Glycoprotein found in alpha(1)-globulin region in human serum. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. It is a member of the serpin superfamily.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.
A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.
The use of fluorescence spectrometry to obtain quantitative results for the FLUORESCENT ANTIBODY TECHNIQUE. One advantage over the other methods (e.g., radioimmunoassay) is its extreme sensitivity, with a detection limit on the order of tenths of microgram/liter.
A mammalian pancreatic extract composed of enzymes with protease, amylase and lipase activities. It is used as a digestant in pancreatic malfunction.
Immunoelectrophoresis in which a second electrophoretic transport is performed on the initially separated antigen fragments into an antibody-containing medium in a direction perpendicular to the first electrophoresis.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
Proteins that are secreted into the blood in increased or decreased quantities by hepatocytes in response to trauma, inflammation, or disease. These proteins can serve as inhibitors or mediators of the inflammatory processes. Certain acute-phase proteins have been used to diagnose and follow the course of diseases or as tumor markers.
A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.
A glycoprotein that is a kallikrein-like serine proteinase and an esterase, produced by epithelial cells of both normal and malignant prostate tissue. It is an important marker for the diagnosis of prostate cancer.
Deficiency of the protease inhibitor ALPHA 1-ANTITRYPSIN that manifests primarily as PULMONARY EMPHYSEMA and LIVER CIRRHOSIS.
Orosomucoid, also known as alpha-1-acid glycoprotein, is an acute phase protein involved in the immune response, functioning as a pattern recognition receptor and having the ability to bind various ligands including drugs and hormones.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.
An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.
A member of the serpin family of proteins that is found in plasma and urine. It is dependent on heparin and is able to inhibit activated PROTEIN C; THROMBIN; KALLIKREIN; and other SERINE ENDOPEPTIDASES.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.
A benign neoplasm derived from connective tissue, consisting chiefly of polyhedral and stellate cells that are loosely embedded in a soft mucoid matrix, thereby resembling primitive mesenchymal tissue. It occurs frequently intramuscularly where it may be mistaken for a sarcoma. It appears also in the jaws and the skin. (From Stedman, 25th ed)
Tumors in any part of the heart. They include primary cardiac tumors and metastatic tumors to the heart. Their interference with normal cardiac functions can cause a wide variety of symptoms including HEART FAILURE; CARDIAC ARRHYTHMIAS; or EMBOLISM.
The type species of LEPORIPOXVIRUS causing infectious myxomatosis, a severe generalized disease, in rabbits. Tumors are not always present.
Pigmentation disorders are conditions that affect the production or distribution of melanin, the pigment responsible for skin, hair, and eye color, leading to changes in the color of these bodily features.
Solitary or multiple benign cutaneous nodules comprised of immature and mature vascular structures intermingled with endothelial cells and a varied infiltrate of eosinophils, histiocytes, lymphocytes, and mast cells.
A sarcoma, usually a liposarcoma or malignant fibrous histiocytoma, with an abundant component of myxoid tissue resembling primitive mesenchyme containing connective tissue mucin. (Stedman, 25th ed)
A type I cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a lower affinity for cAMP than the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIBETA SUBUNIT.

Genes, oxidative stress, and the risk of chronic obstructive pulmonary disease. (1/204)

BACKGROUND: The first-pass metabolism of foreign compounds in the lung is an important protective mechanism against oxidative stress. We investigated whether polymorphisms in the gene for microsomal epoxide hydrolase (mEPHX), an enzyme involved in this protective process, had any bearing on individual susceptibility to the development of chronic obstructive pulmonary disease (COPD) and emphysema. METHODS: We designed PCR-based genotyping assays to detect variant forms of mEPHX that confer slow and fast activity. We used these assays to screen 203 blood-donor controls and groups of patients with asthma (n = 57), lung cancer (n = 50), COPD (n = 68), and emphysema (n = 94), who were attending specialised clinics in Edinburgh, UK. FINDINGS: The proportion of individuals with innate slow mEPHX activity (homozygotes) was significantly higher in both the COPD group and the emphysema group than in the control group (COPD 13 [19%] vs control 13 [6%]; emphysema 21 [22%] vs 13 [6%]). The odds ratios for homozygous slow activity versus all other phenotypes were 4.1 (95% CI 1.8-9.7) for COPD and 5.0 (2.3-10.9) for emphysema. INTERPRETATION: Genetic polymorphisms in xenobiotic enzymes may have a role in individual susceptibility to oxidant-related lung disease. Epoxide derivatives of cigarette-smoke components may be the cause of some of the lung damage characteristics of these diseases.  (+info)

Giardia intestinalis is unlikely to be a major cause of the poor growth of rural Gambian infants. (2/204)

Parasite-specific plasma immunoglobulins have been used to indicate the presence of Giardia intestinalis infection in 60 infants living in a rural area of The Gambia. Infants were studied longitudinally between 2 and 8 mo of age. The median age for first exposure to G. intestinalis was between 3 and 4 mo, and by 8 mo all but 3 infants (95%) showed a positive titer on at least one occasion. Raised Giardia-specific IgM titers were associated with reduced weight gain in the 2 wk preceding a positive titer, but catch-up growth occurred in the following 2 wk. IgM antibody titers were also positively associated with intestinal permeability (lactulose/mannitol ratio), urinary lactose excretion, plasma concentrations of alpha1-antichymotrypsin and total IgM, IgA and IgG immunoglobulins. However, infant growth over the whole 6-mo period (i.e., between 2 and 8 mo of age) was not related to mean Giardia-specific antibody titers, nor the time of first exposure to the parasite. The data suggest that giardiasis in these very young breast-fed children occurs as a mild, acute disease, and its presence could not explain the marked, long-term growth faltering observed in many of the subjects.  (+info)

Anti-free prostate-specific antigen monoclonal antibody epitopes defined by mimotopes and molecular modeling. (3/204)

BACKGROUND: Prostate-specific antigen (PSA) is an important marker for the diagnosis and management of prostate cancer, and the free PSA/total PSA ratio has been shown to be efficient for distinguishing prostate cancer from benign prostatic hyperplasia. We report here the characterization of seven mouse monoclonal antibodies (mAbs) and the partial localization of two conformational epitopes identified by anti-free PSA mAbs. METHODS: The mAbs were studied by competition and sandwich assays, and the epitope localization of the two anti-free PSA mAbs (6C8D8 and 5D3D11) was performed using phage displayed peptide libraries and molecular modeling. RESULTS: The seven mAbs were classified into three groups according to their recognition specificities and their ability to inhibit the enzymatic activity of PSA and the formation of PSA-alpha1-antichymotrypsin (ACT) complex. Among the anti-free PSA mAb group, 6C8D8 recognized the phage displayed peptide RKLRPHWLHFHPVAV, two parts of which presented similarities with two regions distant on the PSA sequence but joined in the tridimensional structure. mAb 5D3D11 recognized the peptide DTPYPWGWLLDEGYD, which is similar to a PSA region located on the board of the groove containing the PSA enzymatic site. Both epitopes were located in the theoretical ACT binding site described previously. Moreover, these mAbs were able to inhibit the enzymatic activity of PSA. CONCLUSIONS: These epitope localizations are in agreement with the ability of both mAbs to inhibit enzymatic activity and ACT fixation. The results presented here could bring information for the generation of clinically relevant PSA assays.  (+info)

Highly sensitive automated chemiluminometric assay for measuring free human glandular kallikrein-2. (4/204)

BACKGROUND: Human glandular kallikrein (hK2) is a serine protease that has 79% amino acid identity with prostate-specific antigen (PSA). Both free hK2 and hK2 complexed to alpha1-antichymotrypsin (ACT) are present in the blood in low concentrations. We wished to measure hK2 in serum with limited contribution from hK2-ACT for the results. METHODS: We developed an automated assay for hK2 with use of a select pair of monoclonal antibodies. The prototype assay was implemented on a Beckman Coulter ACCESS(R) analyzer. RESULTS: The detection limit of the assay was 1.5 ng/L, the "functional sensitivity" (day-to-day CV <15%) was <4 ng/L, cross-reactivity with PSA and PSA-ACT was negligible, and cross-reactivity with hK2-ACT was 2%. After surgical removal of prostate glands, serum hK2 was <7 ng/L and was <15 ng/L in most healthy women. The median serum concentration of hK2 in healthy men without prostate cancer was 26 ng/L. The median concentration of hK2 was 72 ng/L for men having prostate cancer with lower Gleason scores compared with 116 ng/L for men with more advanced cancer. The concentration of hK2 correlated weakly with PSA, with the mean hK2 concentrations generally 30- to 80-fold lower than PSA concentrations. CONCLUSION: The availability of a robust, high sensitivity automated assay for hK2 should facilitate further investigations of the role of hK2 measurements in the management of patients with prostate disease.  (+info)

Measurement of the complex between prostate-specific antigen and alpha1-protease inhibitor in serum. (5/204)

