Vital Zr isotope variations in single zircon grains recording magma evolution historical past
Zircons extensively happen in magmatic rocks and sometimes show inner zonation finely recording the magmatic historical past. Right here, we offered in situ high-precision (2SD <0.15‰ for δ94Zr) and high-spatial-resolution (20 µm) steady Zr isotope compositions of magmatic zircons in a collection of calc-alkaline plutonic rocks from the juvenile a part of the Gangdese arc, southern Tibet.
These zircon grains are internally zoned with Zr isotopically mild cores and more and more heavier rims. Our information recommend the preferential incorporation of lighter Zr isotopes in zircon from the soften, which might drive the residual soften to heavier values. The Rayleigh distillation mannequin can properly clarify the noticed inner zoning in single zircon grains, and the best-fit fashions gave common zircon-melt fractionation components for every pattern starting from 0.99955 to 0.99988.
The common fractionation components are positively correlated with the median Ti-in-zircon temperatures, indicating a robust temperature dependence of Zr isotopic fractionation. The outcomes display that in situ Zr isotope analyses could be one other highly effective contribution to the geochemical toolbox associated to zircon. The findings of this examine remedy the basic difficulty on how zircon fractionates Zr isotopes in calc-alkaline magmas, the main sort of magmas that led to forming continental crust over time. The outcomes additionally present the good potential of steady Zr isotopes in tracing magmatic thermal and chemical evolution and thus presumably continental crustal differentiation.
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: 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: Description of target: This gene encodes a protein that is a member of the dickkopf family. It is a secreted protein with two cysteine rich regions and is involved in embryonic development through its inhibition of the WNT signaling pathway. Elevated levels of DKK1 in bone marrow plasma and peripheral blood is associated with the presence of osteolytic bone lesions in patients with multiple myeloma.;Species reactivity: Human;Application: ELISA;Assay info: Quantitative Colorimentric Sandwich ELISA;Sensitivity: 63 pg/mL
Description: Human Dkk-1 Protein, His Tag, premium grade (DK1-H5221) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # NP_036374.1).
Description: Human Dkk-1 Protein, His Tag, premium grade (DK1-H5221) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # NP_036374.1).
Description: Human Dkk-1 Protein, His Tag, premium grade (DK1-H5221) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # NP_036374.1).
Description: Human Dkk-1 Protein, His Tag, premium grade (DK1-H5221) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # NP_036374.1).
Description: Biotinylated Human Dkk-1, Fc,Avitag (DK1-H82F5) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # O94907-1).
Description: DKK-1 is a protein that is a member of the dickkopf family. It is a secreted protein with two cysteine rich regions and is involved in embryonic development through its inhibition of the WNT signaling pathway. Elevated levels of DKK-1 in bone marrow plasma and peripheral blood is associated with the presence of osteolytic bone lesions in patients with multiple myeloma.
Ab initio quantum chemical research of isotopic fractionation throughout acid digestion response of dolomite for clumped isotope software
acid to extract CO2 that carries the isotopic signature of the reacting carbonates, and the quantity of clumping within the product CO2 is measured. Earlier theoretical fashions for figuring out clumped isotopic fractionation in product CO2 throughout acid digestion of carbonates are impartial of the cations current within the carbonate lattice. Therefore additional examine is required to know the cationic impact.
Strategies: We studied the acid response mechanism primarily based on the protonation of carbonates, calculated the acid fractionation factor for dolomite utilizing the partition features and vibrational frequencies obtained for the transition state construction, and decided the impact of cations on the acid fractionation issue. Experimentally carbonates are reacted utilizing the modified sealed vessel methodology and analyzed within the dual-inlet of a ThermoFinnigan MAT 253 isotope ratio mass spectrometer.
Outcomes: Theoretically obtained acid fractionation issue could be expressed as Δ47 acid fractionation in dolomite = -0.28563 + 0.49508*(105 / T2 ) – 0.08231* (105 /T2 )2 for a temperature vary between 278.15 Okay and 383.15 Okay. The theoretical slope of the dolomite-acid digestion curve is decrease than that of the calcite-acid digestion curve obtained utilizing the an identical response mechanism. Our theoretical slope is in keeping with the end result from the frequent acid bathtub experiments however greater than the slope obtained in our experimental examine utilizing the modified sealed vessel methodology and in a earlier theoretical examine utilizing the H2 CO3 mannequin.
Conclusions: The transition state construction, obtained in our examine, contains the cations current within the carbonate minerals and gives distinct acid fractionation components for calcite and dolomite.
The noticed gentler slope of theoretically calculated dolomite-acid digestion curve than of the calcite curve is predicted contemplating the stronger Mg-O bond. Our experimental strategy invokes post-digestion isotopic trade and agrees with the earlier theoretical estimates the place post-digestion isotopic fractionation was thought-about.
Mercury isotopes of key tissues doc mercury metabolic processes in seabirds
Seabirds accumulate important quantities of mercury (Hg) as a consequence of their long-life span along with their medium to excessive trophic place in marine meals webs. Hg speciation and Hg isotopic analyses of whole Hg in numerous tissues (pectoral muscle tissues, liver, mind, kidneys, blood and feathers) have been assessed to research their cleansing mechanisms.
