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557 results found for “Homeobox”
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Name :
CNTF Rat, HisDescription:
Ciliary Neurotrophic Factor Rat Recombinant, His Tag
Ciliary neurotrophic factor, CNTF, Cntf.
Product # :
CYT-926Price :
Quantity :
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Shipped with Ice Packs
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Description
CNTF Rat Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-200a.a) and having a molecular mass of 25.2kDa.CNTF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNTF protein solution (0.5mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
Ciliary neurotrophic factor, CNTF, Cntf.
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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 MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
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Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 25.2kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
The biological functionality of CNTF Protein will be determined in the future.
What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF 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 :
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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Shipped with Ice Packs
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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 :
BDNF Human, CHODescription:
Brain-Derived Neurotrophic Factor Human Recombinant, CHO
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-1262Price :
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Shipped at Room temp
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Description
Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
CHO Cells
Formulation
The protein was lyophilized with 5% trehalose and 1x PBS
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.sds-page
More Info
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Introduction
BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.
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Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF 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
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
CHO Cells
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.
What is the amino acid sequence of BDNF Protein?
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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References
Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
Link:BDNF prospec publication
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 :
HMGN3 HumanDescription:
High Mobility Group Nucleosomal Binding Domain 3 Human Recombinant
High Mobility Group Nucleosomal Binding Domain 3, TRIP7, TR-Interacting Protein 7, High Mobility Group Nucleosome-Binding Domain-Containing Protein 3, Thyroid Hormone Receptor Interacting Protein 7, Thyroid Receptor-Interacting Protein 7, Thyroid Hormone Receptor Interactor 7, PNAS-24, PNAS-25, TRIP-7, High mobility group nucleosome-binding domain-containing protein 3.
Product # :
PRO-2068Price :
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Description
HMGN3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77 a.a) and having a molecular mass of 10.8 kDa. HMGN3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HMGN3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH7.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
High Mobility Group Nucleosomal Binding Domain 3 (HMGN3), binds thyroid hormone receptor beta, however it occurs only in the presence of thyroid hormone. Thyroid hormone receptors are hormone-dependent transcription factors which regulate expression of a variety of particular target genes. HMGN3 is considered to reduce the compactness of the chromatin fiber in nucleosomes, in that way enhancing transcription from chromatin templates.
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Synonyms
High Mobility Group Nucleosomal Binding Domain 3, TRIP7, TR-Interacting Protein 7, High Mobility Group Nucleosome-Binding Domain-Containing Protein 3, Thyroid Hormone Receptor Interacting Protein 7, Thyroid Receptor-Interacting Protein 7, Thyroid Hormone Receptor Interactor 7, PNAS-24, PNAS-25, TRIP-7, High mobility group nucleosome-binding domain-containing protein 3.
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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 MGSMPKRKSP ENTEGKDGSK VTKQEPTRRS ARLSAKPAPP KPEPKPRKTS AKKEPGAKIS RGAKGKKEEK QEAGKEGTEN.
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 :
HRPDescription:
Horseradish Peroxidase
Horseradish Peroxidase, HRP, EC 1.11.1.7.
Product # :
ENZ-321Price :
Quantity :
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Shipped at Room temp
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Description
HRP consists of the basic isoenzyme having a molecular weight of 44 kDa.The Horseradish Peroxidase is purified by affinity chromatography, which results in an enzyme of high specific activity and purity.
Source
Root extracts of horseradish.
Purity
(A403/A275) = RZ: 3.0.
Biological Activity
276 U/mg (25°C, guaiacol as the hydrogen donor, pH-7 and H2O2 as substrates).
More Info
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Introduction
The enzyme horseradish peroxidase, found in horseradish, is used extensively in molecular biologyand in antibody amplification and detection, among other things. For example, "In recent years the technique of marking neurons with the enzyme horseradish peroxidase (HRP) has become a major tool. In its brief history, this method has probably been used by more neurobiologists than have used the Golgi stainsince its discovery in 1870." Horseradish peroxidase is also highly used in techniques such as Western blottingand ELISAs.
