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1000 results found for “Aprotinin”
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Name :
Cyclophilin A HumanDescription:
Cyclophilin-A Human Recombinant
Peptidylprolyl isomerase A, CYPA, CYPH, MGC12404, MGC23397, MGC117158, PPIase A, Rotamase A, PPIA, Peptidyl-prolyl cis-trans isomerase A, EC 5.2.1.8, Cyclophilin A, Cyclosporin A-binding protein.
Product # :
ENZ-359Price :
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Shipped with Ice Packs
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Description
Cyclophilin-A Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 185 amino acids (1-165 a.a.) and having a molecular mass of 20 kDa. PPIase-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 20mM Tris-HCl 8.0, 20mM NaCl, 0.5mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 650 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37°C in Tris-HCl pH8.0 using chymotrypsin.
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidylprolyl isomerase A, CYPA, CYPH, MGC12404, MGC23397, MGC117158, PPIase A, Rotamase A, PPIA, Peptidyl-prolyl cis-trans isomerase A, EC 5.2.1.8, Cyclophilin A, Cyclosporin A-binding protein.
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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 MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALSTGEKGFGYKG SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSMANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIADCGQLE.
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 :
NAP 2 95 a.a. HumanDescription:
Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Product # :
CHM-277Price :
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Description
NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
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Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
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Physical Appearance
NAP 2 is supplied as a 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
MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD
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 :
APOH Human, sf9Description:
Apolipoprotein-H Human Recombinant, Sf9
Beta-2-glycoprotein 1, Beta-2-glycoprotein I, Apolipoprotein H, Apo-H, B2GPI, Beta(2)GPI, Activated protein C-binding protein, APC inhibitor, Anticardiolipin cofactor, APOH, B2G1, BG, B2GP-1, B2 Glycoprotein-I.
Product # :
PRO-388Price :
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Description
Apolipoprotein-H Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing 326 amino acids and having a molecular mass of 38,200 Dalton (excluding glycosylation), 45kDa total mass. APOH is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
APOH is supplied in 16mM HEPES buffer pH-7.2, 200mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Apolipoprotein H (APOH) attaches to numerous kinds of negatively charged substances for instance heparin, phospholipids, and dextran sulfate. APOH prevents activation of the intrinsic blood coagulation cascade by attaching to phospholipids on the surface of damaged cells. APOH expressed by the liver and secreted in the plasma.
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Synonyms
Beta-2-glycoprotein 1, Beta-2-glycoprotein I, Apolipoprotein H, Apo-H, B2GPI, Beta(2)GPI, Activated protein C-binding protein, APC inhibitor, Anticardiolipin cofactor, APOH, B2G1, BG, B2GP-1, B2 Glycoprotein-I.
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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.
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 :
DPH3P1 HumanDescription:
Diphthamide Biosynthesis 3 Pseudogene 1 Human Recombinant
Diphthamide Biosynthesis 3 Pseudogene 1, C20orf143, DPH3B, ZCSL1, CSL-Type Zinc Finger-Containing Protein 1, Chromosome 20 Open Reading Frame 143, DPH3, KTI11 Homolog (S. Cerevisiae) Pseudogene, DPH3B, KTI11 Homolog B (S. Cerevisiae), Zinc Finger, CSL-Type Containing 1, DPH3 Homolog B (KTI11, S. Cerevisiae), Putative DPH3 Homolog B, Zinc Finger, CSL Domain Containing 1.
Product # :
PRO-1914Price :
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Shipped with Ice Packs
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Description
DPH3P1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 11.1kDa.DPH3P1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DPH3P1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Diphthamide Biosynthesis 3 Pseudogene 1 also known as DPH3P1 may stand for a processed pseudogene of DPH3 since it lacks the exon/intron structurefound in the functional gene. Yet, DPH3P1 does contain an intact open reading frame, though its translation has not been established.