BACKGROUND: Prostate-specific antigen (PSA) occurs in serum both free and in complex with protease inhibitors. The complex with alpha1-antichymotrypsin (ACT) is the major form in serum, and the proportion of PSA-ACT is higher in prostate cancer (PCa) than in benign prostatic hyperplasia (BPH). PSA also forms a complex with alpha1-protease inhibitor (API) in vitro, and the PSA-ACT complex has been detected in serum from patients with prostate cancer. The aim of the present study was to develop a quantitative method for the determination of PSA-API and to determine the serum concentrations in patients with PCa and BPH. METHODS: The assay for PSA-API utilizes a monoclonal antibody to PSA as capture and a polyclonal antibody to API labeled with a Eu-chelate as a tracer. For calibrators, PSA-API formed in vitro was used. Serum samples were obtained before treatment from 82 patients with PCa, from 66 patients with BPH, and from 22 healthy females. RESULTS: The concentrations of PSA-API are proportional to the concentrations of total PSA. PSA-API comprises 1.0-7.9% (median, 2.4%) of total immunoreactive PSA in PCa and 1.3-12.2% (median, 3.6%) in BPH patients with serum PSA concentrations >4 microgram/L. In patients with 4-20 microgram/L total PSA, the proportion of PSA-API serum is significantly higher in BPH (median, 4.1%) than in PCa (median, 3. 2%; P = 0.02). CONCLUSIONS: The proportion of PSA-API in serum is lower in patients with PCa than in those with BPH. These results suggest that PSA-API is a potential adjunct to total and free PSA in the diagnosis of prostate cancer.  (+info)

Antichymotrypsin interaction with chymotrypsin. Intermediates on the way to inhibited complex formation. (6/204)

Serpins form enzymatically inactive covalent complexes (designated E*I*) with their target proteinases, corresponding most likely to the acyl enzyme that resembles the normal intermediate in substrate turnover. Formation of E*I* involves large changes in the conformation of the reactive center loop (residues P17 to P9') and of the serpin molecule in general. The "hinge" region of the reactive center loop, including residues P10-P14, shows facile movement in and out of beta-sheet A, and this movement appears to be crucial in determining whether E*I* is formed (the inhibitor pathway) or whether I is rapidly hydrolyzed to I* (the substrate pathway). Here, we report stopped-flow and rapid quench studies investigating the pH dependence of the conversion of the alpha1-antichymotrypsin.alpha-chymotrypsin encounter complex, E.I, to E*I*. These studies utilize fluorescent derivatives of cysteine variants of alpha1-antichymotrypsin at the P11 and P13 residues. Our results demonstrate three identifiable intermediates, EIa, EIb, and EIc, between E.I and E*I* and permit informed speculation regarding the nature of these intermediates. Partitioning between inhibitor and substrate pathways occurs late in the process of E*I* formation, most likely from a species occurring between EIc and E*I*.  (+info)

Comparative study of assays for prostate-specific antigen molecular forms. (7/204)

BACKGROUND: The detection of prostate-specific antigen (PSA) molecular forms such as free PSA and PSA-ACT and the use of PSA molecular ratios, especially the percentage of free to total PSA, have been reported to improve the diagnostic accuracy of prostate cancer in the patients with slightly elevated serum PSA values. However, the correlation among the values of serum free PSA or PSA-ACT obtained in various assays remains unclear. METHODS: Serum free PSA and PSA-ACT values were detected with the following assays: Hybritech, DPC, EIKEN, Abbott, Roche and Can-Ag for free PSA and Dainippon, Chugai, EIKEN and Bayer for PSA-ACT. The data obtained with each assay were compared with Hybritech (free PSA) and Dainippon (PSA-ACT) as standards. RESULTS: The free PSA data obtained with the Hybritech, EIKEN, Abbott and Can-Ag kits were similar. The values obtained with the DPC and Roche kits showed a linear regression of y = ax + b with those obtained with the Hybritech, with a b value of zero and an a value of 1.20 and 1.57, respectively. The serum PSA-ACT values detected with the Dainippon and Chugai kits were identical. The equation for converting the data obtained with the EIKEN kits to the Dainippon value was 0.7636 x (EIKEN) + 0.1381. CONCLUSIONS: Serum free PSA and PSA-ACT values obtained with various assays were not necessarily the same. Some kits for the assay of free PSA and PSA-ACT gave the same serum values. The free PSA values obtained with the other kits could be converted using appropriate equations. The gamma-Sm values showed wide variations and were not considered suitable as a measurement of free PSA.  (+info)

Effect of the ratio of free to total prostate-specific antigen on interassay variability in proficiency test samples. (8/204)

BACKGROUND: Up to sevenfold differences were observed between total prostate-specific antigen (PSA) methods for New York State Proficiency Test samples prepared with seminal fluid PSA in human female serum. Because the PSA was mainly in its free form under these conditions, we wanted to determine whether a defined mixture of free and complexed PSA would reduce the interassay differences. METHODS: We prepared a series of five solutions of 60 g/L bovine serum albumin with 10 microgram/L total PSA consisting of varied proportions of free, noncomplexible PSA, and alpha(1)-antichymotrypsin (ACT)-complexed PSA from 0% to 100%. Two hundred seventy laboratories measured the total PSA in these samples, and 16 laboratories also analyzed the samples for free PSA. The results were used to calculate free/total PSA ratios. RESULTS: Interassay CVs for total PSA measurements were approximately 7% at 10-15% free PSA but became gradually larger as the free/total PSA ratio increased. Measured free-PSA concentrations were similar within each sample (mean CV, 12%), and the results were relatively independent of the proportion of free PSA in the samples. Twofold discrepancies between actual and expected ratios were observed with some methods at 100% free PSA and to a lesser degree at 30% free PSA. At 100% free PSA, the relatively higher total-PSA values measured by nonequimolar methods yielded low free/total PSA ratios of 50-60%. In contrast, the lower total PSA values obtained by equimolar methods yielded ratios close to the expected 100%. CONCLUSIONS: Preparing proficiency test samples with a 10:90 mixture of free, noncomplexible PSA:PSA-ACT is a viable alternative to the use of seminal fluid PSA. Furthermore, the method used to measure total PSA may have a substantial impact on the calculated proportion of free PSA and hence may have clinical relevance.  (+info)

Alpha 1-Antichymotrypsin (ACT), also known as Serpin A1, is a protein found in the blood that belongs to the serine protease inhibitor family. It functions to regulate enzymes that break down other proteins in the body. ACT helps to prevent excessive and potentially harmful proteolytic activity, which can contribute to tissue damage and inflammation.

Deficiency or dysfunction of alpha 1-Antichymotrypsin has been associated with several medical conditions, including:

1. Alpha 1-Antichymotrypsin Deficiency: A rare genetic disorder characterized by low levels of ACT in the blood, which can lead to increased risk of developing lung and liver diseases.
2. Alzheimer's Disease: Increased levels of ACT have been found in the brains of individuals with Alzheimer's disease, suggesting a possible role in the pathogenesis of this neurodegenerative disorder.
3. Cancer: Elevated levels of ACT have been observed in various types of cancer, including lung, breast, and prostate cancers, potentially contributing to tumor growth and metastasis.
4. Inflammatory and immune-mediated disorders: Increased ACT levels are associated with several inflammatory conditions, such as rheumatoid arthritis, systemic lupus erythematosus (SLE), and vasculitis, suggesting its involvement in the regulation of the immune response.
5. Cardiovascular diseases: Elevated ACT levels have been linked to an increased risk of developing cardiovascular diseases, including atherosclerosis and myocardial infarction (heart attack).

Understanding the role of alpha 1-Antichymotrypsin in various physiological and pathological processes can provide valuable insights into disease mechanisms and potential therapeutic targets.

Alpha 1-antitrypsin (AAT, or α1-antiproteinase, A1AP) is a protein that is primarily produced by the liver and released into the bloodstream. It belongs to a group of proteins called serine protease inhibitors, which help regulate inflammation and protect tissues from damage caused by enzymes involved in the immune response.

Alpha 1-antitrypsin is particularly important for protecting the lungs from damage caused by neutrophil elastase, an enzyme released by white blood cells called neutrophils during inflammation. In the lungs, AAT binds to and inhibits neutrophil elastase, preventing it from degrading the extracellular matrix and damaging lung tissue.

Deficiency in alpha 1-antitrypsin can lead to chronic obstructive pulmonary disease (COPD) and liver disease. The most common cause of AAT deficiency is a genetic mutation that results in abnormal folding and accumulation of the protein within liver cells, leading to reduced levels of functional AAT in the bloodstream. This condition is called alpha 1-antitrypsin deficiency (AATD) and can be inherited in an autosomal codominant manner. Individuals with severe AATD may require augmentation therapy with intravenous infusions of purified human AAT to help prevent lung damage.

Chymotrypsin is a proteolytic enzyme, specifically a serine protease, that is produced in the pancreas and secreted into the small intestine as an inactive precursor called chymotrypsinogen. Once activated, chymotrypsin helps to digest proteins in food by breaking down specific peptide bonds in protein molecules. Its activity is based on the recognition of large hydrophobic side chains in amino acids like phenylalanine, tryptophan, and tyrosine. Chymotrypsin plays a crucial role in maintaining normal digestion and absorption processes in the human body.

Serine proteinase inhibitors, also known as serine protease inhibitors or serpins, are a group of proteins that inhibit serine proteases, which are enzymes that cut other proteins in a process called proteolysis. Serine proteinases are important in many biological processes such as blood coagulation, fibrinolysis, inflammation and cell death. The inhibition of these enzymes by serpin proteins is an essential regulatory mechanism to maintain the balance and prevent uncontrolled proteolytic activity that can lead to diseases.

Serpins work by forming a covalent complex with their target serine proteinases, irreversibly inactivating them. The active site of serpins contains a reactive center loop (RCL) that mimics the protease's target protein sequence and acts as a bait for the enzyme. When the protease cleaves the RCL, it gets trapped within the serpin structure, leading to its inactivation.

