase, which leads to the dissociation of cohesin complexes from the chromosome arms; however, cohesin remains bound to centromeres until anaphase (3,4). RAD21 is cleaved by separin/ESPL1 in anaphase, which leads to dissociation of the remaining cohesin from centromeres, enabling sister chromatids to segregate during mitosis (5). RAD21 is also cleaved by caspase-3 and caspase-7 during apoptosis, resulting in a 64 kDa carboxy-terminal cleavage product that translocates to the cytoplasm and may help to trigger apoptosis (6,7). In addition to mediating cohesion of sister chromatids, the cohesin complex plays important roles in gene regulation and DNA repair, as SMC1 and SMC3 are both phosphorylated by ATM and ATR kinases upon DNA damage (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Rhodopsin is the photoreceptor in the retinal rods. It is activated by photons, transduces visual information through its cognate G protein, transducin, and is inactivated by arrestin binding (1). Using atomic-force microscopy, rhodopsin was found to be arranged into paracrystalline arrays of dimers in mouse disc membranes (2). Rhodopsin is considered to be the prototype of G protein-coupled receptors (GPCRs), and is the first GPCR for which a crystal structure was solved (3). Research studies have linked mutations in the gene encoding rhodopsin to retinitis pigmentosa (4,5), a disease characterized by retinal degeneration resulting in reduced peripheral vision and night blindness (6).

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

Application Methods: Western Blotting

Background: FUS/TLS (fused in sarcoma/translocated in liposarcoma) was initially identified by investigators as a component of fusion proteins found in a variety of cancers such as myxoid liposarcoma, acute myeloid leukemia, and Ewing’s tumor (1). FUS/TLS fusion with the DNA binding domain of transcription activators such as CHOP and ERG leads to aberrant transcription of target genes that is thought by researchers to lead to tumor development (1-5). FUS/TLS is involved in a wide range of RNA processing events such as pre-mRNA splicing, mRNA transcription, and miRNA processing (1,6). In addition to its role in RNA metabolism, FUS/TLS maintains genomic stability and co-regulates gene expression by interacting with various transcription factors such as nuclear receptors, YB-1, p65 subunit of NF-κB, TFIID, and RUNX2 (1,6,7). More recently, researchers have found several mutations of FUS/TLS in ALS (amyotrophic lateral sclerosis) and FTLD (frontotemporal lobar degeneration) patients that causes cytoplasmic mislocalization of FUS/TLS (6,8-11).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated mTOR (7C10) Rabbit mAb #2983.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: PZR (Protein zero related) is an immunoglobulin superfamily protein that specifically binds the tyrosine phosphatase SHP-2 through its intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIMs) (1,2). PZR is phosphorylated by c-Src, c-Fyn, c-Lyn, Csk, and c-Abl (3). PP1, a Src family kinase inhibitor, inhibits PZR phosphorylation (4,5). There are three alternatively spliced isoforms, designated as PZR, PZRa, and PZRb; both PZRa and PZRb lack ITIMs (6,7). PZR is the main receptor of ConA and has an important role in cell signaling via c-Src (4). PZR is expressed in many cell types and is localized to cell contacts and intracellular granules in BAECs and mesothelioma (REN) cells. PZR has been implicated as a cell adhesion protein that may be involved in SHP-2-dependent signaling at interendothelial cell contacts (3). Hypertyrosine phosphorylation of PZR was observed during embryogenesis in a mouse model of Noonan syndrome (8).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Myelin-oligodendrocyte glycoprotein (MOG) is a type I membrane bound glycoprotein of the immunoglobulin superfamily that is enriched in the in the outer lamella of the myelin sheath (1). The myelin sheath is a multi-layered membrane structure composed of oligodendrocytes that increases the conduction velocity of axonal impulses. The specific function of MOG is unknown, but MOG’s structure and expression during later stages of myelinogenesis suggests a role in myelin sheath maturation and maintenance (2). MOG may be an autoimmune target in central nervous system inflammatory diseases such as multiple sclerosis (MS) (3). Induction of MOG autoimmunity is also used as an experimental model for MS as injections of MOG peptide or recombinant protein in rodent models causes severe neurological disease that recapitulates several clinical features of MS (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The human urokinase-type plasminogen activator receptor (uPAR) is a 55-65 kDa, highly glycosylated, GPI-anchored cell surface receptor (the deglycosylated protein is 35 kDa) (1-3). It is a central player in the plasminogen activation pathway. uPAR binds with high affinity to a serine protease urokinase-type plasminogen activator (uPA) and converts plasminogen to its active form plasmin in a spatially restricted manner on the cell surface (4). Plasmin further carries out the activation of uPA, which is inhibited by serpins, such as plasminogen activator inhibitors (5). Therefore, uPAR plays a key role in regulating extracellular proteolysis. In addition, uPAR plays an important role in regulating cell proliferation, adhesion and mobility (6,7). Research studies have shown that overexpression of uPAR is found in various cancer cells and tissues (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Glutamatergic neurons release glutamate, the most common excitatory neurotransmitter. Their synaptic vesicles are filled with glutamate by vesicular glutamate transporters, VGLUTs (1). VGLUT1, also called solute carrier family 17 member 7 (SLC17A7), was first identified as an inorganic phosphate transporter (2). Despite the absence of homology with neurotransmitter transporters, VGLUT1 was later demonstrated to be a glutamate transporter (1) specific to glutamatergic neurons (3). Closely related to VGLUT1, VGLUT2 and VGLUT3 are also involved in glutamate uptake into synaptic vesicles, but define different neuronal subpopulations (4,5). VGLUT1 and VGLUT2 are the most abundant isoforms. VGLUT1 is expressed in the cortex, hippocampus, and cerebellar cortex, while VGLUT2 is mostly found in the thalamus (6,7). VGLUT3 is expressed in hair cells of the auditory system (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). It 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. These proteins are involved in the formation of cytoplasmic vacuoles called autophagosomes that are delivered to lysosomes for degradation.The class III type phosphoinositide 3-kinase (PI3KC3)/Vps34 regulates vacuolar trafficking as well as autophagy (4,5). Multiple proteins have been shown to be associated with Vsp34, including: p105/Vsp15, Beclin-1, UVRAG, Atg14, and Rubicon, which can determine Vsp34 function (6-11). UVRAG (UV radiation resistance-associated gene) is associated with the Beclin-1/PI3KC3 complex and promotes PI3KC3 enzymatic activity and autophagy, while suppressing proliferation (11). Beclin-1 binding to UVRAG promotes both autophagosome maturation and endocytic trafficking (12). UVRAG is also a potential tumor suppressor protein with frameshift mutations observed in colon and gastric carcinomas (13,14).

