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Monoclonal Antibody Immunohistochemistry Paraffin Protein Homooligomerization

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Association of the receptor Fas with its ligand FasL triggers an apoptotic pathway that plays an important role in immune regulation, development, and progression of cancers (1,2). Loss of function mutation in either Fas (lpr mice) or FasL (gld mice) leads to lymphadenopathy and splenomegaly as a result of decreased apoptosis in CD4-CD8- T lymphocytes (3,4). FasL (CD95L, Apo-1L) is a type II transmembrane protein of 280 amino acids (runs at approximately 40 kDa upon glycosylation) that belongs to the TNF family, which also includes TNF-α, TRAIL, and TWEAK. Binding of FasL to its receptor triggers the formation of a death-inducing signaling complex (DISC) involving the recruitment of the adaptor protein FADD and caspase-8 (5). Activation of caspase-8 from this complex initiates a caspase cascade resulting in the activation of caspase-3 and subsequent cleavage of proteins leading to apoptosis. Unlike Fas, which is constitutively expressed by various cell types, FasL is predominantly expressed on activated T lymphocytes, NK cells, and at immune privileged sites (6). FasL is also expressed in several tumor types as a mechanism to evade immune surveillance (7). Similar to other members of the TNF family, FasL can be cleaved by metalloproteinases producing a 26 kDa trimeric soluble form (8,9).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Olfactomedin-4 (OLFM4, hGC-1) is a member of the Olfactomedin family, a small group of extracellular proteins defined by the presence of a conserved "Olfactomedin domain" that is thought to facilitate protein-protein interactions (1). OLFM4 is a secreted glycoprotein, which forms disulfide bond-mediated oligomers, and is thought to mediate cell adhesion through its interactions with extracellular matrix proteins such as lectins (2). Human OLFM4 was first cloned from myeloid cells (3) and is expressed in a distinct subset of neutrophils, though the functional significance of this differential expression pattern remains unclear (4). Among normal tissues, the expression of OLFM4 protein is most abundant in intestinal crypts (5), where it has garnered attention as a possible marker of intestinal stem cells (6). Notably, OLFM4 expression is markedly increased in several tumor types, including colorectal, gastric, pancreas, lung, and breast (reviewed in [1]). Furthermore, research studies show that the expression levels of OLFM4 vary in relation to the severity and/or differentiation status of multiple tumor types (1, 6-8), leading to the suggestion that OLFM4 may have utility as a prognostic marker in some cancer patients (9).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Olfactomedin-4 (OLFM4, hGC-1) is a member of the Olfactomedin family, a small group of extracellular proteins defined by the presence of a conserved "Olfactomedin domain" that is thought to facilitate protein-protein interactions (1). OLFM4 is a secreted glycoprotein, which forms disulfide bond-mediated oligomers, and is thought to mediate cell adhesion through its interactions with extracellular matrix proteins such as lectins (2). Human OLFM4 was first cloned from myeloid cells (3) and is expressed in a distinct subset of neutrophils, though the functional significance of this differential expression pattern remains unclear (4). Among normal tissues, the expression of OLFM4 protein is most abundant in intestinal crypts (5), where it has garnered attention as a possible marker of intestinal stem cells (6). Notably, OLFM4 expression is markedly increased in several tumor types, including colorectal, gastric, pancreas, lung, and breast (reviewed in [1]). Furthermore, research studies show that the expression levels of OLFM4 vary in relation to the severity and/or differentiation status of multiple tumor types (1, 6-8), leading to the suggestion that OLFM4 may have utility as a prognostic marker in some cancer patients (9).

$269
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Western Blotting

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

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

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

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

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

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

Background: Tight junctions, or zonula occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).