Serpin proteinase inhibitors play crucial roles in various physiological processes, including:

1. Blood coagulation and fibrinolysis regulation: Serpins such as antithrombin, heparin cofactor II, and protease nexin-2 control the activity of enzymes involved in blood clotting and dissolution to prevent excessive or insufficient clot formation.
2. Inflammation modulation: Serpins like α1-antitrypsin, α2-macroglobulin, and C1 inhibitor regulate the activity of proteases released during inflammation, protecting tissues from damage.
3. Cell death regulation: Some serpins, such as PI-9/SERPINB9, control apoptosis (programmed cell death) by inhibiting granzyme B, a protease involved in this process.
4. Embryonic development and tissue remodeling: Serpins like plasminogen activator inhibitor-1 (PAI-1) and PAI-2 regulate the activity of enzymes involved in extracellular matrix degradation during embryonic development and tissue remodeling.
5. Neuroprotection: Serpins such as neuroserpin protect neurons from damage by inhibiting proteases released during neuroinflammation or neurodegenerative diseases.

Dysregulation of serpins has been implicated in various pathological conditions, including thrombosis, emphysema, Alzheimer's disease, and cancer. Understanding the roles of serpins in these processes may provide insights into potential therapeutic strategies for treating these diseases.

Cathepsin G is a serine protease, which is a type of enzyme that breaks down other proteins. It is produced and released by neutrophils, a type of white blood cell that plays an important role in the body's immune response to infection. Cathepsin G helps to digest and kill microorganisms that have invaded the body. It can also contribute to tissue damage and inflammation in certain diseases, such as rheumatoid arthritis and cystic fibrosis.

SERPINs are an acronym for "serine protease inhibitors." They are a group of proteins that inhibit serine proteases, which are enzymes that cut other proteins. SERPINs are found in various tissues and body fluids, including blood, and play important roles in regulating biological processes such as inflammation, blood clotting, and cell death. They do this by forming covalent complexes with their target proteases, thereby preventing them from carrying out their proteolytic activities. Mutations in SERPIN genes have been associated with several genetic disorders, including emphysema, cirrhosis, and dementia.

A fluoroimmunoassay (FIA) is a type of biochemical test that uses fluorescence to detect and measure the presence or concentration of a specific component, such as a protein or hormone, in a sample. In a FIA, the sample is mixed with a reagent that contains a fluorescent label, which binds to the target component. When the mixture is exposed to light of a specific wavelength, the labeled component emits light at a different wavelength, allowing it to be detected and measured.

FIAs are often used in clinical laboratories to diagnose and monitor various medical conditions, as they can provide sensitive and accurate measurements of specific components in biological samples. They are also used in research settings to study the interactions between biomolecules and to develop new diagnostic tests.

Pancreatin is a mixture of digestive enzymes, including amylase, lipase, and proteases, naturally produced by the pancreas in humans and other mammals. These enzymes aid in the digestion of carbohydrates, fats, and proteins, respectively, in the small intestine. Pancreatin is often used as a replacement therapy for individuals with conditions like cystic fibrosis, chronic pancreatitis, or pancreatectomy, who have impaired pancreatic function and struggle to digest food properly. It can be obtained from animal pancreases, typically from pigs, and is available in various forms such as tablets, capsules, or powders for medical use.

Two-dimensional immunoelectrophoresis (2DE) is a specialized laboratory technique used in the field of clinical pathology and immunology. This technique is a refined version of traditional immunoelectrophoresis that adds an additional electrophoretic separation step, enhancing its resolution and allowing for more detailed analysis of complex protein mixtures.

In two-dimensional immunoelectrophoresis, proteins are first separated based on their isoelectric points (pI) in the initial dimension using isoelectric focusing (IEF). This process involves applying an electric field to a protein mixture contained within a gel matrix, where proteins will migrate and stop migrating once they reach the pH that matches their own isoelectric point.

Following IEF, the separated proteins are then subjected to a second electrophoretic separation in the perpendicular direction (second dimension) based on their molecular weights using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). SDS is a negatively charged molecule that binds to proteins, giving them a uniform negative charge and allowing for separation based solely on size.

Once the two-dimensional separation is complete, the gel is then overlaid with specific antisera to detect and identify proteins of interest. The resulting precipitin arcs formed at the intersection of the antibody and antigen are compared to known standards or patterns to determine the identity and quantity of the separated proteins.

Two-dimensional immunoelectrophoresis is particularly useful in identifying and quantifying proteins in complex mixtures, such as those found in body fluids like serum, urine, or cerebrospinal fluid (CSF). It can be applied to various clinical scenarios, including diagnosis and monitoring of monoclonal gammopathies, autoimmune disorders, and certain infectious diseases.

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

Acute-phase proteins (APPs) are a group of plasma proteins whose concentrations change in response to various inflammatory conditions, such as infection, trauma, or tissue damage. They play crucial roles in the body's defense mechanisms and help mediate the innate immune response during the acute phase of an injury or illness.

There are several types of APPs, including:

1. C-reactive protein (CRP): Produced by the liver, CRP is one of the most sensitive markers of inflammation and increases rapidly in response to various stimuli, such as bacterial infections or tissue damage.
2. Serum amyloid A (SAA): Another liver-derived protein, SAA is involved in lipid metabolism and immune regulation. Its concentration rises quickly during the acute phase of inflammation.
3. Fibrinogen: A coagulation factor produced by the liver, fibrinogen plays a vital role in blood clotting and wound healing. Its levels increase during inflammation.
4. Haptoglobin: This protein binds free hemoglobin released from red blood cells, preventing oxidative damage to tissues. Its concentration rises during the acute phase of inflammation.
5. Alpha-1 antitrypsin (AAT): A protease inhibitor produced by the liver, AAT helps regulate the activity of enzymes involved in tissue breakdown and repair. Its levels increase during inflammation to protect tissues from excessive proteolysis.
6. Ceruloplasmin: This copper-containing protein is involved in iron metabolism and antioxidant defense. Its concentration rises during the acute phase of inflammation.
7. Ferritin: A protein responsible for storing iron, ferritin levels increase during inflammation as part of the body's response to infection or tissue damage.

These proteins have diagnostic and prognostic value in various clinical settings, such as monitoring disease activity, assessing treatment responses, and predicting outcomes in patients with infectious, autoimmune, or inflammatory conditions.

Pancreatic elastase is a type of elastase that is specifically produced by the pancreas. It is an enzyme that helps in digesting proteins found in the food we eat. Pancreatic elastase breaks down elastin, a protein that provides elasticity to tissues and organs in the body.

In clinical practice, pancreatic elastase is often measured in stool samples as a diagnostic tool to assess exocrine pancreatic function. Low levels of pancreatic elastase in stool may indicate malabsorption or exocrine pancreatic insufficiency, which can be caused by various conditions such as chronic pancreatitis, cystic fibrosis, or pancreatic cancer.

Prostate-Specific Antigen (PSA) is a glycoprotein enzyme produced by the epithelial cells of the prostate gland. It is primarily involved in liquefying semen after ejaculation, allowing sperm mobility.

In clinical medicine, PSA is used as a tumor marker, mainly for monitoring the treatment and recurrence of prostate cancer. Elevated levels of PSA can indicate inflammation, infection, benign prostatic hyperplasia (BPH), or prostate cancer. However, it's important to note that an elevated PSA level does not necessarily confirm cancer; further diagnostic tests like digital rectal examination, transrectal ultrasound, and prostate biopsy are often required for definitive diagnosis.

Doctors may also use PSA isoforms or derivatives, such as free PSA, total PSA, and PSA density, to help improve the specificity of cancer detection and differentiate between malignant and benign conditions.

Alpha 1-Antitrypsin (AAT) deficiency is a genetic disorder that results from insufficient levels of the protective protein AAT in the blood and lungs. This protein is produced by the liver and helps to protect the lungs from damage caused by inflammation and the action of enzymes, such as neutrophil elastase, that are released during the immune response.

In people with AAT deficiency, the lack of adequate AAT levels leads to an uncontrolled increase in neutrophil elastase activity, which can cause damage to lung tissue and result in emphysema, a condition characterized by shortness of breath, coughing, and wheezing. Additionally, some individuals with AAT deficiency may develop liver disease due to the accumulation of abnormal AAT proteins in liver cells.

There are different variants or genotypes associated with AAT deficiency, with the most common and severe form being the PiZZ genotype. This variant is caused by mutations in the SERPINA1 gene, which encodes for the AAT protein. Individuals who inherit two copies of this mutated gene (one from each parent) will have very low levels of AAT in their blood and are at increased risk of developing emphysema and liver disease.

Diagnosis of AAT deficiency typically involves measuring AAT levels in the blood and performing genetic testing to identify specific variants of the SERPINA1 gene. Treatment may include lifestyle modifications, such as smoking cessation, bronchodilators, and corticosteroids to manage lung symptoms, as well as augmentation therapy with intravenous infusions of AAT protein to help slow disease progression in individuals with severe deficiency. Liver transplantation may be considered for those with advanced liver disease.

Orosomucoid, also known as α-1-acid glycoprotein or AAG, is a protein found in human plasma. It's a member of the acute phase proteins, which are produced in higher amounts during inflammation and infection. Orosomucoid has a molecular weight of approximately 41-43 kDa and is composed of a single polypeptide chain with five N-linked glycosylation sites. It plays a role in protecting tissues from various harmful substances, such as proteases and oxidants, by binding to them and preventing their interaction with cells. Additionally, orosomucoid has been studied as a potential biomarker for several diseases due to its altered levels during inflammation and cancer.

Serine endopeptidases are a type of enzymes that cleave peptide bonds within proteins (endopeptidases) and utilize serine as the nucleophilic amino acid in their active site for catalysis. These enzymes play crucial roles in various biological processes, including digestion, blood coagulation, and programmed cell death (apoptosis). Examples of serine endopeptidases include trypsin, chymotrypsin, thrombin, and elastase.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

Trypsin inhibitors are substances that inhibit the activity of trypsin, an enzyme that helps digest proteins in the small intestine. Trypsin inhibitors can be found in various foods such as soybeans, corn, and raw egg whites. In the case of soybeans, trypsin inhibitors are denatured and inactivated during cooking and processing.

