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1000 results found for “Macrophage Migration Inhibitory Factor”
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Name :
GDF5 Human, HisDescription:
Growth differentiation factor 5 Human Recombinant, His Tag
Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.
Product # :
CYT-653Price :
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Shipped with Ice Packs
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Description
GDF5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (382-501 a.a.) and having a total molecular mass of 15.8 kDa. GDF5 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDF5 solution contains 10mM sodium citrate pH-3.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
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Synonyms
Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.
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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 MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.
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Background
What is the molecular weight/Mw of GDF5 HUMAN, HIS Protein?
GDF5 HUMAN, HIS Protein has a total Mw of 15.8kDa.
What is the source or expression system of GDF5 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF5 HUMAN, HIS Protein?
GDF5 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF5 HUMAN, HIS Protein?
The biological functionality of GDF5 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GDF5 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.
What applications can GDF5 HUMAN, HIS Protein be used in?
GDF5 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF5 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF5 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 :
TNFR2 Human, HisDescription:
Tumor Necrosis Factor Receptor Type 2 Human Recombinant, His Tag
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
Product # :
CYT-674Price :
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Description
TNFR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 184 amino acids fragment (23-206) having a molecular weight of 24.45kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TNFR2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFR2 protein is supplied in 20mM Tris HCl pH-8, 5mM EDTA and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury. -
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
LPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWV
PECLSCGSRCSSDQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSD
VVCKPCAPGTFSNTTSSTDICRPHQICNVVAIPGNASMDAVCTSTSPT.
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 :
SCF HumanDescription:
Stem Cell Factor Human Recombinant
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Product # :
CYT-255Price :
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Shipped at Room temp
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Description
Stem Cell Factor Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18409 Dalton. The SCF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
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Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 Stem Cell Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Gly-Ile-Cys.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.52 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Stem Cell Factor 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 :
TPO Mouse, HEKDescription:
Thrombopoietin Mouse Recombinant, HEK
Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 1.
Product # :
CYT-1157Price :
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Description
TPO Mouse Recombinant produced in HEK293 cells is a single, non-glycosylated polypeptide chain containing 341 amino acids ( 22-356 a.a) and having a molecular mass of 36.4kDa. TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293.
Formulation
TPO protein (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 range ≤4ng/ml.
Biological Activity
Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.
More Info
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Introduction
Thrombopoietin or TPO or MGDF, is a protein (glycoprotein hormone) that can be found in the liver and kidney tissues. TPO regulates the creation of platelets. The protein enhances the production & differentiation of cells such as megakaryocytes that are part of the bone marrow cells that secretes a wide number of platelets. The cellular development process that ends up in the production of platelet calls (Megakaryocytopoiesis). Humoral growth factor is needed for the megakaryocyte proliferation & maturation of megakaryocyte, not apart from thrombopoiesis.
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Synonyms
Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 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
SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKFPNRTSG LLETNFSVTA RTAGPGLLSR LQGFRVKITP GQLNQTSRSP VQISGYLNRT HGPVNGTHGL FAGTSLQTLE ASDISPGAFN KGSLAFNLQG GLPPSPSLAP DGHTPFPPSP ALPTTHGSPP QLHPLFPDPS TTMPNSTAPH PVTMYPHPRN LSQETHHHHH 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 :
SCF MouseDescription:
Stem Cell Factor Mouse Recombinant
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.
Product # :
CYT-275Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stem Cell Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18309 Dalton. The SCF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cell line is < 10 ng/ml, corresponding to a Specific Activity of 1x105 IU/mg.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid). -
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 Stem Cell Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MKEICGNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV IQLSLSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVLC MEENAPKNIK ESPKRPETRS FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.52 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Stem Cell Factor 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 :
CXCL8 Human, PichiaDescription:
Interleukin-8 (1-77 a.a.) Human Recombinant, (CXCL8) Pichia
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-349Price :
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Shipped at Room temp
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Description
Interleukin-8 Human Recombinant produced in Yeast is a single, glycosylated polypeptide chain containing 79 amino acids and having a molecular mass of 9 kDa. The IL-8 is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium phosphate buffer pH-8.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
Chemotactic activity was reached at 25ng/ml on human neutrophils.
