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1000 results found for “HINT”
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Name :
IFNW1 HumanDescription:
IFN-Omega 1 Human Recombinant
IFN omega-1, IFN alpha-II-1, IFNW1.
Product # :
CYT-040Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IFN-Omega 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19.9kDa.The IFN-Omega 1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 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 was determined by a cytotoxicity assay using Human TF-1 cells is < 0.01 ng/ml, corresponding to a specific activity of > 100,000,000 units/mg.More Info
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Introduction
IFN-Omega 1 is a type I IFN, that can be induced by virus-infected leukocytes. Type I IFN family members, which include IFN-alpha, IFN-beta, and IFN-omega, signal through IFNAR-1/IFNAR-2 receptor complex, and wield antiviral and antiproliferative activities. IFNW1 exhibits about 75% sequence homology with IFN-a, and contains 2 conserved disulfide bonds, which are essential for full biological activity.
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Synonyms
IFN omega-1, IFN alpha-II-1, IFNW1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFNW1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFNW1 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 IFNW1 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
MCDLPQNHGL LSRNTLVLLH QMRRISPFLC LKDRRDFRFP QEMVKGSQLQ KAHVMSVLHE MLQQIFSLFH TERSSAAWNM TLLDQLHTGL HQQLQHLETC LLQVVGEGES AGAISSPALT LRRYFQGIRV YLKEKKYSDC AWEVVRMEIM KSLFLSTNMQ ERLRSKDRDL GSS.
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Background
What is the molecular weight/Mw of IFNW1 HUMAN Protein?
IFNW1 HUMAN Protein has a total Mw of 19.9kDa.
What is the source or expression system of IFNW1 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFNW1 HUMAN Protein?
IFNW1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNW1 HUMAN Protein?
The ED50 was determined by a cytotoxicity assay using Human TF-1 cells is < 0.01 ng/ml, corresponding to a specific activity of > 100,000,000 units/mg.
What is the amino acid sequence of IFNW1 HUMAN Protein?
MCDLPQNHGL LSRNTLVLLH QMRRISPFLC LKDRRDFRFP QEMVKGSQLQ KAHVMSVLHE MLQQIFSLFH TERSSAAWNM TLLDQLHTGL HQQLQHLETC LLQVVGEGES AGAISSPALT LRRYFQGIRV YLKEKKYSDC AWEVVRMEIM KSLFLSTNMQ ERLRSKDRDL GSS.
What applications can IFNW1 HUMAN Protein be used in?
IFNW1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNW1 HUMAN Protein?
The endotoxin level is minimal, IFNW1 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 :
Vimentin BovineDescription:
Bovine Vimentin
Vimentin, Vim, FLJ36605.
Product # :
PRO-525Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bovine Vimentin protein produced in Bovine Lens, having a molecular weight of 57 kDa.
Source
Bovine Lens.
Formulation
The protein (1mg/ml) was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate pH 7.5, 6M urea, 2mM DTT, 1mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
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Introduction
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.
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Synonyms
Vimentin, Vim, FLJ36605.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bovine Vimentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BovineVimentin 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 Bovine Vimentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
After vimentin is dissolved in 6M urea buffer (see above), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Sodium Phosphate, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco''s PBS).- Hatzfeld M. and Franke W.W. (1985). J. Cell Biol. 101, 1826-1841.- Hatzfeld M. et al. (1987). J. Mol. Biol. 197, 237-255.
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 :
CoV-2-S1 (319-541), BiotinDescription:
Coronavirus 2019 Spike Glycoprotein-S1 Receptor Binding Domain (319-541 a.a), Biotinylated Recombinant
Product # :
SARS-030Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The HEK293 derived Biotinylated recombinant protein contains the Coronavirus 2019 Spike Glycoprotein S1 Receptor Binding Domain [ RBD ], Wuhan-Hu-1 strain, amino acids 319-541 fused to His tag & AVI tag at C-terminal and having a molecular mass of 28.7kDa.
Source
HEK293 Cells.
Formulation
CoV-2 S1 RBD protein is lyophilized from 1x PBS pH-7.4 + 10% trehalose.
Purity
Protein is >90% pure as determined SDS-PAGE.
