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Name :
FDFT1 HumanDescription:
Farnesyl-Diphosphate Farnesyltransferase 1 Human Recombinant
Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.
Product # :
ENZ-820Price :
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Shipped with Ice Packs
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Description
FDFT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-283 a.a) and having a molecular mass of 35.4 kDa. FDFT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FDFT1 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Farnesyl-Diphosphate Farnesyltransferase 1, also known as FDFT1 is a membrane-associated enzyme sited at a branch point in the mevalonate pathway. FDFT1belongs to the phytoene/squalene synthase family. FDFT1 is the 1st specific enzyme in cholesterol biosynthesis, which catalyzes the dimerization of 2 molecules of farnesyl diphosphate in a two-step reaction to form squalene.
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Synonyms
Farnesyl-Diphosphate Farnesyltransferase 1, Squalene Synthase, SQS, SS, FPP:FPP Farnesyltransferase, EC 2.5.1.21, DGPT, ERG9, Presqualene-Di-Diphosphate Synthase, Squalene Synthetase, Farnesyl-Diphosphate, Farnesyltransferase, FDFT1.
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Physical Appearance
Sterile Filtered colorless solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEFVKCL GHPEEFYNLV RFRIGGKRKV MPKMDQDSLS SSLKTCYKYL NQTSRSFAAV IQALDGEMRN AVCIFYLVLR ALDTLEDDMT ISVEKKVPLL HNFHSFLYQP DWRFMESKEK DRQVLEDFPT ISLEFRNLAE KYQTVIADIC RRMGIGMAEF LDKHVTSEQE WDKYCHYVAG LVGIGLSRLF SASEFEDPLV GEDTERANSM GLFLQKTNII RDYLEDQQGG REFWPQEVWS RYVKKLGDFA KPENIDLAVQ CLNELITNAL HHIPDVITYL SRLRNQ.
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.
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Name :
KGF HumanDescription:
Keratinocyte Growth Factor Human Recombinant
HBGF-7, FGF7, FGF-7, KGF.
Product # :
CYT-219Price :
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Shipped at Room temp
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Description
Keratinocyte Growth Factor-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 18995 Dalton.The FGF-7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 8.0, 1M NaCl.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity was determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing KGF receptors yielding an ED50 <10ng/ml, corresponding to a Specific Activity of 1.0×105 IU/mg.More Info
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Introduction
KGF is a member of the fibroblast growth factor (FGF) 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. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.
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Synonyms
HBGF-7, FGF7, FGF-7, KGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Keratinocyte Growth Factor1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 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 (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Keratinocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MCNDMTPEQM ATNVNCSSPE RHTRSYDYME GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNNYNIMEI RTVAVGIVAI KGVESEFYLA MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHNG GEMFVALNQK GIPVRGKKTK KEQKTAHFLP MAIT.
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Background
FGF stands for fibroblast growth factor that have proteins encoded inside them. The FGF family possess broad mitogenetic activities and are involved in a lot of processes in the body. Some of the biological processes that they are included in are embryonic development, cell growth, tumor growth and tissue repair. FGF-7 is often also commonly referred to as keratinocyte growth factor or KGF and studies have focused on the link between the protein and certain tumor growth.
Structure
Studies have found that the crystal structure of FGF7 is comparatively similar to that of FGF10. For instance, FGF7 does interact with D2, linker as well as D3 of the receptor. Similar to other FGFs much of interaction to do with D2 is confined to conserved residues as well as the residue Arg 251 in the linker domain and the hydrophobic surface of D2. That said there are notable differences and some models predict that FGF7 actually interacts with three loops in D3.Mechanism
A member of the FGF family, this factor acts completely exclusively through a subset of FGF receptor isoforms. These are mainly expressed by epithelial cells. Indeed, studies suggest that the factor specifically acts on epithelial cells. This in turn causes increased proliferation differentiation and migrations of the aforementioned cells.Interactions
FGF7 and FGF10 can interact with one of the FGF receptors that is expressed by the epithelial cells. As such, it could be the case that this interaction could cause a protective factor for these epithelial tissues. The protein has also been shown to interact with Perlecan. Also referred to as basement membrane specific heparan sulfate proteoglycan core protein, this is encoded by the HSPG2 gene. A large multi domain this cross-links and binds to various extracellular matrix components as well as self surface molecules. Since FGF7 binds specifically with the perlecan protein, research suggests that i should be considered a novel biological ligand for FGF-7. This could mean that interaction has an influence on both tissue remodeling and cancer growth.Function
Studies have shown that FGF-7 expression is completely unregulated during minor or even chronic injury. This has lead researchers to believe that the protein is used to heal or repair epithelial cells. Furthermore, FGF-1 also triggers the formation of apical ectodermal ridge throughout the development of limbs in the body.