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.
When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor. -
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN, PICHIA Protein?
CXCL8 HUMAN, PICHIA Protein has a total Mw of 9kDa.
What is the source or expression system of CXCL8 HUMAN, PICHIA Protein?
Pichia Pastoris.
What is the Purity of CXCL8 HUMAN, PICHIA Protein?
CXCL8 HUMAN, PICHIA Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, PICHIA Protein?
Chemotactic activity was reached at 25ng/ml on human neutrophils.
What is the amino acid sequence of CXCL8 HUMAN, PICHIA Protein?
CXCL8 HUMAN, PICHIA Protein is composed from 79 amino acids.
What applications can CXCL8 HUMAN, PICHIA Protein be used in?
CXCL8 HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, PICHIA Protein?
The endotoxin level is minimal, CXCL8 HUMAN, PICHIA 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 :
SHH HumanDescription:
Sonic HedgeHog Human Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Product # :
CYT-676Price :
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Shipped at Room temp
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Description
Sonic HedgeHog Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 20.2kDa. The Cys at position 2 has been substituted with 2 Ile’s.
Source
Escherichia Coli.
Formulation
SHH is lyophilized from 10mM Na3PO4, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 is measured by the dose-dependent induction of alkaline phosphatase production by CCL-226 fibroblasts and is 1.47μg/ml corresponding to a specific activity of 680U/mg.
More Info
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Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
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Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SHH 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
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRALDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGGCFP
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 :
VEGFC Human HEKDescription:
Vascular Endothelial Growth Factor C Human Recombinant HEK
VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein, VEGFC.
Product # :
CYT-784Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
VEGFC Human Recombinant produced by transfected human cells is a single polypeptide chain containing 204 amino acids (32-227). VEGFC is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
VEGFC was lyophilized from a 0.2 µM filtered solution of 20mM Tris-HCl and 150mM NaCl, pH 7.2.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. Human VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant human VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT-4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant human VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.
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Synonyms
VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein, VEGFC.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized VEGFC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGFC should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized VEGFC in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
FESGLDLSDAEPDAGEATAYASKDLEEQLRSVSSVDELMTVLYPEYWKMYK
CQLRKGGWQHNREQANLNSRTEETIKFAAAHYNTEILKSIDNEWRKTQCMP
REVCIDVGKEFGVATNTFFKPPCVSVYRCGGCCNSEGQCMNTSTSYLSKTLF
EITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRVDHHHHHH.
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 :
PRLR Human, AntagonistDescription:
Prolactin Receptor Antagonist Human Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-1254Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.
Purity
Greater than 97.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.
Biological Activity
fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).
More Info
-
Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized PRLR in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr
-
Background
Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TGFB1 Human, HisDescription:
Transforming Growth Factor-Beta 1 Human Recombinant, His Tag
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.
Product # :
CYT-672Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (279-390) having a molecular weight of 17.3kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TGF-b 1 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TGF-b 1 His-Tag protein is supplied in 25mM NaAcetate pH 4.8 and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
TGF-b 1 regulates the actions of numerous other growth factors involved in a variety of human diseases including renal disease, hepatic disease, heart failure and cardiomyopathies. -
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Myostatin AntibodyDescription:
Myostatin Polyclonal Rabbit Anti Human Antibody
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Product # :
ANT-041Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- formulation
- purity
- More Info
Formulation
Lyophilized from 1mg/ml solution in 0.2µm sterile filtered solution in phosphate buffered saline.
Purity
Greater than 98.0% as determined by Analysis by SDS-PAGE.
More Info
-
Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
-
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
-
Stability
Store at 4°C. For long term storage freezes in working aliquots at -20°C. Repeated freezing and thawing is not recommended.
-
Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
-
Immunogen
r.Human Myostatin
-
Ig Subclass
Rabbit IgG
-
Applications
To detect Human Myostatin by WB analysis this IgG can be used in a dilution of 1/500.
To optimal usage we suggest overnight incubation. -
Antigen Amino Acid Sequence
HHHHHHDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA PKRYKANYCS GECEFVFLQKYPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII YGKIPAMVVD RCGCS
-
Type
Polyclonal Rabbit Antibody.