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
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Physical Appearance
Lyophilized freezed dried powder.
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Stability
Lyophilized Cov-2 S1 Glycoprotein RBD although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Spike protein 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 CoV-2 S1 protein in sterile 18M-cm H2O at aconcentration of 0.2mg/ml and not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Purification Method
Purified by Metal-Afinity chromatographic technique.
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 :
CD58 Antibody, BiotinDescription:
CD58, Mouse Anti-Human, Biotin
CD58, LFA-3, Ag3, Surface glycoprotein LFA-3.
Product # :
ANT-278Price :
Quantity :
Shipping Method :
Shipped at Room temp
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More Info
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Introduction
CD58 is part of the immunoglobulin superfamily. CD58 is a ligand of the T lymphocyte CD2 protein, and is invloved in adhesion and activation of T lymphocytes. CD58 is localized to the plasma membrane.
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Synonyms
CD58, LFA-3, Ag3, Surface glycoprotein LFA-3.
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Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
Human Erythrocytes.
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Ig Subclass
Mouse IgG1.
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Clone
hCD58.
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Applications
Staining antibody. For staining, use 10µl/1,000,000 cells.
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Available Conjugates
This antibody is also available unconjugated to and conjugated to FITC. For staining with biotin or FITC-conjugated antibody use 5-10µl/1,000,000 cells.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
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Purification Method
Ion-Exchange Column Protein concentration1mg/ml in PBS (after reconstitution).
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 :
HEV ORF2 (403-461 a.a.)Description:
Hepatitis E Virus ORF2 (403-461 a.a.) Recombinant
Product # :
HEV-272Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The e.coli derived HEV protein is fused with beta-galactosidase at the N-Terminus and contains the HEV immunodominant regions from ORF2 403-461 a.a.
Formulation
20mM Tris-HCl pH-8, 8M urea and 10mM B-ME.
Purity
HEV ORF2 Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
Hepatitis E virus (HEV), the major etiologic agent of enterically transmitted non-A, non-B hepatitis worldwide, is a spherical, non-enveloped, single stranded RNA virus that is approximately 32 to 34 nm in diameter. HEV belongs to a genus of HEV-like viruses (unassigned genus). HEV has a single-stranded polyadenylated RNA genome of approximately 8 kb. Based on its physicochemical properties it is presumed to be a calici-like virus.
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Stability
HEV ORF2 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HEV ORF2 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HEV with minimal specificity problems.
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Specificity
Immunoreactive with sera HEV-infected individuals.
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Purification Method
HEV ORF2 was purified by proprietary chromatographic technique.
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 :
TNNI3 Human ChimericDescription:
Cardiac Troponin-I Chimeric Human Recombinant
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Product # :
PRO-2790Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNNI3 Human Chimeric produced in E.Coli is a single, non-glycosylated polypeptide chain (28-110 a.a.) and having a molecular mass of 29072 Dalton.
Source
Escherichia Coli.
Formulation
TNNI3 was lyophilized in 50mM Tris-HCl, 5mM Calcium chloride, 0.7M KCl and 0.1% 2-mercaptoethanol, pH 7.5
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiac Troponin-I Chimeric although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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 TNNI3 in buffer containing BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Troponin I (TNNI3) is a crucial regulatory protein in cardiac muscle, playing a central role in the regulation of muscle contraction. Understanding the structure and function of TNNI3 is essential for unraveling the complexities of cardiac muscle physiology and exploring therapeutic interventions for cardiac diseases. Chimeric TNNI3 proteins, which combine segments from different isoforms or species, offer a unique opportunity to investigate the role of specific regions in TNNI3 function and to potentially develop novel therapies. This research aims to provide a comprehensive exploration of chimeric TNNI3 proteins, elucidating their functions, structural significance, and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the functional significance of chimeric TNNI3 proteins in cardiac muscle. In vitro and ex vivo experiments, utilizing engineered chimeric TNNI3 constructs and cardiac tissue models, will be conducted to investigate how these proteins influence muscle contractility, calcium sensitivity, and response to pathological conditions. Understanding these mechanisms is fundamental for deciphering the roles of specific TNNI3 regions in cardiac muscle function.
