2405 Results for: "BioVendor"

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Free T3 typically reflects a patient’s actual thyroid status more reliably than total T3.

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This gene encodes a protein that catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, one step in the biosynthesis of nicotinamide adenine dinucleotide.

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CRF serves as a potential neurochemical marker of early dementia and possible early AD.

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Estrone is a steroid like estriol and estradiol, belonging to the class of estrogens.

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Cortisol is the most abundant circulating steroid and the major glucocorticoid secreted by the adrenal cortex.

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96 wells (1 kit) - ELISA is a sandwich enzyme immunoassay for the quantitative measurement of chemerin.

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GDF-15/MIC-1 is synthesized as a 62-kDa precursor protein, which, after cleavage by furin-like protease, is secreted as 25-kDa disulfide-linked dimmer.

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96 wells (1 kit) - ELISA is a competitive enzyme immunoassay for the quantitative measurement of IFN-gamma.

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Interleukin 1 receptor antagonist (IL-1RA) is a protein related to the IL-1 family based on its similarities in amino acid sequence to both IL-1 beta and IL-1 alpha.

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Interleukin-17 is involved in the regulation of hematopoiesis and its effects are dependent on the physiological/pathological status of the organism.

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Androstenedione is a precursor of testosterone and estrone.

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LIF is a bioactive protein intended for use in cell culture applications.

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Interleukin-2 (IL-2) plays a central role in the activation and proliferation of lymphocytes that have been primed by antigens.

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Quality control test, Indirect ELISA – to determine titer of the antibody , SDS PAGE – to determine purity of the antibody, and BCA - to determine quantity of the antibody.

Supplier: BioVendor

96 wells (1 kit) - ELISA is a competitive enzyme immunoassay for the quantitative measurement of testosterone.

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Total 200 AA. MW: 22.8 kDa (calculated). UniProtKB acc.no. Q9BQB4 (Gln24-Tyr213). N-terminal His-tag (10 extra AA). Protein identity confirmed by LC-MS/MS.

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Total 80 AA. MW: 9.2 kDa (calculated). N-Terminal His-tag (10 extra AA). UniprotKB acc.no. P11684.

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Retroviral protease from HIV-1 virus is an enzyme important in the life cycle of the virus

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Total 426 AA. MW 45.7 kDa (calculated), C-Terminal Flag-tag (11 extra AA). UniProt entry Q6UXB8.

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S100A8 and S100A9 belong to a family of 25 homologous low-molecular-weight intracellular calcium-binding proteins that exhibit tissue and cell-specific expression. They are characterized by two distinct EF-hand (helix-loop-helix) calcium-binding domains connected by a hinge region. The N-terminal Ca2+ binding domain has lower affinity than the canonical C-terminal domain that allows for functionally important second messenger roles dependent on intracellular Ca2+ levels. Human S100A8 (also known as MRP8, calgranulin A, L1 light chain, cystic fibrosis antigen) is the most closely related member of the human (h) S100 family to mS100A8, although the level of homology is low (69% at the DNA level; 58% at the amino acid level). Human S100A8 is a calcium-binding protein member of the S100 protein family, is highly expressed in the cytosol of neutrophils and monocytes, and is frequently found at high levels in the extracellular milieu during inflammatory conditions. S100A8 is almost exclusively expressed by cells of myeloid lineage and is constitutively expressed in the cytosol of neutrophils. Monocytes and differentiated macrophages from inflamed tissues also express S100A8. Increased serum levels of the S100A8 (MRP-8) protein have been reported in inflammatory conditions including bacterial infection, arthritis, and cystic fibrosis (CF). Preferentially exists as a heterodimer or heterotetramer with S100A9 known as calprotectin (S100A8/A9). Calprotectin (S100A8/9) is predominantly expressed in myeloid cells. Except for inflammatory conditions, the expression is restricted to a specific stage of myeloid differentiation since both proteins are expressed in circulating neutrophils and monocytes but are absent in normal tissue macrophages and lymphocytes. Under chronic inflammatory conditions, such as psoriasis and malignant disorders, also expressed in the epidermis. Found in high concentrations at local sites of inflammation or in the serum of patients with inflammatory diseases such as rheumatoid, cystic fibrosis, inflammatory bowel disease, Crohn's disease, giant cell arteritis, cystic fibrosis, Sjogren's syndrome, systemic lupus erythematosus, and progressive systemic sclerosis. Involved in the formation and deposition of amyloids in the aging prostate known as corpora amylacea inclusions. Strongly up-regulated in many tumors, including gastric, esophageal, colon, pancreatic, bladder, ovarian, thyroid, breast and skin cancers.

