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Lactoferrin ELISA Kit
Lactoferrin is an iron-binding glycoprotein of the transferrin family that is expressed in most biologic fluids, such as the breast milk, particularly the colostrums, tears, sweat, saliva and other exocrine secretions of mammals.
As a major component of mammals’ innate immune system, lactoferrin has been shown to have numerous functions such as below.
- “Antiviral effect”
By binding to the envelope of the Hepatitis C virus (HCV), lactoferrin prevents infiltration of HCV to the target cells, and suppresses viral replication.
- “Antibacterial effect”
By chelating iron, lactoferrin suppresses the proliferation of iron requiring bacteria.
- Anti-inflammatory effect”
By strongly binding to endotoxin (LPS), lactoferrin inhibits the binding of LPS to macrophages and suppresses the production of inflammatory cytokines such as TNF-alpha; and IL-6.
- ”Immunoregulatory effect”
Lactoferrin stimulates cytotoxic activity of natural killer cells (NK cells).
- ”Antitumor effect
Lactoferrin induces the apoptosis of tumor cells, or prevent the propagation of tumors by inhibiting angiogenesis.
Focusing on anti-inflammatory effects, the lactoferrin in various biologic fluids are considered as markers of inflammation. It has been reported that fecal lactoferrin is useful as a sensitive and specific marker in identifying intestinal inflammation such as Crohn’s disease and chronic inflammatory bowel disease (IBD). Combination of several markers, such as S100A8/A9 complex, defensin, elastase, MPO and I-FABP may be useful for classifying IBD.
In addition, bovine milk prior to high temperature pasteurization (raw milk) contains large quantities of lactoferrin, and oral intake of lactoferrin has been reported to cause several effects that maintain and promote health:
1. Proliferation of Lactobacillus biffidus
2. Improvement of anemia
3. Reduction of visceral fat
4. Prevention of arteriosclerosis by inhibiting the uptake of denatured LDL
Because of these effects, taking lactoferrin by milk products and supplements attracts public interest.
Product Code Number
CircuLex Bovine Lactoferrin ELISA Kit
14-3-3 Gamma ELISA Kit
14-3-3 proteins are a family of conserved regulatory molecules expressed in all eukaryotic cells. There are seven genes, β, γ, ε, σ, ζ, τ and η, that encode 14-3-3s in most mammals. The family dynamically regulates the activity of target proteins in various signaling pathways that control diverse physiological and pathological processes. Either an abnormal state of 14-3-3 protein expression or dysregulation of 14-3-3/target protein interactions contributes to the development of many human diseases.
Clinical investigations have demonstrated a correlation between up-regulated 14-3-3 protein levels and poor survival of cancer patients. Several studies have also suggested that 14-3-3 isoforms are differentially regulated in cancer and neurological syndromes. Especially, elevated amounts of the gamma isoform (14-3-3 Gamma) are found in the cerebrospinal fluid (CSF) of Creutzfeldt-Jakob disease (CJD) patients and could be as a specific marker of the disease as well as tau protein level.
Concentrations of 14-3-3 Gamma in CSF from patients with CJD neurological disorders.
The data is kindly provided by the courtesy of:
Dr. Yuki Matsui, Department of Pharmaceutical Care and Health Sciences, Faculty of Pharmaceutical Sciences, Fukuoka University
Dr. Katsuya Satoh, Department of Molecular Microbiology and Immunology, Graduate School of Biomedical Science, Nagasaki University.
Product Code Number
CircuLex 14-3-3 gamma ELISA Kit
UCHL1 ELISA Kit
The UCHL1, also called PARK5 or neuronal-specific protein gene product 9.5, is a carboxyl-terminal ubiquitin hydrolase regulating ubiquitin dependent signaling pathways, recently suggested as a tumor suppressor. UCHL1 is expressed predominantly in neurons, representing 1 to 2% of total soluble brain protein, as well as in testis and ovary. In vivo, UCHL1 has been shown to be involved in the regulation of the ubiquitin pool, apoptosis, learning and memory, and its absence in mice because of spontaneous intragenic deletions yields phenotypes with neurological defects.
