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1000 results found for “Keratinocyte Growth Factor”
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Name :
C19ORF80 MouseDescription:
Chromosome 19 Open Reading Frame 80 Mouse Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, Refeeding-induced fat and liver protein, Gm6484, Angptl8, Rifl, EG624219.
Product # :
PRO-1576Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C19ORF80 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 16-198) containing 193 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 21.8kDa (calculated).
Source
Escherichia Coli.
Formulation
C19ORF80 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer, pH-4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.
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Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, Refeeding-induced fat and liver protein, Gm6484, Angptl8, Rifl, EG624219.
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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 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 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
MKHHHHHHASVRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYRA TEARLTEAGH SLGLYDRALE FLGTEVRQGQ DATQELRTSL SEIQVEEDAL HLRAEATARS LGEVARAQQA LRDTVRRLQV QLRGAWLGQA HQEFETLKAR ADKQSHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHTAA LPA.
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 :
PRKACB HumanDescription:
Protein Kinase CAMP-Dependent Catalytic Beta Human Recombinant
Protein Kinase CAMP-Dependent Catalytic Beta, PKA C-Beta, EC 2.7.11.11, PKACB, CAMP-Dependent Protein Kinase Catalytic Beta Subunit Isoform 4ab, CAMP-Dependent Protein Kinase Catalytic Subunit Beta, Protein Kinase A Catalytic Subunit Beta, EC 2.7.11, PRKACB.
Product # :
PKA-366Price :
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Shipped with Ice Packs
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Description
PRKACB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (1-398) and having a molecular mass of 48.6kDa. PRKACB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PRKACB solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein Kinase CAMP-Dependent Catalytic Beta (PRKACB) belongs to the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. cAMP is a signaling molecule imperative for various cellular functions. cAMP activates the cAMP-dependent protein kinase, which transduces the signal by way of phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of 2 regulatory and 2 catalytic subunits. cAMP triggers the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to 4 cAMP and 2 free monomeric catalytic subunits. PRKACB mediates cAMP-dependent signaling initiated by receptor binding to GPCRs. PKA activation regulates various cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, in addition to regulation of intracellular transport mechanisms and ion flux. PRKACB regulates the abundance of compartmentalized pools of its regulatory subunits via phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their consequent proteolysis.
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Synonyms
Protein Kinase CAMP-Dependent Catalytic Beta, PKA C-Beta, EC 2.7.11.11, PKACB, CAMP-Dependent Protein Kinase Catalytic Beta Subunit Isoform 4ab, CAMP-Dependent Protein Kinase Catalytic Subunit Beta, Protein Kinase A Catalytic Subunit Beta, EC 2.7.11, PRKACB.
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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 MGSMAAYREP PCNQYTGTTT ALQKLEGFAS RLFHRHSKGT AHDQKTALEN DSLHFSEHTA LWDRSMKEFL AKAKEDFLKK WENPTQNNAG LEDFERKKTL GTGSFGRVML VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVRLEYA FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEDIRVSI TEKCAKEFGE 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.
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Name :
BLyS HumanDescription:
B-cell Activating Factor Human Recombinant
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-307Price :
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Shipped at Room temp
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Description
BAFF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17007 Dalton. The BAFF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.More 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.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
MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 17.7kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.
What is the amino acid sequence of BLYS Protein?
MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.
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.
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Name :
Leptin qA Mouse, AntagonistDescription:
Leptin Quadruple Antagonist Mouse Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1257Price :
Quantity :
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Shipped at Room temp
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Description
Leptin Quadruple Antagonist Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino, an additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. The Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. Leptin Quadruple Antagonist Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Leptin Quadruple Antagonist Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Mouse Leptin Quadruple Antagonist also inhibits various leptin effects in several in vitro bioassays. The inhibitory activity of Mouse Leptin Quadruple Antagonist was increased 14 to 60 fold as measured by various criteria such as binding properties to human leptin binding domain and in vitro and in vivo bioassays as compared to mouse leptin antagonist.
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization LEP Antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids of mouse super-active leptin antagonist was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Background
Leptin is produced by adipocytes and its main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene and effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
GYPC HumanDescription:
Glycophorin C Human Recombinant
Glycophorin C (Gerbich Blood Group), Sialoglycoprotein D, Glycoprotein Beta, Glycoconnectin, Glycophorin-D, PAS-2, GPD 3 4, GPC, Glycophorin-C, CD236 Antigen, CD236R, CD236, GYPD, GLPC, GE, Glycophorin-C, Glycoconnectin, Glycophorin-D, GPD, Glycoprotein beta, PAS-2', Sialoglycoprotein D.
