Search results
1000 results found for “Transforming Growth Factor”
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Name :
IL 3 Human, Sf9Description:
Interleukin-3 Human Recombinant, Sf9
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Product # :
CYT-417Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-3 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. The IL-3 CSF is fused to a C-terminal His-tag (6x His) and purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.5X PBS pH-7.4.
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 the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.More Info
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Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
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Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 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 Interleukin-3 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Pro-Thr.
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 :
NRAS HumanDescription:
Neuroblastoma RAS Viral Oncogene Homolog Human Recombinant
GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.
Product # :
PRO-794Price :
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Shipping Method :
Shipped with Ice Packs
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Description
NRAS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-186 a.a.) and having a molecular mass of 20.8kDa. The NRAS is purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The NRAS protein solution contains 20mM Tris-HCl pH-7.5, 100mM NaCl, and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NRAS binds GDP/GTP and has intrinsic GTPase activity. NRAS is a membrane protein that shuttles between the Golgi apparatus and the plasma membrane. This transport is regulated through palmitoylation and depalmitoylation by the ZDHHC9-GOLGA7 complex. NRAS is activated to a GTP-bound form by a GTPase activating protein and inactivated to a GDP-bound form by a guanine nucleotide-exchange factor. Defects in this NRAS gene result in juvenile myelomonocytic leukemia.
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Synonyms
GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.
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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
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSSDDGTQG CMGLPC.
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 :
Insulin Human (20-110)Description:
Insulin (20-110 a.a) Human Recombinant
Product # :
CYT-1237Price :
Quantity :
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Shipped at Room temp
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Description
The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Insulin 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
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Background
Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.
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 :
GHRL HumanDescription:
Ghrelin Human Recombinant
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Product # :
HOR-294Price :
Quantity :
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Shipped with Ice Packs
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Description
Ghrelin Human Recombinant contains 115 amino acids (24-117 a.a.) and a total molecular mass of 12.8 kDa. The GHRL is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ghrelin protein solution contains 20mM Tris-HCl, pH-8 & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
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Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
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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 MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
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Background
What is the molecular weight/Mw of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein has a total Mw of 12.8kDa.
What is the source or expression system of GHRELIN HUMAN Protein?
Escherichia Coli.
What is the Purity of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GHRELIN HUMAN Protein?
The biological functionality of GHRELIN HUMAN Protein will be determined in the future.
What is the amino acid sequence of GHRELIN HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
What applications can GHRELIN HUMAN Protein be used in?
GHRELIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHRELIN HUMAN Protein?
The endotoxin level is minimal, GHRELIN HUMAN 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 :
Flt3 Ligand PorcineDescription:
Flt3 Ligand Porcine Recombinant
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Product # :
CYT-1041Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Flt3-Ligand Porcine Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.3kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein is lyophilized with 10mM Sodium Phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
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Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Porcine Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L 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
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.
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Background
What is the molecular weight/Mw of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein has a total Mw of 17.3kDa.
What is the source or expression system of FLT3 LIGAND PORCINE Protein?
Escherichia Coli.
What is the Purity of FLT3 LIGAND PORCINE Protein?
FLT3 LIGAND PORCINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FLT3 LIGAND PORCINE Protein?
The biological functionality of FLT3 LIGAND PORCINE Protein will be determined in the future.
What is the amino acid sequence of FLT3 LIGAND PORCINE Protein?
MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.
What applications can FLT3 LIGAND PORCINE Protein be used in?
FLT3 LIGAND PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FLT3 LIGAND PORCINE Protein?
The endotoxin level is minimal, FLT3 LIGAND PORCINE 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 :
TPST1 Human, sf9Description:
Tyrosylprotein Sulfotransferase 1, sf9 Human Recombinant
Tyrosylprotein Sulfotransferase 1, EC 2.8.2.20, TPST-1, Transport And Golgi Organization 13 Homolog A (Drosophila), Transport And Golgi Organization 13 Homolog A, Tyrosylprotein Sulfotransferase-1, TANGO13A.
Product # :
ENZ-948Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TPST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 354 amino acids (26-370 a.a.) and having a molecular mass of 40.6kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TPST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TPST1 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
Tyrosylprotein Sulfotransferase 1, also known as TPST1 is the enzyme which catalyzes the sulfation reaction of protein tyrosines, a post-translational modification of proteins. TPST1 belongs to the protein sulfotransferase family. In addition, TPST1 utilizes 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfonate donor and also binds proteins with target tyrosine residues to eventually form the tyrosine O-sulfate ester group in addition to the desulfonated 3’-phosphoadenosine-5’-phosphate.
