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1000 results found for “ephrin”
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Name :
LIF Human, Sf9Description:
Leukemia Inhibitory Factor Human Recombinant, Sf9
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
Product # :
CYT-1003Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LIF Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 189 amino acids (23-202a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). LIF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LIF 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.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 0.5 ng/ml.
More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
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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
ADPSPLPITP VNATCAIRHP CHNNLMNQIR SQLAQLNGSA NALFILYYTA QGEPFPNNLD KLCGPNVTDF PPFHANGTEK AKLVELYRIV VYLGTSLGNI TRDQKILNPS ALSLHSKLNA TADILRGLLS NVLCRLCSKY HVGHVDVTYG PDTSGKDVFQ KKKLGCQLLG KYKQIIAVLA
QAFHHHHHH.
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 :
CCL13 Human, HisDescription:
Monocyte Chemotactic Protein-4 Human Recombinant (CCL13), His-Tag
CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.
Product # :
CHM-275Price :
Quantity :
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Shipped with Ice Packs
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Description
MCP4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 96 amino acids (24-98) and having a molecular mass of 10.8 kDa. The MCP-4 is fused to 21 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The His Tag 0.25mg/ml MCP4 protein solution contains PBS pH-7.4, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CCL13 chemokine is part of the CC chemokine family (TARC). CCL13 protein induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. CCL13 is induced by the inflammatory cytokines IL1 & TNFA.
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Synonyms
CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.
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Physical Appearance
Sterile Filtered colorless clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
.AHTLKT -
Background
What is the molecular weight/Mw of CCL13 HUMAN, HIS Protein?
CCL13 HUMAN, HIS Protein has a total Mw of 10.8kDa.
What is the source or expression system of CCL13 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL13 HUMAN, HIS Protein?
CCL13 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL13 HUMAN, HIS Protein?
The biological functionality of CCL13 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL13 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
.AHTLKT
What applications can CCL13 HUMAN, HIS Protein be used in?
CCL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL13 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL13 HUMAN, HIS 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 HumanDescription:
Vimentin Human Recombinant
Vimentin, Vim, FLJ36605.
Product # :
PRO-309Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vimentin Human Recombinant produced in E.coli cells is a single non-glycosylated protein containing 465 amino acids chain and having a molecular mass of 53.5kDa. The Vimentin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Vimentin was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
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 Vimentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vimentin 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 Vimentin in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
STRSVSSSSY RRMFGGPGTA SRPSSSRSYV TTSTRTYSLG SALRPSTSRS LYASSPGGVY ATRSSAVRLR SSVPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED IMRLREKLQE EMLQREEAEN TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHEEE IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA ANRNNDALRQ AKQESTEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF AVEAANYQDT IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL NLRETNLDSL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE.
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 :
IL1A Human, HEKDescription:
Interleukin-1 alpha Human Recombinant, HEK
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-964Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-1 alpha Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight of 18kDa due to glycosylation.The IL1A is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The IL-1A protein was lyophilized from a 0.2µm filtered solution of PBS pH 7.4 with 10% trehalose as protectant.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Assay # 1: The biological activity was measured by its binding ability in a functional ELISA, the ED50 is typically 0.5-5 µg/ml. Assay # 2: The biological activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells, the ED50 is typically less than 1pg/ml, corresponding to a specific activity of >1x109 unit/mg.More Info
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Introduction
IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
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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 IL-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 IL1A in deionized water to a stock solution of 0.5mg/ml.
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Background
What is the molecular weight/Mw of IL1A HUMAN, HEK Protein?
IL1A HUMAN, HEK Protein has a total Mw of 18kDa.
What is the source or expression system of IL1A HUMAN, HEK Protein?
HEK.
What is the Purity of IL1A HUMAN, HEK Protein?
IL1A HUMAN, HEK Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IL1A HUMAN, HEK Protein?
Assay # 1: The biological activity was measured by its binding ability in a functional ELISA, the ED50 is typically 0.5-5 µg/ml. Assay # 2: The biological activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells, the ED50 is typically less than 1pg/ml, corresponding to a specific activity of >1x109 unit/mg.
What applications can IL1A HUMAN, HEK Protein be used in?
IL1A HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL1A HUMAN, HEK Protein?
The endotoxin level is minimal, IL1A HUMAN, HEK 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 :
Protein-L, HisDescription:
Protein L Recombinant, His Tag
Product # :
PRO-1930Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 372 amino acids in total and having a molecular mass of 41.5kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHHHHHHKEE TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AG.
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 :
MEK1 HumanDescription:
Mitogen Activated Kinase Kinase 1 Human Recombinant
Product # :
PKA-256Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAP2K1 active Human Recombinant produced in Sf9 cells is a glycosylated, polypeptide chain containing amino acids 2-393 having a molecular mass of 47 kDa. MAP2K1 is fused to a polyhistidine tag and is purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
MEK1 is supplied at a concentration of in 40mM Tris, pH-8, 0.15M NaCl, 0.27M sucrose, 1mM DTT, 0.2mM PMSF, 1mM benzamidine, 0.1mM sodium vanadate and 0.03% Brij-35.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
~125-175 units/mg. One unit of MEK1 activity transfers 1 nmol of phosphate to ERK1/2 peptide per minute at 30°C in a reaction containing 100µM ATP.