In a medical context, trypsin inhibitors may be used therapeutically to regulate excessive trypsin activity in certain conditions such as pancreatitis, where there is inflammation of the pancreas leading to the release of activated digestive enzymes, including trypsin, into the pancreas and surrounding tissues. By inhibiting trypsin activity, these inhibitors can help reduce tissue damage and inflammation.

Leukocyte elastase is a type of enzyme that is released by white blood cells (leukocytes), specifically neutrophils, during inflammation. Its primary function is to help fight infection by breaking down the proteins in bacteria and viruses. However, if not properly regulated, leukocyte elastase can also damage surrounding tissues, contributing to the progression of various diseases such as chronic obstructive pulmonary disease (COPD), acute respiratory distress syndrome (ARDS), and cystic fibrosis.

Leukocyte elastase is often measured in clinical settings as a marker of inflammation and neutrophil activation, particularly in patients with lung diseases. Inhibitors of leukocyte elastase have been developed as potential therapeutic agents for these conditions.

Protein C inhibitor is a natural anticoagulant protein found in the blood. It plays a crucial role in regulating the coagulation system by controlling the activity of activated protein C, which is a key enzyme that helps to break down clots and prevent excessive bleeding. Protein C inhibitor works by binding to and inhibiting the activity of activated protein C, thereby ensuring that the coagulation process is balanced and that clots are formed only when necessary.

Inherited or acquired deficiencies in protein C inhibitor can lead to an increased risk of thrombosis or abnormal blood clotting, which can cause serious health complications such as deep vein thrombosis (DVT), pulmonary embolism (PE), and disseminated intravascular coagulation (DIC). Therefore, protein C inhibitor is an essential component of the coagulation system and its activity is tightly regulated to maintain normal hemostasis.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Alpha-macroglobulins are a type of large protein molecule found in blood plasma, which play a crucial role in the human body's immune system. They are called "macro" globulins because of their large size, and "alpha" refers to their electrophoretic mobility, which is a laboratory technique used to separate proteins based on their electrical charge.

Alpha-macroglobulins function as protease inhibitors, which means they help regulate the activity of enzymes called proteases that can break down other proteins in the body. By inhibiting these proteases, alpha-macroglobulins help protect tissues and organs from excessive protein degradation and also help maintain the balance of various biological processes.

One of the most well-known alpha-macroglobulins is alpha-1-antitrypsin, which helps protect the lungs from damage caused by inflammation and protease activity. Deficiencies in this protein have been linked to lung diseases such as emphysema and chronic obstructive pulmonary disease (COPD).

Overall, alpha-macroglobulins are an essential component of the human immune system and play a critical role in maintaining homeostasis and preventing excessive tissue damage.

A myxoma is a type of benign (non-cancerous) tumor that develops in the heart, specifically in the heart's chambers or valves. It is the most common primary cardiac tumor in adults and typically affects the left atrium. Myxomas are composed of gelatinous, mucoid material and may have a stalk-like attachment to the endocardium (the inner lining of the heart).

Myxomas can vary in size and may cause symptoms such as shortness of breath, fatigue, chest pain, coughing, and fever. These symptoms are due to obstruction of blood flow within the heart or embolization (detachment and travel) of tumor fragments to other parts of the body. Surgical removal is usually required to treat myxomas, as they can lead to serious complications if left untreated.

Heart neoplasms are abnormal growths or tumors that develop within the heart tissue. They can be benign (noncancerous) or malignant (cancerous). Benign tumors, such as myxomas and rhabdomyomas, are typically slower growing and less likely to spread, but they can still cause serious complications if they obstruct blood flow or damage heart valves. Malignant tumors, such as angiosarcomas and rhabdomyosarcomas, are fast-growing and have a higher risk of spreading to other parts of the body. Symptoms of heart neoplasms can include shortness of breath, chest pain, fatigue, and irregular heart rhythms. Treatment options depend on the type, size, and location of the tumor, and may include surgery, radiation therapy, or chemotherapy.

Myxoma virus (MYXV) is a member of the Poxviridae family, specifically in the Leporipoxvirus genus. It is a double-stranded DNA virus that naturally infects European rabbits (Oryctolagus cuniculus) and causes a fatal disease called myxomatosis. The virus is transmitted through insect vectors such as mosquitoes and fleas, and it replicates in the cytoplasm of infected cells.

Myxoma virus has been studied extensively as a model organism for viral pathogenesis and host-pathogen interactions. It has also been explored as a potential oncolytic virus for cancer therapy due to its ability to selectively infect and kill certain types of cancer cells while leaving normal cells unharmed. However, it is important to note that the use of Myxoma virus in humans is still experimental and requires further research and development before it can be considered safe and effective for therapeutic purposes.

Pigmentation disorders are conditions that affect the production or distribution of melanin, the pigment responsible for the color of skin, hair, and eyes. These disorders can cause changes in the color of the skin, resulting in areas that are darker (hyperpigmentation) or lighter (hypopigmentation) than normal. Examples of pigmentation disorders include melasma, age spots, albinism, and vitiligo. The causes, symptoms, and treatments for these conditions can vary widely, so it is important to consult a healthcare provider for an accurate diagnosis and treatment plan.

Angiolymphoid hyperplasia with eosinophilia (ALHE) is a rare benign vascular lesion that typically presents as one or multiple papules or nodules, often on the head and neck region. The exact cause of ALHE is unknown, but it has been associated with chronic inflammation and immune dysfunction.

Histologically, ALHE is characterized by the proliferation of blood vessels and lymphoid tissue, with a prominent infiltration of eosinophils. The lesions may also contain other inflammatory cells such as plasma cells, histiocytes, and T-lymphocytes.

Clinically, ALHE presents as red to brownish papules or nodules that can be tender or pruritic (itchy). Lesions typically occur on the head and neck region, particularly around the ears, eyes, and nose. In some cases, lesions may also appear on the trunk, arms, or legs.

While ALHE is a benign condition, it can cause significant cosmetic concerns due to its location. Treatment options include surgical excision, laser therapy, and intralesional corticosteroid injections. Recurrence after treatment is not uncommon. It is important to note that while ALHE may resemble other more serious conditions such as cutaneous lymphoma or angiosarcoma, it has a much more favorable prognosis.

Myxosarcoma is a very rare type of soft tissue sarcoma, a cancer that develops in the soft tissues of the body, such as fat, muscle, nerves, blood vessels, and fibrous tissues. Myxosarcomas are characterized by the presence of mucoid or gelatinous material in the tumor, which is composed of an abnormal accumulation of acid mucopolysaccharides. These tumors typically affect adults, with a peak incidence in the sixth to seventh decade of life. They usually occur in the extremities, particularly the lower limbs, and can also arise in the retroperitoneum or other deep soft tissues. Myxosarcomas are classified into several subtypes based on their histological features, with the most common being the myxofibrosarcoma. Treatment typically involves surgical resection with wide margins, often followed by radiation therapy and/or chemotherapy. The prognosis for patients with myxosarcoma depends on several factors, including the size and location of the tumor, the histological grade, and the patient's age and overall health.

Cyclic AMP-dependent protein kinase RIα subunit, also known as PKA RIα or PRKAR1A, is a type of regulatory subunit of the cyclic AMP (cAMP)-dependent protein kinase (PKA) enzyme. PKA is a key enzyme in many cellular signaling pathways and is composed of two regulatory subunits and two catalytic subunits. The RIα subunit is one of the four different regulatory subunits (RIα, RIβ, RIIα, and RIIβ) that regulate PKA activity by binding to cAMP, which leads to the release and activation of the catalytic subunits.

The RIα subunit is encoded by the PRKAR1A gene and is primarily expressed in many tissues, including the brain, heart, and adrenal glands. Mutations in the PRKAR1A gene have been associated with several genetic disorders, such as Carney Complex, a rare autosomal dominant disorder characterized by multiple tumors and endocrine overactivity. The RIα subunit plays an essential role in regulating various cellular processes, including metabolism, differentiation, proliferation, and apoptosis.