The second objective is to assess the therapeutic potential of chimeric TNNI3 proteins in cardiac diseases. Experimental studies involving animal models and cellular systems will explore the use of chimeric TNNI3 proteins as potential therapeutic agents for heart conditions. These investigations may provide valuable insights into novel treatment strategies targeting cardiac muscle function.
The third objective is to explore the broader applications of chimeric TNNI3 proteins in biotechnology and drug development. Research will investigate the use of chimeric TNNI3-expressing cells and tissues as models for studying cardiac disorders and for developing innovative approaches in regenerative medicine and pharmacology.
By delving into the functions and roles of chimeric TNNI3 proteins, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology, biotechnology, and drug development
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 4 MouseDescription:
Interleukin-4 Mouse Recombinant
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Product # :
CYT-282Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13500 Dalton. The IL-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm concentrated (1mg/ml) solution in PBS pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant induction of HT-2 cell proliferation is less than 2 ng/ml corresponding to a Specific Activity of 500,000IU/mg.More Info
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Introduction
Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.
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Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 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 4 in sterile 10mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHIHGCDKNH LREIIGILNE VTGEGTPCTE MDVPNVLTAT KNTTESELVC RASKVLRIFY LKHGKTPCLK KNSSVLMELQ RLFRAFRCLD SSISCTMNES KSTSLKDFLE SLKSIMQMDY S.
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 HumanDescription:
Leukemia Inhibitory Factor Human Recombinant
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-644Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/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 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 TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.
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Background
Leukemia Inhibitory Factor (LIF) Background
Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.
LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.
Function and Applications of LIF
LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.
Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.
Structure and Interactions
LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.
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 :
GDF15 HumanDescription:
Growth and Differentiation Factor 15 Human Recombinant
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Product # :
CYT-335Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa. The GDF15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF15 is lyophilized from a sterile filtered solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
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Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
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Background
What is the molecular weight/Mw of GDF15 HUMAN Protein?
GDF15 HUMAN Protein has a total Mw of 24.8kDa.
What is the source or expression system of GDF15 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF15 HUMAN Protein?
GDF15 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 HUMAN Protein?
The biological functionality of GDF15 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF15 HUMAN Protein?
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
What applications can GDF15 HUMAN Protein be used in?
GDF15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF15 HUMAN Protein?
The endotoxin level is minimal, GDF15 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 :
C1QTNF6 HumanDescription:
Complement C1q Tumor Necrosis Factor-Related Protein 6 Human Recombinant
CTRP6, C1QTNF6, ZACRP6, Complement C1q tumor necrosis factor-related protein 6.
Product # :
PRO-655Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
C1QTNF6 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 242 amino acids and having a molecular mass of 27 kDa. The protein contains an extra His tag at N-terminus. The C1QTNF6 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXI9 amino acids 29–259.The C1QTNF6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.23mg/ml in 30mM Acetate Buffer pH-4.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
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Introduction
C1QTNF6 is a collagen type-IV specific for basement membranes. C1QTNF6 is vital for embryonic development.
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Synonyms
CTRP6, C1QTNF6, ZACRP6, Complement C1q tumor necrosis factor-related protein 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. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MKHHHHHHAS TFDRAVASGC QRCCDSEDPL DPAHVSSASS SGRPHALPEI RPYINITILK GDKGDPGPMG LPGYMGREGP QGEPGPQGSK GDKGEMGSPG APCQKRFFAF SVGRKTALHS GEDFQTLLFE RVFVNLDGCF DMATGQFAAP LRGIYFFSLN VHSWNYKETY VHIMHNQKEA VILYAQPSER SIMQSQSVML DLAYGDRVWV RLFKRQRENA IYSNDFDTYI TFSGHLIKAEDD.
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 :
FOLH1 MouseDescription:
Folate Hydrolase 1 Mouse Recombinant
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
Product # :
ENZ-957Price :
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Description
FOLH1 Mouse Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 717 amino acids (45-752a.a) and having a molecular mass of 80.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). FOLH1 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The FOLH1 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Folate Hydrolase 1 (Folh1) is a single pass type 2 membrane protein which is expressed mainly in prostate epithelium. Folh1 which is a part of the peptidase M28 family and M28B subfamily has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase activity. Folh1 can be found in urinary bladder, kidney, testis, ovary, stomach, small intestine colon, and the capillary endothelium of various tumors. Therefore, Folh1 plays a role in directed imaging and therapy of recurrent of metastatic disease.
