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1000 results found for “sclerostin”
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Name :
VEGF Mouse, HisDescription:
Vascular Endothelial Growth Factor Mouse Recombinant, His Tag
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, Vegf120, Vegf164, Vegf188, Vegfa.
Product # :
CYT-680Price :
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Shipped with Ice Packs
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Description
VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (205-324 a.a.) and having a total molecular mass of 16.3kDa. Mouse VEGF is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Mouse VEGF contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using NIH-3T3 mouse embryonic fibroblast. The ED50 for this effect is 0.5-1.5ng/ml.More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, Vegf120, Vegf164, Vegf188, Vegfa.
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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 MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKPR R.
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 :
CRMP1 HumanDescription:
Collapsin Response Mediator Protein-1 Human Recombinant
Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, CRMP1, DPYSL1, DRP1.
Product # :
PRO-493Price :
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Description
CRMP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (1-572 a.a) and having a molecular mass of 64.8kDa (Will appear as multiple bands on SDS-PAGE).CRMP1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRMP1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol, 1mM DTT and 0.2mM PMSF.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The X-ray crystal structure of murine CRMP1 was determined at 2.1 resolution and demonstrates that CRMP1 is a bilobed ‘lung-shaped’ protein forming a tetrameric assembly.
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Synonyms
Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, CRMP1, DPYSL1, DRP1.
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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 MGSEFMSYQG KKSIPHITSD RLLIKGGRII NDDQSLYADV YLEDGLIKQI GENLIVPGGV KTIEANGRMV IPGGIDVNTY LQKPSQGMTA ADDFFQGTRA ALVGGTTMII DHVVPEPGSS LLTSFEKWHE AADTKSCCDY SLHVDITSWY DGVREELEVL VQDKGVNSFQ VYMAYKDVYQ MSDSQLYEAF TFLKGLGAVI LVHAENGDLI AQEQKRILEM GITGPEGHAL SRPEELEAEA VFRAITIAGR INCPVYITKV MSKSAADIIA LARKKGPLVF GEPIAASLGT DGTHYWSKNW AKAAAFVTSP PLSPDPTTPD YLTSLLACGD LQVTGSGHCP YSTAQKAVGK DNFTLIPEGV NGIEERMTVV WDKAVATGKM DENQFVAVTS TNAAKIFNLY PRKGRIAVGS DADVVIWDPD KLKTITAKSH KSAVEYNIFE GMECHGSPLV VISQGKIVFE DGNINVNKGM GRFIPRKAFP EHLYQRVKIR NKVFGLQGVS RGMYDGPVYE VPATPKYATP APSAKSSPSK HQPPPIRNLH QSNFSLSGAQ IDDNNPRRTG HRIVAPPGGR SNITSLG.
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 :
CRYGD HumanDescription:
Crystallin, Gamma D Human Recombinant
Gamma-crystallin D, Gamma-D-crystallin, Gamma-crystallin 4, CRYGD, CRYG4, CCP; CACA, CCA3, cry-g-D.
Product # :
PRO-913Price :
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Description
CRYGD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 194 amino acids (1-174 a.a.) and having a molecular mass of 22.9kDa.CRYGD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRYGD protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRYGD is a member of the beta/gamma-crystallin family. Crystallins are the principal structural components of the vertebrate eye lens. The mammalian lens crystallins are divided into alpha, beta, and gamma families. Gamma-crystallins are involved in cataract formation. Defects in the CRYGD gene are responsible for cataract autosomal dominant (ADC), cataract congenital non-nuclear polymorphic autosomal dominant (CCP), cataract congenital cerulean type 3 (CCA3) and cataract crystalline aculeiform (CACA).
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Synonyms
Gamma-crystallin D, Gamma-D-crystallin, Gamma-crystallin 4, CRYGD, CRYG4, CCP; CACA, CCA3, cry-g-D.
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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 MGKITLYEDR GFQGRHYECS SDHPNLQPYL SRCNSARVDS GCWMLYEQPN YSGLQYFLRR GDYADHQQWM GLSDSVRSCR LIPHSGSHRI RLYEREDYRG QMIEFTEDCS CLQDRFRFNE IHSLNVLEGS WVLYELSNYR GRQYLLMPGD YRRYQDWGAT NARVGSLRRV IDFS.
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 :
MIEN1 HumanDescription:
Migration And Invasion Enhancer 1 Human Recombinant
C17orf37, C35, ORB3, RDX12, XTP4, HBV X-transactivated gene 4 protein, HBV XAg-transactivated protein 4, Protein C35, Migration and invasion enhancer 1.
Product # :
PRO-1657Price :
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Description
MIEN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (1-112 a.a.) and having a molecular mass of 14.5kDa.MIEN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIEN1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Migration And Invasion Enhancer 1 (MIEN1) is a member of the SelWTH family. MIEN1 enhances cell migration by stimulating filopodia formation at the leading edge of migrating cells and takes parts in regulation of apoptosis, probably via control of CASP3. MIEN1 participates in a redox-related process as well.
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Synonyms
C17orf37, C35, ORB3, RDX12, XTP4, HBV X-transactivated gene 4 protein, HBV XAg-transactivated protein 4, Protein C35, Migration and invasion enhancer 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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSGEPGQ TSVAPPPEEV EPGSGVRIVV EYCEPCGFEA TYLELASAVK EQYPGIEIES RLGGTGAFEI EINGQLVFSK LENGGFPYEK DLIEAIRRAS NGETLEKITN SRPPC.
