| Description | Native calpain-1 from porcine erythrocytes. Ca2+-dependent heterodimeric cysteine proteinase with low Ca2+ requirement (EC50= 2 µM). Participates in the ATP release reaction of platelets stimulated with thrombin.Native calpain-1 from porcine erythrocytes. Calpains are a family of calcium-Native calpain-1 from porcine erythrocytes. Ca2+-dependent heterodimeric cysteine proteinase with low Ca2+ requirement (EC50= 2 µM). Participates in the ATP release reaction of platelets stimulated with thrombin.Native calpain-1 from porcine erythrocytes. Calpains are a family of calcium-dependent thiol-proteases that degrade a wide variety of cytoskeletal, membrane-associated, and regulatory proteins. The two major isoforms, calpain I (µ-form) and calpain II (m-form), differ in their calcium requirement for activation. Calpain I requires only micromolar amounts of calcium (EC50 = 2 µM), while calpain II requires millimolar amounts (EC50 = 1 mM).Calpains are heterodimers of 80 kDa and 30 kDa subunits. The 80 kDa unit has the catalytic site and is unique to each isozyme. The 30 kDa unit is a regulatory subunit and common to both calpain I and calpain II. The 80 kDa unit consists of four domains (I-IV). The 30 kDa unit has two domains (V and VI).• Domain I is partially removed during autolysis.• Domain II is the protease domain.• Domain III exhibits a homology with typical calmodulin binding proteins and interacts with calcium binding domains (IV and VI) and frees domain II for protease activity.• Domain IV is a calcium binding domain.• Domain V contains a hydrophobic region and is essential for calpain interaction with membranes.• Domain VI is a calcium binding domain.More recently, attention has been focused on the pathological significance of calcium accumulation in the central nervous system following cerebral ischemia and traumatic brain injury. Over-activation of NMDA, kainate, and AMPA receptors in the brain leads to sustained influx in Ca2+ through voltage gated Ca2+ channels. Disturbances in calcium homeostasis result in the activation of several calcium-dependent enzymes including calpains. Over-expression of calpains has been positively linked to both acute and chronic neurodegenerative processes including ischemia, trauma, and Alzheimer′s disease. In Alzheimer′s disease the ratio of active (76 kDa) to inactive (80 kDa) calpain I is reported to be much higher. Calpain proteolysis is usually the late-stage common pathway towards cell death induced by excitotoxic compounds... Read More | Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.974 at 1.0 mg/ml for pure C3bMolecular Weight185,000 Da (2 chains)General DescriptionCynomolgus monkey C3 (cyno C3) is purified from pooled normal cynomolgus monkey serum. C3 is central to the activation of all three pathways of Protein Purity≥85% by SDS PAGEExtinction CoeffA280 nm = 0.974 at 1.0 mg/ml for pure C3bMolecular Weight185,000 Da (2 chains)General DescriptionCynomolgus monkey C3 (cyno C3) is purified from pooled normal cynomolgus monkey 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 & StructureCynomolgus monkey C3 is an uncharacterized protein. The calculated molecular weight based on its amino acid sequence is 184,926 daltons similar to that of human C3 (185,000 daltons). Like human C3, cyno C3 is composed of two disulfide-linked chains. Analysis of purified cyno C3 by SDS/polyacrylamide gel electrophoresis under non-reduced conditions shows the mobility of cyno C3 to be similar to that of human C3. Under reduced conditions, the migration of the alpha chain of cyno C3 is comparable to that of human C3 alpha chain (110,000 daltons) while the beta chain migrates slightly ahead of the human C3 beta chain (75,000daltons).The extinction coefficient of cyno C3 is calculated from its amino acid sequence using ProtParam and assumes all pairs of Cys residues form cystines (i.e. a pair of cystine molecules are joined by a disulfide bond). The theoretical pI value for cyno monkey C3 is 6.03. Employing immunoturbidimetric method the serum concentration of cyno C3 has been reported to be 1.27 mg/ml in males and 1.1 mg/ml in female monkeys (Park H-K et al., (2016)). FunctionThe biological functions of C3 are described above in the General Description and Physical Characteristics sections.GeneticsCynomolgus monkey C3 chromosome location 19. The NCBI Gene ID number for Cynomolgus monkey C3 is 102131458 and UniProt accession number is A0A2K5VPN1.Precautions/Toxicity/HazardsThis protein is purified from animal 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.Park H-K, Cho J-W, Lee B-S, Park H, Han J-S, Yang M-J, Im W-J, Park D-Y, Kim W-J, Han SC, Kim Y-B. (2016) Reference values of clinical pathology parameters in cynomolgus monkeys (Macaca fascicularis) used in preclinical studies. Lab Anim Res. 32(2):79-86... Read More | HIV-1 Tat Protein Peptide is a synthetic peptide that includes the sequence responsible for the cellular uptake of the human immunodeficiency virus-1 Tat protein, consisting of the polycationic region 49-57. The peptide is part of the protein transduction domain (PTD) and was shown to enable the HIV-1 Tat Protein Peptide is a synthetic peptide that includes the sequence responsible for the cellular uptake of the human immunodeficiency virus-1 Tat protein, consisting of the polycationic region 49-57. The peptide is part of the protein transduction domain (PTD) and was shown to enable the introduction of nucleic acids into cells... Read More | Purity>95% as determined by SDS-PAGE and Coomassie blue stainingFunctionThe heparin-binding fibroblast growth factors play important roles in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. They are potent mitogens in vitro.Sequence Purity>95% as determined by SDS-PAGE and Coomassie blue stainingFunctionThe heparin-binding fibroblast growth factors play important roles in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. They are potent mitogens in vitro.Sequence similaritiesBelongs to the heparin-binding growth factors family.Cellular localizationSecreted. Cytoplasm. Cytoplasm > cell cortex. Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1... Read More | Inquire |