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Product listing: RanBP1 Antibody, UniProt ID P43487 #8780 to α-Smooth Muscle Actin Antibody, UniProt ID P62736 #14968

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: RanBP1 is a Ran binding protein that functions in nuclear trafficking for both nuclear import and export (1-3). Its protein sequence contains a Ran binding domain and a C-terminal nuclear export signal, which maintains its cytoplasmic localization (2,3). During nuclear export, RanBP1 forms a complex with RanGTP and CRM1/cargo, leading to dissociation of cargo from CRM1 (2,4). RanBP1 further stimulates RanGTP-RanGAP1 association to facilitate RanGTP hydrolysis and the generation of RanGDP to complete the final steps of nuclear export (5). During nuclear import, RanBP1 stabilizes the formation of a RanGDP-importin/NLS receptor-RanBP1 complex. This complex regulates the release of imported cargo into the nucleus (6,7). In addition to nuclear trafficking, RanBP1 also controls RanGTP distribution along mitotic microtubules, which localizes critical factors, such as cyclin B1 and HURP, to mitotic microtubles and regulates chromosome segregation (8,9). In vivo knock down or overexpression of RanBP1 has been shown to affect cellular ciliogenesis by regulating the local RanGTP concentation at the base of cilia (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: RanBP3 was originally identified as RanGTP binding protein located in the nucleus and involved in the nuclear exporting process (1). It functions as a cofactor for CRM1 nuclear export by binding to CRM1, stabilizing the RanGTP-CRM1-cargo interaction and promoting complex association with nuclear pore proteins (2,3). In the absence of Ran-bound GTP, RanBP3 prevents binding of CRM1 complex to the nuclear pore complex. In addition to CRM1, RanBP3 also has been shown to bind to RanGEF-RCC1 and increase the guanine nucleotide exchange activity of RCC1 for RanGTP-CRM1-Cargo (1,4). In some cases, as with β-catenin and Smad2/3, RanBP3 binding may mediate the target protein nuclear export in a Ran-dependent, but CRM1-independent manner (5,6). RanBP3 is phosphorylated at Ser58 through the PI3K/Akt or ERK/RSK pathway. This phosphorylation is important for RanBP3 function in nuclear export, likely due to stimulation of RCC1 activity (7,8).

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

Application Methods: Flow Cytometry, 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, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The Ras family small GTPase Ran is involved in nuclear envelope formation, assembly of the mitotic spindle, and nuclear transport (1,2). Like other small GTPases, Ran is active in its GTP-bound form and inactive in its GDP-bound form. Nuclear RanGTP concentration is maintained through nuclear localization of guanine nucleotide exchange factor (GEF) activity, which catalyzes the exchange of bound GDP for GTP. Regulator of chromatin condensation 1 (RCC1) is the only known RanGEF (3). RCC1 is dynamically chromatin-bound throughout the cell cycle, and this localization is required for mitosis to proceed normally (4,5). Appropriate association of RCC1 with chromatin is regulated through amino-terminal phosphorylation (5,6) and methylation (7). RCC1 regulation of RanGTP levels in response to histone modifications regulates nuclear import during apoptosis (8). In mitosis RCC1 is phosphorylated at Ser11, possibly by cyclin B/cdc2 (9-11). This phosphorylation may play a role in RCC1 interaction with chromatin and RCC1 RanGEF activity (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: RCC2/TD-60 is a member of the RCC1 (regulator of chromosome condensation 1) family of guanine nucleotide exchange factors. RCC2/TD-60 is associated with the chromosome passenger complex (CPC), which also consists of aurora B kinase, borealin, INCENP (inner centromere protein) and survivin. The CPC acts at various stages of mitosis, interacts with microtubules and is required for proper chromosome segregation and cytokinesis. Regulation of aurora B kinase is key in the regulation of the CPC (reviewed in 1,2). In late mitosis, RCC2/TD-60 is required for spindle assembly and recruitment of survivin and aurora B (3). RCC2/TD-60 is also required for aurora B activation in vitro and localization of the CPC to centromeres (4).