Recently, it has seemed to be the case that FGF-7 has been linked to skin injury repair, and has also been found to play some sort of role in breast cancer. As well as this, it is a vital regulator of HPC’s. It is vital because it can induce de novo activation of these HPCs.Further research has shown that FGF6 is a niche signal that is required for the stimulation of adult liver progenitor cells and this can support liver regeneration. This research has lead to the suggestion that FGF7 could be a possibility therapeutic target for those suffering from liver diseases.
Studies like this are just one of the reasons why researchers continue to explore fgf-7, it’s functions and interactions. -
Protein content
Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.9 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of KGF as a Reference Standard.
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.
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Name :
RAET1L HumanDescription:
Retinoic Acid Early Transcript 1L Human Recombinant
early transcript 1L, ULBP6, UL16-binding protein 6, RAET1L, retinoic acid early transcript 1L protein, retinoic acid early transcript 1L
Product # :
PRO-2723Price :
Quantity :
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Shipped with Ice Packs
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Description
RAET1L Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 202 amino acids (26-218 a.a) and having a molecular mass of 22.9kDa.RAET1L is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The RAET1L solution (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Determined by its binding ability in a functional ELISA with Human KLRK1 (CAT# pro-2474).
More Info
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Introduction
RAET1L plays a role as a stress-induced ligand for NKG2D receptor. Retinoic Acid Early Transcript 1L (RAET1L) is linked to the cell membrane by the GPI anchor. HCMV infection triggers RAET1L’sexpression but HCMV alters its function. HCMV-encoded UL16 glycoprotein retains RAET1L/ULBP6 inside the cells, preventing it from reaching the cell surface and being exposed to cells of the immune system. RAET1L has a more restricted expression profile in cell lines and primary human tissues than other NKG2D ligands.
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Synonyms
early transcript 1L, ULBP6, UL16-binding protein 6, RAET1L, retinoic acid early transcript 1L protein, retinoic acid early transcript 1L
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Physical Appearance
Sterile filtered colorless solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPRRDDPHS LCYDITVIPK FRPGPRWCAV QGQVDEKTFL HYDCGNKTVT PVSPLGKKLN VTMAWKAQNP VLREVVDILT EQLLDIQLEN YTPKEPLTLQ ARMSCEQKAE GHSSGSWQFS IDGQTFLLFD SEKRMWTTVH PGARKMKEKW ENDKDVAMSF HYISMGDCIG WLEDFLMGMD STLEPSAGAP LAMSSGHHHH HH
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.
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Name :
LIF RatDescription:
Leukemia Inhibitory Factor Rat Recombinant
Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.
Product # :
CYT-731Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leukemia Inhibitory Factor (LIF) Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.8 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LIF Rat was lyophilized from 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity of rat LIF is determined by the ability to induce differentiation of M1 myeloid leukemic cells. The minimum detectable concentration of rat LIF in this assay is 0.5ng/mL.More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPLPITPVNA TCAIRHPCHG NLMNQIKSQL AQLNGSANAL FISYYTAQGE PFPNNVDKLC APNMTDFPPF HANGTEKTKL VELYRMVTYL GASLTNITWD QKNLNPTAVS LQIKLNATTD VMRGLLSSVL CRLCNKYHVG HVDVPCVPDN SSKEAFQRKK LGCQLLGTYK QVISVLAQAF .
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.
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Name :
RXRA HumanDescription:
Retinoid X Receptor Alpha Human Recombinant
Retinoic acid receptor RXR-alpha, Retinoid X receptor alpha, Nuclear receptor subfamily 2 group B member 1, RXRA, NR2B1, FLJ00280, FLJ00318, FLJ16020, FLJ16733, MGC102720, RXR Alpha, RXR-a.
Product # :
PRO-437Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RXRA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (111-228) & having a molecular mass of 13.6 kDa.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) containing 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM ?-Mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The retinoid X receptor (RXR) is a pleiotropic nuclear receptor transcription factor that interacts with a variety of nuclear receptor dimeric partner. RXR binds cognate response elements as a homodimer in the presence of its ligand, 9-cis retinoic acid, or as a heterodimer with other members of the nuclear hormone receptor superfamily including retinoic acid receptors (RAR), thyroid hormone receptors (TR), vitamin D receptors and peroxisome proliferators-activated receptors (PPAR). The RXR family includes three different isoforms; RXR a, b, g . Human RXR a gene is localized on 9q34.9 and encodes two major isoforms (RXR a1, RXR a2). The DNA binding domain of RXR (111-228aa) was purified by using conventional column chromatography techniques.
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Synonyms
Retinoic acid receptor RXR-alpha, Retinoid X receptor alpha, Nuclear receptor subfamily 2 group B member 1, RXRA, NR2B1, FLJ00280, FLJ00318, FLJ16020, FLJ16733, MGC102720, RXR Alpha, RXR-a.
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Physical Appearance
Sterile filtered colorless solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MLGLNGVLKV PAHPSGNMAS FTKHICAICG DRSSGKHYGV YSCEGCKGFF KRTVRKDLTY TCRDNKDCLI DKRQRNRCQY CRYQKCLAMG MKREAVQEER QRGKDRNENE VESTSSANE.
