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Product listing: ERp44 Antibody, UniProt ID Q9BS26 #2886 to FKBP4 Antibody, UniProt ID Q02790 #11826

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

Application Methods: Western Blotting

Background: Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Disulfide isomerase (PDI) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum resident protein 44 (ERp44), constitute the PDI family (2). ERp44 is induced upon ER stress and is linked to Ero1-Lα and Ero1-Lβ through mixed disulfide bonds (3). ERp44 was shown to mediate the ER localization of Ero1-Lα (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Disulfide isomerase (PDI) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum stress protein 57 (ERp57), constitute the PDI family (2). ERp57 interacts with calnexin and calreticulin (3) and is suggested to play a role in the isomerization of disulfide bonds on certain glycoproteins (3).

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

Application Methods: Western Blotting

Background: Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Disulfide isomerase (PDI) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum stress protein 57 (ERp57), constitute the PDI family (2). ERp57 interacts with calnexin and calreticulin (3) and is suggested to play a role in the isomerization of disulfide bonds on certain glycoproteins (3).

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

Application Methods: Western Blotting

Background: Secretory proteins translocate into the endoplasmic reticulum (ER) during synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Protein disulfide isomerase (PDI) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess thioredoxin homology domains, including ER stress protein 72 (ERp72), constitute the PDI family (3,4). ERp72 contains three thioredoxin homology domains (3) and plays a role in the formation and isomerization of disulfide bonds (3,4).

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

Application Methods: Western Blotting

Background: ETO belongs to a family of evolutionarily conserved nuclear factors. Although it has no DNA binding domains it is reported to act as a transcriptional corepressor (1). It is best characterized as the fusion partner of AML1 in acute myeloid leukemia with the t(8;21) translocation which gives rise to the AML-ETO fusion protein (2). AML1 is a transcription factor that is involved in the differentiation of all hematopoietic lineages. The fusion protein lacks the activation domain of AML1 and behaves as a dominant negative AML1, repressing AML1 target genes. AML-ETO also causes activation of other genes through a mechanism that involves Bcl-2 and enhanced expression of p21 waf1/cip1 (3,4). The AML-ETO fusion protein is thought to cause the expansion of a hematopoietic stem cell population that has limited lineage commitment and genomic instability (5). Recent evidence derived from chromatin immunoprecipitation (ChIP) experiments has demonstrated that ETO may play a role in the regulation of Notch target genes, and AML-ETO has been shown to disrupt repression of Notch target genes (6). Therefore, both AML and Notch target genes are deregulated by AML-ETO. Epigenetic silencing of the microRNA-223 gene has also been attributed to activities of AML-ETO, contributing to the differentiation block in t(8;21) leukemia (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Evi-1 (Ecotropic virus integration site 1) was originally identified as a common site of viral integration in murine myeloid leukemia. It is involved in human myeloid disorders through chromosome translocation and inversion (1) and is also implicated in solid tumor formation (2). Evi-1 is a zinc finger transcription factor which also plays an important role in animal development (3). It has many isoforms due to alternative usage of 5'-ends (4), alternative splicing (5), and intergenic splicing which results in the formation of a fusion protein with MDS1 in normal tissues (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Ena/VASP-like (EVL) protein is a member of the Ena/VASP family and is involved in actin-associated cytoskeleton remodeling and cell polarity activities including axon guidance and lamellipodia formation in migrating cells (1,2,3). The EVL protein sequence contains an N-terminal EVH1 domain, a Pro-rich SH3 binding domain, and a C-terminal EVH2 domain. EVL domain interactions with G- and F-actin mediates actin nucleation and polymerization (4). Research studies have shown that EVL also regulates DNA repair by direct interaction with RAD51 (5). EVL may function in the DSB repair pathway through the EVH2 domain, which possesses DNA-binding and RAD51 binding activity, thereby coordinating homologous DNA recombination (6,7). Research studies have shown EVL expression is up-regulated in human breast cancer associated with clinical stages and may be implicated in invasion and/or metastasis of human breast cancer (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The Ewing sarcoma (EWS) protein is a member of the multifunctional FET (FUS, EWS, and TAF15) family of proteins (1,2). These proteins are RNA and DNA binding proteins that are thought to be important for both transcriptional regulation and RNA processing. EWS can be found as part of a fusion protein with various E-twenty six (ETS) family transcription factors, most commonly Fli-1, in the Ewing sarcoma family of tumors (1-4). The amino terminus of the EWS protein, containing the transcriptional activation domain, is fused to the DNA binding domain of the ETS transcription factor, causing aberrant expression of target genes (1-5). EWS interacts with the transcription initiation complex via TFIID and RNA polymerase II subunits, as well as transcriptional regulators, such as Brn3A and CBP/p300, which suggests a role for EWS in transcriptional regulation (1,6-9). EWS also interacts with multiple components of the splicing machinery, implicating a role for EWS in RNA processing (1,10-12). EWS regulates the expression of cyclin D1, which controls G1-S phase transition during the cell cycle, at the level of transcriptional activation and mRNA splicing. The EWS-Fli-1 fusion protein has been shown to promote the expression of the cyclin D1b splice variant in Ewing sarcoma cells (13). In addition, EWS regulates the DNA damage-induced alternative splicing of genes involved in DNA repair and stress response and is required for cell viability upon DNA damage (14). Consistent with these results, EWS knockout mice display hypersensitivity to ionizing radiation and premature cellular senescence, suggesting a role for EWS in homologous recombination and maintenance of genomic stability (15).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The polycomb group (PcG) proteins are involved in maintaining the silenced state of several developmentally regulated genes and contribute to the maintenance of cell identity, cell cycle regulation, and oncogenesis (1,2). Enhancer of zeste homolog 2 (Ezh2), a member of this large protein family, contains four conserved regions including domain I, domain II, and a cysteine-rich amino acid stretch that precedes the carboxy-terminal SET domain (3). The SET domain has been linked with histone methyltransferase (HMTase) activity. Moreover, mammalian Ezh2 is a member of a histone deacetylase complex that functions in gene silencing, acting at the level of chromatin structure (4). Ezh2 complexes methylate histone H3 at Lys9 and 27 in vitro, which is thought to be involved in targeting transcriptional regulators to specific loci (5). Ezh2 is deregulated in various tumor types, and its role, both as a primary effector and as a mediator of tumorigenesis, has become a subject of increased interest (6).