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Synonyms
Tyrosylprotein Sulfotransferase 1, EC 2.8.2.20, TPST-1, Transport And Golgi Organization 13 Homolog A (Drosophila), Transport And Golgi Organization 13 Homolog A, Tyrosylprotein Sulfotransferase-1, TANGO13A.
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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
ADPQHAMECH HRIEERSQPV KLESTRTTVR TGLDLKANKT FAYHKDMPLI FIGGVPRSGT TLMRAMLDAH PDIRCGEETR VIPRILALKQ MWSRSSKEKI RLDEAGVTDE VLDSAMQAFL LEIIVKHGEP APYLCNKDPF ALKSLTYLSR LFPNAKFLLM VRDGRASVHS MISRKVTIAG FDLNSYRDCL TKWNRAIETM YNQCMEVGYK KCMLVHYEQL VLHPERWMRT LLKFLQIPWN HSVLHHEEMI GKAGGVSLSK VERSTDQVIK PVNVGALSKW VGKIPPDVLQ DMAVIAPMLA KLGYDPYANP PNYGKPDPKI IENTRRVYKG EFQLPDFLKE KPQTEQVEHH HHHH.
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 1 alpha RatDescription:
Interleukin-1 alpha Rat Recombinant
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Product # :
CYT-381Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-1A Rat Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17703 Dalton. The IL-1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Tris-HCl, pH=8.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.More Info
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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
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Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 Interleukin 1a 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-His-Ser-Phe.
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 :
TAC1 HumanDescription:
Tachykinin-1 Human Recombinant
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 1.
Product # :
PRO-1338Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (20-129 a.a) and having a molecular mass of 15.6kDa.TAC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TAC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 2M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Tachykinin-1 (TAC1) belongs to the tachykinin peptide hormone family. TAC1 are a family of peptides which have similar biologic activities and share a common C-terminal sequence, phe-X-gly-leu-met-NH2, however they have distinct N-terminal sequences that convey receptor specificities. TAC1 is assumed to act as neurotransmitters which interact with nerve receptors and smooth muscle cells. TAC1 induces behavioral responses and serves as vasodilators and secretagogues.
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Synonyms
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 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 MGSHMEEIGA NDDLNYWSDW YDSDQIKEEL PEPFEHLLQR IARRPKPQQF FGLMGKRDAD SSIEKQVALL KALYGHGQIS HKRHKTDSFV GLMGKRALNS VAYERSAMQN YERRR.
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 :
REG4 HumanDescription:
Regenerating Islet-Derived 4 Human Recombinant
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
Product # :
PRO-424Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human REG-4 is manufactured with N-terminal fusion of His Tag. The Recombinant Human REG-IV His-Tagged Fusion Protein is 17.4 kDa protein containing 136 amino acid residues of the Human REG 4 and 12 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system. -
Synonyms
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
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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
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS HMDIIMRPSC APGWFYHKSN CYGYFRKLRN WSDAELECQS YGNGAHLASI LSLKEASTIA EYISGYQRSQ PIWIGLHDPQ KRQQWQWIDG AMYLYRSWSG KSMGGNKHCA EMSSNNNFLT WSSNECNKRQ HFLCKYRP.
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 :
RBP2 HumanDescription:
Retinol Binding Protein-2 Human Recombinant
CRABP-II, CRBP2, CRBPII, RBPC2, Retinol-binding protein 2, Cellular retinol-binding protein II, RBP2.
Product # :
CYT-751Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (1-134 a.a.) and having a molecular mass of 18kDa. RBP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RBP2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Retinol Binding Protein-2 (RBP2) which is present in the small intestinal epithelium takes part in the uptake and intracellular metabolism of vitamin A. Vitamin A is a fat-soluble vitamin essential for growth, reproduction, differentiation of epithelial tissues, and vision. RBP2 moderates the supply of retinoic acid to the nuclei of endometrial cells throughout the menstrual cycle.
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Synonyms
CRABP-II, CRBP2, CRBPII, RBPC2, Retinol-binding protein 2, Cellular retinol-binding protein II, RBP2.
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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 MGSHMTRDQN GTWEMESNEN FEGYMKALDI DFATRKIAVR LTQTKVIDQD GDNFKTKTTS TFRNYDVDFT VGVEFDEYTK SLDNRHVKAL VTWEGDVLVC VQKGEKENRG WKQWIEGDKL YLELTCGDQV CRQVFKKK.
