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Product listing: EphB6 Antibody, UniProt ID O15197 #12560 to FAM129B Antibody, UniProt ID Q96TA1 #5122

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: EphB6 is a kinase-defective receptor and member of the ephrin-B family of transmembrane proteins (1). Although lacking kinase activity, EphB6 can regulate cellular functions through its interaction with adaptor proteins and other Eph family members (2). In hematopoietic cells, EphB6 is specifically expressed in the T cell population (3) and functions as an important regulator of T cell receptor (TCR) mediated signaling. Upon binding with its ephrin-B1 or ephrin-B2 ligand, EphB6 modulates TCR activity through inhibition of JNK signaling, reduction of CD25 expression, and decreased IL-2 secretion (4). Reduced levels of cell proliferation and cytokine secretion are seen in EphB6 knock-out mice relative to wild type (5). In conjunction with EphB3 receptor activation, EphB6 suppresses Fas receptor induced apoptosis by triggering the Akt activation pathway (6). Research indicates that decreased EphB6 expression is associated with a higher degree of metastasis in various cancers, including breast cancer (7), lung cancer (8), and neuroblastoma (9). EphB6 is thought to reduce cancer invasiveness through its effect on cell adhesion and migration. Following EphrinB1 ligand binding, EphB6 is phosphorylated by kinases such as Src and another active EphB kinase (2, 10, 11). Phosphorylated EphB6 forms a stable complex with Cbl and initiates Cbl inhibition of cell adhesion (2,11). EphB6 regulates signal transduction through direct interaction with other active Eph receptor kinases, sequestering these EphB6-bound receptors and inhibiting typical signal transduction function (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: EPRS (Glutamatyl-prolyl-tRNA synthetase) is a bifunctional enzyme in the aminoacyl-tRNA ligase family that attaches the cognate amino acid to the corresponding tRNA for protein translation (1,2). EPRS usually resides in the tRNA multisynthetase complex (MSC) that may facilitate the delivery of aminoacylated tRNAs to the ribosome during protein synthesis (3,4). In monocytic cells, upon interferon (IFN)-gamma activation, EPRS becomes phosphorylated and is released from the MSC to form the so-called GAIT (IFN-Gamma-Activated Inhibitor of Translation) complex with NS1-associated protein (NSAP1), ribosomal protein L13a, and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The GAIT complex binds to a defined RNA element through EPRS in the 3’ untranslated region (UTR) to inhibit translation of target transcripts, including vascular endothelial growth factor (VEGF)-A, ceruloplasmin, and several cytokines and their receptors. Thus, EPRS plays an important role in inflammation regulation (5-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: ERC1, an acronym named for previous protein names ELKS (1), RAB6IP2 (2) and CAST (3), is a RIM-binding protein that plays a role in neurotransmitter release and general membrane trafficking in other cell types (2-5). Interaction with the GTP-binding protein Rab6 suggests that it contributes to membrane traffic at the Golgi (2). In addition to its association with membrane trafficking, ERC1 has also been found as an essential part of the IκB kinase (IKK) complex required for the activation of NF-κB, perhaps by recruiting IκBα to the IKK complex (6). Alternative splicing of ERC1 generates 2 proteins with a divergent carboxy terminus, a long and a short form termed ERC1α and ERC1β, respectively. ERC1α is widely expressed, whereas ERC1β and a related family member ERC2 are expressed in the brain (4). Papillary thyroid carcinomas have been identified with the translocation t(10;12)(p11;p13) resulting in a fusion between ERC1 and the receptor tyrosine kinase Ret (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: ERC1, an acronym named for previous protein names ELKS (1), RAB6IP2 (2) and CAST (3), is a RIM-binding protein that plays a role in neurotransmitter release and general membrane trafficking in other cell types (2-5). Interaction with the GTP-binding protein Rab6 suggests that it contributes to membrane traffic at the Golgi (2). In addition to its association with membrane trafficking, ERC1 has also been found as an essential part of the IκB kinase (IKK) complex required for the activation of NF-κB, perhaps by recruiting IκBα to the IKK complex (6). Alternative splicing of ERC1 generates 2 proteins with a divergent carboxy terminus, a long and a short form termed ERC1α and ERC1β, respectively. ERC1α is widely expressed, whereas ERC1β and a related family member ERC2 are expressed in the brain (4). Papillary thyroid carcinomas have been identified with the translocation t(10;12)(p11;p13) resulting in a fusion between ERC1 and the receptor tyrosine kinase Ret (1).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: DNA repair systems operate in all living cells to manage a variety of DNA lesions. Nucleotide excision repair (NER) is implemented in cases where bulky helix-distorting lesions occur, such as those brought about by UV and certain chemicals (1). Excision Repair Cross Complementing 1 (ERCC1) forms a complex with ERCC4/XPF, which acts as the 5’ endonuclease required to excise the lesion (2). ERCC1-XPF is also required for repair of DNA interstrand crosslinks (ICLs) (3) and involved in repair of double strand breaks (4). Research studies have shown that expression of ERCC1 is related to survival rate and response to chemotherapeutic drugs in several human cancers including non-small cell lung cancer (NSCLC) (5,6).

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

Application Methods: Western Blotting

Background: Efficient termination of mRNA translation in eukaryotes is dependent upon a complex of two polypeptide release factors, eRF1 and eRF3 (1). The eukaryotic translation termination factor 1 (eRF1, ETF1) structurally resembles tRNA, which allows it to participate in stop codon recognition as well as hydrolysis of the peptidyl-tRNA conjugate (2,3). The eRF1 protein contains three functionally distinct domains, including an amino-terminal domain that harbors discrete motifs that participate in stop codon recognition (4,5). Lysine hydroxylation within the amino-terminal domain is required for efficient termination of mRNA translation (6). The central region of eRF1 harbors a GGQ motif that facilitates hydrolysis of peptidyl-tRNA conjugates (7), while its carboxy terminus participates in eRF3 binding (8).