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

Application Methods: Western Blotting

Background: Rho family small GTPases, including Rho, Rac and cdc42, act as molecular switches, regulating processes such as cell migration, adhesion, proliferation and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of bound GDP for GTP, and inhibited by GTPase activating proteins (GAPs), which catalyze the hydrolysis of GTP to GDP. A third level of regulation is provided by the stoichiometric binding of Rho GDP dissociation inhibitor (RhoGDI) (1). RhoA, RhoB and RhoC are highly homologous, but appear to have divergent biological functions. Carboxy-terminal modifications and differences in subcellular localization allow these three proteins to respond to and act on distinct signaling molecules (2,3).

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

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

Background: Rho family small GTPases, including Rho, Rac and cdc42, act as molecular switches, regulating processes such as cell migration, adhesion, proliferation and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of bound GDP for GTP, and inhibited by GTPase activating proteins (GAPs), which catalyze the hydrolysis of GTP to GDP. A third level of regulation is provided by the stoichiometric binding of Rho GDP dissociation inhibitor (RhoGDI). RhoGDI affects Rho activity by inhibiting nucleotide exchange and membrane association, regulating activity and localization (Reviewed in 1, 2). The inhibitory and shuttling functions of RhoGDI have been uncoupled using mutant forms of RhoGDI (3). Phosphorylation of GDIs and/or GTPases can modulate their affinity for each other and, therefore, GTPase mediated signaling. PAK1 phosphorylation of RhoGDI at serines 101 and 174 causes release and activation of Rac1, but not RhoA (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: ROCK (Rho-associated kinase), a family of serine/threonine kinases, is an important downstream target of Rho-GTPase and plays an important role in Rho-mediated signaling. Two isoforms of ROCK have been identified: ROCK1 and ROCK2. ROCK is composed of N-terminal catalytic, coiled-coil, and C-terminal PH (pleckstrin homology) domains. The C-terminus of ROCK negatively regulates its kinase activity (1,2). Caspase-3-induced cleavage of ROCK1 and direct cleavage of ROCK2 by granzyme B (grB) activates ROCK and leads to phosphorylation of myosin light chain and inhibition of myosin phosphatase (3). This phosphorylation may account for the mechanism by which Rho regulates cytokinesis, cell motility, cell membrane blebbing during apoptosis, and smooth muscle contraction (4-6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: There are two isoforms of Sec23 protein: Sec23A and Sec23B. Both isoforms have been shown in the Sec23/24 complex, which is a component of COPII coat (1). COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex, and Sar1. COPII coat is located at the ER/Golgi interface and involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (2). COPII formation is initiated through binding of the activated G protein, Sar1, to the Sec23/24 complex to form a prebudding complex, which directly binds target molecules (2-4). The prebudding complex further recruits Sec13/31 to form mature COPII coat (5,6). In addition to being a COPII component, Sec23 has also been shown to interact with p125 and Sec16 at the transitional ER; these interactions are important for regulation of the COPII transportation function (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Coat Protein Complex II (COPII) is composed of five cytosolic proteins: Sec23/24 complex, Sec13/31 complex, and Sar1. COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex, thereby forming a prebudding complex that directly binds target molecules (1-3). The prebudding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec24 subunit of COPII coat is thought to play a critical role in cargo selection (2,6). It binds directly to cargo proteins at the ER and brings them to COPII vesicles through interaction with Sec23. There are four Sec24 isoforms in human cells: Sec24A, Sec24B, Sec24C, and Sec24D (7). In mice, mutations in Sec24B have been linked to developmental defects (8,9).