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

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

Background: Flotillins belong to a family of lipid raft-associated integral membrane proteins that carry an evolutionarily conserved domain called the prohibitin homology domain (PHB) (1). Flotillin members are ubiquitously expressed and located in noncaveolar microdomains (lipid rafts) on the plasma membrane where they support signal transduction and regulate lipid raft motility and localization (2-5). Two flotillin members have been described, flotillin-1 and flotillin-2. In addition to its colocalization with lipid rafts on the plasma membrane, flotillin-1 also has been found in compartments of the endocytic and autophagosomal pathways, such as recycling/late endosomes, the Golgi complex, and the nucleus (6,7). Flotillin-2 is mainly localized to the plasma membrane and is prevalent in cell-cell contact sites. However, overexpressed flotillin-2 has also been found in the late endosome (4,8,9). Both flotillin-1 and flotillin-2 are commonly used as lipid raft-associated markers.

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Ectonucleoside triphosphate diphosphohydrolase 1 (NTPDase 1, also known as CD39) is a multi-pass membrane ectoenzyme that metabolizes adenosine tri-phosphate (ATP) to regulate purinergic signaling. Purinergic signaling by extracellular ATP and its metabolites regulate many biological processes, including vascular tone, digestion, neuronal function, and inflammation in both normal and diseased states (1). NTPDase 1 is expressed in endothelial cells in the vasculature to regulate local platelet purinergic signaling via metabolism of ATP to adenosine (2). Accordingly, NTPDase 1 regulates platelet activation aggregation and contributes to the antithrombotic properties of endothelial cells (3). ATP and its metabolites also finely modulate the activity of T cells and macrophages (4, 5). Immunomodulation is regulated, in part, by the availability of extracellular ATP and adenosine, suggesting that NTPdase 1 (CD39) may play an immunosuppressive role in the tumor microenvironment.

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Protein kinase-like endoplasmic reticulum kinase (PERK) is an eIF2α kinase and transmembrane protein resident in the endoplasmic reticulum (ER) membrane that couples ER stress signals to translation inhibition (1-3). ER stress increases the activity of PERK, which then phosphorylates eIF2α to promote reduced translation. Research studies have demonstrated that PERK-deficient mice have defects in pancreatic β cells several weeks after birth, suggesting a role for PERK-mediated translational control in protecting secretory cells from ER stress (4). PERK activation during ER stress correlates with autophosphorylation of its cytoplasmic kinase domain (1-3). Phosphorylation of PERK at Thr980 serves as a marker for its activation status.

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The ATPase inhibitor factor 1 (ATPIF1) gene encodes a mitochondrial ATPase inhibitor that limits ATP depletion when mitochondrial respiration is impaired (1). ATPIF1 becomes activated following a drop in pH, binding to β-F1-ATPase, thereby inhibiting the hydrolase activity of the H+-ATP synthase (1,2). In addition to its role as an ATP hydrolase, ATPIF1 has also been shown to play a regulatory role in cellular energy metabolism by triggering the induction of aerobic glycolysis in cancer cells resulting in their Warburg phenotype (3,4). Research studies demonstrate that the overexpression of ATPIF1 in several human carcinomas further supports its participation in oncogenesis and provides insight into the altered metabolism of cancer cells, which includes the reprogramming of energetic metabolism toward glycolysis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin)

Background: Glutamate-ammonia ligase (GLUL), also known as glutamine synthetase (GS), catalyzes the de novo synthesis of glutamine from glutamate and ammonia. GLUL is ubiquitously expressed with particularly high expression in the muscle, liver, and brain (1). GLUL expression is elevated in various cancers. Its expression is upregulated by oncogenic c-Myc (2). High expression of GLUL in breast cancer patients is associated with larger tumor size and high level of HER2 expression. It is a predictor of poor survival in patients with glioma and liver cancers (3-6).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: VWF (Von Willebrand factor) is a multimeric plasma glycoprotein that promotes adhesion of platelets to sites of vascular injury (1). Mature circulating VWF is made up of disulfide-bonded multimers that are in a complex with factor VIII (2). VWF is stored in secretory Weibel-Palade bodies in endothelial cells (3,4). It is synthesized as a large precursor protein and undergoes extensive posttranslational modifications including dimerization in the endoplasmic reticulum followed by cleavage of the pro-peptide and multimerization in the Golgi apparatus (3,4). VWF is important in hemostasis, and genetic defects in the structure and modification of VWF can cause von Willebrand disease (VWD), the most common congenital bleeding disorder in humans (5).  Alternatively, increased levels of VWF have been shown to be involved in acute coronary thrombosis and are a clinical risk marker for atherosclerosis (6). VWF has also been shown to have a role in inflammation, functioning as an adhesive site for a variety of leukocyte subsets (7). Through siRNA experiments and the use VWF-deficient mice, it has also been shown that VWF regulates angiogenesis (8).