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Synonyms
Diphthamide Biosynthesis 3 Pseudogene 1, C20orf143, DPH3B, ZCSL1, CSL-Type Zinc Finger-Containing Protein 1, Chromosome 20 Open Reading Frame 143, DPH3, KTI11 Homolog (S. Cerevisiae) Pseudogene, DPH3B, KTI11 Homolog B (S. Cerevisiae), Zinc Finger, CSL-Type Containing 1, DPH3 Homolog B (KTI11, S. Cerevisiae), Putative DPH3 Homolog B, Zinc Finger, CSL Domain Containing 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAVFHDE VEIEDFQYDE DSETYFCPCP CGDNFSITKE ELENGEGVAM CPGCSLIIKV IYDKDQFACG ETVPVPSVNK E
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 :
SNAPIN HumanDescription:
SNAP Associated Protein Human Recombinant
SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.
Product # :
PRO-663Price :
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Shipped with Ice Packs
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Description
SNAPIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-136) and having a molecular mass of 17 kDa. SNAPIN is fused to 20 amino acid His Tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl pH-8, 5mM DTT, 2mM EDTA, 0.2M NaCl, and 40% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SNAPIN is involved in the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin. SNAPIN is part of the SNARE complex of proteins that is needed for synaptic vesicle docking and fusion. SNAPAP is enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPIN is also an important factor of the BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.
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Synonyms
SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.
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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 MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINEDQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK.
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 :
EFNA5 HumanDescription:
Ephrin A5 Human Recombinant
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
Product # :
PRO-2327Price :
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Shipped with Ice Packs
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Description
EFNA5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 422 amino acids (21-203 a.a.) and having a molecular mass of 48.1kDa. EFNA5 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNA5 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
Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.
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Synonyms
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
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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
QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH 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 :
EFNB3 HumanDescription:
Ephrin- B3 Human Recombinant
Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.
Product # :
PRO-1169Price :
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Shipped with Ice Packs
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Description
EFNB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-226 a.a) and having a molecular mass of 24.6kDa.EFNB3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
EFNB3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.
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Synonyms
Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.
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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 MGSHMLSLEP VYWNSANKRF QAEGGYVLYP QIGDRLDLLC PRARPPGPHS SPNYEFYKLY LVGGAQGRRC EAPPAPNLLL TCDRPDLDLR FTIKFQEYSP NLWGHEFRSH HDYYIIATSD GTREGLESLQ GGVCLTRGMK VLLRVGQSPR GGAVPRKPVS EMPMERDRGA AHSLEPGKEN LPGDPTSNAT SRGAEGPLPP PSMP.
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 :
CCL28 MouseDescription:
Mucosae-Associated Epithelial Chemokine Mouse Recombinant (CCL28)
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-369Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL28 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.6 kDa. The CCL28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer pH-7.4 and 150mM 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 mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 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
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
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Background
What is the molecular weight/Mw of CCL28 MOUSE Protein?
CCL28 MOUSE Protein has a total Mw of 12.6kDa.
What is the source or expression system of CCL28 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL28 MOUSE Protein?
CCL28 MOUSE Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 MOUSE Protein?
Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL28 MOUSE Protein?
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
What applications can CCL28 MOUSE Protein be used in?
CCL28 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 MOUSE Protein?
The endotoxin level is minimal, CCL28 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 :
PINK1 HumanDescription:
PTEN Induced Putative Kinase 1 Human Recombinant
PTEN induced putative kinase 1, PARK6, protein kinase BRPK, Parkinson disease (autosomal recessive) 6, serine/threonine-protein kinase PINK1 mitochondrial, EC 2.7.11.1.
Product # :
PKA-010Price :
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Shipped with Ice Packs
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Description
PINK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (156-507) and having a molecular mass of 37.9 kDa.PINK1 is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PINK1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 5% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
PINK1 is a serine/threonine protein kinase which is found in the mitochondria. PINK1 shields cells from stress-induced mitochondrial dysfunction. Mutations results in one form of autosomal recessive early-onset Parkinson disease.
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Synonyms
PTEN induced putative kinase 1, PARK6, protein kinase BRPK, Parkinson disease (autosomal recessive) 6, serine/threonine-protein kinase PINK1 mitochondrial, EC 2.7.11.1.