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

Application Methods: Western Blotting

Background: Coat Protein Complex II (COPII) is composed of five cytosolic proteins: Sec23/24 complex, Sec13/31 complex, and Sar1. COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex, thereby forming a prebudding complex that directly binds target molecules (1-3). The prebudding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec24 subunit of COPII coat is thought to play a critical role in cargo selection (2,6). It binds directly to cargo proteins at the ER and brings them to COPII vesicles through interaction with Sec23. There are four Sec24 isoforms in human cells: Sec24A, Sec24B, Sec24C, and Sec24D (7). In mice, mutations in Sec24B have been linked to developmental defects (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: SLK (Ste20-like Kinase) is a member of the germinal center kinase (GCK) family of proteins. SLK has a kinase domain located at the N terminus (1). The autophosphorylation of SLK at Thr183 and Ser189 is required for the upregulation of SLK kinase activity (1, 2). The protein also has a caspase cleavage site DXXD and a SH3 binding site PXXP located in the middle part of its sequence, and a regulatory C terminal coiled-coil domain for homodimerization and adaptor binding (1-4). SLK plays important roles in development, tissue regeneration and cancer cell migration by regulating several signaling pathways (5-7). SLK phosphorylates and activates ASK1 to induce downstream p38 phosphorylation and apoptosis (8,9). During cell cycle, SLK phosphorylates Polo-like kinase (PLK) at Thr210 to promote G2/M transition (10,11). SLK also promotes cell division by direct phosphorylation of ERMs and dynactin to activate microtubule reorganization and spindle orientation (12, 13). During focal adhesion and cell migration process, SLK is activated and colocalized to the focal adhesion complex where it promotes complex turnover by phosphorylating paxillin at Ser250 (14, 15).

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

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: SPAK (STE20/SPS1-related Pro/Ala-rich kinase) and OSR1 (oxidative stress responsive 1) are members of the GCK family serine/threonine kinases. Overexpression and in vitro studies demonstrate that SPAK is able to activate p38 MAP kinase indicating a possible role for SPAK in the stress response (1). Yeast two-hybrid screening revealed that SPAK and OSR1 bind to Na-K-2Cl cotransporters NKCC1 and NKCC2 and K-Cl cotransporter KCC3 (2). WNK1 and WNK4 phosphorylate SPAK at Thr243/247 and Ser380 (3-5). Similarly, WNK1 and WNK4 phosphorylate OSR1 at Thr185 and Ser315 (3,4). Phosphorylation at these sites stimulates SPAK and OSR1 activity, leading to NKCC1 phosphorylation and enhanced NKCC1 activity (3-5). SPAK is also phosphorylated at Ser311 by PKCθ in response to T cell activation. Substitution of Ser311 with Ala or specific siRNA knock-down of SPAK dramatically reduces TCR/CD28-induced AP-1 activation, suggesting SPAK is involved in T cell signaling as well (6).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Stathmin is a ubiquitously expressed microtubule destabilizing phosphoprotein that is upregulated in a number of cancers. The amino terminus of the protein contains multiple phosphorylation sites and is involved in the promotion of tubulin filament depolymerization. Phosphorylation at these sites inactivates the protein and stabilizes microtubules. Ser16 phosphorylation by CaM kinases II and IV (1,2) increases during G2/M-phase and is involved in mitotic spindle regulation (3,4). Ser38 is a target for cdc2 kinase (5) and TNF-induced cell death gives rise to reactive oxygen intermediates leading to hyperphosphorylation of stathmin (6). EGF receptor activation of Rac and cdc42 also increases phosphorylation of stathmin on Ser16 and Ser38 (7). Other closely related family members are neuronally expressed and include SCG10, SCLIP, RB3 and its splice variants RB3' and RB3''. Stathmin and SCG10 have been shown to play roles in neuronal-like development in PC-12 cells (8).