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Total 137 AA. MW: 15.5 kDa (calculated). UniProtKB acc.no. P51161. N-Terminal His-tag (10 extra AA)

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FGF-23 is a secreted, nonglycosylated monomeric protein belonging to the FGF family. Full-lenght FGF-23 is a phosphaturic hormone which blocks neural phosphate reabsorbtion. Upon processing, biologically inactive N- and C- terminal fragments are generated. Defects in FGF-23 is associated with autosomal dominant hypophosphatemic rickets. The FGF-23 gene encodes a member of the fibroblast growth factor family that is mutant in autosomal dominant hypophosphatemic rickets (ADHR). Tumor-induced osteomalacia is one of the paraneoplastic disorders characterized by hypophosphatemia caused by renal phosphate wasting. The fact that removal of responsible tumors normalizes phosphate metabolism is evidence that a humoral phosphaturic factor, sometimes called phosphatonin, is the basis of tumor-induced osteomalacia. Thus, overproduction of FGF-23 causes tumor-induced osteomalacia, whereas mutations in the FGF-23 gene result in autosomal hypophosphatemic rickets possibly by preventing proteolytic cleavage, which enhances the biologic activity of FGF-23. The mutations in FGF-23 found in ADHR lie within 3 nucleotides of each other in the proprotein convertase cleavage site. Jonsson et al. (2003) showed that FGF-23 is readily detectable in the plasma or serum of healthy persons and can be markedly elevated in those with oncogenic osteomalacia or X-linked hypophosphatemia, suggesting that this growth factor has a role in phosphate homeostasis.

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Total 137 AA. MW: 15.45 kDa (calculated). UniProtKB acc.no. P07148. N-Terminal His-tag, 10 extra AA

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Total 140 AA. MW: 15.93 kDa (calculated). N-Terminal His-tag (9 extra AA)

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Osteoactivin (OA), also known as Dchil (dendritic cell-associated, heparin sulfate proteoglycan-dependent integrin ligand), Gpnmb (glycoprotein non-metastatic melanomal protein B), or Hgfin (hematopoietic growth factor-inducible neurokinin 1), is a transmembrane glycoprotein. The OA gene, located on human chromosome 7p15.1 encodes a protein of 572 amino acid residues. OA may exist as a 65-kD unglycosylated cellular protein or as multiple glycosylated proteins with molecular size varying between 80-kD to 139-kD. Glycosylation of proteins plays a crucial role in cell differentiation and function. The transmembrane OA can be proteolytically cleaved by extracellular proteases, such as ADAMs and MMPs, in a process called ectodomain shedding, which results in the detachment and release of the extracellular domains which act as cytokines or growth factors. OA is expressed in a wide array of tissues and plays a regulatory role in various cellular functions. OA expression is associated with cell differentiation with high expression levels of OA protein found in the nervous system, basal layer of the skin, germinal cells of hair follicles, and in developing nephrons of the kidney in mouse embryos. In immune cells, OA was detected in differentiated macrophages, lymphocytes, and dendritic cells, but undetectable in proliferating hematopoietic progenitors.