HRP is widely used as an enzymatic label in immunoassays. Usually, the enzyme is coupled to antibodies, lectins or haptens. Coupling to antibodies etc. may be performed through the carbohydrate side chains of the HRP. -
Synonyms
Horseradish Peroxidase, HRP, EC 1.11.1.7.
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Physical Appearance
Sterile Filtered red-brown lyophilized powder.
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Stability
Lyophilized HRP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HRP 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 HRP in sterile 18MΩ-cm H2O not less than 100 µg/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.
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Name :
Epigen Human, HisDescription:
Epigen Human Recombinant, His Tag
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
Product # :
CYT-794Price :
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Shipped with Ice Packs
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Description
EPGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (23-110 a.a) and having a molecular mass of 12.1kDa.EPGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EPGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.
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Synonyms
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K
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Background
What is the molecular weight/Mw of EPIGEN Protein?
EPIGEN Protein has a total Mw of 12.1kDa.
What is the source or expression system of EPIGEN Protein?
Escherichia Coli.
What is the Purity of EPIGEN Protein?
EPIGEN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EPIGEN Protein?
The biological functionality of EPIGEN Protein will be determined in the future.
What is the amino acid sequence of EPIGEN Protein?
MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K
What applications can EPIGEN Protein be used in?
EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPIGEN Protein?
The endotoxin level is minimal, EPIGEN 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 :
LACTB E.coli, HisDescription:
Beta Lactamase E.coli Recombinant, His Tag
Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.
Product # :
ENZ-088Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Beta Lactamase is an E.coli Recombinant protein produced in E.Coli containing 379 amino acids (20-377) and having a molecular mass of 41.8kDa. Beta Lactamase is expressed with a 21 N-terminal His tag.The LACTB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LACTB enzyme (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.
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Synonyms
Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.
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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 MAPQQINDIV HRTITPLIEQ QKIPGMAVAV IYQGKPYYFT WGYADIAKKQ PVTQQTLFEL GSVSKTFTGV LGGDAIARGE IKLSDPTTKY WPELTAKQWN GITLLHLATY TAGGLPLQVP DEVKSSSDLL RFYQNWQPAW APGTQRLYAN SSIGLFGALA VKPSGLSFEQ AMQTRVFQPL KLNHTWINVP PAEEKNYAWG YREGKAVHVS PGALDAEAYG VKSTIEDMAR WVQSNLKPLD INEKTLQQGI QLAQSRYWQT GDMYQGLGWE MLDWPVNPDS IINGSDNKIA LAARPVKAIT PPTPAVRASW VHKTGATGGF GSYVAFIPEK ELGIVMLANK NYPNPARVDA AWQILNALQ.
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 :
UBE2I Human HisDescription:
Ubiquitin-Conjugating Enzyme E2I Human Recombinant, His Tag
SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.
Product # :
ENZ-274Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ubiquitin-Conjugating Enzyme E2I Human Recombinant produced in E.coli is a 19.5 kDa protein containing 171 amino acids.The UBE2I protein contains 6xHis tag and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated (1mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Human Ubquitin Conjugating Enzyme 9 (Ubc9) is a member of the E2 family and is specific for the conjugation of SUMO to a variety of target proteins. SUMO conjugation to target proteins is mediated by a different, but analogous, pathway to ubiquitinylation. This E2 is unusual in that it interacts directly with protein substrates that are modified by sumolyation, and may play a role in substrate recognition. Ubc9 can mediate the conjugation of SUMO-1 to a variety of proteins including RanGAP1, I?B?, and PML without the requirement of an E3 ligase.
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Synonyms
SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized UBE2I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2I 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 UBE2I 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
MHHHHHHAMGTLNMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGT
MNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFH
PNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTI
YCQNRVEYEKRVRAQAKKFAPS.
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 :
CXCL3 Mouse, HisDescription:
GRO-Gamma Mouse Recombinant (CXCL3), His Tag
C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.
Product # :
CHM-283Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GRO-g Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (28-100 a.a.) and having a molecular mass of 10.6kDa.CXCL3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GRO-gamma protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.15M NaCl and 5mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
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Synonyms
C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.