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

Application Methods: Western Blotting

Background: Translationally controlled tumor protein (TCTP/p23/HRF) is a ubiquitously expressed and highly conserved protein involved in various cellular processes, such as its role as a histamine releasing factor in chronic allergic disease (1). TCTP binds tubulin in a cell cycle dependent manner and is associated with the mitotic spindle (2). In addition, TCTP interacts with the actin cytoskeleton to regulate cell shape (3). In mitosis, TCTP is phosphorylated by PLK at Ser46, decreasing microtubule stability (4,5). TCTP interacts with the small GTPase Rheb, possibly acting as a GEF, thereby activating the TORC1 pathway and controlling cell growth and proliferation (6,7). TCTP has also been shown to be involved in apoptosis and cell stress (8-11). In cultured cells, reduction in TCTP expression can cause loss of the malignant phenotype (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Tensin 2 belongs to the Tensin family of cytoskeletal proteins that includes Tensin 1-3 and Cten, which couple integrins to the actin cytoskeleton (1). Tensin proteins contain SH2 and phosphotyrosine binding (PTB) domains, which enable interaction with diverse signaling molecules and proteins. Tensin family proteins play important roles in signal transduction, cell proliferation, and motility (2-5).Tensin 2 is localized to focal adhesions of various tissues with highest expression in the heart, kidney, and liver (6,7). Tensin 2 inhibits Akt/PKB signaling via a phosphatase tensin-type domain (8). However, Tensin 2 also mediates thrombopoietin/c-Mpl signaling, which promotes Akt signaling (9). Interaction with Tensin 2 is essential for the tumor suppressor function of Deleted in Cancer 1 (DLC1) (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: TIAM1 (T-lymphoma invasion and metastasis-inducing protein 1) is a multidomain guanine nucleotide exchange factor (GEF) protein that activates Rac1, a GTPase involved in cytoskeletal dynamics that regulate cell migration, growth and survival. TIAM1 also has been identified as an inhibitor of the YAP/TAZ signaling pathway, with two distinct subcellular mechanisms of action: (1) promoting cytoplasmic (proteosomal) degradation of YAP and TAZ; and (2) blocking the transcriptional co-activator functions of YAP and TAZ in the nucleus (3,4). The effects of TIAM1 on tumor development are also complex and context-dependent. For example, it has been reported that TIAM1 can promote tumor growth and progression in some contexts, while antagonizing tumor metastasis and invasion in other contexts (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Tropomodulin-1 (TMOD1) belongs to a conserved family of cytoskeletal proteins (TMOD1-4) that play an important role in modulating actin cytoskeleton dynamics. TMOD proteins function as actin capping proteins, which stabilize actin filaments by inhibiting both elongation and depolymerization (1). While many proteins have been identified that cap the rapidly growing barbed end of actin filaments, TMODs are the only proteins thus far identified that cap the slowly growing pointed end (2). A research study in triple-negative breast cancer cells identified TMOD1 as a target of NF-κB signaling, and showed that increased TMOD1 expression was associated with enhanced tumor growth in a mouse xenograft model (3). Molecular expression of TMOD1 was also identified as part of a unique gene expression signature that could discriminate ALK-negative anaplastic large-cell lymphoma from other malignancy subtypes (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Troponin, working in conjunction with tropomyosin, functions as a molecular switch that regulates muscle contraction in response to changes in the intracellular Ca2+ concentration. Troponin consists of three subunits: the Ca2+-binding subunit troponin C (TnC), the tropomyosin-binding subunit troponin T (TnT), and the inhibitory subunit troponin I (TnI) (1). In response to β-adrenergic stimulation of the heart, Ser23 and Ser24 of TnI (cardiac) are phosphorylated by PKA and PKC. This phosphorylation stimulates a conformational change of the regulatory domain of TnC, reduces the association between TnI and TnC, and decreases myofilament Ca2+ sensitivity by reducing the Ca2+ binding affinity of TnC (1-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Western Blotting

Background: Troponin, working in conjunction with tropomyosin, functions as a molecular switch that regulates muscle contraction in response to changes in the intracellular Ca2+ concentration. Troponin consists of three subunits: the Ca2+-binding subunit troponin C (TnC), the tropomyosin-binding subunit troponin T (TnT), and the inhibitory subunit troponin I (TnI) (1). In response to β-adrenergic stimulation of the heart, Ser23 and Ser24 of TnI (cardiac) are phosphorylated by PKA and PKC. This phosphorylation stimulates a conformational change of the regulatory domain of TnC, reduces the association between TnI and TnC, and decreases myofilament Ca2+ sensitivity by reducing the Ca2+ binding affinity of TnC (1-3).