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

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

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Bovine, Dog, Hamster, Human, Monkey, Mouse, Rat

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

Background: The 21-24 kDa integral proteins, caveolins, are the principal structural components of the cholesterol/sphingolipid-enriched plasma membrane microdomain caveolae. Three members of the caveolin family (caveolin-1, -2, and -3) have been identified with different tissue distributions. Caveolins form hetero- and homo-oligomers that interact with cholesterol and other lipids (1). Caveolins are involved in diverse biological functions, including vesicular trafficking, cholesterol homeostasis, cell adhesion, and apoptosis, and are also implicated in neurodegenerative disease (2). Caveolins interact with multiple signaling molecules such as Gα subunit, tyrosine kinase receptors, PKCs, Src family tyrosine kinases, and eNOS (1,2). It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Phosphorylation at Tyr14 is essential for caveolin association with SH2 or PTB domain-containing adaptor proteins such as GRB7 (3-5). Phosphorylation at Ser80 regulates caveolin binding to the ER membrane and entry into the secretory pathway (6).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Clusterin (CLU, apolipoprotein J) is a multifunctional glycoprotein that is expressed ubiquitously in most tissues. Clusterin functions as a secreted chaperone protein that interacts with and stabilizes stress-induced proteins to prevent their precipitation (1,2). Research studies show that clusterin plays a protective role in Alzheimer’s disease by sequestering amyloid β(1-40) peptides to form long-lived, stable complexes, which prevents amyloid fibril formation (3-5).In addition to the secreted protein, several intracellular isoforms are localized to the nucleus, mitochondria, cytoplasm, and ER. The subcellular distribution of these multiple isoforms leads to the diversity of clusterin functions. Additional studies report that clusterin is involved in membrane recycling, cell adhesion, cell proliferation, apoptosis, and tumor survival (6-9). The clusterin precursor is post-translationally cleaved into the mature clusterin α and clusterin β forms. Clusterin α and β chains create a heterodimer through formation of disulfide bonds (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: Bax is a key component for cellular induced apoptosis through mitochondrial stress (1). Upon apoptotic stimulation, Bax forms oligomers and translocates from the cytosol to the mitochondrial membrane (2). Through interactions with pore proteins on the mitochondrial membrane, Bax increases the membrane's permeability, which leads to the release of cytochrome c from mitochondria, activation of caspase-9 and initiation of the caspase activation pathway for apoptosis (3,4).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The receptor-interacting protein (RIP) family of serine-threonine kinases (RIP, RIP2, RIP3, and RIP4) are important regulators of cellular stress that trigger pro-survival and inflammatory responses through the activation of NF-κB, as well as pro-apoptotic pathways (1). In addition to the kinase domain, RIP contains a death domain responsible for interaction with the death domain receptor Fas and recruitment to TNF-R1 through interaction with TRADD (2,3). RIP-deficient cells show a failure in TNF-mediated NF-κB activation, making the cells more sensitive to apoptosis (4,5). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNF-R1 signaling complex via interaction with NEMO, leading to IκB phosphorylation and degradation (6,7). Overexpression of RIP induces both NF-κB activation and apoptosis (2,3). Caspase-8-dependent cleavage of the RIP death domain can trigger the apoptotic activity of RIP (8).