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

Application Methods: Western Blotting

Background: Eukaryotic release factor 3 (eRF3, GSPT) is an evolutionarily conserved class II release factor and member of the GTPase superfamily that cooperates with eRF1 in polypeptide translation termination (1). Paralogous genes encode a pair of eRF3 proteins (eRF3a/GSPT1, eRF3b/GSPT2) that share a conserved carboxy-terminal GTPase/eRF1-binding domain and a non-conserved amino-terminal PABP1 binding site (2). The eRF3 carboxy-terminal region is involved in translation termination through binding and activation of the eRF1 release factor (1). The amino-terminal region of eRF3 is not required for eRF1 binding and activation, but is implicated in control of mRNA stability (3,4). Expression of eRF3 proteins vary, with eRF3a ubiquitously expressed and proliferation-dependent, while eRF3b expression is more restricted to brain tissue (2,5,6). Research studies demonstrate that eRF3 undergoes caspase-mediated cleavage and degradation related to reduced protein synthesis during DNA damage-induced apoptosis (7). Additional studies indicate that polyglycine expansion of the eRF3a amino terminus is associated with an increased susceptibility to breast and gastric cancer (8,9). It is likely that the polyglycine expansions of amino-terminal eRF3a may affect the ability of eRF3a to undergo caspase-mediated cleavage (9).

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

Application Methods: Western Blotting

Background: Erk3, also known as MAPK6 or p97 MAPK, is almost 50% identical to Erk1/2 at the kinase domain located in its amino-terminal region (1). However, Erk3 is distinguished from other MAP kinases in that it lacks the conserved TXY motif in its activation loop, possessing instead an SEG motif (1,2). Phosphorylation at Ser189 in the SEG motif has been reported (2,3). With limited information about its upstream kinases and downstream substrates, the significance of this phosphorylation remains to be elucidated (3,4). Erk3 is an inherently unstable protein, rapidly degraded through amino-terminal ubiquitination and proteasome degradation (3,5). A site-specific cleavage, depending on a short stretch of acidic residues of Erk3, might regulate its translocation from the Golgi/ERGIC to the nucleus during the cell cycle (6). Accumulating evidence suggests that Erk3 is involved in cell differentiation (1,3,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Erk5 (Mitogen-activated protein kinase 7, Big mitogen-activated protein kinase 1) is a member of the MAPK superfamily implicated in the regulation numerous cellular processes including proliferation, differentiation, and survival (1-4). Like other MAPK family members, Erk5 contains a canonical activation loop TEY motif (Thr218/Tyr220) that is specifically phosphorylated by MAP2K5 (MEK5) in a growth-factor-dependent, Ras-independent mechanism (5-7). For example, EGF stimulation promotes Erk5 phosphorylation that induces its translocation to the nucleus where it phosphorylates MEF2C and other transcriptional targets (5,6). Erk5 is also activated in response to granulocyte colony-stimulating factor (G-CSF) in hematopoietic progenitor cells where it promotes survival and proliferation (7). In neuronal cells, Erk5 is required for NGF-induced neurite outgrowth, neuronal homeostasis, and survival (8,9). Erk5 is thought to play a role in blood vessel integrity via maintenance of endothelial cell migration and barrier function (10-12). Although broadly expressed, research studies have shown that mice lacking erk5 display numerous cardiac defects, suggesting Erk5 plays a critical role in vascular development and homeostasis (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Erlin-1 and erlin-2 (SPFH1 and SPFH2) are SPFH domain-containing proteins that belong to the prohibitin family (1,2). The N-termal domain of erlin proteins contains ER-targeting sequences responsible for their translocation to the endoplasmic reticulum (ER) (3). In the ER, erlin-1 and erlin-2 specifically associate with the detergent resistant lipid raft microdomain of the membrane (3). Erlin-1 may be involved in dentritic cell activation (4) and erlin-2 has been shown to regulate the ER-associated degradation (ERAD) pathway by interacting with endogenous substrates and resulting in their polyubiquitination and degradation (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Erlin-1 and erlin-2 (SPFH1 and SPFH2) are SPFH domain-containing proteins that belong to the prohibitin family (1,2). The N-termal domain of erlin proteins contains ER-targeting sequences responsible for their translocation to the endoplasmic reticulum (ER) (3). In the ER, erlin-1 and erlin-2 specifically associate with the detergent resistant lipid raft microdomain of the membrane (3). Erlin-1 may be involved in dentritic cell activation (4) and erlin-2 has been shown to regulate the ER-associated degradation (ERAD) pathway by interacting with endogenous substrates and resulting in their polyubiquitination and degradation (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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. Several oxidoreductases of the protein disulfide isomerase (PDI) family essential for disulfide formation and isomerization are localized to the ER (2). Studies have found that the ER-residing protein endoplasmic oxidoreductin-1 (Ero1) provides the oxidizing potential to the ER in Saccharomyces cerevisiae (3). In vitro experiments demonstrated that Ero1 is oxidized by molecular oxygen in a FAD-dependent manner and the oxidized Ero1 in turn serves as an oxidant for PDI (4). Two human homologs of Ero1, Ero1-like (Ero1-Lα and β) have been identified (2,5). Ero1-Lα is an ER membrane-associated N-glycoprotein that promotes oxidative protein folding and has been shown to be expressed in several cell lines and tissues (2).

$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).