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Synonyms
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
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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
ADPKPSNEAT GNVSHSGMKK EFLHELKAEN IKKFLYNFTR TPHLAGTQNN FELAKQIHDQ WKEFGLDLVE LSHYDVLLSY PNKTHPNYIS IINEDGNEIF KTSLSEQPPP GYENISDVVP PYSAFSPQGT PEGDLVYVNY ARTEDFFKLE REMKISCSGK IVIARYGKVF RGNMVKNAQL AGAKGMILYS DPADYFVPAV KSYPDGWNLP GGGVQRGNVL NLNGAGDPLT PGYPANEHAY RHELTNAVGL PSIPVHPIGY DDAQKLLEHM GGPAPPDSSW KGGLKVPYNV GPGFAGNFST QKVKMHIHSY TKVTRIYNVI GTLKGALEPD RYVILGGHRD AWVFGGIDPQ SGAAVVHEIV RSFGTLKKKG RRPRRTILFA SWDAEEFGLL GSTEWAEEHS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVYNLTK ELQSPDEGFE GKSLYDSWKE KSPSPEFIGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWKTNKVSSY PLYHSVYETY ELVVKFYDPT FKYHLTVAQV RGAMVFELAN SIVLPFDCQS YAVALKKYAD TIYNISMKHP QEMKAYMISF DSLFSAVNNF TDVASKFNQR LQELDKSNPI LLRIMNDQLM YLERAFIDPL GLPGRPFYRH IIYAPSSHNK YAGESFPGIY DALFDISSKV NASKAWNEVK RQISIATFTV QAAAETLREV AHHHHHH.
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 :
GCDH HumanDescription:
Glutaryl-Coenzyme A Dehydrogenase Human Recombinant
ACAD5, GCD, EC 1.3.99.7, GCDH, Glutaryl-Coenzyme A Dehydrogenase, glutaryl-CoA dehydrogenase.
Product # :
ENZ-542Price :
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Description
GCDH Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (45-438 a.a.) and having a molecular mass of 45.8 kDa. The GCDH is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5mg/ml solution containing 20mM Tris-HCl, pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GCDH is part of the acyl-CoA dehydrogenase family. GCDH is localized in the mitochondrial matrix as a homotetramer of 45-kD subunits. GCDH catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. GCDH uses electron transfer flavoprotein as its electron acceptor.
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Synonyms
ACAD5, GCD, EC 1.3.99.7, GCDH, Glutaryl-Coenzyme A Dehydrogenase, glutaryl-CoA dehydrogenase.
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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 MRPEFDWQDP LVLEEQLTTD EILIRDTFRT YCQERLMPRI LLANRNEVFH REIISEMGEL GVLGPTIKGY GCAGVSSVAY GLLARELERV DSGYRSAMSV QSSLVMHPIY AYGSEEQRQK YLPQLAKGEL LGCFGLTEPN SGSDPSSMET RAHYNSSNKS YTLNGTKTWI TNSPMADLFV VWARCEDGCI RGFLLEKGMR GLSAPRIQGK FSLRASATGM IIMDGVEVPE ENVLPGASSL GGPFGCLNNA RYGIAWGVLG ASEFCLHTAR QYALDRMQFG VPLARNQLIQ KKLADMLTEI TLGLHACLQL GRLKDQDKAA PEMVSLLKRN NCGKALDIAR QARDMLGGNG ISDEYHVIRH AMNLEAVNTY EGTHDIHALI LGRAITGIQA FTASK.
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 :
RELT HumanDescription:
RELT Human Recombinant
RELT, TNF Receptor, Receptor Expressed In Lymphoid Tissues, Tumor Necrosis Factor Receptor Superfamily Member 19L, RELT Tumor Necrosis Factor Receptor, TNFRSF19L, Tumor Necrosis Factor Receptor Superfamily, Member 19-Like, TRLT.