$305
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 VDAC (D73D12) Rabbit mAb #4661.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Voltage-dependent anion channel (VDAC), ubiquitously expressed and located in the outer mitochondrial membrane, is generally thought to be the primary means by which metabolites diffuse in and out of the mitochondria (1). In addition, this channel plays a role in apoptotic signaling. The change in mitochondrial permeability characteristic of apoptosis is mediated by Bcl-2 family proteins, which bind to VDAC, altering the channel kinetics (2). Homodimerization of VDAC may be a mechanism for changing mitochondrial permeability and supporting release of cytochrome c (3). In mammalian cells, there are three VDAC isoforms, VDAC1, which is the most widely expressed isoform, as well as VDAC2 and VDAC3 (4,5).

$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
Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments and microtubules. Major types of intermediate filaments are distinguished and expressed in particular cell types: cytokeratins (epithelial cells), glial fibrillary acidic protein or GFAP (glial cells), desmin (skeletal, visceral and certain vascular smooth muscle cells), vimentin (mesenchyme origin) and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Vimentin is present in sarcomas, but not carcinomas, and its expression is examined relative to other markers to distinguish between the two forms of neoplasm (3). Desmin is a myogenic marker expressed in early development that forms a network of filaments that extends across the myofibril and surrounds Z discs. The desmin cytoskeleton provides a connection among myofibrils, organelles and the cytoskeleton (4). Desmin knockout mice develop cardiomyopathy, skeletal and smooth muscle defects (5). In humans, desmin related myopathies might be caused by mutations in the corresponding desmin gene or in proteins with which desmin interacts, including αB-crystallin and synemin. Disorganized desmin filaments and the accumulation of protein aggregates comprised predominantly of desmin characterize desmin-related myopathies (reviewed in 6,7).

