plz tell me how to isolate human cytokeratin from tissues.?
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ENDOMETRIOSIS is a common, but complex, gynecological syndrome of unknown pathogenesis that affects 5–15% of reproductive-aged women. It commonly is accompanied by debilitating symptoms of dysmenorrhea, pelvic pain, and reduced fecundity. Although multiple theories of the histogenesis of endometriosis exist, the implantation hypothesis of Sampson (1) is the most widely accepted. Retrograde menstruation (2) and intraperitoneal spillage of viable endometrial cells (3) occur frequently in cycling women, and müllerian tract outflow obstruction is associated with an increased prevalence of endometriosis (4). \n\nThe pathophysiology of endometriosis-associated pain and infertility remains enigmatic, but current evidence suggests that these symptoms result from local inflammation at the implant sites (5). Pelvic implants are associated with gross and microscopic evidence of local inflammatory changes, viz. neovascularization, fibrous scarring, and accumulation of activated inflammatory cells (6). It has been proposed that the recruitment of pelvic immune cells initiates an intraperitoneal cascade of cytokines that mediate the pain and infertility that accompany endometriosis (7). \n\nAutoinflammatory phenomena, including autoantibody production and atopy, have been associated with endometriosis. Mathur and her colleagues (8, 9) were the first to describe, in this disease, autoantibodies that recognize endometrial proteins ranging in size from 34–140 kDa. Similar results have been confirmed by other groups (10, 11). Gleicher and colleagues (12) noted that a significant proportion (40–60%) of women with endometriosis has elevated autoantibody titers when tested against a panel of common, generic autoantigens (e.g. phospholipid, ribonucleoprotein, and double-stranded DNA). Thus, in addition to the development of specific antiendometrial antibodies, generalized polyclonal B-cell activation is associated with some cases of endometriosis (13). \n\nA highly significant correlation has been noted between surgically documented endometriosis and the incidence of atopic allergic symptoms (14). This association was confirmed in a recent survey, conducted by the Endometriosis Association, of 4,000 North American women (15). In that study, 41% and 17% of surveyed endometriosis patients reported a history of pollen allergy and eczema, respectively, compared with 13% and 6% of women in the general population. In a cohort of 40 endometriosis patients with a predominant complaint of fatigue, 65% had allergy symptoms and positive serum IgE and IgG radioallergosorbent tests (D. Metzger, personal communication). On the basis of these clinical findings, which suggest an autoinflammatory or allergic component in endometriosis, we hypothesized that the biochemical mediators of atopic reactivity might be increased in women with this syndrome. As a prototype for such molecules, we selected the 8.4-kDa C-C eosinophil chemokine, eotaxin, and first investigated its peritoneal fluid concentrations in a case-control study of subjects with endometriosis and matched, normal women. These findings were then extended, using an established endometriosis cell model (7), to determine whether eotaxin protein secretion could be induced in vitro via endocrine and/or paracrine effectors.
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Hardening of body tissue.
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The cytoplasm containing the other cell parts.
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Any mitotic division REQUIRES cytokinesis.  It's the split of the cytoplasm and it starts in telophase, the last part of mitosis.
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try palmer's cocoa butter or aloe vera
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isolate the pathogen...
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During electrophorsesis or the electrical separation of protein substances you need a single point of entry into the gel so that the protein or material to be separated can effectively be manipulated by the electrical field created in the gel medium.  The substances then separate themselves by way of electrical charge on the molecule, pH of the gel used, and the strength of the electrical current passed through the gel.  You want the separation to occur in a controlled manner so you can later stain the gel medium with a protein or suitable dye and visualize the different substances separated into unique patterns so they can be identified against a known sample of substance.  A machine called a densitometer can scan the gel medium and calculate the % of each population of substances stained in the gel.
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here u find article for tissue culture
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Try a rough DNA isolation, some things u need are detergent, lemons, and a sample like onion.\n\nSimple diffusion experiments with onions, salt, water, etc..
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If you are in Europe try Novozime (Netherland)\nIf you are in USA try Genencor \n\nTelomerase is an enzyme that take part in replication mechanism, especial in cancer cells (they do not lose a part of its DNA when the two strands are copied)
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TRY A CREAM CALLED KUMASUTRA. IT WORKS REALLY GOOD.
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take an epindorph tube, place about 500 microlitres of blood, centrifuge, remove supernatent, wash with PBS buffer, repeat 3x, by an RNA isolation kit from roche and foolow the instruction!!
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If you have a purified prep of chromatin, you can use the spec to measure the amount of protein at 254 nm.  The problem is that this overlaps with DNA absorbance (260/280nm).  You can use a protein assay such as bradford or BCA to measure protein concentration.  Usually western blots are used to measure relative protein concetrations of specific proteins ie histone, actin.
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To isolate it, take a sample, dilute it then take a sample from that & spread it on a sterile petri-dish.\n\nYou can then take a sample from a pure culture.
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nucleus, cytoplasm and protoplasm ....
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use calamine lotion \nAvoid touching!!!!
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There are many procedures with which to trypsinize cells. All include washing the cell monolayer with TD, or in rare cases, with VE. This removes serum, which contains trypsin inhibitors, and lowers the concentration of both calcium and magnesium, both of which inhibit trypsinization.\n\nI like to rinse the cells with TD, add approximately 1 ml of straight trypsin, rock the dish, aspirate a majority of the trypsin, and then incubate the dish at 37 °C until the cells come off the dish.\n\nSome people put 1 ml of 5 fold diluted, with TD, trypsin on the dish and leave it on. Others do this using full-strength trypsin.\n\nCells vary enormously in how fast they come off the dish. Some cells come off within one minute, some require 15 min. Cells should be trypsinized until they come off the dish, but not longer. Don't rush, but don't over do it.\n\nCells that are extremely hard to dislodge with trypsin should be rinsed with VE prior to trypsinization and then trypsinized in the presence of VE. The EDTA promotes disaggregation. Unfortunately, EDTA is toxic to cells at high concentration--it deprives them of Zn++.\n\nIt is essential to inactivate trypsin and to remove EDTA after you have gotten the cells off the dish. Trypsin inhibition is accomplished in part by trypsin inhibitors in the serum in the growth medium. Bovine serum is a rich source of trypsin inhibitors.\n\nThe best, but most laborious way to reseed cells, is to dilute the suspended cells with medium containing serum and spin them down in the gray table top centrifuge--5/8 speed, 4 min. Then aspirate the supe, resuspend the cells in medium, and reseed them.\n\nA short cut that works with cells that are being seeded at a low cell density is simply to dilute the trypsinized suspension of cells with medium and seed the cells directly.\n\nIf the cells are to be reseeded at a high cell density, the trypsin will not be diluted or inactivated sufficiently and the cells will not attach.\n\nThis is not satisfactory when VE is used because EDTA is growth inhibitory even at low concentrations.\n\nIt is also not satisfactory with chick cells, since they are grown in medium containing only 2% serum and cannot be seeded very sparsely.