Product # :
CYT-1101Price :
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Description
RELT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 376 amino acids (26-162a.a.) and having a molecular mass of 41.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).RELT is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
RELT protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
RELTis expressed in hematopoietic tissues and peripheral blood leukocytesand is a part of thetumor necrosis factor receptor superfamily. RELT mediates activation of NF-kappa-B and takes part in T-cell activation.overexpression of RELT in HEK-293 cells induces p38 and JNK signalling and leads to apoptosis. it can also costimulate T-cell proliferation in the presence of CD3 signalling.
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Synonyms
RELT, TNF Receptor, Receptor Expressed In Lymphoid Tissues, Tumor Necrosis Factor Receptor Superfamily Member 19L, RELT Tumor Necrosis Factor Receptor, TNFRSF19L, Tumor Necrosis Factor Receptor Superfamily, Member 19-Like, TRLT.
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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
STTLWQCPPG EEPDLDPGQG TLCRPCPPGT FSAAWGSSPC QPHARCSLWR RLEAQVGMAT
RDTLCGDCWP GWFGPWGVPR VPCQPCSWAPLGTHGCDEWG RRARRGVEVA AGASSGGETR QPGNGTRAGG PEETAAQVEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK 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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Name :
MIP 1b HumanDescription:
Macrophage Inflammatory Protein-1 Beta Human Recombinant (CCL4)
Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.
Product # :
CHM-276Price :
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Description
Macrophage Inflammatory Protein-1 beta Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7620 Dalton. The CCL4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability to chemoattract Human blood monocytes using a concentration of 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.More Info
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Introduction
Macrophage Inflammatory Proteins belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now also named CCL3 and CCL4. Both factors are produced by macrophages after they are stimulated with bacterial endotoxins. MIP-1a and MIP-1b activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. MIP-1a and MIP-1b induce synthesis and release of other pro-inflammatory cytokines such as interleukin-1 (IL-1), IL-6 and TNF-alpha from fibroblasts and macrophages. CCL3 and CCL4 genes are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL4 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 Macrophage Inflammatory Protein-1b 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-Met-Gly-Ser.
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Background
What is the molecular weight/Mw of MIP 1B HUMAN Protein?
MIP 1B HUMAN Protein has a total Mw of 7.62kDa.
What is the source or expression system of MIP 1B HUMAN Protein?
Escherichia Coli.
What is the Purity of MIP 1B HUMAN Protein?
MIP 1B HUMAN Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1B HUMAN Protein?
The Activity is calculated by the ability to chemoattract Human blood monocytes using a concentration of 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.
What is the amino acid sequence of MIP 1B HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Met-Gly-Ser.
What applications can MIP 1B HUMAN Protein be used in?
MIP 1B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1B HUMAN Protein?
The endotoxin level is minimal, MIP 1B 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 :
Myostatin Human, HisDescription:
Myostatin Human Recombinant, His Tag
GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.
Product # :
CYT-445Price :
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Shipped at Room temp
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Description
Total 152AA. M.W. 16.7kDa (calculated). N-terminal His-tag and spacer (43AA – highlighted). The AA sequence of the human myostatin part of the fusion protein is corresponding to the UniProtKB/Swiss-Prot entry O14793.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M acetate buffer, pH 4.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Myostatin (GDF-8) is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 113 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor ? superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology.
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Synonyms
GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.
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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 0.1M Acetate buffer pH-4 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 this antigen is limited.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDPSSRSAVR SRRDFGLDCD EHSTESRCCR YPLTVDFEAFGWDWIIAPKR YKANYCSGEC EFVFLQKYPH THLVHQANPR GSAGPCCTPT KMSPINMLYF NGKEQIIYGKIPAMVVDRCG CS.
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 :
IGF1 Gilthead SeabreamDescription:
IGF1 Gilthead Seabream Recombinant
Somatomedin C, IGF-I, IGFI.
Product # :
CYT-295Price :
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Shipped at Room temp
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Description
IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.IGF-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.More Info
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Introduction
The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.
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Synonyms
Somatomedin C, IGF-I, IGFI.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 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
MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK
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Background
What is the molecular weight/Mw of IGF1 GILTHEAD SEABREAM Protein?
IGF1 GILTHEAD SEABREAM Protein has a total Mw of 7.54kDa.
