| Description | Complement C3 (C3) is the most abundant component of the complement system, with levels in human plasma of ~1.2-1.5 mg/ml. It is central to the activation of both the classical and alternative complement pathways, both of which lead to the proteolytic processing of C3 to C3a and C3b. C3 exists as a Complement C3 (C3) is the most abundant component of the complement system, with levels in human plasma of ~1.2-1.5 mg/ml. It is central to the activation of both the classical and alternative complement pathways, both of which lead to the proteolytic processing of C3 to C3a and C3b. C3 exists as a heterodimer with molecular masses of 115 kDa and 75 kDa, although it is readily processed to create C3a, C3b or C3c depending on the processed state.Reacts to C3 antisera on Western BlotNegative against C4 antisera on Western BlotRef: Tack BF and JW Prahl. 1976. Biochemistry. 15:4513, Tack BF et al. 1981. Methods Enzymol. 80:64, Janatova, J. 1988. Methods Enzymol. 162:579... Read More | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 8.38 | Crude collagenase preparations contain several isoforms of two different collagenases, a sulfhydryl protease, clostripain, a trypsin-like enzyme, and an aminopeptidase. This combination of collagenolytic and proteolytic activities is effective at breaking down intercellular matrices, the essential Crude collagenase preparations contain several isoforms of two different collagenases, a sulfhydryl protease, clostripain, a trypsin-like enzyme, and an aminopeptidase. This combination of collagenolytic and proteolytic activities is effective at breaking down intercellular matrices, the essential part of tissue dissociation. One component of the complex is a hydrolytic enzyme which degrades the helical regions in native collagen preferentially at the Y-Gly bond in the sequence Pro-Y-Gly-Pro, where Y is most frequently a neutral amino acid. This cleavage yields products susceptible to further peptidase digestion. Crude collagenase is inhibited by metal chelating agents such as cysteine, EDTA or o-phenanthroline but not DFP. It is also inhibited by α2-macroglobulin, a large plasma glycoprotein. Ca2+ is required for enzyme activity. Particular enzymatic profiles of each collagenase have been correlated with the tissues from which the cells for study were obtained (or with the uses to which the cells are put) and as a result of the correlations several types of crude collagenases have been established by Aladdin: Types 1, 2, 3, and 4.This collagenase has been tested with cell lines to verify the product is not cytotoxic. Collagenase is typically used to digest the connective components in tissue samples to liberate individual cells. The concentration for cartilage dispersal is 1-2 mg/ml, but literature searches should be performed for species specific and/or tissue specific concentrations... Read More | Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with anaerobic metabolism and pyruvate reduction.Catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+Recombinant rabbit muscle Lactate Dehydrogenase produced in E.Coli. Chromatographically purified. A lyophilized powder... Read More | Purity> 95 % by SDS-PAGE and HPLC analysesFunctionThis receptor has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen) |