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated LEF1 (C12A5) Rabbit mAb #2230.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: LEF1 and TCF are members of the high mobility group (HMG) DNA binding protein family of transcription factors that consists of the following: Lymphoid Enhancer Factor 1 (LEF1), T Cell Factor 1 (TCF1/TCF7), TCF3/TCF7L1, and TCF4/TCF7L2 (1). LEF1 and TCF1/TCF7 were originally identified as important factors regulating early lymphoid development (2) and act downstream in Wnt signaling. LEF1 and TCF bind to Wnt response elements to provide docking sites for β-catenin, which translocates to the nucleus to promote the transcription of target genes upon activation of Wnt signaling (3). LEF1 and TCF are dynamically expressed during development and aberrant activation of the Wnt signaling pathway is involved in many types of cancers including colon cancer (4,5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Human progesterone receptor (PR) is expressed as two forms: the full length PR-B and the short form PR-A. PR-A lacks the first 164 amino acid residues of PR-B (1,2). Both PR-A and PR-B are ligand activated, but differ in their relative ability to activate target gene transcription (3,4). The activity of PR is regulated by phosphorylation; at least seven serine residues are phosphorylated in its amino-terminal domain. Three sites (Ser81, Ser102, and Ser162) are unique to full length PR-B, while other sites (Ser190, Ser294, Ser345, and Ser400) are shared by both isoforms (5). Phosphorylation of PR-B at Ser190 (equivalent to Ser26 of PR-A) is catalyzed by CDK2 (6). Mutation of Ser190 results in decreased activity of PR (7), suggesting that the phosphorylation at Ser190 may be critical to its biological function.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Myelin basic protein (MBP) is an abundant central nervous system (CNS) myelin membrane protein that plays an important role in nerve myelination. Myelin sheaths are multi-layered membranes derived from oligodendrocytes that increase the conduction velocity of axonal impulses. MBP helps to adhere the cytoplasmic leaflets of adjacent oligodendrocyte membranes to one another. Several splice variants of MBP are expressed in cells and the protein is modified following translation (i.e. phosphorylation, methylation), which suggests additional membrane adhesion functions (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: DOCK180 and its partner, ELMO1, interact directly with one another to form an atypical two-part guanine nucleotide exchange factor (GEF) for the small GTPase Rac (1). Rac activation occurs in association with p130 Cas and Crk, which form a complex with DOCK180 that is targeted to focal adhesions (2,3). DOCK180 is also recruited to the plasma membrane by binding to phosphoinositides (4). ELMO1 may function as an inhibitor of proteasome-dependent degradation of DOCK180 at the plasma membrane to regulate reorganization of the actin cytoskeleton (5). Localized Rac activation allows actin nucleation via WAVE family proteins, signaling to integrins, formation of lamellipodia and filopodia, and regulation of processes such as phagocytosis and cell migration (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Na(+)/glucose cotransporter 2 (SGLT2) is one of the two main glucose transporters in the kidney proximal convoluted tubule. It is activated by Protein Kinase A and Protein Kinase C, likely through phosphorylation of Ser624 (1,2). SGLT2 is responsible for the majority of glucose reabsorption in the kidney (3,4), and mutations in SGLT2 are known to cause familial renal glucosuria (5,6). SGLT2 is a therapeutic target for type 2 diabetes. Inhibitors of SGLT2 have been developed in order to treat people with type 2 diabetes (7).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: HS1 (HCLS1, LckBP1, p75) is a protein kinase substrate that is expressed only in tissues and cells of hematopoietic origin (1,2). HS1 contains four cortactin repeats and a single SH3 domain (2). This intracellular protein is phosphorylated following immune receptor activation, which promotes recruitment of HS1 to the immune synapse (3-5). Phosphorylation of HS1 is required to regulate actin dynamics and provide docking sites for many other signaling molecules, such as Vav1 and PLCγ1 (6). HS1 also plays an important role in platelet activation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as Class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae Sir2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT5, a mammalian homolog of Sir2, is localized to the mitochondria and has been implicated in the regulation of cell metabolism (2,3). SirT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1) in the mitochondrial matrix and increases its activity in response to fasting, allowing for adaptation to increased amino acid catabolism (4). SirT5 has also been shown to deacetylate cytochrome c in the mitochondrial intermembrane space (5). In addition to its deacetylase activity, SirT5 contains lysine desuccinylase and demalonylase activity (6,7). Succinyl-lysine and malonyl-lysine modifications occur in a variety of organisms and these post-translational modifications are found on many metabolic enzymes (6-8). Like phosphorylation of serine, threonine, and tyrosine residues, lysine succinylation and malonylation induces a change of two negative charges from a +1 to a -1 charge at physiological pH, and are thought to serve similar functions in the regulation of protein activity, protein-protein interactions, and protein stability. SirT5 knockout mice show increased levels of succinyl-lysine and malonyl-lysine protein modifications in the liver, including increased succinylation of CPS1, a known target of SirT5, suggesting that SirT5 functions to regulate metabolic enzymes through its deacetylase, desuccinylase, and demalonylase activities (6,7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein K (hnRNP K) belongs to a family of RNA binding multiprotein complexes (hnRNP proteins) that facilitate pre-mRNA processing and transport of mRNA from the nucleus to cytoplasm (1-3). hnRNP K contains three unique structural motifs termed KH domains that bind poly(C) DNA and RNA sequences (4,5). Intricate architecture enables hnRNP K to facilitate mRNA biosynthesis (6), transcriptional regulation (7), and signal transduction. Research studies have shown that cytoplasmic hnRNP K expression is increased in oral squamous cell carcinoma and pancreatic cancer, and may be a potential prognostic factor (8,9). hnRNP K coordinates with p53 to regulate its target gene transcription in response to DNA damage. Proteasome degradation of hnRNP K is mediated by E3 ligase MDM2 (10). The interaction between hnRNP K and c-Src leads to hnRNP K phosphorylation, which allows for hnRNP K activation of silenced mRNA translation (11).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: 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).