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1000 results found for “Sclerostin”
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Name :
GM-CSF MouseDescription:
Granulocyte Macrophage-Colony Stimulating Factor Mouse Recombinant
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF
Product # :
CYT-222Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Granulocyte Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14285.35 Dalton.GM-CSF Mouse is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GM-CSF Mouse was lyophilized with no additives.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.More Info
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GM-CSF 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 Granulocyte Macrophage Colony Stimulating Factor in sterile 20mM AcOH (acetic Acid) 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-Ala-Pro-Thr-Arg.
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Background
What is the molecular weight/Mw of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein has a total Mw of 14.28kDa.
What is the source or expression system of GM-CSF MOUSE Protein?
Escherichia Coli.
What is the Purity of GM-CSF MOUSE Protein?
GM-CSF MOUSE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.
What is the amino acid sequence of GM-CSF MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.
What applications can GM-CSF MOUSE Protein be used in?
GM-CSF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF MOUSE Protein?
The endotoxin level is minimal, GM-CSF MOUSE Protein was purified using conventional chromatography techniques.
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Protein content
GM-CSF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.765 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 calibrated solution of GM-CSF 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 :
HBsAg adwDescription:
Hepatitis B Surface Antigen, adw Recombinant
Product # :
HBS-872Price :
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Description
HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.
Source
Pichia Pastoris.
Formulation
Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
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Physical Appearance
Sterile Filtered pale solution.
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Stability
HBsAg Should be stored at 4°C.DO NOT FREEZE.
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 :
CKMM Human, NativeDescription:
Creatine Kinase Muscle Human
Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM.
Product # :
CKI-273Price :
Quantity :
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Shipped at Room temp
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Description
Human CKMM derived from Human Cardiac Tissue.
Source
Human Cardiac Tissue.
Formulation
The CKMM protein was lyophilized from 40mM Tris-HCL, 1mM EDTA, pH 7.5 & 10mM n-Acetyl cysteine.
Purity
Greater than 10.0% as visualized by sds-page.
Biological Activity
1 unit will transfer 1 µmole of phosphate from Creatine phosphate to ATP/minute at 37 degrees Celsius. Measured at 340nm as one equimolar amount of NADH produced by a coupled reaction. The specific activity was measured and found to be > 100U/mg.
More Info
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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle''s disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
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Synonyms
Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM.
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Physical Appearance
Lyophilized Powder
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Stability
Lyophilized CKMM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 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 CKMM in sterile distilled water not less than 100µg/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.
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Name :
COL4A3 Human, BiotinDescription:
Collagen Type IV Alpha 3 Human Recombinant, Biotinylated
Collagen alpha-3(IV) chain, Goodpasture antigen, COL4A3, Glomerular Basal Membrane, GBM.
Product # :
PRO-2564Price :
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Description
Human α3 chain of collagen IV; identical with the antigen called "glomerular basal membrane antigen" (GBM). Calculated Molecular weight: 48kDa. Calculated isoelectric point: pH 8.9. cDNA coding for a minicollagen version of the human collagen IV α3 chain fused to a 6-histidine purification tag. The term minicollagen designates the removal of most of the epitope-less triplehelical collagenous region (situated between the N-terminal 7S domain and the C-terminal noncollagenous NC1 domain), which is a requirement for recombinant production of this antigen.
Source
Sf9 insect cells.
Formulation
COL4A3 Human biotin contains 20mM HEPES, pH 7.5, 0.02% SDS and 0.01mM EDTA.
Purity
Greater than 87% as determined by Capillary Electrophoresis.
More Info
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Introduction
Type IV collagen is a major structural component of basement membranes. It is a multimeric protein composed of 3 alpha subunits, which are encoded by 6 different genes, alpha 1 through alpha 6. Each of these alpha subunits can form a triple helix structure with 2 other subunits to form type IV collagen. The Goodpasture syndrome is a condition in which autoantibodies bind to the collagen molecules in the basement membranes of alveoli and glomeruli. The epitopes that elicit these autoantibodies are restricted basically to the non-collagenous C-terminal domain of the protein. There are numerous alternative transcripts that appear to be unique to the human COL4A3 and alternative splicing is limited to the six exons that encode this C-terminal domain. COL4A3 is also linked to an autosomal recessive form of Alport syndrome. The mutations contributing to the Alport syndrome are also situated within the exons that encode this C-terminal region. COL4A3 is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Several exons of COL4A3 are interspersed with exons of an uncharacterized gene which is on the opposite strand.