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

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

Background: The ezrin, radixin, and moesin (ERM) proteins function as linkers between the plasma membrane and the actin cytoskeleton and are involved in cell adhesion, membrane ruffling, and microvilli formation (1). ERM proteins undergo intra or intermolecular interaction between their amino- and carboxy-terminal domains, existing as inactive cytosolic monomers or dimers (2). Phosphorylation at a carboxy-terminal threonine residue (Thr567 of ezrin, Thr564 of radixin, Thr558 of moesin) disrupts the amino- and carboxy-terminal association and may play a key role in regulating ERM protein conformation and function (3,4). Phosphorylation at Thr567 of ezrin is required for cytoskeletal rearrangements and oncogene-induced transformation (5). Ezrin is also phosphorylated at tyrosine residues upon growth factor stimulation. Phosphorylation of Tyr353 of ezrin transmits a survival signal during epithelial differentiation (6).

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

Application Methods: Western Blotting

Background: The ezrin, radixin, and moesin (ERM) proteins function as linkers between the plasma membrane and the actin cytoskeleton and are involved in cell adhesion, membrane ruffling, and microvilli formation (1). ERM proteins undergo intra or intermolecular interaction between their amino- and carboxy-terminal domains, existing as inactive cytosolic monomers or dimers (2). Phosphorylation at a carboxy-terminal threonine residue (Thr567 of ezrin, Thr564 of radixin, Thr558 of moesin) disrupts the amino- and carboxy-terminal association and may play a key role in regulating ERM protein conformation and function (3,4). Phosphorylation at Thr567 of ezrin is required for cytoskeletal rearrangements and oncogene-induced transformation (5). Ezrin is also phosphorylated at tyrosine residues upon growth factor stimulation. Phosphorylation of Tyr353 of ezrin transmits a survival signal during epithelial differentiation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunoprecipitation, Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). The predominant fatty acid binding protein found in adipocytes is FABP4, also called adipocyte fatty acid binding protein or aP2. FABP4 is also expressed in macrophages (3). FABP4 knockout mice fed a high-fat and high-calorie diet become obese but develop neither insulin resistance nor diabetes, suggesting that this protein might be a link between obesity and insulin resistance and diabetes (4). Mice deficient in both FABP4 and ApoE show protection against atherosclerosis when compared with mice deficient only in ApoE (3). Mice carrying a FABP4 genetic variant exhibit both reduced FABP4 expression and a reduced potential for developing type 2 diabetes and coronary heart disease. A related study in humans indicated a similar pattern, suggesting that FABP4 may be a potential therapeutic target in the treatment of these disorders (1).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Fas-associated death domain (FADD or Mort 1) functions as an important adaptor in coupling death signaling from membrane receptors, such as the Fas ligand and TNF family (DR3, DR4 and DR5), to caspase-8 (1,2). FADD has a carboxy-terminal death domain, which interacts with the cytoplasmic tail of the membrane receptor, and an amino-terminal death effector domain, which interacts with caspase-8. Clustering of the receptors upon stimulation brings about FADD and caspase-8 oligomerization, activating the caspase signaling pathway. Human FADD is phosphorylated mainly at Ser194, while mouse FADD is phosphorylated at Ser191. In both cases, the phosphorylation is cell cycle-dependent (3) and may be related to its regulatory role in embryonic development and cell cycle progression (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: FAF1 was originally identified though yeast two-hybrid screening, interacting with the cytoplasmic domain of Fas, a member of the TNF receptor superfamily that plays a critical role in in apoptosis during development and immune function (1). FAF1 is widely expressed with highest expression observed in testis, skeletal muscle and heart (2). FAF1 potentiates Fas-mediated apoptosis and may induce apoptosis without Fas stimulation in some cell types. It does not contain typical death motifs, but rather has two amino-terminal domains with structural homology to ubiquitin. While the precise role of FAF1 during apoptosis is still unclear, it has been observed to be one of the components of the death-inducing signaling complex (DISC) during Fas-mediated apoptosis and can bind to caspase-8 and FADD (3). FAF1 has also been shown to suppress the activation of the NF-kappaB transcription factor (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: FAIM (Fas apoptosis inhibitory molecule) was identified as a protein that was inducibly expressed in B lymphocytes resistant to Fas-mediated apoptosis (1). Expression of FAIM inhibits receptor-mediated apoptosis in B cells as well as other cell types (1-3). FAIM is expressed in germinal center B cells, is positively regulated by IRF-4, and is also capable of inducing IRF-4 expression in a feed-forward mechanism (4). FAIM also regulates T cell receptor-mediated apoptosis by modulating Akt activation and Nur77 expression (2). Knockout mice for FAIM show an increased sensitivity to Fas-mediated apoptosis within B and T cells as well as hepatocytes (5). An alternatively spliced form of FAIM, termed FAIM-L, is found predominantly in the brain (6). In the nervous system, the originally identified FAIM does not appear to play a role in apoptosis, but rather can promote neurite outgrowth through the activation of Erk and NF-κB pathways (7). In contrast, FAIM-L does inhibit neuronal cell death triggered by death receptors (3).