Recombinant active MEK1 also phosphorylates ERK1, ERK2, and GSK-3?. Kinase activity may vary depending on the substrate and reaction conditions.
The optimal concentration should be determined for each specific application.More Info
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Introduction
MAP2K1 is a member of the dual specificity protein kinase family, which plays a role as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, are recognized as extracellular signal-regulated kinases (ERKs), that act as an integration position for multiple biochemical signals. MEK1 is located upstream of MAP kinases and stimulates the enzymatic activity of MAP kinases upon wide variety of extra- and intracellular signals. As a key player of MAP kinase signal transduction pathway, MEK1 is involved in many cellular processes such as proliferation, differentiation, transcription regulation and development. MAP2K1 catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a thr-glu-tyr sequence located in map kinases. MEK1 activates erk1 and erk2 map kinases.
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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 1-2 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 :
GHRP6Description:
Growth Hormone Releasing Peptide-6
GHRP-6, GHRP6
Product # :
HOR-298Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Growth Hormone Releasing Peptide-6 Synthetic is a single, non-glycosylated polypeptide chain containing 6 amino acids, having a molecular mass of 873 Dalton and a Molecular formula of C46H56N12O6.
Formulation
The GHRP-6 peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by analysis by RP-HPLC.
More Info
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Introduction
GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH act directly on pituitary somatotrophs to stimulate GH release. Growth hormone (GH) release is stimulated by a variety of synthetic secretagogues, of which growth hormone-releasing hexapeptide (GHRP-6) has been most thoroughly studied; it is thought to have actions at both pituitary and hypothalamic site.
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Synonyms
GHRP-6, GHRP6
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth Hormone Releasing Peptide-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP-6 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 GHRP-6 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
His-D-Trp-Ala-Trp-D-Phe-Lys-NH2.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Activin-A MouseDescription:
Activin-A Mouse Recombinant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-146Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Active form Activin-A Murine Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Mouse Activin-A lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Murine INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.What is the source or expression system of Activin A Protein?
Ecoli
What is the Purity of Activin A Protein?
Activin A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000 units/mg.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Cyclophilin A RatDescription:
Cyclophilin-A Rat Recombinant
Peptidyl-prolyl cis-trans isomerase A, EC:5.2.1.8, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, p1B15, p31, Ppia.
Product # :
ENZ-938Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cyclophilin-A Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val2-Leu164) containing 173 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 19kDa.
Source
Escherichia Coli.
Formulation
Cyclophilin-A was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5%(w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, EC:5.2.1.8, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, p1B15, p31, Ppia.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Cyclophilin-A 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
MKHHHHHHASVNPTVFFDIT ADGEPLGRVC FELFADKVPK TAENFRALST GEKGFGYKGS SFHRIIPGFM CQGGDFTRHN GTGGKSIYGE KFEDENFILK HTGPGILSMA NAGPNTNGSQ FFICTAKTEW LDGKHVVFGK VKEGMSIVEA MERFGSRNGK TSKKITISDC GQL.
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 :
HIF1A Human, HisDescription:
Hypoxia-Inducible Factor-1 Alpha Human Recombinant, His Tag
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
Product # :
PRO-415Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (576-785 a.a.) and having a molecular mass of 25.1 kDa. The HIF1A is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HIF1A Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.
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Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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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 MSFDQLSPLE SSSASPESAS PQSTVTVFQQ TQIQEPTANA TTTTATTDEL KTVTKDRMED IKILIASPSP THIHKETTSA TSSPYRDTQS RTASPNRAGK GVIEQTEKSH PRSPNVLSVA LSQRTTVPEE ELNPKILALQ NAQRKRKMEH DGSLFQAVGI GTLLQQPDDH AATTSLSWKR VKGCKSSEQN GMEQKTIILI PSDLACRLLG Q.
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 :
DBNDD2 HumanDescription:
Dysbindin (Dystrobrevin Binding Protein 1) Domain Containing 2 Human Recombinant
Dysbindin domain-containing protein 2, Casein kinase-1 binding protein, CK1BP, HSMNP1, DBNDD2, C20orf35.
Product # :
PRO-1167Price :
Quantity :
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Shipped with Ice Packs
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Description
DBNDD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (1-161 a.a) and having a molecular mass of 20.1kDa (Molecular weight on SDS-PAGE will appear higher).DBNDD2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DBNDD2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Dysbindin domain-containing protein 2 (DBNDD2) is a member of the dysbindin family. DBNDD2 regulates the activity of casein kinase-1 and inhibits CSNK1D autophosphorylation (in vitro). DBNDD2 also interacts with CSNK1D and CSNK1E. DBNDD2 is detected in brain.