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.
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Name :
MRPS28 HumanDescription:
Mitochondrial Ribosomal Protein S28 Human Recombinant
Mitochondrial Ribosomal Protein S28, MRPS35, 28S Ribosomal Protein S35, Mitochondrial, MRP-S28, MRP-S35, S28mt, S35mt, 28S Ribosomal Protein S28, Mitochondrial, Mitochondrial 28S Ribosomal Protein S35, HSPC007.
Product # :
PRO-2161Price :
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Shipped with Ice Packs
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Description
MRPS28 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (72-187a.a) and having a molecular mass of 15.5kDa. MRPS28 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MRPS28 protein solution (0.25mg/ml) containing 20mM Phosphate buffer saline (pH 8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. Mitochondrial Ribosomal Protein S28, also known as MRPS28, is a protein coding gene which encodes a 28S subunit protein which is known as mitochondrial ribosomal protein S35.
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Synonyms
Mitochondrial Ribosomal Protein S28, MRPS35, 28S Ribosomal Protein S35, Mitochondrial, MRP-S28, MRP-S35, S28mt, S35mt, 28S Ribosomal Protein S28, Mitochondrial, Mitochondrial 28S Ribosomal Protein S35, HSPC007.
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Physical Appearance
Sterile Filtered clear solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGSPKNVE SFASMLRHSP LTQMGPAKDK LVIGRIFHIV ENDLYIDFGG KFHCVCRRPE VDGEKYQKGT RVRLRLLDLE LTSRFLGATT DTTVLEANAV LLGIQESKDS RSKEEHHEK.
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.
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Name :
NCF4 HumanDescription:
Neutrophil Cytosolic Factor 4 Human Recombinant
Neutrophil cytosol factor 4, NCF-4, Neutrophil NADPH oxidase factor 4, SH3 and PX domain-containing protein 4, p40-phox, p40phox, NCF4, SH3PXD4, NCF, SH3PXD4.
Product # :
PRO-1258Price :
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Shipped with Ice Packs
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Description
NCF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-339 a.a) and having a molecular mass of 41.1kDa.NCF4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NCF4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Neutrophil Cytosolic Factor 4 (NCF4) is a cytosolic regulatory factor of the superoxide-producing phagocyte NADPH-oxidase, which is a multicomponent enzyme system imperative for host defense. The NCF4 protein is preferentially expressed in cells of myeloid lineage. NCF4 interacts mainly with neutrophil cytosolic factor 2 (NCF2/p67-phox) to create a complex with neutrophil cytosolic factor (NCF1/p47-phox), which further interacts with the small G protein RAC1 and translocates to the membrane upon cell stimulation. This complex subsequently activates flavocytochrome b, the membrane-integratedcatalytic core of the enzyme system. The PX domain of the NCF4 protein can bind phospholipid products of the PI(3) kinase, suggesting its part in PI(3) kinase-mediated signaling events. The phosphorylation of the NCF4 protein negatively regulates the enzyme activity.
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Synonyms
Neutrophil cytosol factor 4, NCF-4, Neutrophil NADPH oxidase factor 4, SH3 and PX domain-containing protein 4, p40-phox, p40phox, NCF4, SH3PXD4, NCF, SH3PXD4.
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Physical Appearance
Sterile Filtered colorless solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAVAQQLRAE SDFEQLPDDV AISANIADIE EKRGFTSHFV FVIEVKTKGG SKYLIYRRYR QFHALQSKLE ERFGPDSKSS ALACTLPTLP AKVYVGVKQE IAEMRIPALN AYMKSLLSLP VWVLMDEDVR IFFYQSPYDS EQVPQALRRL RPRTRKVKSV SPQGNSVDRM AAPRAEALFD FTGNSKLELN FKAGDVIFLL SRINKDWLEG TVRGATGIFP LSFVKILKDF PEEDDPTNWL RCYYYEDTIS TIKDIAVEED LSSTPLLKDL LELTRREFQR EDIALNYRDA EGDLVRLLSD EDVALMVRQA RGLPSQKRLF PWKLHITQKD NYRVYNTMP.
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.
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Name :
ARHGEF39 HumanDescription:
Rho Guanine Nucleotide Exchange Factor 39 Human Recombinant
Rho guanine nucleotide exchange factor 39, ARHGEF39, C9orf100, RP11-331F9.7.
Product # :
PRO-2101Price :
Quantity :
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Shipped with Ice Packs
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Description
ARHGEF39 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-335 a.a) and having a molecular mass of 40.7kDa.ARHGEF39 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARHGEF39 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Rho Guanine Nucleotide Exchange Factor 39, also known as ARHGEF39, is a protein coding gene which owns one DH (DBL-homology) domain and one PH domain. ARHGEF39 encourages cell proliferation.