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Synonyms
Collagen alpha-3(IV) chain, Goodpasture antigen, COL4A3, Glomerular Basal Membrane, GBM.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG type human auto antibodies.2. Functional Streptavidin based ELISA test (analysis of positive/negative samples.)
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Note
It has been reported that the immunodominant epitope of COL4A3 is a cryptic epitope that is not easily accessible to the corresponding autoantibodies. It is necessary to treat the protein under nonreducing conditions with a denaturant such as urea to unmask the epitopes (see Hellmark et al. in Autoantibodies, Peter, J.B. and Shoenfeld, Y., eds., Elsevier B.V., 1996, pp 291-298).
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 :
STIP1 Human, HisDescription:
Stress-Induced-Phosphoprotein 1 Human Recombinant, His Tag
HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.
Product # :
PRO-753Price :
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Description
Recombinant Human STIP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543 a.a) and having a molecular mass of 64.8kDa. STIP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STIP1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM DTT, 1mM EDTA, 0.2mM PMSF and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.
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Synonyms
HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.
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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 MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPDWGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLRNKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDKAKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH TPDVLKKCQQAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC QLEPTFIKGYTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.
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 :
Epoetin HumanDescription:
Erythropoietin-Alpha Human Recombinant
Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.
Product # :
CYT-201Price :
Quantity :
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Shipped at Room temp
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Description
Erythropoietin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a single, polypeptide chain containing 166 amino acids and having a predicted molecular mass of 21,000 Dalton and apparent glycosylated molecular mass of 36-40kDa. EPO-a is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells(CHO).
Formulation
Each mg of lyophilized powder contains 0.59 mg sodium citrate, 0.58 mg sodium chloride and 0.006 mg citric acid.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Specific Activity was measured by Normocyth -aemic mice and was found to be 150,000 IU/mg.More Info
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Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
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Synonyms
Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Erythropoietin-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha 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 EPO-alpha 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
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDR.
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Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 38kDa.
What is the source or expression system of EPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).
What is the Purity of EPOETIN Protein?
EPOETIN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EPOETIN Protein?
The Specific Activity was measured by Normocyth -aemic mice and was found to be 150,000 IU/mg.
What is the amino acid sequence of EPOETIN Protein?
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDR.
What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN 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 :
PCSK9 HumanDescription:
Proprotein Convertase Subtilisin/Kexin Type 9 Human Recombinant
Proprotein Convertase Subtilisin/Kexin Type 9, NARC1, Subtilisin/Kexin-Like Protease PC9, HCHOLA3, LDLCQ1, NARC-1, FH3, PC9, Convertase Subtilisin/Kexin Type 9 Preproprotein, Hypercholesterolemia, Autosomal Dominant 3, Neural Apoptosis Regulated Convertase 1, Neural Apoptosis-Regulated Convertase 1, Proprotein Convertase 9, EC 3.4.21.111, EC 3.4.21, EC 3.4.21, PCSK9.
Product # :
PRO-2043Price :
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Description
PCSK9 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Gln31-Gln692) containing a total of 672 amino acids, having a calculated molecular mass of 72.4kDa and fused to a 10 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
PCSK9 filtered (0.4µm) solution at a concentration of 0.25-0.7mg/ml in phosphate buffered saline and 20 % (w/v) glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) belongs to the subtilisin-like proprotein convertase family, which includes proteases that process protein and peptide precursors trafficking via regulated or constitutive branches of the secretory pathway. PCSK9 protein goes through an autocatalytic processing event with its prosegment in the ER and is constitutively secreted as an inactive protease into the extracellular matrix and trans-Golgi network. PCSK9 is expressed in the liver, intestine and kidney tissues and escorts specific receptors for lysosomal degradation. PCSK has a role in cholesterol and fatty acid metabolism. PCSK9 gene mutations are linked with autosomal dominant familial hypercholesterolemia.
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Synonyms
Proprotein Convertase Subtilisin/Kexin Type 9, NARC1, Subtilisin/Kexin-Like Protease PC9, HCHOLA3, LDLCQ1, NARC-1, FH3, PC9, Convertase Subtilisin/Kexin Type 9 Preproprotein, Hypercholesterolemia, Autosomal Dominant 3, Neural Apoptosis Regulated Convertase 1, Neural Apoptosis-Regulated Convertase 1, Proprotein Convertase 9, EC 3.4.21.111, EC 3.4.21, EC 3.4.21, PCSK9.