-
Purification Method
Purified IgG prepared by affinity chromatography on protein G.
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 :
FLT4 Fc HumanDescription:
Vascular Endothelial Growth Factor Receptor-3 Fc Chimera Human Recombinant
Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3.
Product # :
PKA-245Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Soluble FLT4 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a monomeric, glycosylated, polypeptide containing 774 amino acids and having a molecular mass of 260 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.The FLT4 Fc Chimera is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
FLT4 Fc Chimera was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.
Purity
Greater than 90.0% as determined by(a)Analysis by RP-HPLC.
(b)Analysis by SDS-PAGE.Biological Activity
Measured by its ability to bind recombinant rat VEGF-C in a functional solid phase binding assay. Immobilised recombinant human VEGFR-3/FLT-4 at 5 µg/ml can bind recombinant rat VEGF-C in a linear range of 8-500 ng/ml.More Info
-
Introduction
All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.
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Synonyms
Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FLT4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized FLT4 Fc Chimera in sterile water not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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 :
TNFRSF4 MouseDescription:
TNF Receptor Superfamily Member 4 Mouse Recombinant
Tumor necrosis factor receptor superfamily member 4, OX40 antigen, OX40L receptor, Txgp1, Tnfrsf4, tax-transcriptionally activated glycoprotein 1 receptor, TXGP1L, ACT35, Txgp, Ly-70, ACT3, OX4, CD134.
Product # :
CYT-1179Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TNFRSF4 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-211) containing 435 amino acids and having a molecular mass of 48.6kDa.TNFRSF4 is fused to a 243 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
TNFRSF4 protein (0.25mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range is ≤ 0.4 ug/ml which measured by its binding ability in a functional ELISA with Mouse OX40 Ligand/TNFSF4.
More Info
-
Introduction
TNFRSF4, also known as TNF Receptor Superfamily Member 4, is a T cell co-stimulatory molecule which belongs to the TNF receptor superfamily. TNFRSF4 coordinates with other co-stimulatory substances such as CD28, CD40, CD30, CD27 and 4-1BB to control the activation of the immune response. TNFRSF4 takes a vital part in antigen-specific T cell expansion as well as survival. TNFRSF4 is up-regulated on CD4+ and CD8+ T cells upon engagement of the TCR by antigen presenting cells along with co-stimulation by CD40-CD40 Ligand and CD28-B7. In addition, TNFRSF4 regulates cytokine production from T cells, antigen presenting cells, natural killer cells and natural killer cells. TNFRSF4 regulates cytokine receptor signaling.
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Synonyms
Tumor necrosis factor receptor superfamily member 4, OX40 antigen, OX40L receptor, Txgp1, Tnfrsf4, tax-transcriptionally activated glycoprotein 1 receptor, TXGP1L, ACT35, Txgp, Ly-70, ACT3, OX4, CD134.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
DGSMVTARRL NCVKHTYPSG HKCCRECQPG HGMVSRCDHT RDTLCHPCET GFYNEAVNYD TCKQCTQCNH RSGSELKQNC TPTQDTVCRC RPGTQPRQDS GYKLGVDCVP CPPGHFSPGN NQACKPWTNC TLSGKQTRHP ASDSLDAVCE DRSLLATLLW ETQRPTFRPT TVQSTTVWPR TSELPSPPTL VTPEGPLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH
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 :
FLT4 HumanDescription:
Vascular Endothelial Growth Factor Receptor-3 Human Recombinant
Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.
Product # :
PKA-244Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Soluble FLT4 Human Recombinant fused with a carboxy-terminal 6X histidine-tag produced in baculovirus is a monomeric, glycosylated, polypeptide containing the extracellular part, 25-774 amino acids and having a total molecular mass of 120 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding. The FLT4 is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
FLT4 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to bind recombinant rat VEGF-C in a functional solid phase binding assay. Immobilised recombinant human VEGFR-3/FLT-4 at 5 µg/ml can bind recombinant rat VEGF-C in a linear range of 8-500 ng/ml.More Info
-
Introduction
All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.
-
Synonyms
Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FLT4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized FLT4 in sterile water not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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 :
UFSP1 HumanDescription:
UFM1-Specific Peptidase 1 Human Recombinant
Inactive Ufm1-specific protease 1, UFSP1, UFSP.