... (symbol α1AC, A1AC, or a1ACT) is an alpha globulin glycoprotein that is a member of the serpin ... Alpha 1-antichymotrypsin inhibits the activity of certain enzymes called proteases, such as cathepsin G that is found in ... Alpha-1 antitrypsin, another serpin that is analogous for protecting the body from excessive effects of its own inflammatory ... Alpha 1-antichymotrypsin is also associated with the pathogenesis of Alzheimer's disease as it enhances the formation of ...
2006). "BIP co-chaperone MTJ1/ERDJ1 interacts with inter-alpha-trypsin inhibitor heavy chain 4". Biochem. Biophys. Res. Commun ... DNAJC1 has been shown to interact with Alpha 1-antichymotrypsin. GRCh38: Ensembl release 89: ENSG00000136770 - Ensembl, May ... 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. Kroczynska B, Evangelista CM, Samant SS, et al. (2004). "The SANT2 domain of ... 83 (1): 153-67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819. Strausberg RL, Feingold EA, Grouse LH, et al. (2003). " ...
Tsuda M, Masuyama M, Katsunuma T (December 1986). "Inhibition of human DNA polymerase alpha by alpha 1-antichymotrypsin". ... DNA polymerase alpha catalytic subunit is an enzyme that in humans is encoded by the POLA1 gene. This gene encodes the p180 ... DNA dependent polymerase alpha (Pol α) has been shown to interact with MCM4 and GINS1, Retinoblastoma protein, PARP1 and RBMS1 ... PDBe-KB provides an overview of all the structure information available in the PDB for Human DNA polymerase alpha catalytic ...
Mellon MB, Frank BT, Fang KC (2002). "Mast cell alpha-chymase reduces IgE recognition of birch pollen profilin by cleaving ... Caughey GH, Raymond WW, Wolters PJ (2000). "Angiotensin II generation by mast cell alpha- and beta-chymases". Biochim. Biophys ... 1993). "Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus ... 286 (1): 163-73. doi:10.1006/jmbi.1998.2462. PMID 9931257. Pereira PJ, Wang ZM, Rubin H, et al. (1999). "The 2.2 A Crystal ...
Skeel A, Leonard EJ (2001). "alpha 1-Antichymotrypsin is the human plasma inhibitor of macrophage ectoenzymes that cleave pro- ... 1999). "Characterization of free alpha- and beta-chains of recombinant macrophage-stimulating protein". Arch. Biochem. Biophys ... 138 (1-2): 171-4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. Waltz SE, Gould FK, Air EL, et al. (1996). "Hepatocyte ... 200 (1-2): 149-56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. Yoshikawa W, Hara H, Takehara T, et al. ( ...
In vitro studies utilizing purified kallikrein were also performed on alpha-synuclein, and it was effective in degrading alpha- ... antichymotrypsin". Clinical Chemistry. 49 (5): 746-751. doi:10.1373/49.5.746. PMID 12709365. Magklara A, Mellati AA, Wasney GA ... Alpha-synuclein build-up is commonly found in Dementia with Lewy bodies, Parkinson's disease, and multiple system atrophy ... Iwata A, Maruyama M, Akagi T, Hashikawa T, Kanazawa I, Tsuji S, Nukina N (October 2003). "Alpha-synuclein degradation by serine ...
The genetic code of protein C inhibitor is similar to alpha 1-antitrypsin and alpha 1-antichymotrypsin. The in vivo half time ... Hayashi S, Wakizaka A (July 1995). "Urinary protein C inhibitor binding region in the A alpha-chain of human fibrinogen". Blood ... Billingsley GD, Walter MA, Hammond GL, Cox DW (February 1993). "Physical mapping of four serpin genes: alpha 1-antitrypsin, ... alpha 1-antichymotrypsin, corticosteroid-binding globulin, and protein C inhibitor, within a 280-kb region on chromosome ...
PSA exists in serum in the free (unbound) form and in a complex with alpha 1-antichymotrypsin; research has been conducted to ... 5 (1): 38-48. doi:10.1016/j.eeus.2006.10.003. ISSN 1871-2592. Carter HB, Pearson JD, Metter EJ, Brant LJ, Chan DW, Andres R, et ... ISBN 978-1-891276-02-6. Catalona WJ, Richie JP, Ahmann FR, Hudson MA, Scardino PT, Flanigan RC, et al. (May 1994). "Comparison ... 154 (2 Pt 1): 407-413. doi:10.1016/S0022-5347(01)67064-2. PMID 7541857. Crawford ED, Schutz MJ, Clejan S, Drago J, Resnick MI, ...
Jensen PH, Hager H, Nielsen MS, Hojrup P, Gliemann J, Jakes R (September 1999). "alpha-synuclein binds to Tau and stimulates ... Tau protein has been shown to interact with: Alpha-synuclein, FYN, Proto-oncogene tyrosine-protein kinase Src S100B, and YWHAZ ... and alpha 1-antichymotrypsin". Proceedings of the National Academy of Sciences of the United States of America. 90 (14): 6825-8 ... 18 (1): 164-77. doi:10.1093/hmg/ddn326. PMC 2644648. PMID 18930955. Lee HG, Perry G, Moreira PI, Garrett MR, Liu Q, Zhu X, et ...
... alpha-1 anti-chymotrypsin and retinol binding protein identified by proteomics as potential biomarkers for lupus nephritis". ... 18 (1): 6. doi:10.1186/s12969-020-0403-9. PMC 6964050. PMID 31941549. Bhattacharya, S; Yadav, A; Aggarwal, A (8 February 2019 ... Aggarwal, A; Sarangi, AN; Gaur, P (1 March 2017). "Gut microbiome in children with enthesitis-related arthritis in a developing ... Aggarwal, A; Gupta, R; Negi, V; Rajasekhar, L; Misra, R; Chaturvedi, P; Sinha, S (1 May 2017). "Urinary haptoglobin, ...
1996). "Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced ... Brecher AS, Yang MP (1998). "Acetaldehyde inhibits chymotrypsin and serum anti-chymotrypsin activity". J. Investig. Med. 46 (4 ... 195 (1-2): 27-39. doi:10.1016/0009-8981(90)90191-T. PMID 2093478. Masson E, Chen JM, Scotet V, et al. (2008). "Association of ... 123 (1): 83-91. doi:10.1007/s00439-007-0459-3. PMID 18172691. S2CID 20466442. Rosendahl J, Witt H, Szmola R, et al. (2008). " ...
The disorder alpha-1 antitrypsin deficiency is one of the most common hereditary diseases. Since the stressed serpin fold is ... The X-ray crystal structures of antithrombin, heparin cofactor II, MENT and murine antichymotrypsin reveal that these serpins ... alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder". The New England Journal of Medicine. 309 (12 ... "Alpha-1-antitrypsin: molecular abnormality of S variant". British Medical Journal. 1 (6002): 130-131. January 1976. doi:10.1136 ...
"Synthesis and release of platelet-activating factor is inhibited by plasma alpha 1-proteinase inhibitor or alpha 1- ... antichymotrypsin and is stimulated by proteinases". The Journal of Experimental Medicine. 168 (4): 1293-306. doi:10.1084/jem. ... If the sn-1 was removed then PAF lacked any sort of biological activity. Finally, the sn-3 position of PAF was experimented ... 10 (1): 1-6. doi:10.1385/ENDO:10:1:1. PMID 10403564. S2CID 43840751. Yaras N, Ugur M, Ozdemir S, Gurdal H, Purali N, Lacampagne ...
See Data sources section Alpha 1-antichymotrypsin, a protein American Academy of Clinical Toxicology American Association of ...
"Gene regulation of the serine proteinase inhibitors alpha1-antitrypsin and alpha1-antichymotrypsin". Biochemical Society ... The alpha region can be further divided into two sub-regions, termed "1" and "2". Alpha-1 antitrypsin is the main protein of ... Alpha-1 antitrypsin or α1-antitrypsin (A1AT, α1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded ... Alpha-1 antitrypsin levels in the blood depend on the genotype. Some mutant forms fail to fold properly and are, thus, targeted ...
... alpha-crystallin a chain MeSH D12.776.306.366.100.300 - alpha-crystallin b chain MeSH D12.776.306.366.300.100 - beta-crystallin ... steroid 12-alpha-hydroxylase MeSH D12.776.422.220.453.915.737 - steroid 16-alpha-hydroxylase MeSH D12.776.422.220.453.915.748 ... Retinoid X receptor alpha MeSH D12.776.826.701.500.625 - Retinoid X receptor beta MeSH D12.776.826.701.500.750 - Retinoid X ... alpha-macroglobulins See List of MeSH codes (D12.776.395). MeSH D12.776.402.150.100.200 - chimerin 1 MeSH D12.776.402.150. ...
The alpha globulins typically have molecular weights of around 93 kDa. Alpha globulins include certain hormones, proteins that ... Haptoglobin Alpha-2u globulin α2-macroglobulin Ceruloplasmin Thyroxine-binding globulin Alpha 2-antiplasmin Protein C Alpha 2- ... Alpha globulins are a group of globular proteins in plasma that are highly mobile in alkaline or electrically charged solutions ... α1-antitrypsin Alpha 1-antichymotrypsin Orosomucoid (acid glycoprotein) Serum amyloid A Alpha 1-lipoprotein ...
... alpha-macroglobulins MeSH D12.776.124.790.720.100.500 - pregnancy-associated alpha 2-macroglobulins The list continues at List ... immunoglobulin alpha-chains MeSH D12.776.124.486.485.114.619.251 - immunoglobulin d MeSH D12.776.124.486.485.114.619.251.500 - ... immunoglobulin alpha-chains MeSH D12.776.124.790.651.114.619.251 - immunoglobulin d MeSH D12.776.124.790.651.114.619.251.500 - ... immunoglobulin alpha-chains MeSH D12.776.124.486.485.705.500.360 - immunoglobulin delta-chains MeSH D12.776.124.486.485.705. ...