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Physical Appearance
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
QEDEDGDYEE LVLALRSEED GLAEAPEHGT TATFHRCAKD PWRLPGTYVV VLKEETHLSQ SERTARRLQA QAARRGYLTK ILHVFHGLLP GFLVKMSGDL LELALKLPHV DYIEEDSSVF AQSIPWNLER ITPPRYRADE YQPPDGGSLV EVYLLDTSIQ SDHREIEGRV MVTDFENVPE EDGTRFHRQA SKCDSHGTHL AGVVSGRDAG VAKGASMRSL RVLNCQGKGT VSGTLIGLEF IRKSQLVQPV GPLVVLLPLA GGYSRVLNAA CQRLARAGVV LVTAAGNFRD DACLYSPASA PEVITVGATN AQDQPVTLGT LGTNFGRCVD LFAPGEDIIG ASSDCSTCFV SQSGTSQAAA HVAGIAAMML SAEPELTLAE LRQRLIHFSA KDVINEAWFP EDQRVLTPNL VAALPPSTHG AGWQLFCRTV WSAHSGPTRM ATAVARCAPD EELLSCSSFS RSGKRRGERM EAQGGKLVCR AHNAFGGEGV YAIARCCLLP QANCSVHTAP PAEASMGTRV HCHQQGHVLT GCSSHWEVED LGTHKPPVLR PRGQPNQCVG HREASIHASC CHAPGLECKV KEHGIPAPQE QVTVACEEGW TLTGCSALPG TSHVLGAYAV DNTCVVRSRD VSTTGSTSEG AVTAVAICCR SRHLAQASQE LQHHHHHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IGF1 N15 HumanDescription:
Insulin Like Growth Factor-1 N15 Labeled Human Recombinant
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Product # :
CYT-128Price :
Quantity :
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Shipped at Room temp
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- sds-page
Description
IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N15 is stable isotope labeled. The IGF1 N15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IGF1 N15 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.
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 serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.sds-page
More Info
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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
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Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF1 N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 N15 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 IGF1 N15 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
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
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Background
What is the molecular weight/Mw of IGF1 N15 HUMAN Protein?
IGF1 N15 HUMAN Protein has a total Mw of 7.74kDa.
What is the source or expression system of IGF1 N15 HUMAN Protein?
Escherichia Coli.
What is the Purity of IGF1 N15 HUMAN Protein?
IGF1 N15 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 N15 HUMAN Protein?
The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.
What is the amino acid sequence of IGF1 N15 HUMAN Protein?
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
What applications can IGF1 N15 HUMAN Protein be used in?
IGF1 N15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 N15 HUMAN Protein?
The endotoxin level is minimal, IGF1 N15 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 :
CLEC2B HumanDescription:
C-type Lectin Domain Family 2, Member B Human Recombinant
C-type lectin domain family 2 member B, Activation-induced C-type lectin, C-type lectin superfamily member 2, IFN-alpha-2b-inducing-related protein 1, CLEC2B, AICL, CLECSF2, IFNRG1, HP10085.
Product # :
PRO-526Price :
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Shipped with Ice Packs
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Description
CLEC2B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids (26-149 a.a) and having a molecular mass of 16.9kDa.CLEC2B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLEC2B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
C-type Lectin Domain Family 2, Member B (CLEC2B) belongs to the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of the CTL/CTLD family share a common protein fold and have various functions, such as cell adhesion, cell-cell signaling, glycoprotein turnover, and roles in inflammation and immune response. The CLEC2B gene is closely connected to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region. CLEC2B is expressed preferentially in lymphoid tissues, and in most hematopoietic cell types.
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Synonyms
C-type lectin domain family 2 member B, Activation-induced C-type lectin, C-type lectin superfamily member 2, IFN-alpha-2b-inducing-related protein 1, CLEC2B, AICL, CLECSF2, IFNRG1, HP10085.
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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 MGSKLTRDSQ SLCPYDWIGF QNKCYYFSKE EGDWNSSKYN CSTQHADLTI IDNIEEMNFL RRYKCSSDHW IGLKMAKNRT GQWVDGATFT KSFGMRGSEG CAYLSDDGAA TARCYTERKW ICRKRIH.