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

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

Background: Axin1 (Axis inhibition protein 1) and Axin2 are multidomain scaffold proteins that negatively regulate Wnt signaling. Axin1 interacts with APC, GSK-3β, Dvl, and β-catenin and promotes the GSK-3β-mediated phosphorylation and subsequent degradation of β-catenin (1,2). Upon stimulation of cells with Wnt, Axin1 is recruited to the membrane by phosphorylated LRP5/6, a process that is believed to be crucial for activation of Wnt signaling (3,4). In addition to its role in the Wnt signaling pathway, Axin1 forms a complex with MEKK1 and activates c-Jun amino-terminal kinase (JNK/SAPK) (5). Axin2 (also known as Conductin or Axil) can functionally substitute for Axin1 in mice (6). Axin2 itself is a direct target of the Wnt signaling pathway and therefore serves to control the duration and/or intensity of Wnt signaling through a negative feedback loop (7-9).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Bcl-2 family consists of a number of evolutionarily conserved proteins containing Bcl-2 homology domains (BH) that regulate apoptosis through control of mitochondrial membrane permeability and release of cytochrome c (1-3). Four BH domains have been identified (BH1-4) that mediate protein interactions. The family can be separated into three groups based upon function and sequence homology: pro-survival members include Bcl-2, Bcl-xL, Mcl-1, A1 and Bcl-w; pro-apoptotic proteins include Bax, Bak and Bok; and "BH3 only" proteins Bad, Bik, Bid, Puma, Bim, Bmf, Noxa and Hrk. Interactions between death-promoting and death-suppressing Bcl-2 family members has led to a rheostat model in which the ratio of pro-apoptotic and anti-apoptotic proteins controls cell fate (4). Thus, pro-survival members exert their behavior by binding to and antagonizing death-promoting members. In general, the "BH3-only members" can bind to and antagonize the pro-survival proteins leading to increased apoptosis (5). While some redundancy of this system likely exists, tissue specificity, transcriptional and post-translational regulation of many of these family members can account for distinct physiological roles.

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: JNK-Interacting Proteins (JIPs), as their name implies, coordinate c-Jun N-terminal Kinase (JNK) signaling by acting as scaffolds for components of the JNK signaling cascade (1). JIPs localize and promote JNK activation in response to stress by amalgamating and co-localizing upstream kinases and downstream effectors in the stress-kinase pathway analogous to the mechanism by which AKAPs orchestrate PKA signaling. JIPs bind to an array of MAPKs and other signaling proteins, including the mixed-lineage kinases, MKK7, p38α MAPK, JNK1-3, Max, Myc, NF-κB, LRRK2, and others (1-4).There are four known JIPs, JIP1-4, of which JIP1 and JIP2 share extensive sequence homology and domain structure. JIP1 and JIP2 are mainly expressed in neurons, testis and in β pancreatic cells, where they have been implicated in cellular responses to metabolic stress, the development of diabetes, and post-traumatic brain damage (5-7). Although architecturally distinct from JIP1 and JIP2, JIP3 and JIP4 share some overlapping functions and are more broadly expressed. JIP4, encoded by the SPAG9 (sperm-associated antigen-9) gene, is a homooligomer that binds to and coordinates the activation of numerous components of the stress-activated kinase cascade including MEK4, MEKK3, p38α MAPK, and JNK1-3 (3,8). However, unlike the other JIP members, JIP4 does not appear to activate JNK directly, instead favoring stimulation of p38 MAPK signaling events in response to cellular stress (3,9).In addition to mediating stress responses, JIP4 (or its splice variant, JLP) has also been shown to interact with ARF6 and PIKfyve, thus regulating microtubule-based endosomal trafficking (10,11). There are extensive reports indicating that JIP4 is phosphorylated in response to stress (UV damage etc.) but it is unclear what effect, if any, this has on its function, localization, or binding properties (12-15).