Three species with contrasted ecological traits have been studied: the Antarctic prion (zooplankton feeder), the white-chinned petrel (pelagic generalist client) and the southern large petrel (scavenger on seabirds and marine mammals). The distinction of mass-dependent fractionation (MDF, δ202Hg) values between liver and muscle tissues (as much as 0.94 ‰) in all three seabirds strongly suggests hepatic demethylation of the isotopically lighter methylmercury (MeHg) and subsequent redistribution of the isotopically heavier fraction of MeHg in direction of the muscle tissues. Equally, greater δ202Hg values in feathers (as much as 1.88 ‰) relative to muscle tissues and better proportion of MeHg in feathers (94-97%) than muscle tissues (30-70%) doubtless point out potential MeHg demethylation in muscle and preferential excretion of MeHg (isotopically heavier) within the rising feathers throughout moult.
The extents of those key cleansing processes have been strongly depending on the species-specific cleansing methods and ranges of dietary MeHg publicity. We additionally discovered greater mass-independent fractionation (MIF, Δ199Hg) values in feathers relative to inner tissues, presumably as a consequence of completely different integration occasions of Hg publicity between completely energetic organs and inert tissues as feathers. Hg isotope variations reported on this examine present proof of cleansing processes in seabirds and suggest a strong strategy for deep investigation of the Hg metabolic processes in seabirds.
Description: Recombinant Human C-X-C Motif Chemokine 14 is produced by our E.coli expression system and the target gene encoding Ser35-Glu111 is expressed.
Description: Recombinant Human C-X-C Motif Chemokine 14 is produced by our E.coli expression system and the target gene encoding Ser35-Glu111 is expressed.
Description: Chemokine (CXC motif) ligand 14, also known as breast and kidney-expressed chemokine (BRAK), is a CXC chemokine that is a potent chemoattractant for neutrophils but not for T-cells, B-cells, monocytes or granulocytes. Mature CXCL14 has many conserved features of the CXC family and is 30% homologous to the MIP-α and MIP-β sequences, but differs in that it has an additional five amino acid sequence in between the third and fourth cysteines and a short N-terminus. It is usually highly expressed near its fibroblast source and in epidermal fibroblasts and keratinocytes of skin, but is absent from cancer cells.
Description: Chemokine (CXC motif) ligand 14, also known as breast and kidney-expressed chemokine (BRAK), is a CXC chemokine that is a potent chemoattractant for neutrophils but not for T-cells, B-cells, monocytes or granulocytes. Mature CXCL14 has many conserved features of the CXC family and is 30% homologous to the MIP-α and MIP-β sequences, but differs in that it has an additional five amino acid sequence in between the third and fourth cysteines and a short N-terminus. It is usually highly expressed near its fibroblast source and in epidermal fibroblasts and keratinocytes of skin, but is absent from cancer cells.
Description: Breast and Kidney-expressed chemokine (BRAK) is a CXC chemokine expressed in normal tissue in the absence of inflammatory stimuli, and infrequently expressed in cancer cell lines. BRAK is known to be a highly selective monocyte chemoattractant. However, main function and receptor selectivity is unknown at this time. BRAK contains the four highly conserved cysteine residues present in CXC chemokines. The sequence of the mature protein consists of 87 amino acid residues, and is approximately 30% homologous to the sequences of MIP-2 alpha and beta. Recombinant human BRAK is a 9.4 kDa protein containing 77 amino acid residues.
Description: Breast and Kidney-expressed chemokine (BRAK) is a CXC chemokine expressed in normal tissue in the absence of inflammatory stimuli, and infrequently expressed in cancer cell lines. BRAK is known to be a highly selective monocyte chemoattractant. However, main function and receptor selectivity is unknown at this time. BRAK contains the four highly conserved cysteine residues present in CXC chemokines. The sequence of the mature protein consists of 87 amino acid residues, and is approximately 30% homologous to the sequences of MIP-2 alpha and beta. Recombinant human BRAK is a 9.4 kDa protein containing 77 amino acid residues.
Description: Breast and Kidney-expressed chemokine (BRAK) is a CXC chemokine expressed in normal tissue in the absence of inflammatory stimuli, and infrequently expressed in cancer cell lines. BRAK is known to be a highly selective monocyte chemoattractant. However, main function and receptor selectivity is unknown at this time. BRAK contains the four highly conserved cysteine residues present in CXC chemokines. The sequence of the mature protein consists of 87 amino acid residues, and is approximately 30% homologous to the sequences of MIP-2 α and β. Recombinant human BRAK is a 9.4 kDa protein containing 77 amino acid residues.
Description: CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.;The CXCL14 is purified by proprietary chromatographic techniques.
Description: CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10.66 kDa. ;The Human BRAK contains a 10 a.a. fusion His tag at N-Terminus. ;The BRAK is purified by proprietary chromatographic techniques.