What is the source or expression system of IGF1 GILTHEAD SEABREAM Protein?
Escherichia Coli.
What is the Purity of IGF1 GILTHEAD SEABREAM Protein?
IGF1 GILTHEAD SEABREAM Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 GILTHEAD SEABREAM Protein?
Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.
What is the amino acid sequence of IGF1 GILTHEAD SEABREAM Protein?
MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK
What applications can IGF1 GILTHEAD SEABREAM Protein be used in?
IGF1 GILTHEAD SEABREAM Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 GILTHEAD SEABREAM Protein?
The endotoxin level is minimal, IGF1 GILTHEAD SEABREAM Protein was purified using conventional chromatography techniques.
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Protein content
Somatomedin C quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.60 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). 2. Analysis by RP-HPLC, using a calibrated solution of IGF1 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL36A Mouse, HisDescription:
Interleukin-36 Alpha Mouse Recombinant, His Tag
Interleukin-36 alpha, FIL1 epsilon, Interleukin-1 epsilon, IL-1 epsilon, Interleukin-1 family member 6, IL-1F6, Interleukin-1 homolog 1, IL-1H1, Il36a, Fil1e, Il1e, Il1f6, Il1h1.
Product # :
CYT-905Price :
Quantity :
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Description
IL36A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-160 a.a) and having a molecular mass of 20.4kDa. IL36A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IL36A protein solution (1mg/ml) containing 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
Human IL-36a belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36a is an 18-22kDa, 158aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential from N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
Human IL-36a (aa 6-158) shares 57-68% aa sequence homology with mouse, rabbit, equine and bovine IL-36a and 27-57% aa sequence homology with other new IL-1 family members. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine. -
Synonyms
Interleukin-36 alpha, FIL1 epsilon, Interleukin-1 epsilon, IL-1 epsilon, Interleukin-1 family member 6, IL-1F6, Interleukin-1 homolog 1, IL-1H1, Il36a, Fil1e, Il1e, Il1f6, Il1h1.
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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 MGSMNKEKEL RAASPSLRHV QDLSSRVWIL QNNILTAVPR KEQTVPVTIT LLPCQYLDTL ETNRGDPTYM GVQRPMSCLF CTKDGEQPVL QLGEGNIMEM YNKKEPVKAS LFYHKKSGTT STFESAAFPG WFIAVCSKGS CPLILTQELG EIFITDFEMI VVH.
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 :
KLK3, HisDescription:
Kallikrein-3 Human Recombinant, His Tag
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
Product # :
ENZ-620Price :
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Shipping Method :
Shipped with Ice Packs
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Description
KLK3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (25-261) and having a molecular mass of 28.8kDa.The KLK3 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KLK3 protein solution (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0) and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-3 (KLK3) belongs to the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 is assumed to act normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.
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Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
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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 MGSHMIVGGW ECEKHSQPWQ VLVASRGRAV CGGVLVHPQW VLTAAHCIRN KSVILLGRHS LFHPEDTGQV FQVSHSFPHP LYDMSLLKNR FLRPGDDSSH DLMLLRLSEP AELTDAVKVM DLPTQEPALG TTCYASGWGS IEPEEFLTPK KLQCVDLHVI SNDVCAQVHP QKVTKFMLCA GRWTGGKSTC SGDSGGPLVC NGVLQGITSW GSEPCALPER PSLYTKVVHY RKWIKDTIVA NP.
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 :
HES2 HumanDescription:
Hairy and Enhancer of Split 2 Human Recombinant
bHLHb40, hairy and enhancer of split 2, Class B basic helix-loop-helix protein 40, HES2.
Product # :
PRO-1649Price :
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Description
HES2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (1-173 a.a.) and having a molecular mass of 20.9kDa.HES2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HES2 protein 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
Hairy and enhancer of split 2 (HES2) belongs to the HES family and comprised of one basic helix-loop-helix (bHLH) domain and one orange domain. The HES family members form a complex with TLE, the mammalian homologue of Groucho, and this interaction is mediated by the carboxy terminal WRPW motif of the HES proteins. Activation of Notch signaling pathway initiates activation of HES family genes throughout the interaction between Notch intracellular domain and RBPSUH (CSL). HES2 is expressed in placenta, pancreatic cancer, colon cancer with RER, cervical cancer, and in head and neck tumors.
