Search results for: anti_Rat SAP
#19167969 2008/11/28 To Up
Matrix metalloproteinase-9 derived from polymorphonuclear neutrophils increases gut barrier dysfunction and bacterial translocation in rat severe acute pancreatitis.
The role of polymorphonuclear neutrophil granulocytes (PMNs) and the PMN-derived protease, which is called matrix metalloproteinase-9 (MMP-9), for the gut barrier dysfunction in severe acute pancreatitis (SAP) has not yet been clarified. The aim of this study was to evaluate the effects of PMNs and MMP-9 on gut barrier dysfunction in rat SAP.Yukio Mikami, Ernst V Dobschütz, Olaf Sommer, Ulrich Wellner, Michiaki Unno, Ulrich Hopt, Tobias Keck
1228 related Products with: Matrix metalloproteinase-9 derived from polymorphonuclear neutrophils increases gut barrier dysfunction and bacterial translocation in rat severe acute pancreatitis.
100 U96tests5mg96T96tests5mg96tests 1 G96 wells (1 kit)96T 5 GRelated Pathways
#3132479 // To Up
Single-step purification of rat C-reactive protein and generation of monospecific C-reactive protein antibody.
Although Sepharose-phosphorylcholine affinity chromatography has been used extensively to purify some acute phase proteins, the operation has usually been a laborious multi-step procedure. By modifying previously described multi-step protein purification assays, centigram quantities of pure rat C-reactive protein (CRP) could be obtained in a single chromatographic step using affinity chromatography. Rat serum was passed over a column of p-aminophenylphosphorylcholine and extraneous proteins eluted with Tris-saline-Ca2+ buffer. Similar to other purification procedures, CRP was eluted with phosphorylcholine in a Tris-saline-Ca2+ buffer. The technical detail which distinguished this procedure from others, was the use of a phosphorylcholine gradient shallow enough (0.95 mM-2.5 mM) to resolve the eluent into two peaks; the first peak was composed largely of the contaminant, serum amyloid protein (SAP), and the second was composed of CRP. Although there was some overlap between the first and second peak, pure CRP could be obtained by pooling fractions from the trailing shoulder of the second peak. Using this single step procedure, a greater than 25% yield of SAP-free, purified CRP could be obtained. The purified CRP was free of SAP contamination as measured by sodium dodecyl sulfate gradient polyacrylamide gel electrophoresis. Purified CRP was determined to be free of rat albumin, IgG and the C3 component of complement using immunoelectrophoresis. This one-step affinity column chromatography procedure provides a simple, efficient method for collecting large quantities of rat CRP pure enough to be used to obtain a monospecific goat, anti-rat CRP antibody.D J Pruden, K M Connolly, V J Stecher
2543 related Products with: Single-step purification of rat C-reactive protein and generation of monospecific C-reactive protein antibody.
1mg1mg100ul1 mg5 ml20 ml1 mg100 ul1 mg1mg100ul1 mgRelated Pathways
#81231 // To Up
Release of arylsulfatase A but not B from rat mast cells by noncytolytic secretory stimuli.
The net percentage of release of arylsulfatase activity from purified rat mast cells induced by rabbit anti-rat F(ab')2 was consistently only about 1/3 that of histamine. Isoelectric focusing of the released and residual arylsulfatase activities demonstrated specific release of the A type without B and a net percentage of immunologic release of arylsulfatase A equivalent to that of histamine. When the net percentage of histamine and arylsulfatase A release were nearly maximal (88 and 76%) in response to the calcium ionophore A23187, specific release of arylsulfatase B did not occur. Thus, arylsulfatase A and not B was associated with the secretory granule released from the rat mast cell by reversed anaphylaxis or the calcium ionophore. In contrast, subcellular fractionation of water-lysed mast cells yielded arylsulfatase B with the heparin- and chymase-containing granule fraction and arylsulfatase A in the aqueous fraction comprised of cell sap and granule water eluate. It may be that arylsulfatase B resides in a minor second granule, whereas arylsulfatase A is loosely associated with the predominant secretory granule of the rat mast cell.S M Lynch, K F Austen, S I Wasserman
2220 related Products with: Release of arylsulfatase A but not B from rat mast cells by noncytolytic secretory stimuli.
500 mg250 mg2.5 mg2.5 lt25 mg50 mg5 mg1 mg5 mg10 mg50 mgRelated Pathways
Contact Us:
Belgium
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45 Fax 0032 16 50 90 45
[email protected]
France
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50 Fax 01 43 25 01 60
[email protected]
Germany
GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Tel 0241 40 08 90 86 Fax 0241 55 91 05 36
[email protected]
United Kingdom
GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
[email protected]
Also in
Luxembourg +35220880274
Schweiz Züri +41435006251
Danmark +4569918806
Österreich +43720880899
Česká republika Praha +420246019719
Ireland Dublin +35316526556
Norge Oslo +4721031366
Finland Helsset +358942419041
Sverige Stockholm +46852503438
Ελλάς Αθήνα +302111768494
Magyarország Budapest +3619980547
Poland
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
Tel 058 710 33 44
Fax 058 710 33 48
[email protected]
skype gentaurpoland
Nederland
GENTAUR Nederland BV
Kuiper 1
5521 DG Eersel Nederland
Tel 0208-080893 Fax 0497-517897
[email protected]
Italy
GENTAUR SRL
IVA IT03841300167
Piazza Giacomo Matteotti, 6, 24122 Bergamo
Tel 02 36 00 65 93 Fax 02 36 00 65 94
[email protected]
Spain
GENTAUR Spain
Tel 0911876558
[email protected]
Bulgaria
GENTAUR Bulgaria
53 Iskar Str. 1191 Kokalyane, Sofia
Sofia 1000
Tel 0035924682280
Fax 0035929830072
[email protected]