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 :
EnfuvirtideDescription:
Enfuvirtide (T-20)
Product # :
PRO-376Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Enfuvirtide has an amino acid sequence Ac-Tyr-Thr-Ser-Leu-Ile-His-Ser-Leu-Ile-Glu-Glu-Ser-Gln-Asn-Gln-Gln-Glu-Lys-Asn-Glu-Gln-Glu-Leu-Leu-Glu-Leu-Asp-Lys-Trp-Ala-Ser-Leu-Trp-Asn-Trp-Phe-NH2, molecular formula of C204H301N51O64 and a molecular weight of 4488.9 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
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Introduction
Enfuvirtide also called human immunodeficiency fusion inhibitor blocks HIV’s ability to infect healthy CD4 cells. It can reduce the amount of HIV in the blood and increase the number of CD4 cells. Enfuvirtide operates by disrupting the HIV-1 molecular machinery at the final phase of fusion with the target cell, preventing uninfected cells from becoming infected. Enfuvirtide mimics components of the HIV-1 fusion apparatus and displace them, preventing normal fusion. HIV attaches to the host CD4+ cell receptor using the viral protein GP120; upon binding, GP120 deforms allowing the viral protein GP41 to insert itself into the host cell's plasma membrane. Entry inhibitors bind to GP41 preventing the formation of an entry pore for the capsid of the virus, keeping it out of the cell.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Enfuvirtide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Enfuvirtide 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
Enfuvirtide lyophilized powder is soluble in water at a concentration of 1mg/ml.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CCL24 MouseDescription:
Eotaxin-2 Mouse Recombinant (CCL24)
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
Product # :
CHM-368Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL24 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.3 kDa. The CCL24 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.15M sodium chloride.
Purity
Greater than 97.0% as determined by:(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3. -
Synonyms
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Mouse Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.
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Background
What is the molecular weight/Mw of CCL24 MOUSE Protein?
CCL24 MOUSE Protein has a total Mw of 10.3kDa.
What is the source or expression system of CCL24 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL24 MOUSE Protein?
CCL24 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL24 MOUSE Protein?
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL24 MOUSE Protein?
VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.
What applications can CCL24 MOUSE Protein be used in?
CCL24 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL24 MOUSE Protein?
The endotoxin level is minimal, CCL24 MOUSE 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 :
CTF1 RatDescription:
Cardiotrophin-1 Rat Recombinant
Cardiotrophin-1, CT-1, Ctf1.
Product # :
CYT-199Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.More Info
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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat 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 CTF1 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
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
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Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.
What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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 :
Betacellulin His HumanDescription:
Betacellulin Human Recombinant, His Tag
Betacellulin, Probetacellulin.
Product # :
CYT-077Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
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Synonyms
Betacellulin, Probetacellulin.
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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 MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y
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Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 11.3kDa.
What is the source or expression system of BETACELLULIN Protein?
Escherichia Coli.
What is the Purity of BETACELLULIN Protein?
BETACELLULIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of BETACELLULIN Protein?
The biological functionality of BETACELLULIN Protein will be determined in the future.
What is the amino acid sequence of BETACELLULIN Protein?
MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y
What applications can BETACELLULIN Protein be used in?
BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN 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 :
TSH HumanDescription:
Thyroid Stimulating Hormone Human
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
Product # :
HOR-001Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thyroid Stimulating Hormone Human produced in Human pituitary glands is an important indicator of thyroid function.
Source
Human pituitary glands
Formulation
Lyophilized from a concentrated solution containing 50mM ammonium bicarbonate.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
11.72 IU/mg vial by Centaur CP. Siemens Centaur CP is standardized against WHO 3rd IRP 81/565.More Info
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Introduction
Thyroid-stimulating hormone (also known as TSH or thyrotropin) is a hormone synthesized and secreted by thyrotrope cells in the anterior pituitary gland which regulates the endocrine function of the thyroid gland.
TSH stimulates the thyroid gland to secrete the hormones thyroxine (T4) and triiodothyronine (T3). TSH production is controlled by a Thyrotropin Releasing Hormone, (TRH), which is manufactured in the hypothalamus and transported to the Anterior Pituitary gland, where it increases TSH production and release. Somatostatin is also produced by the hypothalamus, and has an opposite effect on the pituitary production of TSH, decreasing or inhibiting its release.
The level of Thyroid hormones (T3 and T4) in the blood have an additional effect on the pituitary release of TSH, When the levels of T3 and T4 are low, the production of TSH is increased, and conversely, when levels of T3 and T4 are high, then TSH production is decreased. This effect creates a regulatory negative feedback loop.