Product # :
PRO-1320Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
UFSP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-142 a.a.) and having a molecular mass of 17kDa.UFSP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UFSP1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
UFM1-Specific Peptidase 1 (UFSP1) is similar to other Ufm1-specific proteases. Studies in mice determined that Ufsp1 releases ubiquitin-fold modifier 1 (Ufm1) from its bound conjugated complexes which also makes it into an active form. Sincethe human UFSP1 protein is shorter on the N-terminus and lacks a conserved Cys active site, it is expected to be non-functional.
-
Synonyms
Inactive Ufm1-specific protease 1, UFSP1, UFSP.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGDKPPG FRGSRDWIGC VEASLCLAHF GGPQGRLCHV PRGVGLHGEL ERLYSHFAGG GGPVMVGGDA DARSKALLGV CVGSGTEAYV LVLDPHYWGT PKSPSELQAA GWVGWQEVSA AFDPNSFYNL CLTSLSSQQQ QRTLD.
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 :
FGF2 (147), BovineDescription:
Fibroblast Growth Factor-basic (147 a.a.) Bovine Recombinant
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.
Product # :
CYT-1130Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Fibroblast Growth Factor-basic (147 a.a.) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 147 amino acid and having a molecular mass of approximately 16.5kDa.FGF2 (147) 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 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0 ×107IU/mg.
More Info
-
Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG (CUG) initiation codons resulting in 5 different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. there are differences in the tissue distribution and concentration of these 2 growth factors. -
Synonyms
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-basic (147 a.a.) should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-basic (147 a.a.) in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYSSWYVALK RTGQYKLGPK TGPGQKAILF LPMSAKS.
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Background
What is the molecular weight/Mw of FGF2 (147), BOVINE Protein?
FGF2 (147), BOVINE Protein has a total Mw of 16.5kDa.
What is the source or expression system of FGF2 (147), BOVINE Protein?
Escherichia Coli.
What is the Purity of FGF2 (147), BOVINE Protein?
FGF2 (147), BOVINE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF2 (147), BOVINE Protein?
The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0 ×107IU/mg.
What is the amino acid sequence of FGF2 (147), BOVINE Protein?
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYSSWYVALK RTGQYKLGPK TGPGQKAILF LPMSAKS.
What applications can FGF2 (147), BOVINE Protein be used in?
FGF2 (147), BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF2 (147), BOVINE Protein?
The endotoxin level is minimal, FGF2 (147), BOVINE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IFNW1 Human, HEKDescription:
Interferon-Omega 1 Human Recombinant, HEK
IFN omega-1, IFN alpha-II-1, IFNW1.
Product # :
CYT-1225Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IFNW1 Human Recombinant is a single, glycosylated, polypeptide chain (22-195 a.a) containing a total of 180 amino acids and having a molecular mass of 20.9 kDa. IFNW1 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IFNW1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .
More Info
-
Synonyms
IFN omega-1, IFN alpha-II-1, IFNW1.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.
-
Background
Interferons, a family of signaling proteins, play a pivotal role in the immune system’s defense against viral infections and other threats. Among these, Interferon W1 (IFNW1), a member of the Type I interferon family, has emerged as a key player in orchestrating antiviral responses and modulating immune reactions. This research embarks on a detailed exploration of the IFNW1 protein, unveiling its structural intricacies, signaling pathways, and its broader implications in immune regulation and disease. By delving into IFNW1, scientists aim to comprehend the nuances of its functions, decipher its interactions within the complex interferon network, and explore its potential applications in therapeutic interventions and beyond.
Structural Insights into IFNW1:
IFNW1, like other Type I interferons, exhibits a unique tertiary structure that enables it to interact with specific cell surface receptors. This interaction triggers a cascade of events, leading to the activation of various antiviral genes and immune modulatory pathways. Understanding the structural basis of IFNW1 is crucial for elucidating its binding affinities, biological activities, and its significance in immune responses.