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

Application Methods: Western Blotting

Background: Twinfilin is an actin monomer-binding protein found in all eukaryotes (1). Mammals have three isoforms. Twinfilin-1 and twinfilin-2a are expressed in most non-muscle cell types, whereas twinfilin-2b is the main isoform in adult heart and skeletal muscle (2). Twinfilins are composed of two ADF-homology domains connected by a 30 kDa linker region. All twinfilins have been shown to form a 1:1 complex with G-actin, but not F-actin (reviewed in 3). Twinfilin-1 was originally known as A6 protein tyrosine kinase and thought to be part of a novel class of protein kinases. However, the protein was renamed after further studies showed no evidence of tyrosine kinase activity (4). Twinfilin-1 helps to prevent the actin filament assembly by forming a complex with actin monomers and, in mammals, has been shown to cap the filament barbed ends. It has been suggested that this regulates cell motility (5). Suppression of twinfilin-1 has also been shown to slow lymphoma cell migration to lymph nodes (6).

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

Application Methods: Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Western Blotting

Background: Vav proteins belong to the Dbl family of guanine nucleotide exchange factors (GEFs) for Rho/Rac small GTPases. The three identified mammalian Vav proteins (Vav1, Vav2 and Vav3) differ in their expression. Vav1 is expressed only in hematopoietic cells and is involved in the formation of the immune synapse. Vav2 and Vav3 are more ubiquitously expressed. Vav proteins contain the Dbl homology domain, which confers GEF activity, as well as protein interaction domains that allow them to function in pathways regulating actin cytoskeleton organization (reviewed in 1). Phosphorylation stimulates the GEF activity of Vav protein towards Rho/Rac (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Vav proteins belong to the Dbl family of guanine nucleotide exchange factors (GEFs) for Rho/Rac small GTPases. The three identified mammalian Vav proteins (Vav1, Vav2 and Vav3) differ in their expression. Vav1 is expressed only in hematopoietic cells and is involved in the formation of the immune synapse. Vav2 and Vav3 are more ubiquitously expressed. Vav proteins contain the Dbl homology domain, which confers GEF activity, as well as protein interaction domains that allow them to function in pathways regulating actin cytoskeleton organization (reviewed in 1). Phosphorylation stimulates the GEF activity of Vav protein towards Rho/Rac (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Villin is a member of the gelsolin family of calcium-regulated actin-binding proteins. Unlike the ubiquitously expressed gelsolin, villin expression is restricted to simple epithelia of the gastrointestinal and urogenital tracts. It is localized to the apical cytoplasm and brush borders of these cells. Villin functions in the regulation of actin dynamics in the apical epithelium, capping, nucleating and/or severing actin filaments in a calcium-dependent manner and regulating cell shape in response to external stimuli (1,2). Phosphorylation of villin at Tyr60, 81 and 256 may be involved in the regulation of cell migration (3). Expression of villin is increased in colorectal cancers (4), and villin1 function appears to be involved in progressive cholestasis and hepatic failure (5).

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

Application Methods: 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 by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (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). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

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

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

Application Methods: Immunoprecipitation, Western Blotting

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

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Actin proteins are major components of the eukaryotic cytoskeleton. At least six vertebrate actin isoforms have been identified. The cytoplasmic β- and γ-actin proteins are referred to as “non-muscle” actin proteins as they are predominantly expressed in non-muscle cells where they control cell structure and motility (1). The α-cardiac and α-skeletal actin proteins are expressed in striated cardiac and skeletal muscles, respectively. The smooth muscle α-actin and γ-actin proteins are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. The α-smooth muscle actin (ACTA2) is also known as aortic smooth muscle actin. These actin isoforms regulate the contractile potential of muscle cells (1).