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 :
RBP4 Human, HisDescription:
Retinol Binding Protein-4 Human Recombinant, His tag
Retinol Binding Protein 4 plasma, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
Product # :
CYT-555Price :
Quantity :
Shipping Method :
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Description
RBP-4 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 183 amino acids fragment (19-201) corresponding to the mature Retinol Binding Protein, having a total molecular mass of 25.57kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The RBP4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RBP4 protein solution is supplied in 10mM Tris, 50mM NaCl, 1mM EDTA and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Retinol binding protein 4(RBP4) belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. This protein was found to be expressed and secreted by adipose tissue, and was strongly associated with insulin resistance. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli.
RBP4 delivers retinol from the liver to the peripheral tissues. In plasma, the rbp-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli. -
Synonyms
Retinol Binding Protein 4 plasma, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
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Physical Appearance
Sterile Filtered clear 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. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Insulin HumanDescription:
Insulin Human Recombinant
Product # :
CYT-270Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Insulin Human Recombinant produced in E.Coli is a two chain, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Insulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC analysis.
Biological Activity
The Biological Activity was determined to be 28 units/mg.More Info
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Introduction
Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Insulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Insulin 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 Insulin in sterile 0.005N HCl not more than 1 mg/ml.
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 :
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 :
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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
-
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.
-
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.
- View Data Sheet
Name :
MANF HumanDescription:
Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant
Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.
Product # :
CYT-141Price :
Quantity :
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Description
MANF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids and having a molecular mass of 18.1 kDa. The MANF 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 ED50 was determined by its ability to stimulate the proliferation of rat C6 cells is typically 15-25 µg/ml.More Info
-
Introduction
MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.
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Synonyms
Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MANF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MANF 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.
-
Solubility
It is recommended to reconstitute the lyophilized MANF 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
LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIENELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDKQ IDLSTVDLKK LRVKELKKIL DDWGETCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.
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 :
TPT1 HumanDescription:
Tumor Protein Translationally-Controlled 1 Human Recombinant
TCTP, Fortilin, Histamine-Releasing Factor, Translationally-controlled tumor protein, p23, HRF, Fortilin, p02, FLJ27337, TPT1.
Product # :
PRO-776Price :
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Description
TPT1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 210 amino acids (1-172 a.a.) and having a molecular mass of 23.9 kDa. TPT1 is fused to a 38 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TPT1 solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TPT1 takes part in calcium binding and microtubule stabilization. TPT1 is an immunoglobulin E dependent histamine-releasing factor produced by lymphocytes of atopic children and present in biologic fluids of allergic patients. TPT1 protein is similar to p23, a protein of Ehrlich ascites tumor cells, synthesized in the exponentially growing tumor. TPT1 is similar with IgE-dependent histamine releasing factor. TPT1 has a cell housekeeping function. TPT1 is involved in spermatogenesis and acts as a calcium binding protein of the human placenta that regulates calcium handling in trophoblast cells.
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Synonyms
TCTP, Fortilin, Histamine-Releasing Factor, Translationally-controlled tumor protein, p23, HRF, Fortilin, p02, FLJ27337, TPT1.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMMI IYRDLISHDE MFSDIYKIRE IADGLCLEVE GKMVSRTEGN IDDSLIGGNA SAEGPEGEGT ESTVITGVDI VMNHHLQETS FTKEAYKKYI KDYMKSIKGK LEEQRPERVK PFMTGAAEQI KHILANFKNY QFFIGENMNP DGMVALLDYR EDGVTPYMIF FKDGLEMEKC.
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 :
CPSF4 HumanDescription:
Cleavage And Polyadenylation Specific Factor 4 Human Recombinant
CPSF30, NAR, NEB1, Neb-1, CPSF 30 kDa subunit, NS1 effector domain-binding protein 1.
Product # :
PRO-1406Price :
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Description
CPSF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-244 a.a.) and having a molecular mass of 29.9kDa.CPSF4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CPSF4 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
-
Introduction
Cleavage And Polyadenylation Specific Factor 4 (CPSF4) is a member of the CPSF4/YTH1 family. CPSF4 complex plays a vital role in pre-mRNA 3'-end formation, distinguishing the AAUAAA signal sequence and interacting with poly(A) polymerase and further factors to bring about cleavage and poly(A) additive. CPSF4 binds RNA polymers with a preference for poly(U).
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Synonyms
CPSF30, NAR, NEB1, Neb-1, CPSF 30 kDa subunit, NS1 effector domain-binding protein 1.