Product # :
PRO-2408Price :
Quantity :
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Shipped with Ice Packs
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Description
GYPC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 66 amino acids (1-57a.a.) and having a molecular mass of 7.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). GYPC is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GYPC protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycophorin C, also known as GYPC, is an integral membrane glycoprotein. GYPC is a minor species which is carried by human erythrocytes, however plays an important role in regulating the mechanical stability of red cells. Numeral glycophorin C mutations have been described. The Gerbich and Yus phenotypes are due to deletion of exon 3 & 2, respectively. The Webb & Duch antigens, also identified as glycophorin D, result from single point mutations of the glycophorin C gene. The glycophorin C protein has very slight homology with glycophorins A & B.
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Synonyms
Glycophorin C (Gerbich Blood Group), Sialoglycoprotein D, Glycoprotein Beta, Glycoconnectin, Glycophorin-D, PAS-2, GPD 3 4, GPC, Glycophorin-C, CD236 Antigen, CD236R, CD236, GYPD, GLPC, GE, Glycophorin-C, Glycoconnectin, Glycophorin-D, GPD, Glycoprotein beta, PAS-2', Sialoglycoprotein D.
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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
ADPMWSTRSP NSTAWPLSLE PDPGMASAST TMHTTTIAEP DPGMSGWPDG RMETSTPTIM HHHHHH.
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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Description:
Leptin Super Antagonist Human Recombinant
Product # :
CYT-1238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
ProSpec’s super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile 0.4% NaHCO3 adjusted to pH 8-9, 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 was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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 Human, YeastDescription:
LIF Human Recombinant, Yeast
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-191Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LIF Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 58.5 kDa. The LIF is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from a 0.2 µm filtered PBS.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity of recombinant human LIF was measured by the ability to induce differentiation of murine M1 myeloid leukemic cells. The minimal detectable concentration of human LIF in this assay is <0.05 ng/mL. The specific activity is > 1 x 108 units/mg.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
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LIF 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 LIF 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
S P L P I T P V N A T C A I R H P C H N N L M N Q I R S Q L A Q L N G S A N A L F I L Y Y T A Q G E P F P N N L D K L C G P N V T D F P P F H A N G T E K A K L V E L Y R I V V Y L G T S L G N I T R D Q K I L N P S A L S L H S K L N A T A D I L R G L L S N V L C R L C S K Y H V G H V D V T Y G P D T S G K D V F Q K K K L G C Q L L G K Y K Q I I A V L A Q A 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.
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Name :
PIP HumanDescription:
Prolactin-Induced Protein Human
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, PIP, GCDFP15, GPIP4.
Product # :
CYT-779Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Prolactin-Induced Protein produced from Human Seminal Plasma has a molecular mass of 13.52kDa (calculated without glycosylation) containing 118 amino acid residues.
Source
Human Seminal Plasma.
Formulation
PIP protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Prolactin inducible protein (PIP) is a 17kDa glycoprotein existing in human seminal plasma. PIP is synthesized as a 146 amino acid long polypeptide exhibiting high sequence similarity with mouse submaxillary gland with a single glycosylation site. The precise biological functions of PIP are still ambiguous but various functions have been assigned to PIP due its existence at high concentration in biological fluids. PIP binds to various proteins such as fibrinogen, actin, keratin, myosin and tropomyosin. PIP is also expressed in pathological conditions of the mammary gland and in some exocrine tissues, such as the lacrimal, salivary and sweat glands. Due to PIP’s association with secretory cell differentiation, it has been used in diagnostic evaluation of tumors of breast, salivary gland, and skin.
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Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, PIP, GCDFP15, GPIP4.
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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. PIP 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
QDNTRKIIIK NFDIPKSVRP NDEVTAVLAV QTELKECMVV KTYLISSIPL QGAFNYKYTA CLCDDNPKTF YWDFYTNRTV QIAAVVDVIR ELGICPDDAA VIPIKNNRFY TIEILKVE.
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Human Virus Test
Samples from each donor have been tested and found negative for HBsAg, HIV1+2, HCV, syphilis, aHBc, RRR.