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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 MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.
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Background
What is the molecular weight/Mw of CXCL3 MOUSE, HIS Protein?
CXCL3 MOUSE, HIS Protein has a total Mw of 10.6kDa.
What is the source or expression system of CXCL3 MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL3 MOUSE, HIS Protein?
CXCL3 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 MOUSE, HIS Protein?
The biological functionality of CXCL3 MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL3 MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.
What applications can CXCL3 MOUSE, HIS Protein be used in?
CXCL3 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 MOUSE, HIS Protein?
The endotoxin level is minimal, CXCL3 MOUSE, 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.
- View Data Sheet
Name :
CXCL1 Mouse, HisDescription:
GRO/KC (CXCL1) Mouse Recombinant, His Tag
Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.
Product # :
CHM-002Price :
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Shipping Method :
Shipped with Ice Packs
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Description
GRO1/KC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (25-96 a.a.) and having a molecular mass of 10.5kDa.GRO1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GRO1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
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Synonyms
Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.
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Background
What is the molecular weight/Mw of CXCL1 MOUSE, HIS Protein?
CXCL1 MOUSE, HIS Protein has a total Mw of 10.5kDa.
What is the source or expression system of CXCL1 MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL1 MOUSE, HIS Protein?
CXCL1 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL1 MOUSE, HIS Protein?
The biological functionality of CXCL1 MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL1 MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.
What applications can CXCL1 MOUSE, HIS Protein be used in?
CXCL1 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL1 MOUSE, HIS Protein?
The endotoxin level is minimal, CXCL1 MOUSE, 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.
- View Data Sheet
Name :
HAO1 HumanDescription:
Hydroxyacid Oxidase 1 Human Recombinant
Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.
Product # :
ENZ-162Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HAO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-370 a.a.) and having a molecular mass of 45kDa.HAO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HAO1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.5M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Glycolate oxidase (HAO1) belongs to the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyzes the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate with reduction of oxygen to hydrogen peroxide. HAO1 is most abundantly expressed in the liver and pancreas and is most active on twocarbon substrates such as glycolate. Lately, HAO1 has been identified as a key contributor to hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.
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Synonyms
Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMLPR LICINDYEQH AKSVLPKSIY DYYRSGANDE ETLADNIAAF SRWKLYPRML RNVAETDLST SVLGQRVSMP ICVGATAMQR MAHVDGELAT VRACQSLGTG MMLSSWATSS IEEVAEAGPE ALRWLQLYIY KDREVTKKLV RQAEKMGYKA IFVTVDTPYL GNRLDDVRNR FKLPPQLRMK NFETSTLSFS PEENFGDDSG LAAYVAKAID PSISWEDIKW LRRLTSLPIV AKGILRGDDA REAVKHGLNG ILVSNHGARQ LDGVPATIDV LPEIVEAVEG KVEVFLDGGV RKGTDVLKAL ALGAKAVFVG RPIVWGLAFQ GEKGVQDVLE ILKEEFRLAM ALSGCQNVKV IDKTLVRKNP LAVSKI.
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 :
HBQ1 HumanDescription:
Hemoglobin Theta 1 Human Recombinant
Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.
Product # :
PRO-1616Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HBQ1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-142) and having a molecular mass of 17.9kDa.HBQ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HBQ1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
HBQ1 is a member of the Hemoglobin family. Hemoglobin is a 66.7 kDa protein attached to four iron-binding, methenelinked tetrapyrrole rings (heme). The globin part of Hemoglobin contains 2 alpha chains and 2 beta chains organized as couples creating a tetramer. Every one of the 4 globin chains covalently connects with a heme group. The bonds between alpha and beta chains are frailer than between parallel globin chains, thus creating a cleavage plane which is vital for oxygen binding and release. Relaxation of the alpha1-beta2 cleavage plane results in high affinity for oxygen.
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Synonyms
Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.