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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
MYLIGQSIGK GCSAAVYEAT MPTLPQNLEV TKSTGLLPGR GPGTSAPGEG QERAPGAPAF PLAIKMMWNI SAGSSSEAIL NTMSQELVPA SRVALAGEYG AVTYRKSKRG PKQLAPHPNI IRVLRAFTSS VPLLPGALVD YPDVLPSRLH PEGLGHGRTL FLVMKNYPCT LRQYLCVNTP SPRLAAMMLL QLLEGVDHLV QQGIAHRDLK SDNILVELDP DGCPWLVIAD FGCCLADESI GLQLPFSSWY VDRGGNGCLM APEVSTARPG PRAVIDYSKA DAWAVGAIAY EIFGLVNPFY GQGKAHLESR SYQEAQLPAL PESVPPDVRQ LVRALLQREA SKRPSARVAA NVL.
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 :
FURIN HumanDescription:
Furin Human Recombinant
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
Product # :
PRO-2199Price :
Quantity :
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Shipped with Ice Packs
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Description
FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.
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Synonyms
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.
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 :
Troponin-C ProteinDescription:
Cardiac Troponin-C Human
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Product # :
PRO-2571Price :
Quantity :
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Description
Troponin-C Human produced from Human Cardiac Tissue, having a molecular mass of 18kDa. The Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.
Source
Human cardiac tissue
Formulation
The protein solution contains 150 mM NaCl, 10 mM sodium phosphate and 0.05% NaN3, (pH 7.0).
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.
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Synonyms
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
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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.
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 :
REN HumanDescription:
Renin Human Recombinant
Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.
Product # :
PRO-1529Price :
Quantity :
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Description
REN Human Recombinant produced in E. coli is a single polypeptide chain containing 365 amino acids (67-406) and having a molecular mass of 39.9kDa. REN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The REN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
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Synonyms
Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.
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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 MGSHMLTLGN TTSSVILTNY MDTQYYGEIG IGTPPQTFKV VFDTGSSNVW VPSSKCSRLY TACVYHKLFD ASDSSSYKHN GTELTLRYST GTVSGFLSQD IITVGGITVT QMFGEVTEMP ALPFMLAEFD GVVGMGFIEQ AIGRVTPIFD NIISQGVLKE DVFSFYYNRD SENSQSLGGQ IVLGGSDPQH YEGNFHYINL IKTGVWQIQM KGVSVGSSTL LCEDGCLALV DTGASYISGS TSSIEKLMEA LGAKKRLFDY VVKCNEGPTL PDISFHLGGK EYTLTSADYV FQESYSSKKL CTLAIHAMDI PPPTGPTWAL GATFIRKFYT EFDRRNNRIG FALAR.
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 :
AK3L1 HumanDescription:
Adenylate Kinase-3 Like 1 Human Recombinant
AK3, Adenylate kinase 3 alpha like 1, AK3L1, AK4.
Product # :
PKA-346Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AK3L1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 259 amino acids (1-223) and having a molecular mass of 29.3 kDa. The AK3L1 is fused with 35 amino acid His-tag at N-terminus.AK3L1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AK3L1 solution containing 20mM Tris-HCl pH-8, 2mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
AK3L1 is an affiliate of the adenylate kinase family of enzymes. AK3L1 enzyme is restricted to the mitochondrial matrix. Adenylate kinases-3 regulates the adenine and guanine nucleotide compositions within a cell by means of catalyzing the reversible transfer of phosphate group among these nucleotides. 5 different isozymes of adenylate kinase have been identified in vertebrates. The enzyme expression of various adenylate kinase isozymes is growth regulated and tissue-specific.
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Synonyms
AK3, Adenylate kinase 3 alpha like 1, AK3L1, AK4.
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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 KDRWGSMASK LLRAVILGPP GSGKGTVSQR IAQNFGLQHL SSGHFLRENIKASTEVGEMA KQYIEKSLLV PDHVITRLMM SELENRRGQH WLLDGFPRTL GQAEALDKIC EVDLVISLNI PFETLKDRLS RRWIHPPSGR VYNLDFNPPH VHGIDDVTGE PLVQQEDDKP EAVAARLRQY KDVAKPVIEL YKSRGVLHQF SGTETNKIWP YVYTLFSNKI TPIQSKEAY.