Mutations in UCHL1 have been discovered in a German family with Parkinson’s disease (PD), which caused a partial loss of the catalytic activity of this thiol protease. This mutation has been linked to an increased risk of developing an autosomal-dominant form of PD. Based on the abundance in the CNS, UCHL1 has been proposed as a candidate biomarker for brain injury and ischemic strokes. It was demonstrated that UCHL1 was released from injured neurons and flow into the cerebrospinal fluid and eventually into circulating bl
DJ-1 PARK7 ELISA Kit Ver.2
DJ-1 (PARK7/CAP1/RS) was originally cloned as a putative oncogene capable of transforming NIH-3T3 cells in cooperation with H-ras, a protein expressed in sperm, and a regulator of RNA-protein interactions. DJ-1 has also been isolated as a gene associated with autosomal early-onset Parkinson’s disease (PD). Several lines of evidence suggest that DJ-1 plays a role in the oxidative stress response. In cultured mammalian ce11s, DJ-1 quenches reactive oxygen species and is converted into a variant with a more acidic isoelectric point. Therefore, DJ-1 protects against reactive oxygen species-induced cell death, and its suppression with small interfering RNA (siRNA) sensitizes cells to such insults. Mutations in DJ-1 that are associated with familial Parkinson’s disease have been shown to decrease the anti-oxidative stress function.
In addition, DJ-1 concentration is reported to be elevated within 3 hours after cerebral infarction, suggesting the possibility that DJ-1 could be a promising biomarker for early stage of cerebral infarction. Moreover, breast cancer patients have elevated levels of circulating DJ-1 and anti-DJ-1 autoantibodies compared to healthy and non-breast cancer patients.
Product Code Number
CircuLex Human DJ-1/PARK7 ELISA Kit Ver.2
ISG15 ELISA Kit
ISG15 (Interferon (IFN)-Stimulated Gene 15) is a ubiquitin-like protein containing two ubiquitin homology domains and becomes conjugated to a variety of proteins when cells are treated with type I interferon or lipopolysaccharide. Therefore this modification (so called, ISGylation) appears to be involved in type I interferon signal transduction. Unlike ubiquitylation, ISGylation does not drive protein degradation (regulated by K48-linked ubiquitin).
ISG15 can also be found extracellularly in an unconjugated form (free form). Human lymphocytes and monocytes were reported to release free ISG15 following treatment with IFN-β. More than 50 % of the total ISG15 could be detected in the culture medium after 24 hours following IFN stimulation. In addition, ISG15 is highly elevated and extensively conjugated to cellular proteins in many tumors and tumor cell lines. The increased levels of ISG15 in tumor cells were found to be associated with decreased levels of polyubiquitinated proteins.
Fibulin-1 ELISA Kit
Fibulin-1 is the first described member of a seven-gene family of extracellular matrix (ECM) proteins that have a common structural signature consisting of a series of repeated EGF-like domains followed by a fibulin-type module at its carboxyl terminus. Fibulin-1 is a secreted glycoprotein that is an intercellular component of a wide range of connective tissues. In blood vessel walls, fibulin-1 is a component of elastic lamina and ECM fibers that surround smooth muscle cells and underlie the endothelium. Although its actual function remains to be elucidated, fibulin-1 has been suggested to be involved in cell adhesion, migration, proliferation, and malignant transformation through binding to many ECM proteins, including laminin, fibrinogen, fibronectin, nidogen-1, endostatin, β-amyloid precursor protein and proteoglycans, aggrecan, versican, receptors and growth factors. In addition, fibulin-1 has been found to bind to the plasma protein fibrinogen and to incorporate into fibrin clots formed in vitro and in vivo. Targeted inactivation of fibulin-1 gene in mice caused dilation and ruptures in the endothelial lining of small blood vessels, indicating that fibulin-1 was important in the stabilization of blood vessel walls.
Fibulin-1 is one of a few ECM proteins normally found in blood in high concentrations. It was reported that plasma fibulin-1 concentrations increased in T2DM patients with prevalent cardiovascular disease destined for vascular surgery as well as in asthmatics.
Hsp27 ELISA Kit
Hsp27 is an abundant and ubiquitous family of small HSP (heat shock protein) that acts as an ATP-independent chaperone and mainly localized in the cytosol. Small HSPs are potent mediator of protein folding and also involved in architecture of cytoskeleton, cell migration, cell growth/differentiation, and tumor progression. Hsp27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9.