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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 MGSMALSAED RALVRALWKK LGSNVGVYTT EALERTFLAF PATKTYFSHL DLSPGSSQVR AHGQKVADAL SLAVERLDDL PHALSALSHL HACQLRVDPA SFQLLGHCLL VTLARHYPGD FSPALQASLD KFLSHVISAL VSEYR
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 :
4 1BBL Human, HisDescription:
4-1BB Ligand Human Recombinant, His Tag
CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.
Product # :
CYT-649Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
TNFSF9 Human Recombinant fused to 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (71-254 a.a.) and having a molecular mass of 23.8 kDa. The TNFSF9 37 aa His tag fusion protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Recombinant 4-1BBL solution (1mg/ml) contains 20mM Tris-HCl buffer pH-8, 100mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE
sds-page
More Info
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Introduction
4-1BBL is a transmembrane cytokine that is part of the tumor necrosis factor (TNF) ligand family. 4-1BBL is a bidirectional signal transducer that performs as a ligand for TNFRSF9, which is a costimulatory receptor molecule in T lymphocytes. TNFSF9 and its TNFRSF9 take part in the antigen presentation development and in the generation of cytotoxic T cells. 4-1BBR is absent from resting T lymphocytes but rapidly expressed upon antigenic stimulation. TNFSF9 reactivates anergic T lymphocytes as well as promoting T lymphocyte proliferation. 4-1BB Ligand is needed for the optimal CD8 responses in CD8 T cells. 4-1BBL is expressed in carcinoma cell lines, and is thought to be involved in T cell-tumor cell interaction. 4-1BBL is expressed by activated B cells, macrophages, dendritic cells, activated T cells, neurons and astrocytes. The interaction of 4-1BB with TNFRSF9 strongly regulates immunity and has been proposed to preferentially control T cell responses based on studies in various murin
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Synonyms
CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMRE GPELSPDDPA GLLDLRQGMF AQLVAQNVLL IDGPLSWYSD PGLAGVSLTGGLSYKEDTKE LVVAKAGVYY VFFQLELRRV VAGEGSGSVS LALHLQPLRS AAGAAALALT VDLPPASSEA RNSAFGFQGR LLHLSAGQRL GVHLHTEARA RHAWQLTQGA TVLGLFRVTP EIPAGLPSPR SE.
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 :
Omentin HumanDescription:
Omentin Human Recombinant
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-301Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 313 amino acids and having a molecular mass of 35 kDa. Intelectin is purified by proprietary chromatographic techniques.
Source
E.Coli.
Formulation
Each mg of lyophilized powder contains 10mM NaP, pH-7.5 and 5:1 mannitol to protein.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase INSstimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of INS presence. Its role in glucose metabolism and obesity remains to be described; an INS-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
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Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Intelectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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 Omentin 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
MNQLSFLLFL IATTRGWSTD EANTYFKEWTCSSSPSLPRS CKEIKDECPS AFDGLYFLRT ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKADY PEGDGNWANY NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS REITEAAVLLFYR.
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 :
BHMT AntibodyDescription:
Betaine Homocysteine S-Methyltransferase, Mouse Anti Human
BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.
Product # :
ANT-373Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
Betaine-homocysteine methyltransferase (BHMT) is a cytosolic enzyme that catalyzes the conversion of betaine and homocysteine to dimethylglycine and methionine, respectively. BHMT displays differential expression in a model of liver cirrhosis.
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Synonyms
BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human BHMT mAb is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human BHMT amino acids 1-406 purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
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Clone
P3D6AT.
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Applications
BHMT antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
BHMT antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
GMNN AntibodyDescription:
Geminin, Mouse Anti Human
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
Product # :
ANT-319Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
-
Introduction
Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. G
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Synonyms
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
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Immunogen
Anti-human Geminin mAb is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Geminin amino acids 1-209 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P2H7AT.
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Applications
Geminin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1,000. Recommended starting dilution is 1:500.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
Geminin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
SF20 Mouse, HisDescription:
MYDGF Mouse Recombinant, His Tag
D17Wsu104e, Il25, Ly6elg, MYDGF, Interleukin-25, IL-25, Stromal cell-derived growth factor SF20.