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 :
Activin-A Human Plant-ActiveDescription:
Activin-A Human Recombinant, Plant-Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-414Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana.
Formulation
Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4
Purity
Greater than 98% as obsereved by SDS-PAGE.
Biological Activity
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.
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Solubility
INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.
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Amino Acid Sequence
HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS. -
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.What is the source or expression system of Activin A Protein?
Nicotiana benthamiana.What is the Purity of Activin A Protein?
Activin A Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
What applications can ACTIVIN-A Protein be used in?
ACTIVIN A 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.
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Name :
CD40 HumanDescription:
CD40 Human Recombinant
CD40 Molecule, TNF Receptor Superfamily Member 5, TNFRSF5, Tumor Necrosis Factor Receptor Superfamily, Member 5, Bp50, B-Cell Surface Antigen CD40, CD40L Receptor, CDW40, B Cell Surface Antigen CD40, B Cell-Associated Molecule, CD40 Antigen (TNF Receptor Superfamily Member 5), CD40 Type II Isoform, Nerve Growth Factor Receptor-Related B-Lymphocyte Activation Molecule, p50, Tumor Necrosis Factor Receptor Superfamily Member 5, CDw40, CD40 Antigen.
Product # :
PRO-1911Price :
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Description
CD40 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (21-193a.a) and having a molecular mass of 21.6kDa.CD40 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CD40 protein solution (0.25mg/ml) containing 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
CD40 belongs to the TNF-receptor super family. CD40 has been found to be vital in mediating a wide range of immune and inflammatory responses including T cell-dependent immunoglobulin classswitching, memory B cell development, and germinal center formation. AT-hook transcription factor AKNA isaccounted to coordinately regulate the expression of CD40 and its ligand, which is significant forhomotypic cell interactions. Adaptor protein TNFR2 interacts with CD40 and functions as a mediator of thesignal transduction. The interaction of CD40 and its ligand is found to be essential for amyloid-beta-inducedmicroglial activation, and therefore is considered to be an early event in Alzheimer disease pathogenesis.
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Synonyms
CD40 Molecule, TNF Receptor Superfamily Member 5, TNFRSF5, Tumor Necrosis Factor Receptor Superfamily, Member 5, Bp50, B-Cell Surface Antigen CD40, CD40L Receptor, CDW40, B Cell Surface Antigen CD40, B Cell-Associated Molecule, CD40 Antigen (TNF Receptor Superfamily Member 5), CD40 Type II Isoform, Nerve Growth Factor Receptor-Related B-Lymphocyte Activation Molecule, p50, Tumor Necrosis Factor Receptor Superfamily Member 5, CDw40, CD40 Antigen.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEPPTACR EKQYLINSQC CSLCQPGQKL VSDCTEFTET ECLPCGESEF LDTWNRETHC HQHKYCDPNL GLRVQQKGTS ETDTICTCEE GWHCTSEACE SCVLHRSCSP GFGVKQIATG VSDTICEPCP VGFFSNVSSA FEKCHPWTSC ETKDLVVQQA GTNKTDVVCG PQDRLR
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 :
EMG1 HumanDescription:
EMG1 Nucleolar Protein Human Recombinant
EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.
Product # :
PRO-1122Price :
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Description
EMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 267 amino acids (1-244) and having a molecular mass of 29.1kDa.EMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EMG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
EMG1 is a 244 aa protein which has a role in ribosome biogenesis. EMG1 is a key protein in the small ribosomal subunit assembly, controls methylation during ribosome synthesis and takes part in pre-18S rRNA processing. EMG1 is localized to the nucleolus and a mutation in this gene is linked with Bowen-Conradi syndrome.
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Synonyms
EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.
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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
MGSSHHHHHH SSGLVPRGSH MGSMAAPSDG FKPRERSGGE QAQDWDALPP KRPRLGAGNK IGGRRLIVVL EGASLETVKV GKTYELLNCD KHKSILLKNG RDPGEARPDI THQSLLMLMD SPLNRAGLLQ VYIHTQKNVL IEVNPQTRIP RTFDRFCGLM VQLLHKLSVR AADGPQKLLK VIKNPVSDHF PVGCMKVGTS FSIPVVSDVR ELVPSSDPIV FVVGAFAHGK VSVEYTEKMV SISNYPLSAA LTCAKLTTAF EEVWGVI
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 :
RCHY1 HumanDescription:
Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant
ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.