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Physical Appearance
Sterile Filtered clear 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
MGSSHHHHHH SSGLVPRGSH MGSMQEIIAS VDHIKFDLEI AVEQQLGAQP LPFPGMDKSG AAVCEFFLKA ACGKGGMCPF RHISGEKTVV CKHWLRGLCK KGDQCEFLHE YDMTKMPECY FYSKFGECSN KECPFLHIDP ESKIKDCPWY DRGFCKHGPL CRHRHTRRVI CVNYLVGFCP EGPSCKFMHP RFELPMGTTE QPPLPQQTQP PAKQRTPQVI GVMQSQNSSA GNRGPRPLEQ VTCYKCGEKG HYANRCTKGH LAFLSGQ.
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 :
ARF1 HumanDescription:
ADP-Ribosylation Factor 1 Human Recombinant
ARF-1, ADP-ribosylation factor 1.
Product # :
PRO-867Price :
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Description
ARF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8 kDa. The ARF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARF1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
ARF1 is a small guanine nucleotide-binding protein that increases the enzymatic activities of cholera toxin. ARF1 is necessary and ubiquitous in eukaryotes. ARF1 takes part in vesicular transport and functioning via phospholipase D activation. ARF1 is involved in membrane traffic and organelle integrity which are closely tied to their reversible association with membranes and distinct interactions with membrane phospholipids.
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Synonyms
ARF-1, ADP-ribosylation factor 1.
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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
MGSSHHHHHH SSGLVPRGSH MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ K.
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 :
C1QTNF3 HumanDescription:
Complement C1q Tumor Necrosis Factor-Related Protein 3 Human Recombinant
Complement C1q tumor necrosis factor-related protein 3, Secretory protein CORS26, C1QTNF3, CTRP3, Cors, Corcs, CORS26, FLJ37576, Cartducin.
Product # :
PRO-653Price :
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Shipped at Room temp
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Description
C1QTNF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 234 amino acids and having a molecular mass of 25.4 kDa. The protein contains an extra 10 aa His tag at N-terminus. The C1QTNF3 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXJ4 amino acids 23–246. The C1QTNF3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Human C1QTNF3 was filtered (0.4µm) and lyophilized in 0.5 mg/ml in 0.05M Acetate buffer pH4.
Purity
The purity of C1QTNF3 is greater than 95% as determined by SDS PAGE.
More Info
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Introduction
C1QTNF3 also called Cartducin is a novel angiogenic factor in the formation of neointima following angioplasty. C1QTNF3 a paralog of Acrp30 (adiponectin). C1QTNF3 is a secretory protein produced by chondrogenic precursors & proliferating chondrocytes, and belongs to a novel C1q family of proteins. Cartducin promotes the growth of mesenchymal chondroprogenitor cells & chondrosarcoma-derived chondrocytic cells in vitro. Cartducin stimulates mesenchymal chondroprogenitor cell proliferation through extracellular signal-regulated kinase and phosphatidylinositol 3-kinase/Akt pathways. C1QTNF3 promotes proliferation & the migration of endothelial cells.
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Synonyms
Complement C1q tumor necrosis factor-related protein 3, Secretory protein CORS26, C1QTNF3, CTRP3, Cors, Corcs, CORS26, FLJ37576, Cartducin.
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Stability
Store lyophilized C1QTNF3 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted C1QTNF3 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 pH4 to prepare a working stock solution of approximately 0.5 mg/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 the protein is limited. Product 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 QDEYMESPQT GGLPPDCSKC CHGDYSFRGY QGPPGPPGPP GIPGNHGNNG NNGATGHEGA KGEKGDKGDL GPRGERGQHG PKGEKGYPGI PPELQIAFMA SLATHFSNQN SGIIFSSVET NIGNFFDVMT GRFGAPVSGV YFFTFSMMKH EDVEEVYVYL MHNGNTVFSM YSYEMKGKSD TSSNHAVLKL AKGDEVWLRM GNGALHGDHQ RFSTFAGFLLFETK.
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 :
PEX19 HumanDescription:
Peroxisomal Biogenesis Factor 19 Human Recombinant
Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.
Product # :
PRO-925Price :
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Description
PEX19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 34.6 kDa.The PEX19 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PEX19 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
PEX19 is vital for peroxisome biogenesis in Saccharomyces cerevisiae. PEX19 is limited to the outer surface of peroxisomes in liver cells and is has a part in the early stage of peroxisome membrane assembly, prior to the import of matrix protein.
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Synonyms
Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.
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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
MGSSHHHHHH SSGLVPRGSH MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQC
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 :
PRLR Human, AntagonistDescription:
Prolactin Receptor Antagonist Human Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-1254Price :
Quantity :
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Shipped at Room temp
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Description
Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.
Biological Activity
fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).