Signaling Pathways and Antiviral Defense:
IFNW1 engages with its cognate receptors, initiating Janus kinase (JAK)-Signal Transducer and Activator of Transcription (STAT) signaling pathways. This activation leads to the transcription of interferon-stimulated genes (ISGs) with potent antiviral properties. IFNW1’s ability to induce an antiviral state in infected and neighboring cells is fundamental for restricting viral replication and curtailing the spread of infections. Additionally, IFNW1 plays a role in modulating adaptive immune responses, contributing to the broader immune defense mechanisms.
IFNW1 in Immunomodulation and Disease:
Beyond its antiviral functions, IFNW1 is implicated in immunomodulation and disease pathogenesis. Dysregulation of IFNW1 signaling is associated with autoimmune disorders, including lupus and rheumatoid arthritis, highlighting its involvement in immune-related diseases. Moreover, IFNW1 is being explored in cancer immunotherapy, where its ability to modulate the tumor microenvironment and enhance immune surveillance presents opportunities for novel treatment strategies.
Therapeutic Potential and Future Prospects:
The unique properties of IFNW1, particularly its role in immune regulation and antiviral defense, position it as a potential therapeutic target. Research efforts are directed towards harnessing its immunomodulatory functions for developing therapies against infectious diseases, autoimmune disorders, and certain cancers. Additionally, understanding IFNW1’s interactions with other components of the immune system opens avenues for innovative approaches in personalized medicine and targeted immunotherapies.
IFNW1 Protein, as an integral component of the interferon network, stands as a sentinel in the body’s defense against viral invasions and immune dysregulations. Its multifaceted roles in antiviral defense, immune modulation, and disease pathogenesis underscore its significance in biology and medicine. As researchers delve deeper into the intricacies of IFNW1, they pave the way for innovative therapies, immunomodulatory interventions, and a deeper understanding of immune responses. This research not only illuminates the pivotal role of IFNW1 but also holds the promise of transformative advancements in medicine, shaping the future of immunology and disease therapeutics.
What is the molecular weight/Mw of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein has a total Mw of 20.9kDa.
What is the source or expression system of IFNW1 HUMAN, HEK Protein?
HEK293 Cells.
What is the Purity of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNW1 HUMAN, HEK Protein?
The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .
What is the amino acid sequence of IFNW1 HUMAN, HEK Protein?
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.
What applications can IFNW1 HUMAN, HEK Protein be used in?
IFNW1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNW1 HUMAN, HEK Protein?
The endotoxin level is minimal, IFNW1 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.
- View Data Sheet
Name :
TNF a CanineDescription:
Tumor Necrosis Factor-Alpha Canine Recombinant
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
Product # :
CYT-140Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TNF-a Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.3 kDa. The TNF-a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Specific Activity is >3.3×105 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.More Info
-
Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VKSSSRTPSD KPVAHVVANP EAEGQLQWLS RRANALLANG VELTDNQLIV PSDGLYLIYS QVLFKGQGCP STHVLLTHTI SRFAVSYQTK VNLLSAIKSP CQRETPEGTE AKPWYEPIYL GGVFQLEKGD RLSAEINLPN YLDFAESGQV YFGIIAL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TGFBRAP1 HumanDescription:
Transforming Growth Factor Beta Receptor Associated Protein 1 Human Recombinant
TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.
Product # :
PRO-1890Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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Description
TGFBRAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (601-860 a.a) and having a molecular mass of 33kDa.TGFBRAP1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TGFBRAP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
TGF-beta receptor-associated protein 1 also known as TGFBRAP1 takes part in the TGF-beta/activin signaling pathway. TGFBRAP1 is related with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. TGFBRAP1recruits SMAD4 to the vicinity of the receptor complex and smoothes the progress of its interaction with receptor-regulated Smads, such as SMAD2.
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Synonyms
TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSKRLQ KEEYHTHLAV LYLEEVLLQR ASASGKGAEA TETQAKLRRL LQKSDLYRVH FLLERLQGAG LPMESAILHG KLGEHEKALH ILVHELQDFA AAEDYCLWCS EGRDPPHRQQ LFHTLLAIYL HAGPTAHELA VAAVDLLNRH ATEFDAAQVL QMLPDTWSVQ LLCPFLMGAM RDSIHARRTM QVALGLARSE NLIYTYDKMK LKGSSIQLSD KKLCQICQNP FCEPVFVRYP NGGLVHTHCA ASRHTNPSSS SPGTRT
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 :
GCSF RatDescription:
Granulocyte-Colony Stimulating Factor Rat Recombinant
Granulocyte colony stimulating factor, Protein Csf3, Csf3.