Product # :
PRO-1536Price :
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Description
RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RCHY1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.
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Synonyms
ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.
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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 MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.
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 :
CFI HumanDescription:
Complement Factor I Human
Complement factor I, C3B/C4B inactivator, CFI, IF.
Product # :
PRO-2701Price :
Quantity :
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Description
Human Complement Factor I produced in Human plasma is glycosylated polypeptide composed of 2 disulfide-linked chains having a total molecular mass of 88kDa.
Source
Human Plasma.
Formulation
CFI protein solution contains Sodium phosphate, pH 7.2.
Purity
Greater than 93.0% as determined by SDS-PAGE.
More Info
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Introduction
CFI cleaves and inactivates C3b and C4b. CFI is inactive without a cofactor such as the soluble factor H and C4b binding protein. CFI cleaves the alpha-peptide chain of C3b and C4b when these binds1 of the cofactors. This cleavage inactivates all of the complement activating functions of these proteins producing iC3b and iC4b.CFI cleaves the alpha chain of C3b twice and this releases a small fragment called C3f. CFI can cleave iC3b releasing C3c from C3dg in the presence of CR1.C4b is cleaved rapidly at 2 sites separating C4c from C4d.
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Synonyms
Complement factor I, C3B/C4B inactivator, CFI, IF.
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Physical Appearance
Sterile filtered solution.
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Stability
CFI Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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 :
C19ORF80 RatDescription:
Chromosome 19 Open Reading Frame 80 Rat Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
Product # :
PRO-2024Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C19ORF80 Rat Recombinant produced in E. coli is a polypeptide chain containing 193 amino acids and having a total molecular mass of 22.0 kDa. C19ORF80 has a N-Terminal His-tag (10 AA residue).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from a 0.5mg/ml solution containing 0.03M Acetate buffer pH 4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.
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Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
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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 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 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
MKHHHHHHAS VRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYKA TEARLTEAGR NLGLFDQALE FLGREVNQGR DATRELRTSL SEIQAEEDTL HLRAEATARS LREVARAQHA LRNSVRRLQV QLRGAWLGQA HQEFENLKDR ADKQNHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHMAA LPA
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 :
TYMP HumanDescription:
Thymidine Phosphorylase Human Recombinant
Thymidine phosphorylase, Gliostatin, Platelet-derived endothelial cell growth factor, PD-ECGF, TdRPase, TYMP, ECGF1, TP, MNGIE, MEDPS1, MTDPS1, PDECGF, hPD-ECGF.
Product # :
ENZ-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TYMP Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 493 amino acids (11-482 a.a.) and having a molecular mass of 51.3kDa. The TYMP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TYMP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Thymidine phosphorylase precursor (TYMP) is a platelet-derived endothelial cell growth factor that catalyzes the formation of thymine and 2-deoxy-D-ribose-1-phosphate from thymidine and orthophosphate. TYMP is an angiogenic inducer that potently stimulates the growth of endothelial cells and induces chemotaxis. TYMP has a highly restricted target cell specificity acting only on endothelial cells. An increased expression of TYMP is found in a broad array of different solid tumors and inflammatory diseases and is frequently associated with poor prognosis. Mutations in the TYMP gene are linked to mitochondrial neurogastrointestinal encephalomyopathy.
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Synonyms
Thymidine phosphorylase, Gliostatin, Platelet-derived endothelial cell growth factor, PD-ECGF, TdRPase, TYMP, ECGF1, TP, MNGIE, MEDPS1, MTDPS1, PDECGF, hPD-ECGF.
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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 MAPPAPGDFS GEGSQGLPDP SPEPKQLPEL IRMKRDGGRL SEADIRGFVA AVVNGSAQGA QIGAMLMAIR LRGMDLEETS VLTQALAQSG QQLEWPEAWR QQLVDKHSTG GVGDKVSLVL APALAACGCK VPMISGRGLG HTGGTLDKLE SIPGFNVIQS PEQMQVLLDQ AGCCIVGQSE QLVPADGILY AARDVTATVD SLPLITASIL SKKLVEGLSA LVVDVKFGGA AVFPNQEQAR ELAKTLVGVG ASLGLRVAAA LTAMDKPLGR CVGHALEVEE ALLCMDGAGP PDLRDLVTTL GGALLWLSGH AGTQAQGAAR VAAALDDGSA LGRFERMLAA QGVDPGLARA LCSGSPAERR QLLPRAREQE ELLAPADGTV ELVRALPLAL VLHELGAGRS RAGEPLRLGV GAELLVDVGQ RLRRGTPWLR VHRDGPALSG PQSRALQEAL VLSDRAPFAA PSPFAELVLP PQQ.