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Synonyms
Rho guanine nucleotide exchange factor 39, ARHGEF39, C9orf100, RP11-331F9.7.
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Physical Appearance
Sterile Filtered clear solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMELSCPG SRCPVQEQRA RWERKRACTA RELLETERRY QEQLGLVATY FLGILKAKGT LRPPERQALF GSWELIYGAS QELLPYLEGG CWGQGLEGFC RHLELYNQFA ANSERSQTTL QEQLKKNKGF RRFVRLQEGR PEFGGLQLQD LLPLPLQRLQ QYENLVVALA ENTGPNSPDH QQLTRAARLI SETAQRVHTI GQKQKNDQHL RRVQALLSGR QAKGLTSGRW FLRQGWLLVV PPHGEPRPRM FFLFTDVLLM AKPRPPLHLL RSGTFACKAL YPMAQCHLSR VFGHSGGPCG GLLSLSFPHE KLLLMSTDQE ELSRWYHSLT WAISSQKN.
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.
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Name :
Beta NGF MouseDescription:
Beta Nerve Growth Factor Mouse Recombinant
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Product # :
CYT-581Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Mouse b-NGF produced in E.Coli is a noncovalently disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 identical chains of 120 amino acids each and having a molecular mass of 13,471 Dalton each.The Recombinant Mouse-beta-NGF is purified by advanced biology purification technology.
Source
Escherichia Coli.
Formulation
The Recombinant Mouse b-NGF was lyophilized without additives.
Purity
Greater than 98% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE .Biological Activity
The Mouse b-NGF activity was measured in a cell proliferation assay using a factor-dependent human erythroleukemic cell line, TF-1, the ED50 for this effect is 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 units/mg.More Info
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Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis. Nerve Growth Factor was the 1st protein found from the family of neurotrophic factors that influence the growth and differentiation of sympathetic and sensory neurons. NGF consists of 3 different subunits: alpha, beta, and gamma. The beta subunit is accountable for its growth stimulating activity. The synthesis of NGF in astrocytes is enhanced by a range of cytokines such as IL1, TNF-a, PDGF & TGF-b.
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Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse Beta-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Murine NGF-Beta should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Murine NGF-beta in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSSTHPVFHM GEFSVCDSVS VWVGDKTTAT DIKGKEVTVL AEVNINNSVF RQYFFETKCR ASNPVESGCR GIDSKHWNSY CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR G.
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Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 13kDa.
What is the source or expression system of B NGF Protein?
Escherichia Coli.
What is the Purity of B NGF Protein?
B NGF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of B NGF Protein?
The Mouse b-NGF activity was measured in a cell proliferation assay using a factor-dependent human erythroleukemic cell line, TF-1, the ED50 for this effect is 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 units/mg.
What is the amino acid sequence of B NGF Protein?
MSSTHPVFHM GEFSVCDSVS VWVGDKTTAT DIKGKEVTVL AEVNINNSVF RQYFFETKCR ASNPVESGCR GIDSKHWNSY CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR G.
What applications can B NGF Protein be used in?
B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.
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.
- View Data Sheet
Name :
RELM g MouseDescription:
RELM-Gamma Mouse Recombinant
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
Product # :
CYT-1035Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
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- More Info
Description
RELM g Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 18.9kDa. The RELM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
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Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized RELM g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM g Mouse 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 (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized RELM g in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.
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.
- View Data Sheet
Name :
Resistin Human, HisDescription:
Resistin Human Recombinant, His Tag
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-256Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Resistin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing a 92 amino acids fragment (17-108) of the mature Human Resistin, having a total molecular mass of 14.23kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Resistin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Resistin protein solution is supplied in 20mM Tris-HCl pH 8.0, 5mM EDTA and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. -
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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Physical Appearance
Sterile filtered colorless solution.
-
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.Please avoid 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.
- View Data Sheet
Name :
G CSF HumanDescription:
Granulocyte-Colony Stimulating Factor Human Recombinant
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-220Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
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Description
Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8 KD.GCSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GCSF was lyophilized after extensive dialysis against 10mM sodium acetate buffer pH= 4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.More Info
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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF 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 (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GCSF in sterile 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids of GCSF was determined and was found to be Met-Thr-Pro-Leu-Gly.
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Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 18.8kDa.
What is the source or expression system of GDF15 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 HUMAN, HIS Protein?
The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.
What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is composed from 175 amino acids.
What applications can GDF15 HUMAN, HIS Protein be used in?
GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 HUMAN, HIS Protein was purified using conventional chromatography techniques.
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Protein content
GCSF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.815 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GCSF as a Reference Standard.
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.
- View Data Sheet
Name :
BLyS Human, PlantDescription:
BAFF (BLyS) Human Recombinant, Plant
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-054Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BAFF human Recombinant produced in Nicotiana benthamiana plant is a single glycosilated polypeptide chain containing 151 amino acids fragment (134-285).BAFF (C830H1277N223O242S5) is fused to a 10-His-tag at the N-terminal having the total molecular mass of 18-20kDa and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in 20 mM PBS buffer pH 7 and 0.2 M NaCl.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
*activity results may vary with PBMC donors.