Product # :
CYT-940Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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Description
GCSF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.5kDa.The G-CSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 5mM Sodium Citrate, pH 4.0.
Purity
Greater than 97.0% as determined by:
(a)Analysis by RP-HPLC.
(b)Analysis by SDS-PAGE.Biological Activity
The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.More Info
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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
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Synonyms
Granulocyte colony stimulating factor, Protein Csf3, Csf3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GCSF in sterile 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
KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.
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Background
What is the molecular weight/Mw of G CSF RAT Protein?
G CSF RAT Protein has a total Mw of 21.5kDa.
What is the source or expression system of G CSF RAT Protein?
Escherichia Coli.
What is the Purity of G CSF RAT Protein?
G CSF RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF RAT Protein?
The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.
What is the amino acid sequence of G CSF RAT Protein?
KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.
What applications can G CSF RAT Protein be used in?
G CSF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF RAT Protein?
The endotoxin level is minimal, G CSF RAT 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 :
Prolactin Ovine AntagonistDescription:
Prolactin Ovine Antagonsit Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-311Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Prolactin Ovine Antagonist Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 23kDa. Ovine Prolactin Antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Ovine Prolactin was lyophilized from a concentrated (1mg/ml) solution with 0.02%-0.03% NaHCO3.
Purity
Greater than 99.0% as determined by SDS-PAGE.
Biological Activity
Ovine Prolactin Antagonist is devoid of agonistic activity and capable of inhibiting biological activity of Ovine Prolactin or other lactogenic hormones as evidenced by proliferation assay of Nb2 or other cells.More Info
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Introduction
Prolactin is a lactogenic hormone secreted by the adenohypophysis .Besides its major action on lactation, in some species prolactin exerts effects on reproduction, maternal behavior, fat metabolism, immunomodulation and osmoregulation.Prolactin has been shown also to have cytokine-like activities and to have important immunoregulatory activities. It contributes to the development of lymphoid tissues and the maintenance of physiological immune function and also modulates a variety of T-cell immune responses. Prolactin has been reported to activate cellular proliferation in nonreproductive tissue, such as liver, spleen, and thymus. It induces significant proliferation in aortic smooth muscle cells and also enhances proliferation of these cells induced by PDGF . Prolactin also appears to be directly mitogenic for pancreatic beta cells. Prolactin is also mitogenic for cultured astrocytes.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Ovine Prolactin Antagonist although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Ovine Prolactin Antagonist 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 Ovine Prolactin Antagonist 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-Thr-Pro-Val-Cys-Pro.
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 :
MOBKL1B HumanDescription:
MOB1, Mps One Binder Kinase Activator-Like 1B Human Recombinant
Mps one binder kinase activator-like 1B, Mob1 alpha, Mob1A, Mob1 homolog 1B, Protein Mob4B, MOBKL1B, C2orf6, MOB4B, MOBK1B, MOB1, MATS1, FLJ10788, FLJ11595.
Product # :
PRO-068Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MOBKL1B Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 27.2kDa. The MOBKL1B is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MOBKL1B solution (0.5mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MOBKL1B is a member of the MOB1/phocein family. MOBKL1B stimulates the kinase activity of STK38 and STK38L. MOBKL1B also binds to and regulates downstream targets such as the NDR-family protein kinases and LATS1 kinase. Thus, MOBKL1B participates in cell cycle checkpoint control and tumor inhibition.
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Synonyms
Mps one binder kinase activator-like 1B, Mob1 alpha, Mob1A, Mob1 homolog 1B, Protein Mob4B, MOBKL1B, C2orf6, MOB4B, MOBK1B, MOB1, MATS1, FLJ10788, FLJ11595.