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Synonyms
bHLHb40, hairy and enhancer of split 2, Class B basic helix-loop-helix protein 40, HES2.
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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 MGSMGLPRRA GDAAELRKSL KPLLEKRRRA RINQSLSQLK GLILPLLGRE NSNCSKLEKA DVLEMTVRFL QELPASSWPT AAPLPCDSYR EGYSACVARL ARVLPACRVL EPAVSARLLE HLWRRAASAT LDGGRAGDSS GPSAPAPAPA SAPEPASAPV PSPPSPPCGP GLWRPW.
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 :
Desmin HumanDescription:
Desmin Human Recombinant
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
Product # :
PRO-520Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Desmin Human Recombinant having a calculated molecular mass of 53,539 Dalton, showing a 55kDa band on SDS-page, pI-5.16.
Source
Escherichia Coli.
Formulation
Desmin was lyophilized from a 1mg/ml solution containing 30mM Tris-HCl pH 8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Desmin is a muscle-specific class III intermediate filament. Homopolymers of this protein form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. Mutations in this gene are associated with desmin-related myopathy, a familial cardiac and skeletal myopathy (CSM), and with distal myopathies.
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Synonyms
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Desmin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
After Desmin is dissolved in 9.5M urea buffer (see formulation), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Tris-HCl, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).
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 :
DLAT HumanDescription:
Dihydrolipoamide S-Acetyltransferase Human Recombinant
Dihydrolipoamide S-Acetyltransferase, PDC-E2, dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex mitochondrial, Pyruvate dehydrogenase complex component E2, 70 kDa mitochondrial autoantigen of primary biliary cirrhosis, DLAT, PBC, M2 antigen complex 70 kDa subunit, EC 2.3.1.12, EC 2.3.1.
Product # :
ENZ-082Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DLAT is a full-length cDNA coding for the mature form of the human PDC-E2 protein having a molecular mass of 60,630 Dalton (pH 5.8). DLAT protein is fused to a hexa-histidine purification tag.
Source
Sf9 insect cells.
Formulation
DLAT is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
DLAT purity was found to be greater than 75% as determined by SDS-PAGE.
More Info
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Introduction
DLAT gene encodes component E2 of the multi-enzyme pyruvate dehydrogenase complex (PDC). PDC is located in the inner mitochondrial membrane and catalyzes the conversion of pyruvate to acetyl coenzyme A. The protein product of this gene, dihydrolipoamide acetyltransferase, takes acetyl groups created by the oxidative decarboxylation of pyruvate and transfers them to coenzyme A. Dihydrolipoamide acetyltransferase is the antigen for antimitochondrial antibodies which are found in about 95% of patients with the autoimmune liver disease primary biliary cirrhosis (PBC). In patients who suffer from this illness, activated T lymphocytes attack and destroy epithelial cells in the bile duct where this protein is abnormally distributed and overexpressed. PBC ultimately leads to cirrhosis and liver failure. Mutations in DLAT are also a cause of pyruvate dehydrogenase E2 deficiency which causes primary lactic acidosis in infancy and early childhood.
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Synonyms
Dihydrolipoamide S-Acetyltransferase, PDC-E2, dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex mitochondrial, Pyruvate dehydrogenase complex component E2, 70 kDa mitochondrial autoantigen of primary biliary cirrhosis, DLAT, PBC, M2 antigen complex 70 kDa subunit, EC 2.3.1.12, EC 2.3.1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store DLAT 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.
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Name :
DNAJB2 HumanDescription:
DnaJ (Hsp40) homolog, subfamily B, member 2 Human Recombinant
DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, Heat shock 40 kDa protein 3, Heat shock protein J1, HSJ-1, DNAJB2, HSJ1, HSPF3.