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 :
Adiponectin Mouse, HEKDescription:
Adiponectin Mouse Recombinant, HEK
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-435Price :
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Shipped at Room temp
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Description
The Acrp30 Mouse Recombinant is fused with FLAG tag having a total Mw of 26kDa.
Source
HEK293 (Human embryonic kidney cell line).
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M PBS buffer,0.075M NaCl, pH7.4.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml. An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.
More Info
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Introduction
Adiponectin is an important negative regulator in hematopoiesis and immune systems. It may be involved in ending inflammatory responses through its inhibitory functions. Inhibits endothelial nf-kappa-b signaling through a camp-dependent pathway. Inhibits tnf-alpha- induced expression of endothelial adhesion molecules. Involved in the control of fat metabolism and insulin sensitivity.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Stability
Store lyophilized APM-1 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to reconstitute the lyophilized Acrp30 Mouse in sterile 18M-cm H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml. An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.
What is the amino acid sequence of ADIPONECTIN Protein?
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
AHSG Human HEKDescription:
Alpha-2-HS-Glycoprotein Human Recombinant HEK
Alpha-2-HS-glycoprotein, Fetuin-A, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, AHSG, FETUA, AHS, A2HS, HSGA, PRO2743.
Product # :
PRO-1644Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
AHSG Human Recombinant produced by transfected human cells is a single polypeptide chain containing 357 amino acids (19-367). AHSG is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
AHSG was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Fetuin is a liver-produced negative acute phase protein composed of two subunits, the A and B chains.
Fetuin homologs have been identified in several species including rat, sheep, pig, rabbit, guinea pig, cattle, mouse and human. Multiple physiological roles for these homologs have been suggested, including ability to bind to hydroxyapatite crystals and to specifically inhibit the tyrosine kinase (TK) activity of the receptor (IR).
Fetuin-A (alpha2-Heremans-Schmid glycoprotein; AHSG) is an important circulating inhibitor of calcification in vivo, and is downregulated during the acute-phase response.
Sera from patients on long-term dialysis with low AHSG concentrations showed impaired ex-vivo capacity to inhibit CaxPO4 precipitation.
Fetuin may influence the resolution of inflammation by modulating the phagocytosis of apoptotic cells by macrophages.
ASHG blocks TGF-beta-dependent signaling in osteoblastic cells, and mice lacking ASHG display growth plate defects, increased bone formation with age, and enhanced cytokine-dependent osteogenesis. -
Synonyms
Alpha-2-HS-glycoprotein, Fetuin-A, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotein, AHSG, FETUA, AHS, A2HS, HSGA, PRO2743.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized AHSG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AHSG 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 AHSG in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIE
IDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRK
VCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTD
CVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCTVFQTQPVTSQPQPEGANEAVPTP
VVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSH
PRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKVVDHHHHHH.
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 :
MRPL28 HumanDescription:
Mitochondrial Ribosomal Protein L28 Human Recombinant
MAAT1, p15, 39S ribosomal protein L28, mitochondrial, L28mt, MRP-L28, Melanoma-associated antigen recognized by T-lymphocytes.
Product # :
PRO-1279Price :
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Description
MRPL28 Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (56-256) and having a molecular mass of 25.8 kDa. MRPL28 is fused to 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MRPL28 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.5), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
MRPL28 is found in a variety of normal tissues such as spleen, testis, thymus, liver, kidney, brain, adrenal, lung and retinal tissue. 39S ribosomal protein L28, mitochondrial (MRPL28), is a part of the ribosomal protein L28P family. Mammalian mitochondrial ribosomal proteins encoded by nuclear genes and helps in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL28 is an important therapeutic reagent for HLA-A24 (A24) patients since this antigen is distinguished by tumor-infiltrating lymphocyte (TIL) 1290, which targets the A24 serotype.
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Synonyms
MAAT1, p15, 39S ribosomal protein L28, mitochondrial, L28mt, MRP-L28, Melanoma-associated antigen recognized by T-lymphocytes.