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Synonyms
Dysbindin domain-containing protein 2, Casein kinase-1 binding protein, CK1BP, HSMNP1, DBNDD2, C20orf35.
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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 MGSHMDPNPR AALERQQLRL RERQKFFEDI LQPETEFVFP LSHLHLESQR PPIGSISSME VNVDTLEQVE LIDLGDPDAA DVFLPCEDPP PTPQSSGMDN HLEELSLPVP TSDRTTSRTS SSSSSDSSTN LHSPNPSDDG ADTPLAQSDE EEERGDGGAE PGACS.
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 :
Apo D HumanDescription:
Apolipoprotein-D Human Recombinant
Apolipoprotein D, Apo-D, ApoD.
Product # :
CYT-547Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Apolipoprotein-D Human Recombinant His Tag fusion protein at C-terminus (7 highlighted a.a.) produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 174 amino acids and having a molecular mass of 19.82kDa. The protein a.a sequence corresponds to the UniProtKB/Swiss-Prot entry P05090.The Following gene modifications were made:Trp99His, Cys116Ser, Ile118Ser, Leu120Ser amino acids exchanges were introduced at the surface of Apolipoprotein-D to enhance the protein’s solubility and another three Leu23Pro, Pro133Val, Asn134Ala amino acids exchanges which facilitate its genetic manipulation. The Apolipoprotein-D is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 1mg/ml in 4mM KH2PO4, 16mM Na2HPO4 and 115mM NaCl pH 7.5.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Apolipoprotein-D is mainly associated with high density lipoproteins in human plasma. Apolipoprotein-D is an atypical apolipoprotein and, based on its primary structure, Apolipoprotein-D is a member of the lipocalin family. Lipocalins adopt a beta-barrel tertiary structure and transport small hydrophobic ligands. Apolipoprotein-D binds cholesterol, progesterone, pregnenolone, bilirubin and arachidonic acid.
Apolipoprotein-D is expressed in numerous tissues having high levels of expression in spleen, testes and brain. Apolipoprotein-D is present at high concentrations in the cyst fluid of women with gross cystic disease of the breast, a condition associated with increased risk of breast cancer. Apolipoprotein-D accumulates in regenerating peripheral nerves and in the cerebrospinal fluid of patients with neurodegenerative conditions, such as Alzheimer's disease. Apolipoprotein-D participates in maintenance and repair within the central and peripheral nervous systems. Apolipoprotein-D is a multi-ligand, multi-functional transporter and transports a ligand from 1 cell to another within an organ, scavenge a ligand within an organ for transport to the blood or could transport a ligand from the circulation to specific cells within a tissue. -
Synonyms
Apolipoprotein D, Apo-D, ApoD.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized H2O to a working volume of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter this product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
FHLGKCPNPP VQENFDVNKY PGRWYEIEKI PTTFENGRCI QANYSLMENG KIKVLNQELR ADGTVNQIEG EATPVNLTEP AKLEVKFSWF MPSAPYHILA TDYENYALVY SCTSISQSFH VDFAWILARN VALPPETVDS LKNILTSNNI DVKKMTVTDQ VNCPKLSAHHHHHH.
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Background
Apolipoprotein-D Human Recombinant: Illuminating the Role of a Multifaceted Lipid-Binding Protein
Abstract:
Apolipoprotein-D (ApoD), a multifunctional lipid-binding protein, has emerged as a fascinating player in lipid metabolism and neuroprotection. This research paper aims to provide an insightful overview of ApoD human recombinant, exploring its physiological functions, production methods, and potential therapeutic applications. By unraveling the complexities of ApoD, we gain valuable insights into its role in lipid homeostasis and its potential as a therapeutic target for neurodegenerative diseases. This article presents a concise yet comprehensive analysis of ApoD, humanizing its significance in the context of human health.Introduction:
Understanding the intricate mechanisms underlying lipid metabolism and neuroprotection is crucial for the development of novel therapeutic strategies. ApoD, a versatile protein expressed in various tissues, offers unique insights into these areas. This paper delves into the multifaceted nature of ApoD, shedding light on its significance in lipid homeostasis and neuronal health.Structure and Function of Apolipoprotein-D:
ApoD exhibits a complex molecular structure, comprising distinct domains that facilitate its binding to lipids and other biomolecules. It engages in diverse functions, including lipid transport, antioxidant defense, and modulation of neuroinflammatory responses. The versatility of ApoD underscores its pivotal role in maintaining cellular and tissue integrity.Regulation of Apolipoprotein-D Expression:
The expression of ApoD is subject to intricate regulatory mechanisms influenced by hormonal and environmental cues. Understanding the factors governing ApoD expression provides valuable insights into its physiological roles and potential therapeutic applications.Apolipoprotein-D and Neurodegenerative Diseases:
Growing evidence implicates ApoD in neuroprotection, particularly in the context of neurodegenerative diseases. ApoD exhibits neuroprotective properties by modulating oxidative stress, lipid peroxidation, and inflammatory responses, making it an intriguing target for therapeutic interventions.Production of Apolipoprotein-D Human Recombinant:
Advanced biotechnological approaches, including recombinant DNA technology and protein expression systems, enable the production of ApoD human recombinant. These methods facilitate large-scale production, purification, and characterization of ApoD, paving the way for potential therapeutic applications.Therapeutic Potential of Apolipoprotein-D Human Recombinant:
Targeting ApoD holds promise for the development of therapeutics aimed at neurodegenerative diseases. Modulating ApoD expression or function may provide neuroprotection, enhance neuronal survival, and mitigate the progression of neurodegenerative disorders.Conclusion:
Apolipoprotein-D human recombinant represents a captivating area of research, bridging the fields of lipid metabolism and neurodegeneration. Understanding the intricate interplay between ApoD, lipid homeostasis, and neuroprotection is crucial for unraveling its full therapeutic potential. Continued investigation into the functions and mechanisms of ApoD will likely lead to novel therapeutic strategies for neurodegenerative diseases.What is the molecular weight/Mw of APO D Protein?