Turk B, Brieditis I, Bock SC, Olson ST, Björk I (1997). "The oligosaccharide side chain on Asn-135 of alpha-antithrombin, ... alpha 1-antichymotrypsin and MENT. The conformational change most relevant for Factor IXa and Xa inhibition involves the P14 ... alpha 2-antiplasmin and Heparin cofactor II. The physiological target proteases of antithrombin are those of the contact ... 17 (1): 81-86. PMID 6724355. Lane DA, Olds RJ, Boisclair M, Chowdhury V, Thein SL, Cooper DN, Blajchman M, Perry D, Emmerich J ...
It includes alpha 1-antitrypsin (which protects the body from excessive effects of its own inflammatory proteases), alpha 1- ... antichymotrypsin (which does likewise), C1-inhibitor (which protects the body from excessive protease-triggered activation of ... ISBN 978-1-4160-2973-1. Rodriguez J, Gupta N, Smith RD, Pevzner PA (January 2008). "Does trypsin cut before proline?". Journal ... 7 (1): 300-305. doi:10.1021/pr0705035. PMID 18067249. Renicke C, Spadaccini R, Taxis C (2013-06-24). "A tobacco etch virus ...
Obligate heterodimers of one alpha and one beta subunits Alpha subunits A1 A2 A3 A4 A5 A6 A7 A8 A9 A10 A11 AD AE AL (CD11a) AM ... Alpha-v beta-3 Alpha-v beta-5 Immunoglobulin superfamily CAMs SynCAMs - Synaptic cell adhesion molecules NCAMs - Neural cell ... Fc-alpha receptors (FcαR) FcαRI (CD89, FCAR) Fcα/μR Fc-epsilon receptors (FcεR) FcεRI - Tetramer: FCER1A / FCER1B / two FCER1G ... reflex Inflammasome Granuloma Acute-phase proteins Amyloid SAP SAA Positive Alpha 1-antichymotrypsin Alpha 1-antitrypsin Alpha ...
... resulting in a typical elevation in the alpha-2 zone during inflammation. A normal alpha-2 and an elevated alpha-1 zone is a ... Alpha-2 macroglobulin may be elevated in children and the elderly. This is seen as a sharp front to the alpha-2 band. AMG is ... Stevenson, FT; Greene, S; Kaysen, GA (January 1998). "Serum alpha 2-macroglobulin and alpha 1-inhibitor 3 concentrations are ... Alpha-1 antitrypsin has an SG group and thiol compounds may be bound to the protein altering their mobility. A decreased band ...
... alpha amylase I, hemoglobin, etc. Metabolomics and lipidomic studies are used to determine what metabolic categories (amino ... 27 (1): 11-22. doi:10.1111/j.2041-1014.2011.00630.x. ISSN 2041-1006. PMC 4049603. PMID 22230462. (Use dmy dates from March 2022 ... 85 (1): 90-100. doi:10.1111/prd.12353. ISSN 0906-6713. PMID 33226710. S2CID 227132686. Velsko, Irina M.; Fellows Yates, James A ... 7 (1): 102. doi:10.1186/s40168-019-0717-3. ISSN 2049-2618. PMC 6612086. PMID 31279340. Adler, Christina J; Dobney, Keith; ...
Alpha 1-antichymotrypsin (symbol α1AC, A1AC, or a1ACT) is an alpha globulin glycoprotein that is a member of the serpin ... Alpha 1-antichymotrypsin inhibits the activity of certain enzymes called proteases, such as cathepsin G that is found in ... Alpha-1 antitrypsin, another serpin that is analogous for protecting the body from excessive effects of its own inflammatory ... Alpha 1-antichymotrypsin is also associated with the pathogenesis of Alzheimers disease as it enhances the formation of ...
Heterozygous alpha 1-antichymotrypsin deficiency may be associated with cold urticaria. *. Faith Featherstone ... There were no findings of C1-inhibitor, alpha 1-antitrypsin, alpha 2-antiplasmin, antithrombin III, tissue plasminogen ... The prevalence of heterozygous alpha 1-antichymotrypsin deficiency was significantly higher than expected (prevalence ratio ... This finding is in concert with previous studies that have shown lower mean levels of alpha 1-antichymotrypsin among patients ...
Joseph J Maleszewski, MD is a member of the following medical societies: Alpha Omega Alpha, College of American Pathologists, ... Myxoma cells exhibit immunoreactivity to calretinin (75-100%), vimentin (, 50%), and alpha-1 antichymotrypsin. [37, 21, 38] ... Cardiac myxomas have shown to be variably immunoreactive to S-100, smooth muscle actin, desmin, alpha-1 antitrypsin, ... 1, 11, 27] Such symptoms may include fever, arthralgia, myalgia, and weight loss. [23] Laboratory findings may include elevated ...
Alpha-Fetoprotein (AFP) Catalog No: 105-12 Form: Lyophilized 105-12. Human Cord Serum. > 99% (SDS-PAGE). Lyophilized. More Info ... Alpha-1 Antitrypsin (A1AT) Catalog No: 106-11 Form: Lyophilized 106-11. Human Plasma. > 95% (SDS-PAGE). Lyophilized. More Info ... Alpha-1 Microglobulin (A1M) Catalog No: 110-11 Form: Lyophilized 110-11. Human Urine. > 96% (SDS-PAGE). Lyophilized. More Info ... Alpha-2 Antiplasmin (A2AP) Catalog No: 107-50 Form: Lyophilized 107-50. Human Plasma. > 95% (SDS-PAGE). Lyophilized. More Info ...
Karashima, S.; Kataoka, H.; Itoh, H.; Maruyama, R.; Koono, M. Prognostic significance of alpha-1-antitrypsin in early stage of ... Higashiyama, M.; Doi, O.; Kodama, K.; Yokouchi, H.; Tateishi, R. An evaluation of the prognostic significance of alpha-1- ... Tahara, E.; Ito, H.; Taniyama, K.; Yokozaki, H.; Hata, J. Alpha 1-antitrypsin, alpha 1-antichymotrypsin, and alpha 2- ... Table 1. GB patients clinical characteristics.. Study Number. Age. Gender. Lobe Affected. Surgery. Oncological Treatment. ...
IHC of MART-1/Melan-A (A103) on an FFPE Melanoma Tissue ... Alpha-1-Antichymotrypsin - Rabbit Polyclonal. Add to quote This ... The MART-1/Melan-A antigen is specific for the melanocyte lineage found in normal skin, retina, and melanocytes, but not in ... MART-1/Melan-A is a putative 18 kDa transmembrane protein consisting of 118 amino acids. It has a single transmembrane domain. ... MART-1/ Melan- A is a protein antigen found on melanocytes. Antibodies against this antigen are used to recognize cells of ...
Joseph J Maleszewski, MD is a member of the following medical societies: Alpha Omega Alpha, College of American Pathologists, ... Myxoma cells exhibit immunoreactivity to calretinin (75-100%), vimentin (, 50%), and alpha-1 antichymotrypsin. [37, 21, 38] ... Cardiac myxomas have shown to be variably immunoreactive to S-100, smooth muscle actin, desmin, alpha-1 antitrypsin, ... 1, 11, 27] Such symptoms may include fever, arthralgia, myalgia, and weight loss. [23] Laboratory findings may include elevated ...
The Celltechgen BCA (bicinchoninic) protein assay is a widely used method for colorimetric Copper-based detection and quantitation of total protein in a solution.
Alpha-1 antitrypsin deficiency: from Italy to the world. 1-gen-2007 B., Balbi; Luisetti, Maurizio; L., Corda; N., Gatta ... Alpha-1 antitrypsin deficiency in Italy: regional differences of the PIS and PIZ deficiency alleles. 1-gen-2005 de Serres, F. J ... A national program for detection of alpha 1-antitrypsin deficiency in Italy. Gruppo I.D.A. 1-gen-1999 Luisetti, Maurizio; G., ... alpha 1-antitrypsin TAQ I polymorphism and alpha 1-antichymotrypsin mutations in patients with obstructive pulmonary disease.. ...
... tumor necrosis factor-alpha, the soluble tumor necrosis factor receptors I and II, and alpha1-antichymotrypsin. Alzheimer Dis ... As summarized elsewhere (1), the combination of a declining birth rate and an increased average life span is expected to ... Decreased B-amyloid 1-42 and increased tau levels in cerebrospinal fluid of patients with Alzheimer disease. JAMA 2003;289:2094 ... Subcortical ischaemic vascular dementia. Lancet Neurol 2002;1:426-36.. *Hofman A, Ott A, Breteler MM, Bots ML, Slooter AJ, van ...
alpha 1-Antichymotrypsin. *alpha 1-Antitrypsin. *alpha-Linolenic Acid. *alpha-Mannosidase. *Altruism ...
Apolipoprotein E and alpha-1-antichymotrypsin polymorphisms in sporadic inclusion body myositis. European neurology 2004 51 (4 ... Journal of neuroimmunology 2012 Sep 250 (1-2): 66-70. Scott Adrian P, Laing Nigel G, Mastaglia Frank, Dalakas Marinos, Needham ... Journal of neuroimmunology 2012 Sep 250 (1-2): 77-82. Rojana-udomsart Arada, James Ian, Castley Alison, Needham Merrilee, Scott ... Journal of neuroimmunology 2013 Jan 254 (1-2): 174-7. Rojana-udomsart Arada, Mitrpant Chalermchai, James Ian, Witt Campbell, ...
Alpha-fetoprotein. *Erythropoietin (EPO). Functions. Some functions served by glycoproteins[3] Function Glycoproteins ... N-linked protein glycosylation (N-glycosylation of N-glycans) at Asn residues (Asn-x-Ser/Thr motifs) in glycoproteins[1].. ...
... antichymotrypsin, 90 kDa, Rh > 3 nm), since its steric hindrance overcame the increased availability of antigen binding sites ... prostate-specific antigen-alpha(1) ... 1. Orientation of capture antibodies on gold nanoparticles to ... In this study, 20 primary liver transplantation recipients of older grafts (≥70 years) were randomized 1:1 to NMP or cold ... We tested 12 different SI using blood tests from patients with isocitrate dehydrogenase 1 and 2 wild-type glioblastomas, ...