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Regenerating (Reg) gene family belongs to the calcium depending lectin gene super family. It represents a group of small, multi‑functional secreted proteins, which can function as acute phase reactants, lectins and anti‑apoptotic or growth agents. These agents play an important role in proliferation and differentiation in the entire GI tract. The Reg family consists of seven members in mice (Reg I, Reg II, Reg IIIa, Reg IIIb, Reg IIId and Reg IIIge and Reg IV). Four members are recognized in humans (Reg Ia, Reg Ib, Reg III and Reg IV), but there are most probably a few more. Reg genes are up‑regulated following tissue injury, and play a major role in the healing of gastrointestinal mucosal lesions. Different members of the Reg gene family were shown to be expressed in pancreatic, gastric and colorectal cancers, and may serve as markers for poor prognosis. Reg IV, a novel member of the family, was suggested to play an important role in initiating the multi‑step process of colorectal cancer carcinogenesis, at the level of adenoma, by increasing the resistance for programmed cell death. Regenerating gene family member 4 (REG4) was originally identified by sequencing of a cDNA library derived from patients with inflammatory bowel disease.

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Alpha-2 Macroglobulin is a serine proteases inhibitor, which inhibits coagulation by inactivating thrombin and Kallikrein, it inhibits fibrinolysis by inactivating plasmin and involved in insulin transport. Alpha-2-Macroglobulin is a large plasma protein, which is produced by the liver, it’s composed of 4 identical subunits bound together by -S-S- bonds. A2M is able to inactivate many kinds of proteinases (including serine-, cysteine-, aspartic- and metalloproteinases). A2M has a 35 amino acid "bait" region in its structure. Proteinases bind and cleave the “bait” region become bound to A2M. Macrophage receptors recognize the proteinase-A2M complex and clear it from the system. A2M binds to and removes MMP-2 and MMP-9 (active forms of the gelatinase) from the circulation using scavenger receptors on the phagocytes. The levels of Alpha-2-macroglobulin are increased in nephrotic syndrome which is a condition where the kidneys start to leak out some of the smaller blood proteins. Due to its large size, A2-macroglobulin is retained in the bloodstream. Increased production of all proteins causes A2-macroglobulin concentration to increase. Chronic renal failure might lead to amyloid by alpha-2-macroglobulin. A2M is raised in cirrhosis, pregnancy and diabetes.

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Cystatin C is a non-glycosilated basic single-chain protein consisting of 120 amino acids with a molecular weight of 13.36 kDa and is characterized by two disulfide bonds in the carboxy-terminal region. It belongs to the cystatins superfamilly which inactivates lysosomal cysteine proteinases, e.g. cathepsin B, H,.K, L and S. Imbalance between Cystatin C and cysteine proteinases is associated with inflammation, renal failure, cancer, Alzheimer's disease, multiple sclerosis and hereditary Cystatin C amyloid angiopathy. Its increased level has been found in patients with autoimune diseases, with colorectal tumors and in patients on dyalisis. Serum Cystatin C seems to be better marker of glomerular filtration rate than creatinine. On the other hand, low concentration of Cystatin C presents a risk factor for secondary cardiovascular events.

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Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 aminoacid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells. The protein belongs to the soluble defence collagen superfamily; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. Adiponectin forms homotrimers, which are the building blocks for higher order complexes found circulating in serum. Together, these complexes make up approximately 0.01% of total serum protein. Adiponectin receptors AdipoR1 and AdipoR2 have been recently cloned; AdipoR1 is abundantly expressed in skeletal muscle, whereas AdipoR2 is predominantly expressed in the liver. Paradoxically, adipose tissue-expressed adiponectin levels are inversely related to the degree of adiposity. Adiponectin concentrations correlate negatively with glucose, insulin, triglyceride concentrations, liver fat content and body mass index and positively with high-density lipoprotein-cholesterol levels, hepatic insulin sensitivity and insulin-stimulated glucose disposal.

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Interactions of PEDF with three different types of molecules have been discovered: glycosaminoglycans of extracellular matrixes, collagens and receptors on the surface of neuronal cells. Negatively charged, acidic PEDF binds to collagen, lacks neurotrophic activity, and may confer antiangiogenic properties. PEDF has gliastatic, neuronotrophic, neuroprotective and antitumorigenic properties. PEDF acts in neuronal differentiation and survival in cells derived from retina and the central nervous system .