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 :
SDC1 HumanDescription:
Syndecan-1 Human Recombinant
Heparan Sulfate proteoglycan fibroblast growth factor receptor, syndecan proteoglycan 1, Syndecan 1, SYND1, CD138 antigen, SDC.
Product # :
PRO-1065Price :
Quantity :
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Description
SDC1 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (18-254) and having a molecular mass of 27kDa (molecular size on SDS-PAGE will appear higher).SDC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SDC1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CD138 takes a part in cell adhesion. CD138 is expressed on the surface of pre-B cells and plasma cells but is absent from mature B cells. SDC1 is a selective marker for B cell lymphoblastic leukemia and lymphoplasmacytoid leukemia. SDC1 is missing from the apoptotic myeloma cells; therefore is a valuable marker for plasma cell and myeloma cells.
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Synonyms
Heparan Sulfate proteoglycan fibroblast growth factor receptor, syndecan proteoglycan 1, Syndecan 1, SYND1, CD138 antigen, SDC.
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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 MGSHMQPALP QIVATNLPPE DQDGSGDDSD NFSGSGAGAL QDITLSQQTP STWKDTQLLT AIPTSPEPTG LEATAASTST LPAGEGPKEG EAVVLPEVEP GLTAREQEAT PRPRETTQLP TTHQASTTTA TTAQEPATSH PHRDMQPGHH ETSTPAGPSQ ADLHTPHTED GGPSATERAA EDGASSQLPA AEGSGEQDFT FETSGENTAV VAVEPDRRNQ SPVDQGATGA SQGLLDRKEV LG.
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 :
TNF a CanineDescription:
Tumor Necrosis Factor-Alpha Canine Recombinant
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
Product # :
CYT-140Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNF-a Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.3 kDa. The TNF-a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Specific Activity is >3.3×105 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.More Info
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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha 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
VKSSSRTPSD KPVAHVVANP EAEGQLQWLS RRANALLANG VELTDNQLIV PSDGLYLIYS QVLFKGQGCP STHVLLTHTI SRFAVSYQTK VNLLSAIKSP CQRETPEGTE AKPWYEPIYL GGVFQLEKGD RLSAEINLPN YLDFAESGQV YFGIIAL.
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 :
NOV MouseDescription:
Nephroblastoma Overexpressed Mouse Recombinant
Protein NOV homolog, NovH, CCN family member 3, Nephroblastoma-overexpressed gene protein homolog, Nov, Ccn3, C130088N23Rik.
Product # :
CYT-171Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NOV Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 333 amino acids and having a molecular mass of 36.4kDa.The NOV is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NOV protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.5 and 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 μg/ml, corresponding to a specific activity of > 1000 IU/mg.More Info
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Introduction
Nephroblastoma Overexpressed (NOV) is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein is comprised of 4 structural domains, which present distinct, and sometimes opposing, biological activities. An elevated expression of NOV is linked with certain tumors, including Wilm’s tumor and most nephroblastomas. On the other hand, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is associated with decreased NOV expression.
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Synonyms
Protein NOV homolog, NovH, CCN family member 3, Nephroblastoma-overexpressed gene protein homolog, Nov, Ccn3, C130088N23Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NOV although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NOV 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 NOV 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
QVSASLRCPS RCPPKCPSIS PTCAPGVRSV LDGCSCCPVC ARQRGESCSE MRPCDQSSGL YCDRSADPNN QTGICMVPEG DNCVFDGVIY RNGEKFEPNC QYFCTCRDGQ IGCLPRCQLD VLLPGPDCPA PRKVAVPGEC CEKWTCGSDE QGTQGTLGGL ALPAYRPEAT VGVEVSDSSI NCIEQTTEWS ACSKSCGMGV STRVTNRNRQ CEMVKQTRLC IVRPCEQEPE EVTDKKGKKC LRTKKSLKAI HLQFENCTSL YTYKPRFCGV CSDGRCCTPH NTKTIQVEFQ CLPGEIIKKP VMVIGTCTCY SNCPQNNEAF LQDLELKTSR GEI.