The basic structure of most small HSPs is a homologous and highly conserved amino acid sequence, with an alpha-crystallin-domain at the C-terminus and the WD/EPF domain at the N-terminus. Hsp27 exists as both large oligomers that are proposed to have chaperone-like activity and as smaller oligomers that bind and cap barbed end microfilaments and stabilize them. The up-regulation of Hsp27 correlates with the rate of phosphorylation and with an increase of large oligomers.
High levels of Hsp27 have been observed in many cancer cells including breast carcinoma, ovarian cancer and rectal cancer, compared to normal cells in which expression is undetectable or relatively low. Hsp27 is expressed constitutively in many tissues and its expression is increased to high levels after various types of stress including elevated temperatures, toxic metals, drugs and oxidants . Hsp27 can redistribute to the nucleus from the cytoplasm in response to stress, where it may function to stabilize DNA and/or the nuclear membrane.
Hsp27 was reported to be associated with poor prognosis in gastric, liver, and prostate carcinoma and osteosarcomas. However, other study showed that Hsp27 was not detectable in metastatic tumors and could be found only in samples derived from non-metastatic tumors. It was reported that the concentration of Hsp27 in serum from pancreatic tumor patients was found to be significantly higher than in serum from healthy controls.
Clusterin Apo-J ELISA Kit
Clusterin, also called apolipoprotein J, sulfated glycoprotein-2, and testosterone-repressed prostate message-2, is a highly conserved secreted heterodimeric glycoprotein constitutively expressed by diverse epithelial cells. Clusterin has been implicated in diverse physiological processes, including lipid transportation, complement inhibition, tissue remodeling, membrane recycling, clearance of cellular debris, regulation of apoptosis, membrane protection, and promotion of cell-cell interactions. Clusterin is induced in injured organs in various disease states, such as Alzheimer’s disease, atherosclerosis, myocardial infarction, and multiple forms of acute and chronic renal disease. Clusterin has been shown to associate with both normal in vitro aging, namely replicative senescence, as well as with stress induced premature senescence. In vivo, the protein is up-regulated in many severe physiological disturbances that relate to advanced aging, including accumulation in the artery wall during the development of atherosclerosis. In cancer, clusterin up-regulation has been described in renal cell carcinoma, breast carcinoma, ovarian cancer, anaplastic large cell lymphomas, desmoplastic melanoma , transitional cell carcinoma of the bladder, pancreatic cancer, and serous carcinoma and hepatocellular carcinoma. However, a number of tumor processes where clusterin is downregulated have also been described such as esophageal squamous cell carcinoma, testicular germ cell tumors and prostate cancer. The structure of clusterin has not provided much insight into function. Mammalian clusterins are approximately 80-kDa heterodimers consisting of two 40-kDa chains joined by a unique five-disulfide-bond motif. The protein has limited homology to other proteins and lacks clear functional motifs. It does contain three putative amphipathic α-helical regions, which could allow it to interact with lipids and hydrophobic regions of other proteins.
Lacritin ELISA Kit
Lacritin is a 12.3 kDa tear glycoprotein that is apically released from human lacrimal acinar cells during reflex tearing and can be detected in mixed reflex and basal human tears. Lacritin is produced by corneal, conjunctival, meibomian as one of the most eye-restricted genes. However it has been detected in a subpopulation of ductal cells in salivary glands, thyroid and mammary glands. Lacritin modulates lacrimal acinar cell secretion, promotes ductal cell proliferation, and stimulates signaling through tyrosine phosphorylation and release of calcium. Since a decrease of tear lacritin was reported in patients with blepharitis and in contact lens–related dry eye, lacritin might play an important role in maintaining tear fluid and the ocular surface. In fact, ocular instillation of recombinant human lacritin stimulated basal tear flow in rabbits. Lacritin also promotes basal tear secretion by cultured rat and monkey lacrimal acinar cells and stimulates human corneal epithelial cell growth. Thus, lacritin appears to be a multifunctional eye-specific factor with a potential role in tear secretion and corneal epithelial renewal.
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