ED50 ? 50ng/mlMore Info
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Introduction
BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity.A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin. -
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF 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 (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized BAFF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 19kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
What is the amino acid sequence of BLYS Protein?
HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL
What applications can BLYS Protein be used in?
BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS Protein was purified using conventional chromatography techniques.
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.
- View Data Sheet
Name :
ACVRL1 HumanDescription:
Activin A Receptor Type II-Like 1 Human Recombinant
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
Product # :
CYT-920Price :
Quantity :
Shipping Method :
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Description
ACVRL1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids (22-118a.a.) and having a molecular mass of 11.5kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).ACVRL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
ACVRL1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
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Physical Appearance
Sterile filtered colorless solution.
-
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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
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Background
The Physiological Implications and Therapeutic Potential of Activin A Receptor Type II-Like 1 Human Recombinant
1. Abstract
This research paper investigates the Activin A Receptor Type II-Like 1 Human Recombinant (ACVRL1), a significant protein involved in the TGF-beta superfamily signaling pathway. We provide an extensive understanding of ACVRL1’s structure, signaling mechanism, biological functions, and implications in disease pathology. Additionally, we explore the therapeutic potential of ACVRL1 in various pathological conditions.
2. Introduction
ACVRL1, also known as ALK1, plays an essential role in the TGF-beta signaling pathway, which has implications in cellular proliferation, differentiation, and apoptosis. Understanding ACVRL1 and its signaling mechanisms could provide insights into its potential therapeutic applications in various diseases.
3. Structure and Signaling of ACVRL1
ACVRL1 is a type I receptor protein involved in the TGF-beta signaling pathway. It is a transmembrane protein that consists of a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Binding of ligands to ACVRL1 triggers phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVRL1
ACVRL1 plays pivotal roles in multiple biological processes, including vascular development, angiogenesis, and maintenance of vascular integrity. It is known to influence cellular processes such as proliferation, differentiation, and apoptosis, thereby implicating it in organogenesis and homeostasis.
5. ACVRL1 in Disease Pathology
Mutations in the ACVRL1 gene have been associated with hereditary hemorrhagic telangiectasia (HHT), a genetic disorder characterized by abnormal blood vessel formation. This link underscores the critical role of ACVRL1 in vascular biology and disease.
6. Therapeutic Potential of ACVRL1
Given its crucial role in vascular biology and its link to HHT, ACVRL1 presents a promising target for therapeutic interventions. Modulation of ACVRL1 signaling could potentially provide treatment options for pathological conditions related to abnormal blood vessel formation and function.
7. Conclusion and Future Perspectives
Our understanding of ACVRL1 and its functions has grown significantly in recent years, but there is much yet to be discovered. Continued research into ACVRL1's precise molecular mechanisms and its roles in disease will undoubtedly open new doors for therapeutic developmen
What is the molecular weight / Mw of ACVRL1 Protein?
ACVRL1 Protein has a total Mw of 11.5kDa.What is the source or expression system of ACVRL1 Protein?
Sf9, Insect cells.
What is the Purity of ACVRL1 Protein?
ACVRL1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVRL1 Protein?
The biological functionality of ACVRL1 Protein will be determined in the future.
What is the amino acid sequence of ACVRL1 Protein?
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
What applications can ACVRL1 Protein be used in?
ACVRL1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ACVRL1 Protein?
The endotoxin level is minimal, ACVRL1 Protein was purified using conventional chromatography techniques.
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.
- View Data Sheet
Name :
HERPUD1 HumanDescription:
HERPUD1 Human Recombinant
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
Product # :
PRO-2105Price :
Quantity :
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Shipped with Ice Packs
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Description
HERPUD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 31.6kDa.HERPUD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HERPUD1 solution (0.5mg/1ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
HERPUD1 is a multi-pass membrane protein which is a part of the endoplasmic reticulum quality control system. HERPUD1 owns 1 N-terminal ubiquitin-like domain and is expressed highly in the brain. HERPUD1 is also known as ER-associated degradation (ERAD) which takes part in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins.
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Synonyms
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
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Physical Appearance
Sterile Filtered clear solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMESETEP EPVTLLVKSP NQRHRDLELS GDRGWSVGHL KAHLSRVYPE RPRPEDQRLI YSGKLLLDHQ CLRDLLPKQE KRHVLHLVCN VKSPSKMPEI NAKVAESTEE PAGSNRGQYP EDSSSDGLRQ REVLRNLSSP GWENISRPEA AQQAFQGLGP GFSGYTPYGW LQLSWFQQIY ARQYYMQYLA ATAASGAFVP PPSAQEIPVV SAPAPAPIHN QFPAENQPAN QNAAPQVVVN PGANQNLRMN AQGGPIVEED DEINRD.
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.