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 :
RNF181 HumanDescription:
Ring Finger Protein 181 Human Recombinant
Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.
Product # :
PRO-1218Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RNF181 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 20.3 kDa.RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RNF181 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
E3 ubiquitin-protein ligase RNF181 (RNF181) accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the thioester form and subsequently directly transfers the ubiquitin to targeted substrates. RNF181 is widely expressed, with the highest levels in the liver and heart and the lowest levels in the brain and skeletal muscle. RNF181 is also expressed in platelets (at protein level).
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Synonyms
Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.
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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 MGSMASYFDE HDCEPSDPEQ ETRTNMLLEL ARSLFNRMDF EDLGLVVDWD HHLPPPAAKT VVENLPRTVI RGSQAELKCP VCLLEFEEEE TAIEMPCHHL FHSSCILPWL SKTNSCPLCR YELPTDDDTY EEHRRDKARK QQQQHRLENL HGAMYT.
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 :
IL 9 Human, Sf9Description:
Interleukin-9 Human Recombinant, Sf9
Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.
Product # :
CYT-866Price :
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Shipped with Ice Packs
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Description
IL-9 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-144 a.a.) including an 18 aa signal peptide (1-18 aa) and fused to a 6 aa His Tag at C-terminus containing a total of 150 amino acids and having a molecular mass of 14.5kDa.IL9 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL-9 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
IL-9 is a factor which is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
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Synonyms
Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.
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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
MLLAMVLTSA LLLCSVAGQG CPTLAGILDI NFLINKMQED PASKCHCSAN VTSCLCLGIP SDNCTRPCFS ERLSQMTNTT MQTRYPLIFS RVKKSVEVLK NNKCPYFSCE QPCNQTTAGN ALTFLKSLLE IFQKEKMRGM RGKIHHHHHH.
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 :
IL17F RatDescription:
Interleukin-17F Rat Recombinant
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
Product # :
CYT-643Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL17F Rat Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 270 amino acids and having a molecular mass of 30 kDa. The Rat IL-17F is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL17F Rat was lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM-CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway. -
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat IL17F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL17F 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 Rat IL17F 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
MARRNPKVGL SALQKAGNCP PLEDNSVRVD IRIFNQNQGI SVPRDFQNRS SSPWDYNITR DPDRFPSEIA EAQCRHSGCI NAQGQEDGSM NSVPIQQEIL VLRREPQGCS NSFRLEKMLI KVGCTCVTPI VHHAA.
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 :
BAFF R HumanDescription:
B-cell Activating Factor Receptor Human Recombinant
TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.
Product # :
CYT-429Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
B Lymphocyte Stimulator Receptor Human Recombinant extracellular produced in E.Coli is a single, non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 7.7 kDa.The BAFF-R is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 8.0, 500mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to block BAFF induced mouse splenocyte survival. The expected ED50 for this effect is 1.0-5.0 µg/ml in the presence of 1.0µg/ml of human soluble BAFF.More Info
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Introduction
B cell-activating factor (BAFF) enhances B-cell survival in vitro and is a regulator of the peripheral B-cell population. Overexpression of Baff in mice results in mature B-cell hyperplasia and symptoms of systemic lupus erythematosus (SLE). Also, some SLE patients have increased levels of BAFF in serum. Therefore, it has been proposed that abnormally high levels of BAFF may contribute to the pathogenesis of autoimmune diseases by enhancing the survival of autoreactive B cells. The protein encoded by this gene is a receptor for BAFF and is a type III transmembrane protein containing a single extracellular cysteine-rich domain. It is thought that this receptor is the principal receptor required for BAFF-mediated mature B-cell survival.
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Synonyms
TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BAFF-R although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution B Lymphocyte Stimulator Receptor 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 B Lymphocyte Stimulator Receptor Recombinant 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
MRRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAG
ASSPAPRTALQPQESVGAGAGEAALPLPG. -
Background
B-cell Activating Factor Receptor Human Recombinant: Unlocking the Potential of a Key Immunomodulatory Target
Abstract:
B-cell Activating Factor Receptor (BAFF-R) human recombinant is a critical component of the B-cell immune response, playing a pivotal role in B-cell survival, maturation, and antibody production. This research paper provides a comprehensive analysis of BAFF-R, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BAFF-R human recombinant are proposed, shedding light on its future implications in the field of immunotherapy.