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

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

Background: Focal adhesion kinase (FAK) is a widely expressed cytoplasmic protein tyrosine kinase involved in integrin-mediated signal transduction. It plays an important role in the control of several biological processes, including cell spreading, migration, and survival (1). Activation of FAK by integrin clustering leads to autophosphorylation at Tyr397, which is a binding site for the Src family kinases PI3K and PLCγ (2-5). Recruitment of Src family kinases results in the phosphorylation of Tyr407, Tyr576, and Tyr577 in the catalytic domain, and Tyr871 and Tyr925 in the carboxy-terminal region of FAK (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: FAM129B/Niban-like protein 1 (family with sequence similarity 129, member B) belongs to a poorly characterized family of Niban proteins that also includes FAM129A/Niban and FAM129C/Niban-like protein 2. FAM129A/Niban is implicated in the ER stress response and is upregulated at the protein level in thyroid carcinoma (1,2). FAM129C/Niban-like protein 2 is preferentially expressed in B-cells and is one of five biomarkers upregulated in whole blood from patients with colorectal carcinoma (3,4). FAM129B is broadly expressed and has been shown to be a downstream target of B-Raf in melanoma cells (5). Though FAM129B does not appear to regulate cell growth and division, phosphorylation of FAM129B by B-Raf is essential for the invasive potential of melanoma and non-melanoma cell lines (5). Deletion of FAM129B in melanoma cells significantly impairs B-Raf/MEK/Erk-dependent invasion into the extracellular matrix (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: FAM134B (family with sequence similarity 134, member B), also referred to as JK-1 and RETREG1, is a cis-Golgi endoplasmic reticulum (ER) transmembrane protein that plays a role in ER homeostasis and may contribute to several human diseases (1). FAM134B contains a conserved LC3 interacting domain (LIR) that facilitates binding to LC3 and GABARAP family members and targets impaired ER to the autophagsome for degradation by ER-phagy (2). Deletion of FAM134B leads to ER expansion and stress-induced apoptosis (2). Expression of FAM134B has been linked to a number of pathological conditions, including viral infection, cancer, and neuronal disorders (1). FAM134B can potentially inhibit viral infection, as demonstrated by studies of FAM134B knockouts that resulted in significantly higher rates of Ebola virus replication (3). Mutations in FAM134B that lead to an accumulation of mis-folded proteins have also been associated with neuronal sensory disorders (2, 4, 5). The expression and mutational state of FAM134B can also have varying effects on cancer. Oncogenic effects of FAM134B were described in esophageal squamous carcinoma; whereas, it appears to have tumor suppressor activity in colorectal cancer (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Fatty acid synthase (FASN) catalyzes the synthesis of long-chain fatty acids from acetyl-CoA and malonyl-CoA. FASN is active as a homodimer with seven different catalytic activities and produces lipids in the liver for export to metabolically active tissues or storage in adipose tissue. In most other human tissues, FASN is minimally expressed since they rely on circulating fatty acids for new structural lipid synthesis (1).According to the research literature, increased expression of FASN has emerged as a phenotype common to most human carcinomas. For example in breast cancer, immunohistochemical staining showed that the levels of FASN are directly related to the size of breast tumors (2). Research studies also showed that FASN is highly expressed in lung and prostate cancers and that FASN expression is an indicator of poor prognosis in breast and prostate cancer (3-5). Furthermore, inhibition of FASN is selectively cytotoxic to human cancer cells (5). Thus, increased interest has focused on FASN as a potential target for the diagnosis and treatment of cancer as well as metabolic syndrome (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: FE65, FE65L1 and FE65L2 are members of the FE65 protein family. FE65 is an adaptor protein with protein-protein interaction domains including a WW domain followed by two phosphotyrosine interaction domains (PID1 and PID2) (1). Amyloid beta precursor protein (APP) binds to PID2 and undergoes sequential cleavage. First alpha-/beta secretases cleave and release the ectodomain into the extracellular environment. Subsequent processing by the gamma-secretase complex results in the APP intracellular domain (AICD) and the beta-amyloid peptides. The latter A-beta fragments form the main components of amyloid plaques in patients with Alzheimer's disease (2). FE65 family members can regulate APP processing, resulting in elevated levels of A-beta (3). Double knock-out mice of FE65 and FE65L1 display a phenotype that occurs in animals lacking APP family members, supporting a functional interaction between FE65 and APP (4).

