Thioredoxin-Associated TransmembraneProteins: TMX1 and Little Brothers TMX2, TMX3, TMX4 and TMX5
The endoplasmic reticulum (ER) is web site of synthesis and maturation of membrane and secretory proteins in eukaryotic cells. The ER comprises greater than 20 members of the Protein Disulfide Isomerase (PDI) household.
These enzymes regulate formation, isomerization and disassembly of covalent bonds between cysteine residues. As such, PDIs guarantee protein folding, which is required to achieve purposeful and transport-competent construction, and protein unfolding, which facilitates dislocation of faulty gene merchandise throughout the ER membrane for ER-associated degradation (ERAD). The PDI household contains over a dozen of soluble members and few membrane-bound ones. Amongst these latter, there are 5 PDIs grouped within the thioredoxin-related transmembrane (TMX) protein household.
On this evaluation, we summarize the present data on TMX1, TMX2, TMX3, TMX4 and TMX5, their structural options, regulation and roles in biogenesis and management of the mammalian cell’s proteome.
Ectopic Expression of a Transmembrane Protein KaCyt b 6 from a Crimson Seaweed Kappaphycus alvarezii in Transgenic Tobacco Augmented the Photosynthesis and Progress
Cytochrome b6f complicated is a thylakoid membrane-localized protein and catalyses the switch of electrons from plastoquinol to plastocyanin in photosynthetic electron transport chain. Within the current research, Cytochrome b6 (KaCyt b6) gene from Kappaphycus alvarezii (a purple seaweed) was overexpressed in tobacco. A 935 base pair (bp) lengthy KaCyt b6 cDNA contained an open studying body of 648 bp encoding a protein of 215 amino acids with an anticipated isoelectric level of 8.67 and a molecular mass of 24.37 kDa. The KaCyt b6 gene was overexpressed in tobacco beneath management of CaMV35S promoter.
The transgenic tobacco had greater electron switch fee and photosynthetic yield over wild-type and vector management tobacco. The KaCyt b6 tobacco additionally exhibited considerably greater photosynthetic fuel trade (PN) and improved water use effectivity.
The transgenic crops had greater ratio of PN and intercellular CO2. The KaCyt b6 transgenic tobacco confirmed greater estimates of photosystem II quantum yield, greater exercise of the water-splitting complicated, PSII photochemistry, and photochemical quenching. The basal quantum yield of nonphotochemical processes in PSII was recorded decrease in KaCyt b6 tobacco. Transgenic tobacco contained greater contents of carotenoids and complete chlorophyll and likewise had higher ratios of chlorophyll a and b, and carotenoids and complete chlorophyll contents therefore improved photosynthetic effectivity and manufacturing of sugar and starch.
The KaCyt b6 transgenic crops carried out superior beneath management and greenhouse circumstances. To one of the best of our data by way of literature survey, that is the primary report on characterization of KaCyt b6 gene from Okay. alvarezii for enhanced photosynthetic effectivity and progress in tobacco.
Description: Recombinant human Interleukin-8 is a disulfide-linked monomer protein consisting of 78 amino acid residues, migrates as an approximately 9 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Interleukin-8 mature chain was expressed in E. coli.
Description: Recombinant human Interleukin-8 is a disulfide-linked monomer protein consisting of 78 amino acid residues, migrates as an approximately 9 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Interleukin-8 mature chain was expressed in E. coli.
Description: Il-8 or CXCL8 was originally discovered and purified as a neutrophil chemotactic and activating factor. It was also referred to as neutrophil chemotactic factor (NCF), neutrophil activating protein (NAP), monocytederived neutrophil chemotactic factor (MDNCF), T lymphocyte chemotactic factor (TCF), granulocyte chemotactic protein (GCP) and leukocyte adhesion inhibitor (LAI). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes, and various tumor cell lines, can produce CXCL8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS, and viruses. CXCL8 is a member of the alpha (CXC) subfamily of chemokines, which also includes platelet factor-4, GRO, and IP10.
Description: Il-8 or CXCL8 was originally discovered and purified as a neutrophil chemotactic and activating factor. It was also referred to as neutrophil chemotactic factor (NCF), neutrophil activating protein (NAP), monocytederived neutrophil chemotactic factor (MDNCF), T lymphocyte chemotactic factor (TCF), granulocyte chemotactic protein (GCP) and leukocyte adhesion inhibitor (LAI). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes, and various tumor cell lines, can produce CXCL8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS, and viruses. CXCL8 is a member of the alpha (CXC) subfamily of chemokines, which also includes platelet factor-4, GRO, and IP10.
Description: Fully biologically active when compared to standard. The ED50 as determined by a chemotaxis bioassay using human CXCR2 transfected mouse BaF3 cells is less than 2 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.
Description: Fully biologically active when compared to standard. The ED50 as determined by a chemotaxis bioassay using human CXCR2 transfected mouse BaF3 cells is less than 2 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.
Description: Interleukin 8 (IL-8 or chemokine (C-X-C motif) ligand 8, CXCL8) is a chemokine produced by macrophages and other cell types such as epithelial cells, airway smooth muscle cells and endothelial cells. IL-8, also known as neutrophil chemotactic factor, has two primary functions. It induces chemotaxis in target cells, primarily neutrophils but also other granulocytes, causing them to migrate toward the site of infection. IL-8 also stimulates phagocytosis once they have arrived. IL-8 is also known to be a potent promoter of angiogenesis. In target cells, IL-8 induces a series of physiological responses required for migration and phagocytosis, such as increases in intracellular Ca2+, exocytosis (e.g. histamine release), and the respiratory burst. IL-8 can be secreted by any cells with toll-like receptors that are involved in the innate immune response and has been demonstrated to be a signatory chemokine of CR2+ naive T cells, also known as recent thymic emigrants. Usually, it is the macrophages that see an antigen first, and thus are the first cells to release IL-8 to recruit other cells. Both monomer and homodimer forms of IL-8 have been reported to be potent inducers of the chemokine receptors CXCR1 and CXCR2. The homodimer is more potent, but methylation of Leu25 can block the activity of homodimers.