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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 MNGQRERVED VPIPIYFPPE SQRGLWGGEG WILGQIYANN DKLSKRLKKV WKPQLFEREF YSEILDKKFT VTVTMRTLDL IDEAYGLDFY ILKTPKEDLC SKFGMDLKRG MLLRLARQDP QLHPEDPERR AAIYDKYKEF AIPEEEAEWV GLTLEEAIEK QRLLEEKDPV PLFKIYVAEL IQQLQQQALS EPAVVQKRAS GQ.
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 :
HP-NAPDescription:
Neutrophil-activating protein A Helicobacter Pylori Recombinant
DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.
Product # :
PRO-2035Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
HP-NAP Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Ala144) containing 154 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 18.2kDa.
Source
Escherichia Coli.
Formulation
HP-NAP was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.
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Synonyms
DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. HP-NAP 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
MKHHHHHHASMKTFEILKHL QADAIVLFMK VHNFHWNVKG TDFFNVHKAT EEIYEEFADM FDDLAERIVQ LGHHPLVTLS EAIKLTRVKE ETKTSFHSKD IFKEILEDYK YLEKEFKELS NTAEKEGDKV TVTYADDQLA KLQKSIWMLQ AHLA.
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 :
APTX HumanDescription:
Aprataxin Human Recombinant
AXA1, AOA, FHA-HIT, AOA11, ataxia 1, early onset with hypoalbuminemia1 EOAHA1, EAOH1, Forkhead-associated domain histidine triad-like protein, APTX, Aprataxin, AOA1, EAOH, EOAHA, MGC1072, FLJ20157.
Product # :
PRO-790Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
APTX Human Recombinant fused to a 37 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids (1-168 a.a) and having a molecular mass of 23.9 kDa. The APTX is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The APTX solution contains 20mM Tris-HCl pH-7.5, 0.1M NaCl, 0.1mM PMSF and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
APTX is a DNA-binding protein which participates in single-strand DNA break repair, double-strand DNA break repair and base excision repair. APTX determines abortive DNA ligation intermediates created each at base excision sites, or while DNA ligases attempt to restore non-ligatable breaks induced by reactive oxygen species. APTX catalyzes the release of adenylate groups covalently linked to 5''-phosphate termini, resulting in the production of 5''-phosphate termini that can be efficiently rejoined. APTX hydrolyzes adenosine 5''-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity.
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Synonyms
AXA1, AOA, FHA-HIT, AOA11, ataxia 1, early onset with hypoalbuminemia1 EOAHA1, EAOH1, Forkhead-associated domain histidine triad-like protein, APTX, Aprataxin, AOA1, EAOH, EOAHA, MGC1072, FLJ20157.
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Physical Appearance
Sterile Filtered clear 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 KDRWAGSMQD PKMQVYKDEQ VVVIKDKYPK ARYHWLVLPW TSISSLKAVA REHLELLKHM HTVGEKVIVD FAGSSKLRFR LGYHAIPSMS HVHLHVISQD FDSPCLKNKK HWNSFNTEYF LESQAVIEMV QEAGRVTVRD GMPELLKLPL RCHECQQLLP SIPQLKEHLR KHWTQ.
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 HumanDescription:
Noggin Human Recombinant
SYM1, SYNS1, NOG.
Product # :
CYT-475Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.
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
SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC. -
Background
Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.
Abstract:
Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.
Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.
This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.
Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
- Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.
Molecular Characteristics of Noggin :
- This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.
Inhibition of BMP Signaling by Noggin:
- Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.
Physiological Functions of Noggin:
- Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.
Therapeutic Implications of Noggin:
- The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.
Clinical Studies and Translational Research:
- This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.
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 :
EFNB1 Human, Sf9Description:
Ephrin-B1 Human Recombinant, Sf9
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
Product # :
PRO-2543Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
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- More Info
Description
EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNB1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.
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Synonyms
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPLAKNLEP VSWSSLNPKF LSGKGLVIYP KIGDKLDIIC PRAEAGRPYE YYKLYLVRPE QAAACSTVLD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL EFKKHHDYYI TSTSNGSLEG LENREGGVCR TRTMKIIMKV GQDPNAVTPE QLTTSRPSKE ADNTVKMATQ APGSRGSLGD
SDGKHETVNQ EEKSGPGASG GSSGDPDGFF NSKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN
QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH 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.