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

Application Methods: Western Blotting

Background: Flap endonuclease-1 (FEN-1) is a structure-specific nuclease with multiple functions in DNA processing pathways (1,2). The replication and DNA repair activities of FEN-1 are critical for genomic stability in the eukaryotic cell. Through interaction with proliferation cell nuclear antigen (PCNA), FEN-1 helps coordinate Okazaki fragment maturation by removing RNA-DNA primers (3). FEN-1 is also required for non-homologous end joining of double stranded DNA breaks in long patch base excision repair (4,5). The multi-functional activities of FEN-1 are regulated by various mechanisms, including protein partner interactions (6,7), post-translational modifications (8,9), and subcellular re-localization in response to cell cycle or DNA damage (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Fes/Fps and Fer are the only two members of a unique family of cytoplasmic protein tyrosine kinases (1,2). Fes and Fer contain a central Src homology-2 (SH2) domain and a carboxy-terminal tyrosine kinase catalytic domain. They are structurally distinguished from other members of cytoplasmic protein tyrosine kinase subfamilies by the presence of amino-terminal Fer/CIP4 homology and coiled-coil domains (3). Fes/Fps was originally identified as an oncogene from avian (Fps) and feline (Fes) retroviruses. Human c-Fes has been implicated in myeloid, vascular endothelial and neuronal cell differentiation. Mutations may activate the Fps kinase and thereby contribute to cancer (4). However, recent data strongly suggests that the c-Fes protein-tyrosine kinase is a tumor suppressor rather than a dominant oncogene in colorectal cancer (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Fetuin A is produced by liver and secreted to plasma, and selectively concentrated in bone matrix. It is synthesized as a precursor and processed to generate 2 chains that are held together by a disulfide bond. It is a systemically acting calcification inhibitor (1). Reduced level of fetuin A in serum is associated with increased cardiovascular mortality in dialysis patients (2,3). Fetuin A can inhibit insulin-induced tyrosine phosphorylation of the insulin receptor tyrosine kinase and insulin receptor substrate-1 (4). Fetuin A deficient mice show high insulin sensitivity and high levels of serum fetuin A are associated with insulin resistance in humans (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through cell surface receptor tyrosine kinases. There are four members of the FGF receptor family: FGFR1 (flg), FGFR2 (bek, KGFR), FGFR3, and FGFR4. Each receptor contains an extracellular ligand binding domain, a transmembrane domain, and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR1 can be phosphorylated: Tyr463, 583, 585, 653, 654, 730, and 766. Tyr653 and Tyr654 are important for catalytic activity of activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCγ (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through cell surface receptor tyrosine kinases. There are four members of the FGF receptor family: FGFR1 (flg), FGFR2 (bek, KGFR), FGFR3, and FGFR4. Each receptor contains an extracellular ligand binding domain, a transmembrane domain, and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR1 can be phosphorylated: Tyr463, 583, 585, 653, 654, 730, and 766. Tyr653 and Tyr654 are important for catalytic activity of activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCγ (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Fgr is a member of the Src tyrosine kinase family. It has a membrane-associated amino-terminal domain that is highly divergent from other family members, internal conserved SH2 and SH3 domains and a highly conserved carboxy-terminal tyrosine kinase catalytic domain (1,2). Tyrosine 412 is located in the activation loop, and phosphorylation of this residue is critical for the activation of Fgr tyrosine kinase activity. c-Fgr is predominantly expressed in cells of hematopoietic origin including differentiated myeloid cells, NK and B cells (3,4). Fgr plays an important role in the signaling cascade from membrane receptors lacking intrinsic tyrosine kinase activity such as Bcr, FcR, and the integrin family of receptors (5). It was demonstrated that Fgr functions as a selective inhibitor of beta2 integrin-mediated signaling and Syk kinase function in monocytes (5).