More Info
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PRLR 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 six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr
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Background
Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
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 :
Midkine RatDescription:
Midkine Rat Recombinant
Midkine, MK, Mdk.
Product # :
CYT-747Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Midkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a molecular mass of 13.2kDa.The Midkine Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-100 ng/ml.More Info
-
Introduction
Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis. -
Synonyms
Midkine, MK, Mdk.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Midkine Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Midkine Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Midkine Rat 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
VAKKKDKVKK GSECSEWTWG PCTPSSKDCG MGFREGTCGA QTQRIHCKVP CNWKKEFGAD CKYKFESWGA CDGSTGTKAR QGTLKKARYN AQCQETIRVT KPCTSKTKSK AKAKKGKGKD.
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 :
Leptin tA HumanDescription:
Leptin Antagonist Triple Mutant Human Recombinant
Product # :
CYT-352Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant 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 Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, 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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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 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.
- View Data Sheet
Name :
C1QTNF2 HumanDescription:
Complement C1q Tumor Necrosis Factor-Related Protein 2 Human Recombinant
Complement C1q tumor necrosis factor-related protein 2, CTRP2, zacrp2.
Product # :
PRO-133Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- More Info
Description
C1QTNF2 Protein is a 29,640 Da protein containing 280 aa fused to a 10 aa N-Terminal His-tag.
Source
E. coli
Formulation
C1QTNF2 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 0.03M Acetate buffer, pH 4.
More Info
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Introduction
C1QTNF2 can be found in many different organism parts such as the testis, cervix. C1QTNF2 is located in the extracellular space and has various roles such as activation of MAPK activity, positive regulation of fatty acid oxidation, positive regulation of glycogen biosynthetic process, and positive regulation of glucose import.
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Synonyms
Complement C1q tumor necrosis factor-related protein 2, CTRP2, zacrp2.
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Stability
Store lyophilized C1QTNF2 uman at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted C1QTNF2 an 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
Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/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 10?g/ml. In higher concentrations the solubility of this antigen is limited. Product 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 DPLLGAFARR DFRKGSPQLV CSLPGPQGPP GPPGAPGPSG MMGRMGFPGK DGQDGHDGDR GDSGEEGPPG DPLLGAFARR DFRKGSPQLV CSLPGPQGPP GPPGAPGPSG MMGRMGFPGK DGQDGHDGDR GDSGEEGPPG RTGNRGKPGP KGKAGAIGRA GPRGPKGVNG TPGKHGTPGK KGPKGKKGEP GLPGPCSCGS GHTKSAFSVA VTKSYPRERL PIKFDKILMN EGGHYNASSG KFVCGVPGIY YFTYDITLAN KHLAIGLVHN GQYRIRTFDA NTGNHDVASG STILALKQGD EVWLQIFYSE QNGLFYDPYW TDSLFTGFLI YADQDDPNEV.
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 :
PEDF HumanDescription:
Pigment Epithelium-Derived Factor Human Recombinant
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Product # :
CYT-580Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
PEDF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 400 amino acids and having a molecular mass of 44.5 kDa. The Human PEDF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile filtered concentrated (1mg/ml) protein solution was lyophilized with 20mM sodium phosphate buffer & 150mM NaCl pH-7.4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.
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Synonyms
Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PEDF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PEDF Human 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 PEDF 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
MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.
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Background
About PEDF Human
Also known as “Pigment Epithelium-Derived Factor” or “SERPINF1,” PEDF is a
multifunctional protein found in vertebrates. It has anti-tumorigenic, anti-angiogenic, and
neurotrophic functions. Currently, it’s being researched as a candidate for treatment for
several conditions, including heart disease and cancer.What’s the Function of PEDF Human Recombinant?
PEDF is created/secreted in several tissues across the body. It has a unique anti-angiogenic
action because of its induction of apoptosis in proliferating endothelial cells. Also, PEDF
can inhibit many angiogenic factors, including VEGF and FGF-2. PEDF-R is currently the
only known signaling receptor to be used by a serpin family member.
What’s the Application of PEDF Human Recombinant?This version of PEDF is produced in E. Coli. It’s a single, non-glycosylated, polypeptide
chain that contains 400 amino acids. It has a molecular mass of 44.5 kDa, and it’s purified
by proprietary chromatographic techniques.The main purpose of PEDF human recombinant is for research. It has the potential to
become a potential treatment for different angiogenesis-related diseases, including
various cancers. Moreover, it can become crucial during the recovery from vasculature-
related neurodegenerative illness.Such a discovery could be revolutionary for the world, which is why more research is
needed to determine the effect of this non-inhibitory serpin on the body.
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.