GM-CSF Receptor Beta, also known as CSF2RB is a member of the type I cytokine receptor family. CSF2RB is a high affinity receptor for interleukin-3, interleukin-5 as well as granulocyte-macrophage colony-stimulating factor. CSF2RB unique form of receptor assembly applies also to IL-3 and IL-5 receptors, providing a structural basis for understanding their activation mechanism which is essential for the development of therapeutics.
Description
CSF2RB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 435 amino acids and having a molecular mass of 49.7kDa. CSF2RB is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Physical Appearance
Sterile Filtered clear solution.
Formulation
CSF2RB protein solution containing Phosphate Buffered Saline and 10% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Acidic fibroblast growth factor is a member of the fibroblast growth factor family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF1 functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor.FGF1 acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Description
Fibroblast Growth Factor-acidic Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids and having a molecular mass of 17.3kDa. The FGF1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4, with 0.5mM DTT, 2mM EDTA, and 5 % Trehalose.
Solubility
It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-acidic Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized FGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-acidic should be stored at 4°C between 2-7 days and for future use below -18°C.
The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×106 IU/mg in the presence of 10µg/ml Heparin.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Description
Growth Hormone Bovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21.8 kDa. The GH Bovine Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The Bovine Growth Hormone protein was lyophilized from a concentrated solution with 4.5mM NaHCO3 adjusted to pH 8-9.
Solubility
It is recommended to reconstitute the lyophilized Bovine Growth Hormone in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized Bovine Growth Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH Bovine should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein . Please prevent freeze-thaw cycles.
Purity
Greater than 98.0% as determined by: Analysis by RP-HPLC. Analysis by -PAGE.
The activity as determined by the PDFP13B9 cells stably transfected with rabbit GH receptors. Bovine GH is also capable of forming a 1:2 complex with the recombinant ovine growth hormone receptor extracellular domain .
Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.63 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GENE computer analysis program of protein sequences.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Description
Growth Hormone Ovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 22015 Dalton. The GH Ovine Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein was lyophilized from a concentrated solution with 0.0045mM NaHCO3.
Solubility
It is recommended to reconstitute the lyophilized Growth Hormone in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized Growth Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH Ovine should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein . Please prevent freeze-thaw cycles.
Purity
Greater than 98.0% as determined by: Analysis by SEC-HPLC. Analysis by -PAGE.
The activity as determined by the dose-dependant stimulation of the proliferation FDCP13B9 cells.
Protein content
Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 0.7 as the extinction coefficient for a 0.1% solution. This value is calculated by the PC GENE computer analysis program of protein sequences .
2. Analysis by RP-HPLC, using a calibrated solution of GH as a Reference Standard.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Myostatin , a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.
Description
Recombinant Human Myostatin Propeptide is a 27.8kDa protein containing 244 amino acid residues of the human Myostatin Propeptide.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered white lyophilized powder.
Formulation
Lyophilized with no additives.
Solubility
It is recommended to reconstitute the lyophilized Myostatin Propeptide in sterile 20mM HCl at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
The protein has full biological activity when compared to a standard. The activity is determined by its ability to inhibit 50ng/ml of Myostatin on MPC-11 cells and is typically 0.13-0.2 μg/ml.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
GDF8 is a member of the bone morphogenetic protein family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
Description
Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa. Myostatin Propetide is fused to a 10 aa C-terminal His tag.
Source
HEK 293.
Physical Appearance
Filtered colorless solution.
Formulation
Myostatin Propetide solution at a concentration of 0.25mg/ml in phosphate buffered saline pH 8.0 and 20% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein . Avoid multiple freeze-thaw cycles.
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
Description
Prolactin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.5 kDa. The Prolactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein was lyophilized from a concentrated solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.
Solubility
It is recommended to reconstitute the lyophilized Prolactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein . Please prevent freeze-thaw cycles.
Purity
Greater than 95.0% as determined by: Analysis by RP-HPLC. Analysis by -PAGE.
Amino acid sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Pro-Ile-Cys.
Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of rat lymphoma, Nb2-11 was found to be < 0.065 ng/ml corresponding to a specific activity of 15,400,000 Units/mg.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
Description
Prolactin Mouse produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids and having a molecular mass of 25 kDa. Prolactin Mouse protein is fused to a 23 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Physical Appearance
Sterile filtered colorless solution.
Formulation
The Prolactin Mouse solution contains Phosphate Buffered Saline and 20% glycerol.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein .
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
Description
Prolactin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.6 kDa. The Prolactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein was lyophilized from a concentrated solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.
Solubility
It is recommended to reconstitute the lyophilized Prolactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein . Please prevent freeze-thaw cycles.
Purity
Greater than 95.0% as determined by: Analysis by SEC-HPLC. Analysis by -PAGE.
Amino acid sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Pro-Val-Cys.
Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of rat lymphoma, Nb2-11 was found to be < 0.065 ng/ml corresponding to a specific activity of 15,400,000 Units/mg.
Usage
ProSpec’s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
TET phosphoramidite for synthesis of fluorescently labeled oligonucleotides, pure 6-isomer.
TET (tetrachlorofluorescein) is a green-fluorescent fluorescein derivate (absorption maximum at 519 nm, emission maximum at 535 nm).
TET phosphoramidite is used for synthesis of fluorescently-labeled primers and hybridization probes for qPCR. TET can be used with DusQ1 fluorescence quencher (can be used with 500 Å DusQ1 CPG 500).
5’-labeled primers are used with non-labeled reverse primers for microsatellite amplification via RCR followed by fragment analysis. TET-labeled amplification products can be analyzed using various sequencers for capillary electrophoresis, including ABI PRISM® 310 Genetic Analyzer.
5′ 标记的引物与未标记的反向引物一起使用，通过 RCR 进行微卫星扩增，然后进行片段分析。 TET 标记的扩增产物可以使用各种毛细管电泳测序仪进行分析，包括 ABI PRISM® 310 遗传分析仪。
Recommendations for using the reagent:
使用试剂的建议：
Condensation: 3 min.
Deprotection: standard conditions with 25% aqueous ammonium solution; deprotection time depends on nucleic base profile and their protective properties (deprotection for 17 hours at 55°C removes all protection groups from standard nucleic acids). AMA (1:1 mixture of concentrated aqueous ammonium/40% aqueous methylamine) can be used with ~5% non-fluorescent by-product forming. To avoid formation of the by-product, start deprotection with ammonium (30 min at room temperature), then add an equivalent volume of 40% aqueous methylamine solution and continue deprotection as usual with AMA (10 min at 65°C).
Storage: 12 months after receival at -20°C in the dark. Transportation: at room temperature for up to 3 weeks. Avoid prolonged exposure to light. Desiccate.