- View Data Sheet
Name :
SPINT2 Human, Sf9Description:
Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant, Sf9
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
Product # :
PRO-2219Price :
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Shipped with Ice Packs
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Description
SPINT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 176 amino acids (28-197 a.a.) and having a molecular mass of 20kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SPINT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SPINT2 protein solution (0.2mg/ml) contains phosphate buffered saline (pH 7.4) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
SPINT2 is a transmembrane protein acts as an inhibitor of HGF activator. SPINT2 inhibits plasmin, plasma and tissue kallikrein, and factor XIa. SPINT2 has two extracellular Kunitz domains that inhibit few serine proteases. SPINT2 is assumed tumor suppressor, mutations in SPINT2 leads to a congenital sodium diarrhea.
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Synonyms
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
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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.
-
Amino Acid Sequence
ADRERSIHDF CLVSKVVGRC RASMPRWWYN VTDGSCQLFV YGGCDGNSNN YLTKEECLKK CATVTENATG DLATSRNAAD SSVPSAPRRQ DSEDHSSDMF NYEEYCTANA VTGPCRASFP RWYFDVERNS CNNFIYGGCR GNKNSYRSEE ACMLRCFRQQ ENPPLPLGSK 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.
- View Data Sheet
Name :
Omentin Human, HisDescription:
Omentin Human Recombinant, His Tag
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-551Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
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Description
Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
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 insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-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 His Tag 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 His Tag 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
MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.
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Applications
Elisa
Western blot.
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 :
EPHB4 HumanDescription:
EPH Receptor B4 Human Recombinant
Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.
Product # :
PRO-2592Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EPHB4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (16-539a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 532 amino acids and having a molecular mass of 58.1 kDa. EPHB4 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPHB4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
EPHB4 or Ephrin type-B receptor 4 is encoded by the EPHB4 gene in humans. The receptor and its ligands (the ephrins) take part in different developmental stages, mainly in the nervous system. EPHB4 and other Ephrin receptors are the biggest subgroup of the RTK receptors. EPHB4 binds to ephrin B2 and has a crucial part in the development of the vascular system.
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Synonyms
Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.
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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
LEETLLNTKL ETADLKWVTF PQVDGQWEEL SGLDEEQHSV RTYEVCDVQR APGQAHWLRT GWVPRRGAVH VYATLRFTML ECLSLPRAGRSCKETFTVFY YESDADTATA LTPAWMENPY IKVDTVAAEH LTRKRPGAEA TGKVNVKTLR LGPLSKAGFY LAFQDQGACM ALLSLHLFYK KCAQLTVNLT RFPETVPREL VVPVAGSCVV DAVPAPGPSP SLYCREDGQW AEQPVTGCSC APGFEAAEGN TKCRACAQGT FKPLSGEGSC QPCPANSHSN TIGSAVCQCR VGYFRARTDP RGAPCTTPPS APRSVVSRLN GSSLHLEWSA PLESGGREDL TYALRCRECR PGGSCAPCGG DLTFDPGPRD LVEPWVVVRG LRPDFTYTFE VTALNGVSSL ATGPVPFEPV NVTTDREVPP AVSDIRVTRS SPSSLSLAWA VPRAPSGAVL DYEVKYHEKG AEGPSSVRFL KTSENRAELR GLKRGASYLV QVRARSEAGY GPFGQEHHSQ TQLDESEGWR EQLAVEHHHH 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.
- View Data Sheet
Name :
OTOR HumanDescription:
Otoraplin Human Recombinant
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
Product # :
CYT-582Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Otoraplin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.7 kDa.The OTOR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OTOR protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM NaCl.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness. -
Synonyms
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized OTOR Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OTOR should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Otoraplin 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
VHGIFMDRLASKKLCADDECVYTISLASAQEDYNAPDCRFINVKKGQQIYVYS
KLVKENGAGEFWAGSVYGDGQDEMGVVGYFPRNLVKEQRVYQEATKEVPTT
DIDFFCE.
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.