Mogi, M.; Harada, M.; Riederer, P.; Narabayashi, H.; Fujita, K.; Nagatsu, T. Tumor necrosis factor-alpha (TNF-alpha) increases ... Lee, E.J.; Woo, M.S.; Moon, P.G.; Baek, M.C.; Choi, I.Y.; Kim, W.K.; Junn, E.; Kim, H.S. Alpha-synuclein activates microglia by ... Pirttila, T.; Mehta, P.D.; Frey, H.; Wisniewski, H.M. Alpha 1-antichymotrypsin and IL-1 beta are not increased in CSF or serum ... Dobbs, R.J.; Charlett, A.; Purkiss, A.G.; Dobbs, S.M.; Weller, C.; Peterson, D.W. Association of circulating TNF-alpha and IL-6 ...
Alpha 1-antichymotrypsin - is an alpha globulin glycoprotein that is a member of the serine proteinase inhibitor (serpin) ... SERPINA6 - Serpin peptidase inhibitor, clade A (alpha 1 antiproteinase, antitrypsin), member 6, also known as SERPINA6, is a ... SERPINA4 - Serpin peptidase inhibitor, clade A (alpha 1 antiproteinase, antitrypsin), member 4, also known as SERPINA4, is a ... SERPINA9 - protein name=serpin peptidase inhibitor, clade A (alpha 1 antiproteinase, antitrypsin), member 9 caption= width= ...
Stanley A Brosman, MD is a member of the following medical societies: Alpha Omega Alpha, American Academy of Pediatrics, ... antichymotrypsin is the major form of prostate-specific antigen in serum of patients with prostatic cancer: assay of the ... Erik T Goluboff, MD is a member of the following medical societies: Alpha Omega Alpha, American Medical Association, American ... and is bound to either alpha2 -macroglobulin (AMG) or alpha1 -antichymotrypsin (ACT). These are the 2 major serine protease ...
Serpina3n, a murine orthologue of human antichymotrypsin. 2ach. CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT ... Crystal structure of alpha-1-antitrypsin, crystal form B. 3cwm. Crystal structure of alpha-1-antitrypsin complexed with citrate ... CLEAVED ANTICHYMOTRYPSIN A349R. 1ath. THE INTACT AND CLEAVED HUMAN ANTITHROMBIN III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE ... CLEAVED ANTICHYMOTRYPSIN A347R. 3cvm. High resolution structure of a stable Plasminogen activator inhibitor type-1 in its ...
Zn-Alpha-2-Glycoprotein [D12.776.395.985] Zn-Alpha-2-Glycoprotein * CHEMICALS AND DRUGS. Amino Acids, Peptides, and Proteins [ ...
alpha-2-Antiplasmin. *Angiotensinogen. *Antithrombin Proteins. *Complement C1 Inactivator Proteins. *HSP47 Heat-Shock Proteins ...
Mouse PDHa(Pyruvate Dehydrogenase Alpha) ELISA Kit. *Mouse PIK3C2a(Phosphoinositide-3-Kinase Class-2-Alpha Polypeptide) ELISA ... Mouse PDHa(Pyruvate Dehydrogenase Alpha) ELISA Kit. *Mouse PIK3C2a(Phosphoinositide-3-Kinase Class-2-Alpha Polypeptide) ELISA ... Human aFPL3(Alpha-Fetoprotein Lens Culinaris Agglutinin 3) ELISA Kit. *Human AGER(Advanced Glycosylation End Product Specific ... Human aFPL3(Alpha-Fetoprotein Lens Culinaris Agglutinin 3) ELISA Kit. *Human AGER(Advanced Glycosylation End Product Specific ...
Mouse PDHa(Pyruvate Dehydrogenase Alpha) ELISA Kit. *Mouse PIK3C2a(Phosphoinositide-3-Kinase Class-2-Alpha Polypeptide) ELISA ... Mouse PDHa(Pyruvate Dehydrogenase Alpha) ELISA Kit. *Mouse PIK3C2a(Phosphoinositide-3-Kinase Class-2-Alpha Polypeptide) ELISA ... Lipopolisacharyd indukuje ekspresję białka translokatora myszy (18 kDa) poprzez kompleks AP-1 w mikrogleju ... Lipopolisacharyd indukuje ekspresję białka translokatora myszy (18 kDa) poprzez kompleks AP-1 w mikrogleju ...
alpha-2-Antiplasmin [D12.776.395.080] alpha-2-Antiplasmin * alpha-2-HS-Glycoprotein [D12.776.395.086] ...
Mouse PIK3C2a(Phosphoinositide-3-Kinase Class-2-Alpha Polypeptide) ELISA Kit. *Rat TNNI3(Troponin I Type 3, Cardiac) ELISA Kit ... Human PPARa(Peroxisome Proliferator Activated Receptor Alpha) ELISA Kit. *Mouse PPARa(Peroxisome Proliferator Activated ... Human FBN1(Fibrillin 1) ELISA Kit. Human FBN1(Fibrillin 1) ELISA Kit. To Order Contact us: [email protected] ... Description: Fibrillin-1 / FBN1 is an extracellular matrix glycoprotein that serves as a structural component of calcium- ...
alpha (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5) · beta (LAMB1, LAMB2, LAMB3, LAMB4) · gamma (LAMC1, LAMC2, LAMC3) ... TGF-beta 1s bioactivity has been shown to be inhibited. Because of this, it is believed the primary function of decorin lies ... Activin and inhibin · ADAM · Alpha 1-antichymotrypsin · Apolipoprotein H · CD70 · Asialoglycoprotein · Avidin · B-cell ... Decorin has been shown to interact with Epidermal growth factor receptor[2][3] and TGF beta 1.[4][5][6] ...
... which was inhibited by 1,10 Phenanthroline, suggesting the presence of a C3α chain specific metalloprotease in Micrurus spp ... alpha 1-antichymotrypsin and alpha 2-antiplasmin. Biochim Biophys Acta. 1983, 15: 113-120. ... Figure 1. Action of Micrurus spp venoms on the complement pathways. Samples (50 μl) of normal human serum (NHS), as complement ... After 1 h of incubation at 37°C, plates were washed with BVB++ (VBS++, pH 7.2, containing 0.1% BSA) and incubated with anti- ...
Alpha-amylase type A isozyme [Precursor]; SWP:P00693; PDB:1HT6A MGKNGSLCCFSLLLLLLLAGLASGHQVLFQGFNWESWKQSGGWYNMMMGKVDDIAAAGVT ... Antichymotrypsin-1 [Precursor]; SWP:Q03383 MDKLLLLVTLVCGTQAFYMFGHEFSRTRLGDTIDKTSLKILKESYNLADDKNVIASPLGV SSSSSSSSSSSSSSSS ... Alpha-amylase type B isozyme [Precursor]; SWP:P04063; PDB:1AMY_ MANKHLSLSLFLVLLGLSASLASGQVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGITH ... Alpha-amylase A type-1/2 [Precursor]; SWP:P0C1B3; PDB:2TAAA MMVAWWSLFLYGLQVAAPALAATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCG ...
Mark Time-resolved fluorescence imaging (TRFI) for direct immunofluorescence of PSA and alpha-1-antichymotrypsin in prostatic ... Debruyne, Frans (2003) In Prostate Cancer and Prostatic Diseases 6(Suppl 1). p.1-1 ... iframe src="https://lup.lub.lu.se/search/publication?embed=1&q=issn+exact+%221365-7852%22&hide_pagination=1&hide_info=1 ...
Patel, C.A.; Owen, M.P.; Gu, J. 1996: Immunohistochemical detection of alpha-2-adrenoceptor subtypes using alpha-2 subtype- ... Immunohistochemical detection of tumour necrosis factor alpha tnf alpha and interferon gamma ifn gamma in the liver of children ... Inoue, S.; Seno, S. 1995: Immunohistochemical demonstration of human type IV collagen alpha-1 to alpha-6 chains on paraffin ... Bird, R.P. 1996: Immunohistochemical detection of transforming growth factor alpha in normal crypts, aberrant crypt foci and ...
  • Alpha 1-antichymotrypsin (symbol α1AC, A1AC, or a1ACT) is an alpha globulin glycoprotein that is a member of the serpin superfamily. (wikipedia.org)
  • There were no findings of C1-inhibitor, alpha 1-antitrypsin, alpha 2-antiplasmin, antithrombin III, tissue plasminogen activator inhibitor or thyroxine binding protein deficiency. (chaen-rcah.ca)
  • American Thoracic Society/European Respiratory Society Statement: Standards for the diagnosis and management of individuals with alpha-1 antitrypsin deficiency]. (unipv.it)
  • A fast amplification-reverse hybridization assay kit to detect the most frequent deficient variants in the alpha-1-antitrypsin gene. (unipv.it)
  • A national program for detection of alpha 1-antitrypsin deficiency in Italy. (unipv.it)
  • A novel method for rapid genotypic identification of alpha 1-antitrypsin variants. (unipv.it)
  • alpha 1-antitrypsin TAQ I polymorphism and alpha 1-antichymotrypsin mutations in patients with obstructive pulmonary disease. (unipv.it)
  • Alpha 1-antitrypsin variants produced by recombinant DNA: differences in elastase inhibitory activity and resistance to oxidant agents. (unipv.it)
  • Transcortin - Serpin peptidase inhibitor, clade A (alpha 1 antiproteinase, antitrypsin), member 6, also Corticosteroid Binding Globulin or Transcortin Structure of corticosteroid binding globulin in complex with cortisol. (en-academic.com)
  • This finding is in concert with previous studies that have shown lower mean levels of alpha 1-antichymotrypsin among patients with cold urticaria and suggests that heterozygous deficiency of this antiprotease, which controls neutrophil cathepsin G and mast cell chymase may predispose to cold urticaria. (chaen-rcah.ca)
  • MART-1/Melan-A is a putative 18 kDa transmembrane protein consisting of 118 amino acids. (affordableihcinstruments.com)
  • MART-1/ Melan- A is a protein antigen found on melanocytes. (affordableihcinstruments.com)
  • N-linked protein glycosylation (N-glycosylation of N-glycans) at Asn residues (Asn-x-Ser/Thr motifs) in glycoproteins [1] . (wikidoc.org)
  • All of the above also share the presence of protein aggregates on neuropathology, so they have been termed as protein misfolding diseases (PMDs) [1] and since tau or α-synuclein (α-syn) can be found frequently in protein aggregates, many of these diseases have been grouped as tauopathies i.e. (austinpublishinggroup.com)
  • Inhibitory serpins comprise several alpha-helix and beta-strands together with an external reactive centre loop (RCL) containing the active site recognised by the target enzyme. (embl.de)
  • Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. (embl.de)
  • We reported previously that human interleukin-1 beta converting enzyme (ICE) is regulated by the CrmA serpin encoded by cowpox virus. (embl.de)
  • Alpha 1-antichymotrypsin inhibits the activity of certain enzymes called proteases, such as cathepsin G that is found in neutrophils, and chymases found in mast cells, by cleaving them into a different shape or conformation. (wikipedia.org)
  • Various molecules in the cerebrospinal fluid (CSF), such as α-synuclein, DJ-1, amyloid-β, tau, and lysosomal enzymes, may be biomarkers of PD [ 9 ] [ 10 ] . (encyclopedia.pub)
  • We tested 12 different SI using blood tests from patients with isocitrate dehydrogenase 1 and 2 wild-type glioblastomas, treated with radio-chemotherapy. (bvsalud.org)
  • Oral diseases are included among the on NCD in this Region and to stress the World Health Organization (WHO) defini- importance of oral health issues in medicine tion of chronic diseases [ 1 ], and the im- in relation to the risk of NCD. (who.int)
  • Although mural thrombi tend to occur in individuals with underlying heart disease and in many locations within the heart (eg, atrial appendages, atria, and ventricles), myxomas arise with astonishing consistency in 1 location: primarily adjacent to the fossa ovalis. (medscape.com)
  • The MEROPS online database for peptidases and their inhibitors: I04.002 Alpha+1-antichymotrypsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Human SERPINA3 genome location and SERPINA3 gene details page in the UCSC Genome Browser. (wikipedia.org)
  • Several the leading causes of death in every region pathophysiological pathways of association of the world [ 1 ]. (who.int)
  • Alpha 1-antichymotrypsin is also associated with the pathogenesis of Alzheimer's disease as it enhances the formation of amyloid-fibrils in this disease. (wikipedia.org)
  • Alpha 1-antichymotrypsin has been shown to interact with DNAJC1. (wikipedia.org)
  • In some publications, decorin has been shown to enhance the bioactivity of TGF-beta 1, in other publications, TGF-beta 1's bioactivity has been shown to be inhibited. (en-academic.com)
  • Decorin has been shown to interact with Epidermal growth factor receptor [ 2 ] [ 3 ] and TGF beta 1 . (en-academic.com)
  • Database: Signal Peptide (Eukaryote) DB # Date of preparation: Jan.03, 2007 # Total number of sequences: 17693 # Total number of residues: 7712280 # Size: 16768.004 kB # Version: 1 # This database consists of sequences extracted from the SwissProt database [1] that have their signal peptides annotated and fully demarcated in the SwissProt data file. (pptdb.ca)
  • Description: Quantitativesandwich ELISA kit for measuring Human Fibrillin-1 (FBN1) in samples from serum, plasma, tissue homogenates. (knoblauchpublishing.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Fibrillin 1 (FBN1) in samples from serum, plasma, tissue homogenates or other biological fluids. (knoblauchpublishing.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Fibrillin 1 (FBN1) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids. (knoblauchpublishing.com)
  • Overview of all the structural information available in the PDB for UniProt: P01011 (Human Alpha-1-antichymotrypsin) at the PDBe-KB. (wikipedia.org)
  • This preparation of Creatine Kinase MM (CK-MM) is purified from human skeletal muscle and is supplied as a liquid in 5 mM Sodium Succinate, 10 mM Sodium Chloride, 1 mM EDTA, 5 mM b -Mercaptoethanol, 50% Glycerol, pH 7.0. (scrippslabs.com)
  • this leads to increased PKCδ-dependent activation of the NFκB pathway, followed by increased IL-1β production [ 25 ] . (encyclopedia.pub)
  • As summarized elsewhere (1), the combination of a declining birth rate and an increased average life span is expected to increase the proportion of the population aged 65 years and older in the United States from 12.4% in 2000 to 19.6% in 2030. (cdc.gov)
  • MART-1 is a mouse monoclonal antibody derived from cell culture supernatant that is concentrated, dialyzed, filter sterilized and diluted in buffer pH 7.5, containing BSA and sodium azide as a preservative. (affordableihcinstruments.com)
  • Journal of neuroimmunology 2013 Jan 254 (1-2): 174-7. (cdc.gov)
  • Journal of neuroimmunology 2012 Sep 250 (1-2): 66-70. (cdc.gov)
  • Journal of neuroimmunology 2012 Aug 249 (1-2): 66-70. (cdc.gov)
  • A study by Li et al reported finding evidence for HSV-1 infection in 70% of a relatively small cohort (n=17) of surgically resected sporadic cardiac myxomas. (medscape.com)
  • CrmA rapidly inhibits ICE with an association rate constant (kon) of 1.7 x 10(7) M-1 s-1, forming a tight complex with an equilibrium constant for inhibition (Ki) of less than 4 x 10(-12) M. These data indicate that CrmA is a potent inhibitor of ICE, consistent with the dramatic effects of CrmA on modifying host responses to virus infection. (embl.de)
  • The MART-1/Melan-A antigen is specific for the melanocyte lineage found in normal skin, retina, and melanocytes, but not in other normal tissues. (affordableihcinstruments.com)
  • examples include Alpha 1 antitrypsin, alpha 1 antichymotrypsin, and serum amyloid A. (loinc.org)
  • Glycoprotein found in alpha(1)-globulin region in human serum. (bvsalud.org)
  • Prostate-specific antigen in human serum occurs predominantly in complex with alpha 1-antichymotrypsin. (siemens-healthineers.com)
  • A complex between prostate-specific antigen and alpha-1-antichymotrypsin is the major form of prostate-specific antigen in serum of patients with prostatic cancer: Assay of the complex improves clinical sensitivity for cancer. (siemens-healthineers.com)
  • TNF-alpha-induced corticosterone elevation but not serum protein or corticosteroid binding globulin reduction is vagally mediated. (ucdenver.edu)
  • 1. Immunohistochemical study of lysozyme, alpha 1-anti-chymotrypsin, tissue polypeptide antigen, keratin and carcinoembryonic antigen in effusion sediments. (nih.gov)
  • 1 Siemens Healthineers offers a full menu of Prostate Specific Antigen (PSA) tests that aid in the detection, monitoring and management of prostate cancer. (siemens-healthineers.com)
  • The major form of PSA is believed to be enveloped by alpha-2 macroglobulin. (cdc.gov)
  • Most prostate-specific antigens entering the blood circulation are rapidly combined with proteolytic enzyme inhibitors, mainly with α-1 antichymotrypsin (ACT) and α-2 macroglobulin (MG) proteolytic enzymes inactivate some. (sekbio.com)
  • A new promoter polymorphism in the alpha-1-antichymotrypsin gene is a disease modifier of Alzheimer's disease. (nih.gov)
  • The fasting venous blood was collected in order to evaluate the levels of interleukin-6 (IL-6), interleukine-1 beta (IL-1β), antichymotrypsin (ACT) and human tumor necrosis factor α (TNF-α), which were measured with the enzyme-linked immunosorbent assay (ELISA) kits. (nih.gov)
  • Apolipoprotein E, angiotensin-converting enzyme and alpha-1-antichymotrypsin genotypes are not associated with post-stroke dementia. (alzforum.org)
  • Arpa A, del Ser T, Goda G, Barba R, Bornstein B . Apolipoprotein E, angiotensin-converting enzyme and alpha-1-antichymotrypsin genotypes are not associated with post-stroke dementia . (alzforum.org)
  • Alpha globulins are a group of plasma proteins, belonging to the serpin superfamily, that are highly mobile in alkaline or electrically charged solutions. (loinc.org)
  • Glicoproteína que se encuentra en la región alfa(1)-globulina del suero humano. (bvsalud.org)
  • We have 3 reviews tested in 1 species: Human. (novusbio.com)
  • Sandwich ELISA: Serpin A3/alpha 1-Antichymotrypsin Antibody Pair [H00000012-AP21] - Detection sensitivity ranging from 0.03 ng/ml to 100 ng/ml. (novusbio.com)
  • Reagents are sufficient for at least 1-2 x 96 well plates using recommended protocols. (novusbio.com)
  • Heart disease, stroke, cancer, diabetes and chronic respiratory disease are the leading causes of death in every region of the world [1]. (who.int)
  • Several the leading causes of death in every region pathophysiological pathways of association of the world [ 1 ]. (who.int)
  • Oral diseases are included among the on NCD in this Region and to stress the World Health Organization (WHO) defini- importance of oral health issues in medicine tion of chronic diseases [ 1 ], and the im- in relation to the risk of NCD. (who.int)
  • A study by Li et al reported finding evidence for HSV-1 infection in 70% of a relatively small cohort (n=17) of surgically resected sporadic cardiac myxomas. (medscape.com)
  • The present study investigates global alterations in the proteome of bronchoalveolar lavage fluid taken from rats 1, 7, or 30 days after exposure to 5, 35, or 50 mg/kg of animal weight of DEPs. (nih.gov)