TSH is a glycoprotein and consists of two subunits, the alpha and the beta subunit.
The a (alpha) subunit is identical to that of human chorionic gonadotropin (HCG), luteinising hormone (LH), follicle-stimulating hormone (FSH).
The b (beta) subunit is unique to TSH, and therefore determines its function. -
Synonyms
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSH 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 TSH 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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Background
What is the source or expression system of TSH HUMAN Protein?
Human pituitary glands
What is the Purity of TSH HUMAN Protein?
TSH HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of TSH HUMAN Protein?
11.72 IU/mg vial by Centaur CP. Siemens Centaur CP is standardized against WHO 3rd IRP 81/565.
What applications can TSH HUMAN Protein be used in?
TSH HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TSH HUMAN Protein?
The endotoxin level is minimal, TSH 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 :
PLAUR HumanDescription:
PLAUR Human Recombinant
PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.
Product # :
PRO-2340Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PLAUR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (23-305 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57 kDa).PLAUR is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PLAUR protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PLAUR is one of 2 activators which convert the extracellular zymogen plasminogen to plasmin, a serine protease involved in a various normal and pathological processes that require cell migration and/or tissue destruction. PLAUR protein is synthesized and released from cells as a single-chain proenzyme with narrow enzymatic activity and is converted to an active two-chain disulfide-linked active enzyme by plasmin and other specific proteinases.
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Synonyms
PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.
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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
LRCMQCKTNG DCRVEECALG QDLCRTTIVR LWEEGEELEL VEKSCTHSEK TNRTLSYRTG LKITSLTEVV CGLDLCNQGN SGRAVTYSRS RYLECISCGS SDMSCERGRH QSLQCRSPEE QCLDVVTHWI QEGEEGRPKD DRHLRGCGYL PGCPGSNGFH NNDTFHFLKC CNTTKCNEGP ILELENLPQN GRQCYSCKGN STHGCSSEET FLIDCRGPMN QCLVATGTHE PKNQSYMVRG CATASMCQHA HLGDAFSMNH IDVSCCTKSG CNHPDLDVQY RSGLEHHHHH 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 :
MT IIDescription:
Melanotan-II
Melanotan-II, MT-II, Melanotan.
Product # :
HOR-289Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The molecular formula of Melanotan-II is C50H69N15O9. It has the amino acid sequence of Ac-Nle-cyclo [Asp-His-D-Phe-Arg-Trp-Lys]-NH2 and a molecular weight of 1024.2 Dalton. The CAS Number is 121062-08-6.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 99% as determined by by RP-HPLC.
More Info
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Introduction
Melanotan and Melanotan-II are both analogs of the peptide hormone alpha melanocyte stimulating hormone (a-MSH) that tend to induce skin tanning. Unlike Melanotan, Melanotan-II has the additional effect of increasing libido. Melanotan II has aphrodisiac properties.
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Synonyms
Melanotan-II, MT-II, Melanotan.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Melanotan-II although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MT-II 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 Melanotan-II in sterile 18MΩ-cm H2O 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 :
Prolactin RatDescription:
Prolactin Rat Recombinant
Mammotropin, Luterotropic hormone, Lutetropin, PRL.
Product # :
CYT-322Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Prolactin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.6 kDa. The Prolactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.
Purity
Greater than 95.0% 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 the proliferation of rat lymphoma, Nb2-11 was found to be < 0.065 ng/ml corresponding to a specific activity of 15,400,000 Units/mg.More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luterotropic hormone, Lutetropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin 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 Prolactin 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-Leu-Pro-Val-Cys.
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 :
SPON1 HumanDescription:
Recombinant Human Spondin-1
F-Spondin, VSGP
Product # :
pro-2758Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPON1 Human Recombinant produced in HEK293 cells is a single, glycosylated, polypeptide chain (29-807 a.a) containing a total of 785 amino acids, having a molecular mass of 88.9 kDa. SPON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
POR protein solution (0.25mg/ml) contains Phosphate buffer saline (pH 7.4) and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SPON1 is a cell adhesion protein which take part in the regulation of protein binding activity, regulation of protein processing and regulation of amyloid precursor protein catabolic mechanism. SPON1 is found in the extracellular space and it co-localizes with collagen-containing extracellular matrix. SPON1 stimulates the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro.