APO D Protein has a total Mw of 19.82kDa.
What is the source or expression system of APO D Protein?
Escherichia Coli.
What is the Purity of APO D Protein?
APO D Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of APO D Protein?
The biological functionality of APO D Protein will be determined in the future.
What is the amino acid sequence of APO D Protein?
FHLGKCPNPP VQENFDVNKY PGRWYEIEKI PTTFENGRCI QANYSLMENG KIKVLNQELR ADGTVNQIEG EATPVNLTEP AKLEVKFSWF MPSAPYHILA TDYENYALVY SCTSISQSFH VDFAWILARN VALPPETVDS LKNILTSNNI DVKKMTVTDQ VNCPKLSAHHHHHH.
What applications can APO D Protein be used in?
APO D Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APO D Protein?
The endotoxin level is minimal, APO D 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 :
NKIRAS2 HumanDescription:
NFKB Inhibitor Interacting Ras-Like 2 Human Recombinant
NF-kappa-B inhibitor-interacting Ras-like protein 2, I-kappa-B-interacting Ras-like protein 2, Kappa B-Ras protein 2, KappaB-Ras2, NKIRAS2, KBRAS2.
Product # :
PRO-1091Price :
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Shipped with Ice Packs
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Description
NKIRAS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids (1-191 a.a) and having a molecular mass of 24kDa.NKIRAS2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NKIRAS2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NFKB inhibitor interacting Ras-like 2 (NKIRAS2) is an inhibitor of the transcription factor NF-kappaB. NKIRAS2 is similar to the Ras-like small GTPases which associate with IkappaB. The Ras-like proteins- NKIRAS1 and NKIRAS2, interact with the PEST domains of I?B? and I?B? and reduce their rate of degradation. NKIRAS2 is an atypical Ras-like protein which functions as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more impervious to degradation.
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Synonyms
NF-kappa-B inhibitor-interacting Ras-like protein 2, I-kappa-B-interacting Ras-like protein 2, Kappa B-Ras protein 2, KappaB-Ras2, NKIRAS2, KBRAS2.
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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 MGSHMGKSCK VVVCGQASVG KTSILEQLLY GNHVVGSEMI ETQEDIYVGS IETDRGVREQ VRFYDTRGLR DGAELPRHCF SCTDGYVLVY STDSRESFQR VELLKKEIDK SKDKKEVTIV VLGNKCDLQE QRRVDPDVAQ HWAKSEKVKL WEVSVADRRS
LLEPFVYLAS KMTQPQSKSA FPLSRKNKGS GSLDG.
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 :
ECSIT HumanDescription:
ECSIT homolog Human Recombinant
ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.
Product # :
PRO-1241Price :
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Description
ECSIT Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (19-217) and having a molecular mass of 24.6 kDa.ECSIT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ECSIT solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ECSIT homolog (ECSIT) is a ubiquitously expressed protein which has a vital role as an adaptor protein in the cytosolic signal transduction cascade events triggered by Toll receptor activation. ECSIT promotes proteolytic activation of MAP3K1. ECSIT is also involved in the BMP signaling pathway. ECSIT is essential for normal embryonic development. ECSIT was originally classified as a cytoplasmic protein interacting specifically with TNF receptor associated factor (TRAF)-6 in the TLR pathway. ECSIT gene knockdown results in gravely impaired complex I assembly and disrupted mitochondrial function.
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Synonyms
ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.