Product # :
CYT-1040Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
MYDGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (25-166 a.a) and having a molecular mass of 18.1kDa. MYDGF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYDGF protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Myeloid-derived growth factor (Mydgf) is a paracrine-acting protein and a bone marrow-derived monocyte which stimulates cardiac myocyte survival and adaptive angiogenesis for cardiac protection and repair after myocardial infarction. Mydgf induces endothelial cell proliferation through a MAPK1/3-, STAT3- and CCND1-mediated signaling lane. When comparing wild-type mice to mice with a Mydgf-deficiency, the later develop larger infarct scars and more acute contractile dysfunction.
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Synonyms
D17Wsu104e, Il25, Ly6elg, MYDGF, Interleukin-25, IL-25, Stromal cell-derived growth factor SF20.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVSEPTTV PFDVRPGGVV HSFSQDVGPG NKFTCTFTYA SQGGTNEQWQ MSLGTSEDSQ HFTCTIWRPQ GKSYLYFTQF KAELRGAEIE YAMAYSKAAF ERESDVPLKS EEFEVTKTAV SHRPGAFKAE LSKLVIVAKA ARSEL.
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 :
Noggin Human, HEKDescription:
Noggin Human Recombinant, HEK
Noggin, Symphalangism 1 (Proximal), Synostoses (Multiple) Syndrome 1, SYNS1A, SYNS1, SYM1.
Product # :
CYT-977Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Noggin produced in HEK293 cells is a polypeptide chain containing 211 amino acids (28-232a.a.) and having a molecular mass of 23.8kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).Noggin is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
Recombinant Human Noggin hek293 derived protein is provided as a solution (0.25mg/ml) containing 50mM MES (pH 6.5) and 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
Noggin, Symphalangism 1 (Proximal), Synostoses (Multiple) Syndrome 1, SYNS1A, SYNS1, SYM1.
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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
QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSCHHHHH 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.
- View Data Sheet
Name :
TGFB2 Human, HEKDescription:
Transforming Growth Factor-Beta 2 Human Recombinant, HEK
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Product # :
CYT-112Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
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Description
TGF-b 2 Human Recombinant produced in HEK cells is a non-glycosylated homodimer, having a total molecular weight of 25kDa.The TGF-b 2 is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
TGF-b 2 was lyophilized from a 0.2µm filtered solution containing 50mM sodium acetate pH 4.5.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2), the ED50 is 0.16ng/ml.More Info
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Introduction
TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-beta (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.
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Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGF-b 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 2 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 TGF-b 2 in sterile solution containing 20% ethanol, 50mM sodium acetate and 75mM acetic acid.
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 :
SORBS3 HumanDescription:
Sorbin And SH3 Domain Containing 3 Human Recombinant
Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.
Product # :
PRO-1829Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SORBS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329) and having a molecular mass of 39.1 kDa. SORBS3 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The SORBS3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.
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Synonyms
Sorbin And SH3 Domain Containing 3, SCAM1, Vinexin Beta (SH3-Containing Adaptor Molecule-1), vinexin, SH3-Containing Adapter Molecule 1.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADGGSP FLGRRDFVYP SSTRDPSASN GGGSPARREE KKRKAARLKF DFQAQSPKEL TLQKGDIVYI HKEVDKNWLE GEHHGRLGIF PANYVEVLPA DEIPKPIKPP TYQVLEYGEA VAQYTFKGDL EVELSFRKGE HICLIRKVNE NWYEGRITGT GRQGIFPASY VQVSREPRLR LCDDGPQLPT SPRLTAAARS ARHPSSPSAL RSPADPIDLG GQTSPRRTGF SFPTQEPRPQ TQNLGTPGPA LSHSRGPSHP LDLGTSSPNT SQIHWTPYRA MYQYRPQNED ELELREGDRV DVMQQCDDGW FVGVSRRTQK FGTFPGNYVA PV
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 :
IL19 Human, HEKDescription:
Interleukin-19 Human Recombinant, HEK
Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19
Product # :
CYT-1192Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL19 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-177) containing 164 amino acids and having a molecular mass of 19.1 kDa.IL19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
IL19 protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
IL19 is a cytokine that belongs to the IL10 cytokine subfamily. IL-19 is found to be preferentially expressed in monocytes. IL19 binds the IL20 receptor complex and lead to the activation of the signal transducer and activator of transcription 3 (STAT3). A similar cytokine in mouse is reported to up-regulate the expression of IL6 and TNF-alpha and induce apoptosis, which suggests a role of this cytokine in inflammatory responses. Alternatively spliced transcript variants encoding the distinct isoforms have been described.