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Synonyms
F-Spondin, VSGP
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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
FSDETLDKVP KSEGYCSRIL RAQGTRREGY TEFSLRVEGD PDFYKPGTSY RVTLSAAPPS YFRGFTLIAL RENREGDKEE DHAGTFQIID EEETQFMSNC PVAVTESTPR RRTRIQVFWI APPAGTGCVI LKASIVQKRI IYFQDEGSLT KKLCEQDSTF DGVTDKPILD CCACGTAKYR LTFYGNWSEK THPKDYPRRA NHWSAIIGGS HSKNYVLWEY GGYASEGVKQ VAELGSPVKM EEEIRQQSDE VLTVIKAKAQ WPAWQPLNVR AAPSAEFSVD RTRHLMSFLT MMGPSPDWNV GLSAEDLCTK ECGWVQKVVQ DLIPWDAGTD SGVTYESPNK PTIPQEKIRP LTSLDHPQSP FYDPEGGSIT QVARVVIERI ARKGEQCNIV PDNVDDIVAD LAPEEKDEDD TPETCIYSNW SPWSACSSST CDKGKRMRQR MLKAQLDLSV PCPDTQDFQP CMGPGCSDED GSTCTMSEWI TWSPCSISCG MGMRSRERYV KQFPEDGSVC TLPTEETEKC TVNEECSPSS CLMTEWGEWD ECSATCGMGM KKRHRMIKMN PADGSMCKAE TSQAEKCMMP ECHTIPCLLS PWSEWSDCSV TCGKGMRTRQ RMLKSLAELG DCNEDLEQVE KCMLPECPID CELTEWSQWS ECNKSCGKGH VIRTRMIQME PQFGGAPCPE TVQRKKCRIR KCLRNPSIQK LRWREARESR RSEQLKEESE GEQFPGCRMR PWTAWSECTK LCGGGIQERY MTVKKRFKSS QFTSCKDKKE IRACNVHPC-HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
sCD23 HumanDescription:
Soluble CD23 Human Recombinant
Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.
Product # :
PRO-1789Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
sCD23 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19.2kDa.The sCD23 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 is determined by its ability to induce TNF-alpha production by human PBMCs.More Info
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Introduction
CD23 is a 45kDa glycoprotein, which is present on a subpopulation of freshly isolated peripheral blood and tonsil B cells and strongly expressed on EBV-transformed B lymphoblasts. The CD23 molecule is identical to the low affinity IgE receptor found on B cells. Expression of CD23 has been detected in neoplastic cells from cases of B cell chronic lymphocyctic leukaemia and some cases of centroblastic/centrocytic lymphoma.
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Synonyms
Low affinity immunoglobulin epsilon Fc receptor, Lymphocyte IgE receptor, Fc-epsilon-RII, BLAST-2, Immunoglobulin E-binding factor, CD23 antigen, FCER2, CD23, FCE2, CD23A, IGEBF, CLEC4J.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized sCD23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sCD23 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 sCD23 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
MELQVSSGFV CNTCPEKWIN FQRKCYYFGK GTKQWVHARY ACDDMEGQLV SIHSPEEQDF LTKHASHTGS WIGLRNLDLK GEFIWVDGSH VDYSNWAPGE PTSRSQGEDC VMMRGSGRWN DAFCDRKLGA WVCDRLATCT PPASEGSAES MGPDSRPDPD GRLPTPSAPL HS
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 :
TesamorelinDescription:
Tesamorelin
Product # :
HOR-062Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Tesamorelin is a synthetic single, non-glycosylated polypeptide chain containing 44 amino acids, having a molecular mass of 5135.78 Dalton and a Molecular formula of C221H366N72O67S.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tesamorelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Tesamorelin 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 Tesamorelin 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
trans-3-hexenoyl-Tyr-Ala-Asp-Ala-IlePhe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-GluArg-Gly-Ala-Arg-Ala-Arg-Leu-NH2.
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Background
Tesamorelin is a growth hormone-releasing hormone (GHRH) analogue. Tesamorelin stimulates the pituitary gland to produce endogenous growth hormone, which targets visceral adipose tissue. Tesamorelin has evolved from a HIV treatment into an effective metabolic and regenerative therapy.
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 :
MMP 8 Human, HisDescription:
Matrix Metalloproteinase-8 Human Recombinant, His Tag
CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.
Product # :
ENZ-766Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
MMP 8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (101-467a.a) and having a molecular mass of 44.3kDa. MMP 8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP 8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form.
Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I.
Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes. -
Synonyms
CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.
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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 MGSLTPGNPK WERTNLTYRI RNYTPQLSEA EVERAIKDAF ELWSVASPLI FTRISQGEAD INIAFYQRDH GDNSPFDGPN GILAHAFQPG QGIGGDAHFD AEETWTNTSA NYNLFLVAAH EFGHSLGLAH SSDPGALMYP NYAFRETSNY SLPQDDIDGI QAIYGLSSNP IQPTGPSTPK PCDPSLTFDA ITTLRGEILF FKDRYFWRRH PQLQRVEMNF ISLFWPSLPT GIQAAYEDFD RDLIFLFKGN QYWALSGYDI LQGYPKDISN YGFPSSVQAI DAAVFYRSKT YFFVNDQFWR YDNQRQFMEP GYPKSISGAF PGIESKVDAV FQQEHFFHVF SGPRYYAFDL IAQRVTRVAR GNKWLNCRYG.
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 :
I TAC HumanDescription:
I-TAC Human Recombinant (CXCL11)
Small inducible cytokine B11, CXCL11, I-TAC, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
Product # :
CHM-334Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
I-TAC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 8300 Dalton. The I-TAC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2?m filtered concentrated (0.5mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human IL-2 activated T-Lymphocytes using a concentration range of 0.1-10.0 ng/ml.More Info
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Introduction
Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokinen family that is also called inducible T-cell alpha chemoattractant (I-TAC) and (IP-9). I-TAC is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. I-TAC is chemotactic for activated T cells. The CXCL11 gene is located on human chromosome 4 along with many other members of the CXC chemokine family.
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Synonyms
Small inducible cytokine B11, CXCL11, I-TAC, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized I-TAC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution I-TAC 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 I-TAC 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
FPMFKRGRCLCIGPGVKAVKVADIEKASIMYPSNNCDKIEVIITLKENKGQRCLNPKSKQARLIIKKVERKNF.
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 :
STX4 HumanDescription:
Syntaxin-4 Human Recombinant
Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.
Product # :
PRO-1176Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
STX4 Human Recombinant produced in E. coli is a single polypeptide chain containing 300 amino acids (1-275) and having a molecular mass of 34.7 kDa.STX4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The STX4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Syntaxin 4 (STX4) is a member of the syntaxin/epimorphin family of proteins. The Syntaxin family is cellular receptors for transport vesicles which participate in exocytosis in neutrophils. Syntaxin 4 is vital for normal regulation of glucose metabolism uptake in skeletal muscle and decline in STX4 protein levels lead to reduction of whole-body hormone-stimulated glucose metabolism. STX4 is expressed in neutrophils and neutrophil-differentiated HL-60 cells. The STX4 expression in neutrophils increases with differentiation.
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Synonyms
Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMMRDRT HELRQGDDSS DEEDKERVAL VVHPGTARLG SPDEEFFHKV RTIRQTIVKL GNKVQELEKQ QVTILATPLP EESMKQELQN LRDEIKQLGR EIRLQLKAIE PQKEEADENY NSVNTRMRKT QHGVLSQQFV ELINKCNSMQ SEYREKNVER IRRQLKITNA GMVSDEELEQ MLDSGQSEVF VSNILKDTQV TRQALNEISA RHSEIQQLER SIRELHDIFT FLATEVEMQG EMINRIEKNI LSSADYVERG QEHVKTALEN QKKARKKKVL
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 :
Betacellulin HumanDescription:
Betacellulin Human Recombinant
Product # :
CYT-330Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
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Description
Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Betacellulin Human Recombinant was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.More Info
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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Betacellulin Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized BTC Human 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
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY
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Background
Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine
Introduction
In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.
BTC: The Architect of Cellular Revitalization
BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.
Crafting the Alchemist: Pioneering Methodologies
Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.
Unveiling the Biological Tapestry
Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.
A Flourish of Results
The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.
Charting a Transformative Future
As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.
What is the molecular weight/Mw of BTC Protein?
BTC Protein has a total Mw of 9kDa.
What is the source or expression system of BTC Protein?
Escherichia Coli.
What is the Purity of BTC Protein?
BTC Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BTC Protein?
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.
What is the amino acid sequence of BTC Protein?
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY
What applications can BTC Protein be used in?
BTC Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BTC Protein?
The endotoxin level is minimal, BTC 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.