Introduction:
The immune system relies on the precise regulation of B-cell functions, with BAFF-R serving as a key modulator of B-cell development and activation. This paper explores the unique features of BAFF-R and presents novel approaches for its production and optimization, aiming to uncover its therapeutic potential.
Characteristics and Signaling Pathways:
BAFF-R is a type III transmembrane protein expressed primarily on B-cells. It belongs to the tumor necrosis factor receptor superfamily and binds specifically to B-cell activating factor (BAFF). Engagement of BAFF-R by BAFF initiates intracellular signaling cascades, including the activation of nuclear factor-kappa B (NF-κB) and mitogen-activated protein kinase (MAPK) pathways, promoting B-cell survival, proliferation, and differentiation.
Production of BAFF-R Human Recombinant:
Efficient production methodologies are crucial for the therapeutic application of BAFF-R human recombinant. Various expression systems, such as mammalian cell-based platforms, have been explored to ensure proper folding and post-translational modifications of the protein. Optimization strategies, including codon optimization and vector design, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality BAFF-R recombinant.
Potential Therapeutic Applications:
BAFF-R human recombinant holds great promise in the field of immunotherapy. Dysregulation of the BAFF/BAFF-R signaling axis has been implicated in autoimmune diseases, such as systemic lupus erythematosus and rheumatoid arthritis. Thus, modulating BAFF-R activity using BAFF-R human recombinant may provide a targeted therapeutic approach for these conditions. Additionally, BAFF-R represents a potential target for B-cell malignancies, and BAFF-R human recombinant may serve as an adjuvant therapy in combination with existing treatments.
Conclusion:
BAFF-R human recombinant represents a crucial immunomodulatory target with diverse therapeutic applications in immunotherapy. Optimizing production methodologies and further understanding its signaling pathways will enhance its clinical utility. With its potential implications in autoimmune diseases and B-cell malignancies, BAFF-R human recombinant holds immense promise as an innovative therapeutic tool for immune-related disorders.
What is the molecular weight/Mw of BAFF R Protein?
BAFF R Protein has a total Mw of 7.7kDa.
What is the source or expression system of BAFF R Protein?
Escherichia Coli.
What is the Purity of BAFF R Protein?
BAFF R Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BAFF R Protein?
Determined by its ability to block BAFF induced mouse splenocyte survival. The expected ED50 for this effect is 1.0-5.0 µg/ml in the presence of 1.0µg/ml of human soluble BAFF.
What is the amino acid sequence of BAFF R Protein?
MRRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAG
ASSPAPRTALQPQESVGAGAGEAALPLPG.
What applications can BAFF R Protein be used in?
BAFF R Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BAFF R Protein?
The endotoxin level is minimal, BAFF R 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 :
SLAMF6 HumanDescription:
SLAMF6 Human Recombinant
CD352, KALI, KALIb, Ly108, NTB-A, NTBA, Activating NK receptor, SLAM family member 6.
Product # :
PRO-1286Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
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Description
SLAMF6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (22-226 a.a.) and having a molecular mass of 25.5kDa. SLAMF6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SLAMF6 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
SLAM family member 6 (SLAMF6) is a member of the SLAM family of immune cell receptors. SLAMF6 is a unique receptor on T cells which, when triggered potentiates T cell expansion in a CD28-independent manner. SLAMF6 has a high expression on NK-, T-, and B cells. SLAMF6 exhibits homotypic interactions and can connect with adaptor molecules such as SAP to alter immune cell function.
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Synonyms
CD352, KALI, KALIb, Ly108, NTB-A, NTBA, Activating NK receptor, SLAM family member 6.
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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 MGSQSSLTPL MVNGILGESV TLPLEFPAGE KVNFITWLFN ETSLAFIVPH ETKSPEIHVT NPKQGKRLNF TQSYSLQLSN LKMEDTGSYR AQISTKTSAK LSSYTLRILR QLRNIQVTNH SQLFQNMTCE LHLTCSVEDA DDNVSFRWEA LGNTLSSQPN LTVSWDPRIS SEQDYTCIAE NAVSNLSFSV SAQKLCEDVK IQYTDTKM.
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.