- View Data Sheet
Name :
NENF HumanDescription:
Neudesin Neurotrophic Factor Human Recombinant
Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.
Product # :
CYT-778Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NENF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 32-172) containing 151 amino acids including a 10 a.a N-terminal His tag and having a molecular mass of 16.9kDa.
Source
Escherichia Coli.
Formulation
NENF was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Neudesin Neurotrophic Factor (NENF) is a member of the cytochrome b5 family, MAPR subfamily. NENF contains 1 cytochrome b5 heme-binding domain. NENF exhibits neurotrophic activity and activates phosphorylation of MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT in primary cultured neurons. NENF doesn’t have mitogenic activity in primary cultured astrocytes. NENF may play a part in neuronal differentiation and may have a transient influence on neural cell proliferation in neural precursor cells. NENF neurotrophic activity is increased by binding to heme. NENF is up-regulated in immortal cells and induced in estrogen receptor positive breast cancer expressing progesterone receptor.
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Synonyms
Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. NENF is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASGQTPRPAERG PPVRLFTEEE LARYGGEEED QPIYLAVKGV VFDVTSGKEF YGRGAPYNAL TGKDSTRGVA KMSLDPADLT HDTTGLTAKE LEALDEVFTK VYKAKYPIVG YTARRILNED GSPNLDFKPE DQPHFDIKDE F.
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.
- View Data Sheet
Name :
ASCC1 HumanDescription:
Activating Signal Cointegrator 1 Complex Subunit 1 Human Recombinant
Activating signal cointegrator 1 complex subunit 1, ASC1p50, CGI-18, p50, ASC-1 complex subunit p50, Trip4 complex subunit p50, ASCC1.
Product # :
PRO-1682Price :
Quantity :
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Shipped with Ice Packs
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Description
ASCC1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-357) and having a molecular mass of 43.6 kDa.ASCC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASCC1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ASCC1 is a subunit of the triggering signal cointegrator 1 (ASC-1) complex which is a transcriptional coactivator. ASC-1 complex takes a vital part in gene transactivation using various transcription factors such as activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and serum response factor (SRF). ASCC1 has an N-terminal KH-type RNA-binding motif, essential for AP-1 transactivation by the ASC-1 complex. Alterations in ASCC1 result in Barrett esophagus and esophageal adenocarcinoma.
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Synonyms
Activating signal cointegrator 1 complex subunit 1, ASC1p50, CGI-18, p50, ASC-1 complex subunit p50, Trip4 complex subunit p50, ASCC1.
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Physical Appearance
Sterile Filtered colorless solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEVLRPQ LIRIDGRNYR KNPVQEQTYQ HEEDEEDFYQ GSMECADEPC DAYEVEQTPQ GFRSTLRAPS LLYKHIVGKR GDTRKKIEME TKTSISIPKP GQDGEIVITG QHRNGVISAR TRIDVLLDTF RRKQPFTHFL AFFLNEVEVQ EGFLRFQEEV LAKCSMDHGV DSSIFQNPKK LHLTIGMLVL LSEEEIQQTC EMLQQCKEEF INDISGGKPL EVEMAGIEYM NDDPGMVDVL YAKVHMKDGS NRLQELVDRV LERFQASGLI VKEWNSVKLH ATVMNTLFRK DPNAEGRYNL YTAEGKYIFK ERESFDGRNI LKLFENFYFG SLKLNSIHIS QRFTVDSFGN YASCGQIDFS.
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.
- View Data Sheet
Name :
SPSB1 HumanDescription:
SPRY Domain-Containing SOCS Cox Protein 1 Human Recombinant
SPRY domain-containing SOCS box protein 1, SSB-1, SPSB1, SSB1.
Product # :
PRO-223Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
SPSB1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (24-223 a.a.) and having a molecular mass of 26.1kDa.SPSB1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SPSB1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SPRY domain-containing SOCS box protein 1 (SPSB1) belongs to the SOCS box protein subfamily. SPSB1 includes a central SPRY domain and a C-terminal SOCS box. Even though, some of the SOCS protein subfamilies function as adaptors for a large family of ubiquitin-protein isopeptide ligases to regulate certain signaling pathways, the function of the SSB subfamily remains to be determined. SPSB1 may have an imperative role in enhancing the HGF-induced Erk-Elk-1-SRE pathway. SPSB1 overexpression exhibited no effect on the basal level or epidermal growth factor-induced SRE-luciferase activity.
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Synonyms
SPRY domain-containing SOCS box protein 1, SSB-1, SPSB1, SSB1.
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Physical Appearance
Sterile Filtered colorless solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQELQGLDYC KPTRLDLLLD MPPVSYDVQL LHSWNNNDRS LNVFVKEDDK LIFHRHPVAQ STDAIRGKVG YTRGLHVWQI TWAMRQRGTH AVVGVATADA PLHSVGYTTL VGNNHESWGW DLGRNRLYHD GKNQPSKTYP AFLEPDETFI VPDSFLVALD
MDDGTLSFIV DGQYMGVAFR GLKGKKLYPV VSAVWGHCEI RMRYLNGLDP E.
