| Description | β-Defensin-4 human is an inducible peptide with a specific salt-sensitive spectrum of antimicrobial activity | Inquire | Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 10.16 at 1.0 mg/ml for pure C3Molecular Weight187,000 Da (2 chains)General DescriptionRat C3 is purified from pooled normal rat serum. C3 is central to the activation of all three pathways of complement activation (Law, S.K.A. and Reid, KProtein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 10.16 at 1.0 mg/ml for pure C3Molecular Weight187,000 Da (2 chains)General DescriptionRat C3 is purified from pooled normal rat serum. C3 is central to the activation of all three pathways of complement activation (Law, S.K.A. and Reid, K.B.M. (1995)). Initiation of each pathway generates proteolytic enzyme complexes (C3 convertases) which are bound to the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. For a brief time (~60 µs) this nascent C3b is capable of reacting with and covalently coupling to hydroxyl groups on the target surface. Carbohydrates are the favored target, but protein hydroxyls and amino groups also react. This process of tagging the target surface with C3b is called opsonization. The reactive site in nascent C3b is a thioester (Tack B.J., et al. (1980); Pangburn M.K. and MüllerEberhard H.J. (1980)) and C3b is linked to the target through a covalent ester bond (an amide bond is formed if C3b is attached to amino groups). Most of the C3 activated during complement activation never attaches to the surface because its thioester reacts with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all three pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane. Surface-bound C3b and its breakdown products iC3b and C3d are recognized by numerous receptors on lymphoid and phagocytic cells which use the C3b ligand to stimulate antigen presentation to cells of the adaptive immune system. The end result is an expansion of target-specific B-cell and T-cell populations.Physical Characteristics & StructureThe calculated molecular weight of rat C3 based on its amino acid sequence is 184,111daltons (without the signal peptide) and is similar to that of human C3 (185,000 daltons).The molecular weight of rat C3 as determined by SDS/polyacrylamide gel electrophoresis has been reported by Daha, M.R. et al., (1979) to be 187,000 daltons composed of two disulfide linked chains, alpha chain (123,000 daltons) and beta chain (76,000 daltons). The extinction coefficient of rat C3 (E1%/280nm = 10.16) is calculated based on its amino acid sequence using ProtParam and assumes all pairs of Cys residues form cystines (i.e. a pair of cysteine molecules are joined by a disulfide bond). The theoretical pI of rat C3 is 6.12. The normal plasma concentration of C3 inWistar rats has been reported to be 0.581mg/ml (Daha, M.R. et al., (1979)).FunctionThe biological functions of C3 are described above in the General Description section.GeneticsRat C3 chromosome location 9. The NCBI Gene ID number for rat C3 is 24232 and UniProt accession number is P01026.Precautions/Toxicity/HazardsThis protein is purified from animal plasma/serum and therefore precautions appropriate for handling any animal blood-derived product must be used.ReferencesLaw, S.K.A. and Reid, K.B.M. (1995) Complement 2nd Edition (ISBN 0199633568) Oxford University Press, Oxford.Tack BF, Harrison RA, Janatova J, Thomas ML, Prahl JW. (1980) Evidence for presence of an internal thiolester bond in third component of human complement. Proc Natl Acad Sci U S A. 77:5764-8.Pangburn M.K. and Müller-Eberhard H.J. (1980) Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement. J Exp Med. 152:1102-14.Daha MR, Stuffers-Heiman M, Kijlstra A and Van ES LA. (1979) Isolation and characterization of the third component of rat complement. Immunology 36:63-70... Read More | Fibronectin (FN) is a particularly important and well-studied component of the extracellular matrix, and is known to play a key role in cell adhesion, growth, spreading, migration, differentiation and proliferation. Fn is a 200-250 kDa glycoprotein composed of 2 subunits bound via a disulfide bond. Fibronectin (FN) is a particularly important and well-studied component of the extracellular matrix, and is known to play a key role in cell adhesion, growth, spreading, migration, differentiation and proliferation. Fn is a 200-250 kDa glycoprotein composed of 2 subunits bound via a disulfide bond. Currently, the Fn is purified from the plasma, which however is limited by the availability of supply. The the recombinant human fibronectin (OsrhFN) was expressed in the rice endosperm platform, which is animal component free and has high purity, and has been demonstrated has the same physical and chemical with the plasma derived Fn. OsrhFN provides a safety solution to replace the plasma derived FN.pH value: 6.0-8.0... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:ROR1 (Receptor tyrosine kinase-like orphan receptor 1), also known as neurotrophic tyrosine kinase receptor-related 1 (NTRKR1), is a member of the ROR family within the receptor tyrosine kinases (RTK) superfamily. Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:ROR1 (Receptor tyrosine kinase-like orphan receptor 1), also known as neurotrophic tyrosine kinase receptor-related 1 (NTRKR1), is a member of the ROR family within the receptor tyrosine kinases (RTK) superfamily. Two ROR family members (ROR1 and ROR2) have been identified and are characterized by their intracellular tyrosine kinase domains, which are highly related to those of the Trk-family receptor tyrosine kinases, and by their extracellular Frizzled-like cysteine-rich domains and kringle domains, common to receptors of the Wnt family members. Human ROR1 is a type I transmembrane protein with 937 amino acids in length. It contains a 29 amino acid signal sequence, a 377 amino acid extracellular domain (ECD), a 21 amino acid transmembrane segment, and a 510 amino acid cytoplasmic region. Human ROR1 shares 97% and 58% amino acid sequence identity with mouse ROR1 and human ROR2, respectively. ROR1 has been shown to play crucial roles in developmental morphogenesis by acting as receptors or co-receptors to mediate Wnt5a-induced signaling. The bioactivity of ROR1 is measured by its ability to bind biotinylated recombinant mouse Wnt-5a in a functional ELISA... Read More |