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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 MGSGTCGAAL TGTSISQVPL PKDSTGAADP PQPHIVGIQS PDQQAALARH NPARPVFVEG PFSLWLRNKC VYYHILRADL LPPEEREVEE TPEEWNLYYP MQLDLEYVRS GWDNYEFDIN EVEEGPVFAM CMAGAHDQAT MAKWIQGLQE TNPTLAQIPV VFRLAGSTRE LQTSSAGLEE PPLPEDHQEE DDNLQRQQQG QS
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 :
IFNGR1 HumanDescription:
IFN Gamma Receptor 1 Human Recombinant
IFNGR1, CD119, IFNGR, IMD27A, IMD27B, CDw119.
Product # :
CYT-1074Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IFNGR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 234 amino acids (18-245a.a.) and having a molecular mass of 26.6kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).IFNGR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IFNGR1 protein solution (1mg/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
IFNGR1 is a part of the hematopoietic cytokine receptor superfamily. IFNGR1 forms a site that is recognized by the extracellular domain of IFNGR2 by inducing the rapid dimerization of chains. IFNGR1 Plays an important role in the IFN-gamma pathway that is essential for the cellular response to infectious agents. IFNGR1 is expressed in a membrane-bound form in various cells, and is over-expressed in tumor cells.
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Synonyms
IFNGR1, CD119, IFNGR, IMD27A, IMD27B, CDw119.
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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
EMGTADLGPS SVPTPTNVTI ESYNMNPIVY WEYQIMPQVP VFTVEVKNYG VKNSEWIDAC INISHHYCNI SDHVGDPSNS LWVRVKARVG QKESAYAKSE EFAVCRDGKI GPPKLDIRKE EKQIMIDIFH PSVFVNGDEQ EVDYDPETTC YIRVYNVYVR MNGSEIQYKI LTQKEDDCDE IQCQLAIPVS SLNSQYCVSA EGVLHVWGVT TEKSKEVCIT IFNSSIKGHH HHHH.
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Background
What is the molecular weight/Mw of IFNGR1 HUMAN Protein?
IFNGR1 HUMAN Protein has a total Mw of 16.8kDa.
What is the source or expression system of IFNGR1 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFNGR1 HUMAN Protein?
IFNGR1 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNGR1 HUMAN Protein?
The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is < 20.0 ng/ml, corresponding to a specific activity of > 5.0 × 104 IU/mg.
What is the amino acid sequence of IFNGR1 HUMAN Protein?
QDPYVKEAEN LKKYFNAGDP DVADNGTLFL DILRNWKEES DRKIMQSQIV SFYFKLFKNF KDDQRIQKSV ETIKEDINVK FFNSNKKKRD DFEKLTNYSV TDSNVQRKAV HELIQVMAEL SPAAKIGKRK RSQMFRGRRA SQ.
What applications can IFNGR1 HUMAN Protein be used in?
IFNGR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNGR1 HUMAN Protein?
The endotoxin level is minimal, IFNGR1 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 :
BCDIN3D HumanDescription:
BCDIN3D Human Recombinant
Pre-miRNA 5'-monophosphate methyltransferase, BCDIN3 domain-containing protein, BCDIN3D.
Product # :
PRO-1262Price :
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Shipped with Ice Packs
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Description
BCDIN3D Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292 a.a) and having a molecular mass of 35kDa.BCDIN3D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BCDIN3D protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 1mM DTT and 2mM EDTA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
BCDIN3D is a member of the methyltransferase superfamily and contains 1 Bin3-type SAM domain. BCDIN3D acts in the catalysis of the transfer of a methyl group to an acceptor molecule. BCDIN3D is an O-methyltransferase which specifically dimethylates the 5' monophosphate of pre-miRNAs, serving as a negative regulator of miRNA processing. BCDIN3D mediates the methylation of pre-miR-145, as well as other pre-miRNAs.
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Synonyms
Pre-miRNA 5'-monophosphate methyltransferase, BCDIN3 domain-containing protein, BCDIN3D.
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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 MGSMAVPTEL DGGSVKETAA EEESRVLAPG AAPFGNFPHY SRFHPPEQRL RLLPPELLRQ LFPESPENGP ILGLDVGCNS GDLSVALYKH FLSLPDGETC SDASREFRLL CCDIDPVLVK RAEKECPFPD ALTFITLDFM NQRTRKVLLS SFLSQFGRSV FDIGFCMSIT MWIHLNHGDH GLWEFLAHLS SLCHYLLVEP QPWKCYRAAA RRLRKLGLHD FDHFHSLAIR GDMPNQIVQI LTQDHGMELI CCFGNTSWDR SLLLFRAKQT IETHPIPESL IEKGKEKNRL SFQKQ.
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 :
NXPH1 Human, Sf9Description:
Neurexophilin 1 Human Recombinant, Sf9
NXPH1, Nbla00697, NPH1 , Neurexophilin-1, Neurexophilin 1.
Product # :
PRO-2418Price :
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Description
NXPH1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 259 amino acids (22-271) and having a molecular mass of 29.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).NXPH1 is fused to 9 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NXPH1 protein solution (0.5mg/ml) containing 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
Neurexophilin 1 (NXPH1) is a part of the neurexophilin family which encodes a secreted protein with a variable N terminal domain, an extremely conserved, N-glycosylated central domain, a short linker region, and a cysteine-rich Cterminal domain. NXPH1 shapes a very tight complex with alpha neurexins, a group of proteins which promote adhesion among dendrites and axons.