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.
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Name :
PDGFRB HumanDescription:
Platelet-Derived Growth Factor Receptor, Beta Human Recombinant
Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b AntigenNDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,Platelet-Derived Growth Factor Receptor Beta.
Product # :
CYT-1051Price :
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Description
PDGFRB produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 739 amino acids (33-532a.a.) and having a molecular mass of 83.3kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).PDGFRB is expressed with an 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
PDGFRB protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Platelet-derived growth factor receptor beta (PDGFRB), belongs to the class III subfamily of receptor tyrosine kinases (RTK) which also consist of the receptors for Flt3-ligand, SCF and M-CSF. PDGFRB takes a vital part in blood vessel development by promoting growth, migration as well as recruitment of pericytes and smooth muscle cells to endothelial cells. PDGFRB helps in rearrangement of the actin cytoskeleton in addition the formation of membrane ruffles. PDGFRB phosphorylates, NCK1, PIK3R1, PTPN11, CBL, SHC1, RASA1/GAP and PLCG1.
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Synonyms
Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b Antigen
NDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,
Platelet-Derived Growth Factor Receptor Beta. -
Physical Appearance
Sterile filtered colorless solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
LVVTPPGPEL VLNVSSTFVL TCSGSAPVVW ERMSQEPPQE MAKAQDGTFS SVLTLTNLTG LDTGEYFCTH NDSRGLETDE RKRLYIFVPD PTVGFLPNDA EELFIFLTEI TEITIPCRVT DPQLVVTLHE KKGDVALPVP YDHQRGFSGI FEDRSYICKT TIGDREVDSD AYYVYRLQVS SINVSVNAVQ TVVRQGENIT LMCIVIGNEV VNFEWTYPRK ESGRLVEPVT DFLLDMPYHI RSILHIPSAE LEDSGTYTCN VTESVNDHQD EKAINITVVE SGYVRLLGEV GTLQFAELHR SRTLQVVFEA YPPPTVLWFK DNRTLGDSSA GEIALSTRNV SETRYVSELT LVRVKVAEAG HYTMRAFHED AEVQLSFQLQ INVPVRVLEL SESHPDSGEQ TVRCRGRGMP QPNIIWSACR DLKRCPRELP PTLLGNSSEE ESQLETNVTY WEEEQEFEVV STLRLQHVDR PLSVRCTLRN AVGQDTQEVI VVPHSLPFKV LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.
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.
- View Data Sheet
Name :
CANT1 HumanDescription:
Calcium Activated Nucleotidase 1 Human Recombinant
Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.
Product # :
PRO-1010Price :
Quantity :
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Shipped with Ice Packs
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Description
CANT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (63-401 a.a.) and having a molecular mass of 40.5kDa. CANT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CANT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Calcium-activated nucleotidase 1 (CANT1) is a member of the apyrase family. The CANT1 protein is calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is as follows: UDP > GDP > UTP > GTP. Moreover, CANT1 has a very low activity towards ADP and an even lower activity towards ATP. As well as it doesn’t hydrolyze AMP and GMP. CANT1’s specific function is yet unknown, nevertheless its substrates are involved in several key signaling functions, including Ca2+ release, through activation of pyrimidinergic signaling. Mutations in the CANT1 gene are linked with Desbuquois dysplasia with hand anomalies.
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Synonyms
Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.
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Physical Appearance
Sterile Filtered colorless solution.
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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 (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMRPAPG RPPTHNAHNW RLGQAPANWY NDTYPLSPPQ RTPAGIRYRI AVIADLDTES RAQEENTWFS YLKKGYLTLS DSGDKVAVEW DKDHGVLESH LAEKGRGMEL SDLIVFNGKL YSVDDRTGVV YQIEGSKAVP WVILSDGDGT VEKGFKAEWL AVKDERLYVG GLGKEWTTTT GDVVNENPEW VKVVGYKGSV DHENWVSNYN ALRAAAGIQP PGYLIHESAC WSDTLQRWFF LPRRASQERY SEKDDERKGA NLLLSASPDF GDIAVSHVGA VVPTHGFSSF KFIPNTDDQI IVALKSEEDS GRVASYIMAF TLDGRFLLPE TKIGSVKYEG IEFI.
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.
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Name :
FGFR2 HumanDescription:
Fibroblast Growth Factor Receptor 2 Fc Chimera Human Recombinant
Keratinocyte growth factor receptor 2, CD332, FGFR2.
Product # :
PKA-231Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Soluble FGFR-2a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain containing 602 amino acids and having a molecular mass of 170 kDa. The FGFR2 is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
CD332 was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Determined by its ability to inhibit human FGF-2 dependent proliferation on HUVE cells. The ED50 for this effect is typically at 15 - 30ng/ml.
More Info
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Introduction
Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.