Description: IL-8, also known as neutrophil chemotactic factor, has two primary functions. It induces chemotaxis in target cells, primarily neutrophils but also other granulocytes, causing them to migrate toward the site of infection. IL-8 also stimulates phagocytosis once they have arrived. IL-8 is also known to be a potent promoter of angiogenesis. In target cells, IL-8 induces a series of physiological responses required for migration and phagocytosis, such as increases in intracellular Ca2+, exocytosis (e.g. histamine release), and the respiratory burst.IL-8 can be secreted by any cells with toll-like receptors that are involved in the innate immune response. Usually, it is the macrophages that see an antigen first, and thus are the first cells to release IL-8 to recruit other cells. Both monomer and homodimer forms of IL-8 have been reported to be potent inducers of the chemokine receptors CXCR1 and CXCR2. The homodimer is more potent, but methylation of Leu25 can block the activity of homodimers.
Description: Quantitative sandwich ELISA kit for measuring Human Interleukin 8, IL-8 in samples from serum, cell culture supernates, saliva, urine, cerebrospinalfluid (CSF), tissue homogenates, cell lysates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.
Description: Quantitative sandwich ELISA kit for measuring Human Interleukin 8, IL-8 in samples from serum, cell culture supernates, saliva, urine, cerebrospinalfluid(CSF), tissue homogenates, cell lysates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.
The Transmembrane Proteins M6 and Anakonda Cooperate to Provoke Tricellular Junction Meeting in Epithelia of Drosophila
Cell vertices in epithelia comprise specialised tricellular junctions (TCJs) that seal the paracellular area between three adjoining cells [1, 2]. Though TCJs play basic roles in tissue homeostasis, pathogen protection, and in sensing pressure and cell form [3-5], how they’re assembled, maintained, and transformed is poorly understood. In Drosophila, the transmembrane proteins Anakonda (Aka [6]) and Gliotactin (Gli [7]) are TCJ elements important for epithelial barrier formation.
Moreover, the conserved four-transmembrane-domain protein M6, the one myelin proteolipid protein (PLP) member of the family in Drosophila, localizes to TCJs [8, 9]. PLPs affiliate with cholesterol-rich membrane domains and induce filopodia formation [10, 11] and membrane curvature [12], and Drosophila M6 acts as a tumor suppressor [8], however its function in TCJ formation remained unknown.
Right here, we present that M6 is crucial for the meeting of tricellular, however not bicellular, occluding junctions, and for barrier perform in embryonic epithelia. M6 and Aka localize to TCJs in a mutually dependent method and are collectively required for TCJ localization of Gli, whereas Aka and M6 localize to TCJs independently of Gli. Aka acts instructively and is adequate to direct M6 to cell vertices within the absence of septate junctions, whereas M6 is required permissively to take care of Aka at TCJs.
Moreover, M6 and Aka are mutually dependent for his or her accumulation in a low-mobility pool at TCJs. These findings counsel a hierarchical mannequin for TCJ meeting, the place Aka and M6 promote TCJ formation by way of synergistic interactions that demarcate a definite plasma membrane microdomain at cell vertices.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.
Description: Human Dkk-1 Recombinant Protein expressed in Baculovirus with His-tag. Sequence domain: 32-266aa. Application(s): SDS-PAGE. Endotoxin: < 1 EU per 1ug of protein (determined by LAL method).
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-l1 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-3 has been shown to potentiate, rather than inhibit, Wnt signaling through interactions with the high-affinity, transmembrane coreceptors Kremen-1 (Krm1) and Kremen-2 (Krm2). Recombinant human DKK-3 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 36.3 kDa and contains 329 amino acid residues. Due to glycosylation, human DKK-3 migrates at an apparent molecular weight of approximately 39-49 kDa by SDS-PAGE analysis under non-reducing conditions.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-l1 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-3 has been shown to potentiate, rather than inhibit, Wnt signaling through interactions with the high-affinity, transmembrane coreceptors Kremen-1 (Krm1) and Kremen-2 (Krm2). Recombinant human DKK-3 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 36.3 kDa and contains 329 amino acid residues. Due to glycosylation, human DKK-3 migrates at an apparent molecular weight of approximately 39-49 kDa by SDS-PAGE analysis under non-reducing conditions.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 25.8 kDa and contains 234 amino acid residues. Due to glycosylation, human DKK-2 migrates at an apparent molecular weight of approximately 31-36 kDa by SDS-PAGE analysis under non-reducing conditions.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 25.8 kDa and contains 234 amino acid residues. Due to glycosylation, human DKK-2 migrates at an apparent molecular weight of approximately 31-36 kDa by SDS-PAGE analysis under non-reducing conditions.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 fused to a C terminal His-tag derived from E. coli has a molecular weight of 26.0 kDa and contains 234 amino acid residues.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 fused to a C terminal His-tag derived from E. coli has a molecular weight of 26.0 kDa and contains 234 amino acid residues.
Description: Human Dkk-3 Recombinant Protein expressed in Baculovirus with His-tag. Sequence domain: 22-350aa. Application(s): SDS-PAGE. Endotoxin: < 1 EU per 1ug of protein (determined by LAL method).
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