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Synonyms
NXPH1, Nbla00697, NPH1 , Neurexophilin-1, Neurexophilin 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
ADPANLTNGG KSELLKSGSS KSTLKHIWTE SSKDLSISRL LSQTFRGKEN DTDLDLRYDT PEPYSEQDLW DWLRNSTDLQ EPRPRAKRRP IVKTGKFKKM FGWGDFHSNI KTVKLNLLIT GKIVDHGNGT FSVYFRHNST GQGNVSVSLV PPTKIVEFDL AQQTVIDAKD SKSFNCRIEY EKVDKATKNT LCNYDPSKTC YQEQTQSHVS WLCSKPFKVI CIYISFYSTD YKLVQKVCPD YNYHSDTPYF PSGHHHHHH.
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 :
C10ORF54 HumanDescription:
Chromosome 10 Open Reading Frame 54 Human Recombinant
C10orf54, Chromosome 10 Open Reading Frame 54, V-Domain Ig Suppressor Of T Cell Activation, Stress-Induced Secreted Protein-1, Sisp-1, SISP1, Stress Induced Secreted Protein 1, Death Domain1alpha, DD1alpha, PP2135, B7-H5, VISTA, B7H5, GI24.
Product # :
PRO-2259Price :
Quantity :
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Description
C10ORF54 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (33-194 a.a) and having a molecular mass of 19.1kDa. (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). C10ORF54 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
C10ORF54 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 10 Open Reading Frame 54, also known as C10ORF54 is part of the immunoglobulin superfamily. Like a transmembrane molecule, C10ORF54 is expressed in the bone on embryonic stem cells (ESCs), and on tumor cell surface as well. Accordingly, C10ORF54 supports the differentiation of ESC and ehhances BMP4 induced signaling in ESC, however C10ORF54 is also down regulated following to BMP4 exposure.
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Synonyms
C10orf54, Chromosome 10 Open Reading Frame 54, V-Domain Ig Suppressor Of T Cell Activation, Stress-Induced Secreted Protein-1, Sisp-1, SISP1, Stress Induced Secreted Protein 1, Death Domain1alpha, DD1alpha, PP2135, B7-H5, VISTA, B7H5, GI24.
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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
FKVATPYSLY VCPEGQNVTL TCRLLGPVDK GHDVTFYKTW YRSSRGEVQT CSERRPIRNL TFQDLHLHHG GHQAANTSHD LAQRHGLESA SDHHGNFSIT MRNLTLLDSG LYCCLVVEIR HHHSEHRVHG AMELQVQTGK DAPSNCVVYP SSSQDSENIT AAVEHHHHHH.
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 :
C12ORF5 Human, HisDescription:
Chromosome 12 Open Reading Frame 5 Human Recombinant, His Tag
Probable fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.
Product # :
PRO-051Price :
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Description
C12ORF5 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids (1-270 a.a.) and having a molecular mass of 32.6kDa. The C12ORF5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C12ORF5 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TP53-induced glycolysis and apoptosis regulator (TIGAR or C12ORF5), is a 270 amino acid protein induced by the p53 tumor suppressor pathway that functions to protect against oxidative stress. C12ORF5 specifically functions to block glycolysis, leading the pathway to the pentose phosphate shunt and decreasing the intracellular concentration of reactive oxygen species. Therefore, it is thought that C12ORF5 may act to modulate the apoptotic response to p53, thus allowing cells to survive mild or transient stresses.
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Synonyms
Probable fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.
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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 MGSHMARFAL TVVRHGETRF NKEKIIQGQG VDEPLSETGF KQAAAAGIFL NNVKFTHAFS SDLMRTKQTM HGILERSKFC KDMTVKYDSR LRERKYGVVE GKALSELRAM AKAAREECPV FTPPGGETLD QVKMRGIDFF EFLCQLILKE ADQKEQFSQG SPSNCLETSL AEIFPLGKNH SSKVNSDSGI PGLAASVLVV SHGAYMRSLF DYFLTDLKCS LPATLSRSEL MSVTPNTGMS LFIINFEEGR EVKPTVQCIC MNLQDHLNGL TETR.
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 :
IL21R HumanDescription:
Interleukin-21 Receptor Human Recombinant
Interleukin 21 Receptor, Novel Interleukin Receptor, IL-21 Receptor, NILR, Interleukin-21 Receptor, CD360 Antigen, IL-21R, CD360.