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Synonyms
Keratinocyte growth factor receptor 2, CD332, FGFR2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FGFR2A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFR2 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 (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized FGFR-2 in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
RPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWT KDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVT DAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKF RCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNY TCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVY SDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVT FEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEDPRRASIE GRGDPEEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTC VVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDW LNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSL TCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW QQGNVFSCSVMHEALHNHYTQKSLSLSPGK
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.
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Name :
FLT1 MouseDescription:
Vascular Endothelial Growth Factor receptor-1 Mouse Recombinant
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Product # :
PKA-139Price :
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Shipped with Ice Packs
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Description
FLT1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (23-759 a.a) containing a total of 970 amino acids, having a molecular mass of 108.9kDa. FLT1 is fused to a 233 amino acid hIgG-his tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
FLT1 protein solution (1mg/ml) containing 10% glycerol and PBS.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 50ng/ml and is measured by its ability to inhibit proliferation using HUVEC human umbilical vein endothelial cells in the presence of Human VEGF165.
More Info
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Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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Physical Appearance
Sterile Filtered colorless solution.
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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 (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
YGSGSKLKVP ELSLKGTQHV MQAGQTLFLK CRGEAAHSWS LPTTVSQEDK RLSITPPSAC GRDNRQFCST LTLDTAQANH TGLYTCRYLP TSTSKKKKAE SSIYIFVSDA GSPFIEMHTD IPKLVHMTEG RQLIIPCRVT SPNVTVTLKK FPFDTLTPDG QRITWDSRRG FIIANATYKE IGLLNCEATV NGHLYQTNYL THRQTNTILD VQIRPPSPVR LLHGQTLVLN CTATTELNTR VQMSWNYPGK ATKRASIRQR IDRSHSHNNV FHSVLKINNV ESRDKGLYTC RVKSGSSFQS FNTSVHVYEK GFISVKHRKQ PVQETTAGRR SYRLSMKVKA FPSPEIVWLK DGSPATLKSA RYLVHGYSLI IKDVTTEDAG DYTILLGIKQ SRLFKNLTAT LIVNVKPQIY EKSVSSLPSP PLYPLGSRQV LTCTVYGIPR PTITWLWHPC HHNHSKERYD FCTENEESFI LDPSSNLGNR IESISQRMTV IEGTNKTVST LVVADSQTPG IYSCRAFNKI GTVERNIKFY VTDVPNGFHV SLEKMPAEGE DLKLSCVVNK FLYRDITWIL LRTVNNRTMH HSISKQKMAT TQDYSITLNL VIKNVSLEDS GTYACRARNI YTGEDILRKT EVLVRDSEAP HLLQNLSDYE VSISGSTTLD CQARGVPAPQ ITWFKNNHKI QQEPGIILGP GNSTLFIERV TEEDEGVYRC RATNQKGAVE
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Background
Endothelial cells express 3 different vascular endothelial growth factor receptors: VEGFR-1 (Flt1), VEGFR-2 (KDR/Flk1), VEGFR-3 (Flt4) which are a part of the receptor tyrosine kinases family. Those receptors express mostly in endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. Flt1 contains 7 immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Flt-1, when compared to VEGFR-2 receptor has a higher affinity for VEGF but a weaker signalling activity. VEGFR-1 also mediates signals for differentiation.
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.
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Name :
G CSF Human, HisDescription:
Granulocyte-Colony Stimulating Factor Human Recombinant, His Tag
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-476Price :
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Description
Granulocyte Colony Stimulating Factor-His Tag Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids, fragment (31-204) and having a molecular mass of 23.19 kDa with an amino-terminal hexahistidine tag.G-CSF-His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Granulocyte Colony Stimulating Factor His is supplied in 1x PBS and 50% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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Physical Appearance
Sterile Filtered clear solution.
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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. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of G CSF Protein?
G CSF Protein has a total Mw of 23.19kDa.
What is the source or expression system of G CSF Protein?
Escherichia Coli.
What is the Purity of G CSF Protein?
G CSF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF Protein?
The biological functionality of G CSF Protein will be determined in the future.
What is the amino acid sequence of G CSF Protein?
G CSF Protein is composed from 174 amino acids.
What applications can G CSF Protein be used in?
G CSF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF Protein?
The endotoxin level is minimal, G CSF Protein was purified using conventional chromatography techniques.
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.
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Name :
POU5F1 Human, PolyRDescription:
POU Class 5 Homeobox 1 Human Recombinant, Polyarginine-Tag
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
Product # :
PRO-091Price :
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Shipping Method :
Shipped with Ice Packs
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Description
POU5F1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 360 amino acids and having a molecular mass of 38.6kDa.The POU5F1 is fused to a C-terminal poly-arginine tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
POU5F1 0.2µm filtered solution in PBS, pH7.4 and 5% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.
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Synonyms
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
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Physical Appearance
Sterile filtered colorless solution.
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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.Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Gly-His-Leu.
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.