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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 MSFLFSSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRQAVMLPEG EDLNEWIAVN TVDFFNQINM LYGTITEFCT EASCPVMSAG PRYEYHWADG TNIKKPIKCS APKYIDYLMT WVQDQLDDET LFPSKIGVPF PKNFMSVAKT ILKRLFRVYA HIYHQHFDSV MQLQEEAHLN TSFKHFIFFV QEFNLIDRRE LAPLQELIEK LGSKDR.
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 :
MTHSFD HumanDescription:
Methenyltetrahydrofolate Synthetase Domain Containing Human Recombinant
Methenyltetrahydrofolate synthase domain-containing protein, Methenyltetrahydrofolate synthase domaincontaining protein, Methenyltetrahydrofolate synthase
Product # :
PRO-2646Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MTHSFD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-383 a.a.) and having a molecular mass of 44.5kDa. MTHSFD is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MTHSFD solution (0.25mg/ml) contains 30% glycerol, 1mM DTT and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MTHSFD, also known as Methenyltetrahydrofolate Synthetase Domain Containing protein, is linked to Pancreas, Annular and Gastrointestinal Defects. It has also been associated with Immunodeficiency Syndrome. Some of the Gene Ontology annotations that are related to the MTHSFD gene are nucleic acid binding and nucleotide binding.
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Synonyms
Methenyltetrahydrofolate synthase domain-containing protein, Methenyltetrahydrofolate synthase domaincontaining protein, Methenyltetrahydrofolate synthase
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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 MGSMEPRAVG VSKQDIREQI WGYMESQNLA DFPRPVHHRI PNFKGASHAA EQLPRLQAFK TARTIKVNPD APQKSARFFV LESKKTLLVP TPRLRTGLFN KITPPPGATK DILRKCATSQ GVRNYSVPIG LDSRVLVDLV VVGSVAVSEK GWRIGKGEGY ADLEYAMMVS MGAVSKETPV VTIVHDCQVV DIPEELVEEH DITVDYILTP TRVIATGCKR PKPMGITWFK ISLEMMEKIP ILRSLRAREQ QAGKDVTLQG EHQHLPEPGC QQTVPLSVGR RPPDTPGPET NSMEAAPGSP PGEGAPLAAD VYVGNLPGDA RVSDLKRALR ELGSVPLRLT WQGPRRRAFL HYPDSAAAQQ AVSCLQGLRL GTDTLRVALA RQQRDK
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 :
AS3MT HumanDescription:
Arsenic Methyltransferase Human Recombinant
Arsenite methyltransferase, Methylarsonite methyltransferase, S-adenosyl-L-methionine:arsenic(III) methyltransferase, AS3MT, CYT19, RP11-753C18.6.
Product # :
ENZ-615Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AS3MT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 399 amino acids (1-375 a.a.) and having a molecular mass of 44.3kDa.AS3MT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AS3MT protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Arsenic Methyltransferase (AS3MT) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to trivalent arsenical and may have a role in arsenic metabolism. AS3MT methylates arsenite to produce methylarsonate, Me-AsO3H2, which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite which is also a substrate, is transformed into the much less toxic complex dimethylarsinate (cacodylate), Me2As(O)-OH.
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Synonyms
Arsenite methyltransferase, Methylarsonite methyltransferase, S-adenosyl-L-methionine:arsenic(III) methyltransferase, AS3MT, CYT19, RP11-753C18.6.
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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 MGSHMAALRD AEIQKDVQTY YGQVLKRSAD LQTNGCVTTA RPVPKHIREA LQNVHEEVAL RYYGCGLVIP EHLENCWILD LGSGSGRDCY VLSQLVGEKG HVTGIDMTKG QVEVAEKYLD YHMEKYGFQA SNVTFIHGYI EKLGEAGIKN ESHDIVVSNC
VINLVPDKQQ VLQEAYRVLK HGGELYFSDV YTSLELPEEI RTHKVLWGEC LGGALYWKEL AVLAQKIGFC PPRLVTANLI TIQNKELERV IGDCRFVSAT FRLFKHSKTG PTKRCQVIYN GGITGHEKEL MFDANFTFKE GEIVEVDEET AAILKNSRFA QDFLIRPIGE KLPTSGGCSA
LELKDIITDP FKLAEESDSM KSRCVPDAAG GCCGTKKSC.
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.