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

Application Methods: Western Blotting

Background: Filamins are a family of dimeric actin binding proteins that function as structural components of cell adhesion sites. They also serve as a scaffold for subcellular targeting of signaling molecules (1). The actin binding domain (α-actinin domain) located at the amino terminus is followed by as many as 24 tandem repeats of about 96 residues and the dimerization domain is located at the carboxy terminus. In addition to actin filaments, filamins associate with other structural and signaling molecules such as β-integrins, Rho/Rac/Cdc42, PKC and the insulin receptor, primarily through the carboxy-terminal dimerization domain (1-3). Filamin A, the most abundant, and filamin B are widely expressed isoforms, while filamin C is predominantly expressed in muscle (1). Filamin A is phosphorylated by PAK1 at Ser2152, which is required for PAK1-mediated actin cytoskeleton reorganization (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Filamins are a family of dimeric actin binding proteins that function as structural components of cell adhesion sites. They also serve as a scaffold for subcellular targeting of signaling molecules (1). The actin binding domain (α-actinin domain) located at the amino terminus is followed by as many as 24 tandem repeats of about 96 residues and the dimerization domain is located at the carboxy terminus. In addition to actin filaments, filamins associate with other structural and signaling molecules such as β-integrins, Rho/Rac/Cdc42, PKC and the insulin receptor, primarily through the carboxy-terminal dimerization domain (1-3). Filamin A, the most abundant, and filamin B are widely expressed isoforms, while filamin C is predominantly expressed in muscle (1). Filamin A is phosphorylated by PAK1 at Ser2152, which is required for PAK1-mediated actin cytoskeleton reorganization (4).

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

Application Methods: Western Blotting

Background: FKBP4 (also known as FKBP52) is a member of the immunophilin protein family. FKBP4 does not demonstrate appreciable immunosuppressant activity typical of this family, despite its ability to bind the immunosuppressants FK506 and rapamycin (1,2). While FKBP4 plays an important role in immunoregulatory gene expression in B and T lymphocytes, its role in regulating steroid hormone receptor signaling and cytoskeletal dynamics is garnering significant interest. FKBP4 contains two petidyl-prolyl cis-trans isomerase (PPIase) domains, the first of which is implicated in steroid receptor signaling while the second interacts with tubulin and other cytoskeletal components. The maturation of cytoplasmic steroid hormone receptors into a functional conformation requires multiple chaperone and co-chaperone components, including HSP90, p23, and FKBP4 (3,4). FKBP4 interacts with HSP90 to facilitate the folding of androgen, glucocorticoid, and progesterone steroid hormone receptors. Indeed, the functionality of these receptors is impaired in the absence of FKBP4, and research studies have found that null mice demonstrate signs of androgen insensitivity syndrome (5). In addition, FKBP4, which is expressed at high levels in the brain, interacts with hyperphosphorylated Tau and antagonizes Tau's ability to promote microtubule polymerization (6). FKBP4 can also suppress amyloid β toxicity in Drosophila by processing APP (Alzheimer's Amyloid Precursor Protein) to unfold aggregates (7).