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Synonyms
Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19
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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
DGSHMLRRCL ISTDMHHIEE SFQEIKRAIQ AKDTFPNVTI LSTLETLQII KPLDVCCVTK NLLAFYVDRV FKDHQEPNPK ILRKISSIAN SFLYMQKTLR QCQEQRQCHC RQEATNATRV IHDNYDQLEV HAAAIKSLGE LDVFLAWINK NHEVMFSAHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Tamm HorsfallDescription:
Recombinant Human Tamm Horsfall Glycoprotein
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Product # :
ENZ-1206Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- SDS-PAGE
Description
Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.
Source
HEK293
Formulation
The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE analysis.
SDS-PAGE
More Info
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Introduction
Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
Reduced Uromodulin levels is associated with chronic kidney disease.
UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.
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Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD should be stored at 4C between 2-7 days and for future use below -18C.
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
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH
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Background
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.
What is the molecular weight/Mw of UMOD Protein?
UMOD Protein has a total Mw of 65kDa.
What is the source or expression system of UMOD Protein?
HEK293.
What is the Purity of UMOD Protein?
UMOD Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of UMOD Protein?
The biological functionality of UMOD Protein will be determined in the future.
What is the amino acid sequence of UMOD Protein?
UMOD Protein is composed from 595 amino acids.
What applications can UMOD Protein be used in?
UMOD Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for UMOD Protein?
The endotoxin level is minimal, UMOD 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 :
NT 3 HumanDescription:
Neurotrophin-3 Human Recombinant
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
Product # :
CYT-257Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 0.1% TFA.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.
More Info
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Introduction
NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.
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Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.
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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 2.165 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 NT-3 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 :
IFN tau OvineDescription:
IFN-Tau Ovine Recombinant
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
Product # :
CYT-377Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
IFN-Tau Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19914.7 Dalton.The IFN-Tau is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by both:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.More Info
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Introduction
IFN-tau is also known as TP-1 (trophoblast protein-1) is a new class of type I IFN that is secreted by the trophoblast and is the signal for maternal recognition of pregnancy in sheep. IFN- tau has potent immunosuppressive and antiviral activities similar to other type I IFN but is less cytotoxic than IFN-alpha and IFN-beta. The current investigation concerns the effect of recombinant ovine IFN- tau (rOIFN- tau) on the modulation of MHC class I and II expression on cloned mouse cerebrovascular endothelial (CVE) cells.
IFN-tau induced tyrosine phosphorylation of Stat1 and upregulated the expression of MHC class I on CVE. One proposed action by which type I IFN reduces the relapse rate in MS is via interference with IFN-?-induced MHC class II expression. IFN- tau was shown to downregulate IFN-?-induced MHC class II expression on CVE and, hence, may be of potential therapeutic value in downregulating inflammation in the central nervous system (CNS). IFN- tau did not upregulate the expression of MHC class II on CVE. IFN- tau also inhibited the replication of Theiler's virus in CVE. -
Synonyms
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-Tau although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Tau 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 IFN Tau 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 Cys-Tyr-Leu-Ser-Arg.
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Background
What is the molecular weight/Mw of IFN TAU OVINE Protein?
IFN TAU OVINE Protein has a total Mw of 19.9kDa.
What is the source or expression system of IFN TAU OVINE Protein?
Escherichia Coli.
What is the Purity of IFN TAU OVINE Protein?
IFN TAU OVINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN TAU OVINE Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.
What is the amino acid sequence of IFN TAU OVINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.
What applications can IFN TAU OVINE Protein be used in?
IFN TAU OVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN TAU OVINE Protein?
The endotoxin level is minimal, IFN TAU OVINE 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.