Product # :
CYT-911Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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Description
IL21R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (20-232 a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 221 amino acids and having a molecular mass of 25.6kDa.IL21R shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL21R protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-21 receptor, also known as IL21R is a member of the type I cytokine receptors family. IL21R forms a heterodimeric receptor complex with the common gamma-chain, a receptor subunit which is also shared by the receptors for interleukin 2, 4, 7, 9, and 15. Furthermore, IL21 receptor transduces the growth promoting signal of IL21, and is significant for the proliferation as well as differentiation of T cells, B cells, and natural killer (NK) cells. The ligand binding of IL21 receptor leads to the activation of numerous downstream signaling molecules, including JAK1, JAK3, STAT1, as well as STAT3.
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Synonyms
Interleukin 21 Receptor, Novel Interleukin Receptor, IL-21 Receptor, NILR, Interleukin-21 Receptor, CD360 Antigen, IL-21R, CD360.
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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
CPDLVCYTDY LQTVICILEM WNLHPSTLTL TWQDQYEELK DEATSCSLHR SAHNATHATY TCHMDVFHFM ADDIFSVNIT DQSGNYSQEC GSFLLAESIK PAPPFNVTVT FSGQYNISWR SDYEDPAFYM LKGKLQYELQ YRNRGDPWAV SPRRKLISVD SRSVSLLPLE FRKDSSYELQ VRAGPMPGSS YQGTWSEWSD PVIFQTQSEE LKEVEHHHHH H
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 :
FGF19 Human, HEKDescription:
Fibroblast Growth Factor-19 Human Recombinant, HEK
fibroblast growth factor 19, FGF19.
Product # :
CYT-1180Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FGF19 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 23-216) containing 205 amino acids and having a molecular mass of 23.0 kDa.FGF19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
FGF19 protein (0.5mg/ml) contains 20mM Tris-HCl(pH8.0), 20% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Fibroblast Growth Factor-19 (FGF-19) is a member of the FGF family. FGF-19 interacts with FGFR1, FGFR2, FGFR3 and FGFR4. T FGF-19 takes part in the suppression of bile acid biosynthesis through downregulation of CYP7A1 expression, following positive regulation of the JNK and EPK1/2 cascades. FGF-19 stimulates glucose uptake in adiposytes and is a high affinity, heparin dependent ligand for FGFR4.
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Synonyms
fibroblast growth factor 19, FGF19.
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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
DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH
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Background
What is the molecular weight/Mw of FGF19 HUMAN,HEK Protein?
FGF19 HUMAN,HEK Protein has a total Mw of 23kDa.
What is the source or expression system of FGF19 HUMAN,HEK Protein?
HEK293 cells.
What is the Purity of FGF19 HUMAN,HEK Protein?
FGF19 HUMAN,HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF19 HUMAN,HEK Protein?
The biological functionality of FGF19 HUMAN,HEK Protein will be determined in the future.
What is the amino acid sequence of FGF19 HUMAN,HEK Protein?
DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH
What applications can FGF19 HUMAN,HEK Protein be used in?
FGF19 HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF19 HUMAN,HEK Protein?
The endotoxin level is minimal, FGF19 HUMAN,HEK 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 :
THBD HumanDescription:
Thrombomodulin Human Recombinant
THBD, Thrombomodulin, TM, Fetomodulin, CD141, CD141 antigen, THRM, BDCA-3, BDCA3, blood dendritic cell antigen 3, AHUS6, THPH12.
Product # :
PRO-2697Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
THBD Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 500 amino acids (22-515a.a) and having a molecular mass of 52.6kDa.THBD is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
THBD protein solution (0.5mg/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
Thrombomodulin, also referred to THBD, is an endothelial cell-expressed, transmembrane glycoprotein that can form a complex with the coagulation factor, thrombin. This complex increasethe activation of protein C in the anticoagulant pathway by forming a 1:1 stoichiometric complex with thrombin. Thrombomodulinbound thrombin has procoagulant effect at the same time by inhibiting fibrinolysis by cleaving thrombinactivatable fibrinolysis inhibitor (TAFI) into its active form. Reduced levels of thrombomodulin or increased serum levels of THBD can correlate with pathogenesis of certain cardiovascular diseases, such as atherosclerosis and thrombosis. Furthermore, it associated with, diabetes mellitus, liver cirrhosis, cerebral & myocardial infarction, and multiple sclerosis.
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Synonyms
THBD, Thrombomodulin, TM, Fetomodulin, CD141, CD141 antigen, THRM, BDCA-3, BDCA3, blood dendritic cell antigen 3, AHUS6, THPH12.