Product # :
HSP-035Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DNAJB2 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 300 amino acids (1-277 a.a.) and having a molecular mass of 33kDa. The DNAJB2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DNAJB2 solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DnaJB2 is a member of the DnaJ family. The DnaJ family is one of the largest of all the chaperone families which has evolved with diverse cellular localization and functions. DnaJB2 are important mediators of proteolysis which are involved in the regulation of protein degradation, exocytosis and endocytosis. The DnaJ proteins play a significant role in the HSP70 chaperone machine by interacting with HSP70 to stimulate ATP hydrolysis. DnaJB2 is expressed almost solely in the brain, with the highest levels in the frontal cortex and hippocampus.
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Synonyms
DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, Heat shock 40 kDa protein 3, Heat shock protein J1, HSJ-1, DNAJB2, HSJ1, HSPF3.
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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 MGSMASYYEI LDVPRSASAD DIKKAYRRKA LQWHPDKNPD NKEFAEKKFK EVAEAYEVLS DKHKREIYDR YGREGLTGTG TGPSRAEAGS GGPGFTFTFR SPEEVFREFF GSGDPFAELF DDLGPFSELQ NRGSRHSGPF FTFSSSFPGH SDFSSSSFSF SPGAGAFRSV STSTTFVQGR RITTRRIMEN GQERVEVEED GQLKSVTING VPDDLALGLE LSRREQQPSV TSRSGGTQVQ QTPASCPLDS DLSEDEDLQL AMAYSLSEME AAGKKPADVF.
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 :
BAT1 HumanDescription:
HLA-B Associated Transcript 1 Human Recombinant
HLA-B associated transcript 1, UAP56, D6S81E, DDX39B, ATP-dependent RNA helicase p47, DEAD-box protein UAP56
Product # :
ENZ-563Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BAT1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 448 amino acids (1-428) and having a molecular mass of 51.1kDa. BAT1 is fused to 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BAT1 protein (0.5mg/ml) solution contains 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl,1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
BAT1 belongs to the DEAD box family of RNA-dependent ATPases that mediate ATP hydrolysis during pre-mRNA splicing. UAP56 protein is a vital splicing factor which is needed for connecting U2 small nuclear ribonucleoprotein with pre-mRNA, as well as takes a key part in mRNA export from the nucleus to the cytoplasm. Mutations in this protein may be connected to rheumatoid arthritis.
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Synonyms
HLA-B associated transcript 1, UAP56, D6S81E, DDX39B, ATP-dependent RNA helicase p47, DEAD-box protein UAP56
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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 MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV LATLQQLEPV TGQVSVLVMC HTRELAFQIS KEYERFSKYM PNVKVAVFFG GLSIKKDEEV LKKNCPHIVV GTPGRILALA RNKSLNLKHI KHFILDECDK MLEQLDMRRD VQEIFRMTPH EKQVMMFSAT LSKEIRPVCR KFMQDPMEIF VDDETKLTLH GLQQYYVKLK DNEKNRKLFD LLDVLEFNQV VIFVKSVQRC IALAQLLVEQ NFPAIAIHRG MPQEERLSRY QQFKDFQRRI LVATNLFGRG MDIERVNIAF NYDMPEDSDT YLHRVARAGR FGTKGLAITF VSDENDAKIL NDVQDRFEVN ISELPDEIDI SSYIEQTR
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 :
FABP12 HumanDescription:
Fatty Acid Binding Protein-12 Human Recombinant
Fatty acid-binding protein 12, FABP12.
Product # :
PRO-738Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FABP12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-140 a.a) and having a molecular mass of 18kDa.FABP12 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FABP12 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
FABP12 is a member of the calycin superfamily and fatty-acid binding protein (FABP) family. The FABPs are a family of carrier proteins for fatty acids and other lipophilic substances for example eicosanoids and retinoids. These proteins are believed to enable the transfer of fatty acids between extra- and intracellular membranes. FABP12 has a role in lipid transport. FABP12 is expressed in several retinoblastoma cell lines. FABP12 has not been detected in fetal tissues.
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Synonyms
Fatty acid-binding protein 12, FABP12.
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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 MGSHMIDQLQ GTWKSISCEN SEDYMKELGI GRASRKLGRL AKPTVTISTD GDVITIKTKS IFKNNEISFK LGEEFEEITP GGHKTKSKVT LDKESLIQVQ DWDGKETTIT RKLVDGKMVV ESTVNSVICT RTYEKVSSNS VSNS.
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.