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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
EPQPGGSQCV EHDCFALYPG PATFLNASQI CDGLRGHLMT VRSSVAADVI SLLLNGDGGV GRRRLWIGLQ LPPGCGDPKR LGPLRGFQWV TGDNNTSYSR WARLDLNGAP LCGPLCVAVS AAEATVPSEP IWEEQQCEVK ADGFLCEFHF PATCRPLAVE PGAAAAAVSI TYGTPFAARG ADFQALPVGS SAAVAPLGLQ LMCTAPPGAV QGHWAREAPG AWDCSVENGG CEHACNAIPG
APRCQCPAGA ALQADGRSCT ASATQSCNDL CEHFCVPNPD QPGSYSCMCE TGYRLAADQH RCEDVDDCIL EPSPCPQRCV NTQGGFECHC YPNYDLVDGE CVEPVDPCFR ANCEYQCQPL NQTSYLCVCA EGFAPIPHEP HRCQMFCNQT ACPADCDPNT QASCECPEGY ILDDGFICTD IDECENGGFC SGVCHNLPGT FECICGPDSA LARHIGTDCD SGKVDGGDSG SGEPPPSPTP
GSTLTPPAVG LVHSHHHHHH
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 :
PIGR HumanDescription:
Polymeric Immunoglobulin Receptor Human Recombinant
Polymeric immunoglobulin receptor, PIGR, PIgR, Poly-Ig receptor, Hepatocellular carcinoma-associated protein TB6, polymeric immunoglobulin receptor precursor.
Product # :
PRO-2671Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PIGR Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 629 amino acids (19-638 aa) and having a molecular mass of 68.9 kDa.PIGR is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PIGR protein solution (1mg/ml) containing Phosphate-Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human IgM. The ED50 range ≤10 ug/ml.
More Info
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Introduction
Polymeric immunoglobulin receptor (PIGR) is responsible for transcytosis of soluble dimeric IgAs and immune. PIGR binds polymeric IgA and IgM at the basolateral surface of epithelial cells, then the complex is transported across the cell to be secreted at the apical surface.cytokines, hormones, and pathogenic stimuliregulate PIGR expression. The expression of PIGR is critically regulated by the pro-inflammatory cytokines, such as IL-1, IL-4, TNF-α, and IFN-γ.
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Synonyms
Polymeric immunoglobulin receptor, PIGR, PIgR, Poly-Ig receptor, Hepatocellular carcinoma-associated protein TB6, polymeric immunoglobulin receptor precursor.
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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
ADLKSPIFGP EEVNSVEGNS VSITCYYPPT SVNRHTRKYW CRQGARGGCI TLISSEGYVS SKYAGRANLT NFPENGTFVV NIAQLSQDDS GRYKCGLGIN SRGLSFDVSL EVSQGPGLLN DTKVYTVDLG RTVTINCPFK TENAQKRKSL YKQIGLYPVL VIDSSGYVNP NYTGRIRLDI QGTGQLLFSV VINQLRLSDA GQYLCQAGDD SNSNKKNADL QVLKPEPELV YEDLRGSVTF
HCALGPEVAN VAKFLCRQSS GENCDVVVNT LGKRAPAFEG RILLNPQDKD GSFSVVITGL RKEDAGRYLC GAHSDGQLQE GSPIQAWQLF VNEESTIPRS PTVVKGVAGG SVAVLCPYNR KESKSIKYWC LWEGAQNGRC PLLVDSEGWV KAQYEGRLSL LEEPGNGTFT VILNQLTSRD AGFYWCLTNG DTLWRTTVEI KIIEGEPNLK VPGNVTAVLG ETLKVPCHFP CKFSSYEKYW
CKWNNTGCQA LPSQDEGPSK AFVNCDENSR LVSLTLNLVT RADEGWYWCG VKQGHFYGET AAVYVAVEER KAAGSRDVSL AKADAAPDEK VLDSGFREIE NKAIQDPRLF AEEKAVADTR DQADGSRASV DSGSSEEQGG SSRHHHHHH
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 :
TPO Human, HEKDescription:
Thrombopoietin Human Recombinant, HEK
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.
Product # :
CYT-115Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thrombopoietin Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 80-85kDa due to glycosylation.The TPO is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The TPO protein was filtered (0.2µm) and lyophilized from 0.74mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The activity was determined by the dose-dependent stimulation of the proliferation of MO7e cells, the ED50 is 1.15ng/ml.
More Info
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Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney that regulates the production of platelets by the bone marrow. It stimulates the production and differentiation of megakaryocytes, the bone marrow cells that fragment into large numbers of platelets.
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Synonyms
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thrombopoietin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TPO 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 Thrombopoietin in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
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Amino Acid Sequence
SPAPPACDLRVLSKLLRDSHVLHSRLSQCPEVHPLPTPVLLPAVDFSLG EWKTQMEETKAQDILGAVTLLLEGVMAARGQLGPTCLSSLLGQLSGQV RLLLGALQSLLGTQLPPQGRTTAHKDPNAIFLSFQHLLRGKVRFLMLVGG STLCVRRAPPTTAVPSRTSLVLTLNELPNRTSGLLETNFTASARTTGSGLLK WQQGFRAKIPGLLNQTSRSLDQIPGYLNRIHELLNGTRGLFPGPSRRTLGAP DISSGTSDTGSLPPNLQPGYSPSPTHPPTGQYTLFPLPPTLPTPVVQLHPLLPDPSAPTPT
PTSPLLNTSYTHSQNLSQEG
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.