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 :
CSTA Human, HisDescription:
Cystatin A Human Recombinant, His tag
Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.
Product # :
PRO-504Price :
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Description
CSTA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-98 a.a.) and having a molecular mass of 13.1kDa.CSTA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cystatin-A (1mg/ml) in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.
More Info
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Introduction
Cystatin-A is the intracellular inhibitor of cysteine proteinase cathepsin B (CatB) and belongs to family 1 of the cystatin superfamily of inhibitor proteins. CSTA is a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. It has been proposed that extracellular CatB together with other classes of proteinases are all subjected to a cascade-like manner of activation. CatB and its inhibitor Cystatin-A are involved in degradation of extracellular matrix proteins during tissue remodeling. CSTA is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Cystatin-A has been reported to be found in high concentrations in epithelial cells, polymorphonuclear leukocytes and lymphoid tissue. Stefins may be used as prognostic and diagnostic tools for cancer.
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Synonyms
Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.
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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 MIPGGLSEAK PATPEIQEIV DKVKPQLEEK TNETYGKLEA VQYKTQVVAG TNYYIKVRAG DNKYMHLKVF KSLPGQNEDL VLTGYQVDKN KDDELTGF.
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 :
CTACK HumanDescription:
CTACK Human Recombinant (CCL27)
ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.
Product # :
CHM-373Price :
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Description
CTACK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids (25-112 a.a.) and having a molecular mass of 10.3kDa. CTACK protein is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CTACK Human solution containing 10mM sodium citrate pH-3.5 & 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.
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Synonyms
ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.
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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
MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.
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Background
What is the molecular weight/Mw of CTACK HUMAN Protein?
CTACK HUMAN Protein has a total Mw of 10.3kDa.
What is the source or expression system of CTACK HUMAN Protein?
Escherichia Coli.
What is the Purity of CTACK HUMAN Protein?
CTACK HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTACK HUMAN Protein?
The biological functionality of CTACK HUMAN Protein will be determined in the future.
What is the amino acid sequence of CTACK HUMAN Protein?
MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.
What applications can CTACK HUMAN Protein be used in?
CTACK HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTACK HUMAN Protein?
The endotoxin level is minimal, CTACK HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Activin A HumanDescription:
Activin A Human Recombinant
Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.
Product # :
CYT-569Price :
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Shipped with Ice Packs
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- sds-page
Description
Activin-A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 137 amino acids (311-426) and having a molecular mass of 15.2kDa.Activin-A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Activin-A protein solution (1mg/ml) contains 20mM Tris pH 8.0 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
Synonyms
Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.
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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 MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 15.2 kDa.What is the source or expression system of Activin A Protein?
E.ColiWhat is the Purity of Activin A Protein?
Activin A Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological functionality of Activin-A Protein will be determined in the future.What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.What is the amino acid sequence of ACTIVIN A Protein?MGSSHHHHHH SSGLVPRGSH MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS
What applications can ACTIVIN-A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CTSE HumanDescription:
Cathepsin-E Human Recombinant
Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.
Product # :
ENZ-776Price :
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Shipped with Ice Packs
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Description
CTSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (57-363 a.a) and having a molecular mass of 35.4kDa.CTSE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CTSE protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin-E also known as CTSE is a gastric aspartyl protease which functions as a disulfide-linked homodimer. CTSE belongs to the peptidase C1 family; furthermore it has specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase which does not seem to be involved in the digestion of dietary protein and is found in the uppermost concentration in the surface of epithelial mucus-producing cells of the stomach. CTSE is the first aspartic proteinaseexpressed in the fetal stomach and is discovered in more than half of gastric cancers. For that reason CTSE is anoncofetal antigen. In addition, transcript variants utilizing alternative polyadenylation signals and two transcript variantsencoding different isoforms exist for this gene.
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Synonyms
Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, 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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTESCSMD QSAKEPLINY LDMEYFGTIS IGSPPQNFTV IFDTGSSNLW VPSVYCTSPA CKTHSRFQPS QSSTYSQPGQ SFSIQYGTGS LSGIIGADQV SVEGLTVVGQ QFGESVTEPG QTFVDAEFDG ILGLGYPSLA VGGVTPVFDN MMAQNLVDLP MFSVYMSSNP EGGAGSELIF GGYDHSHFSG SLNWVPVTKQ AYWQIALDNM LWSVPTLTSC RMSPSPLTES PIPSAQLPTP YWTSWMECSS AAVAFKDLTS TLQLGPSGSW GMSSFDSFTQ SLTVGITVWD WPQQSPKEGP CVCACLSDRP
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Cyclophilin A MouseDescription:
Cyclophilin A Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
Product # :
ENZ-857Price :
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Shipped with Ice Packs
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Description
Cyclophilin A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
Cyclophilin A protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
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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 MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL.
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 :
SAT1 HumanDescription:
Spermidine/Spermine N1-Acetyltransferase 1 Human Recombinant
Diamine acetyltransferase 1, Spermidine/spermine N(1)-acetyltransferase 1, Putrescine acetyltransferase, Polyamine N-acetyltransferase 1, SSAT-1, SSAT, SAT1, SAT, DC21, KFSD, KFSDX.
Product # :
ENZ-433Price :
Quantity :
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Shipped with Ice Packs
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Description
SAT1 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 191 amino acids (1-171 a.a.) and having a molecular mass of 22.1kDa.The SAT1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SAT1 solution contains 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
SAT-1 is a member the acetyltransferase family, and is a rate-limiting enzyme in the catabolic pathway of polyamine metabolism. SAT1 catalyzes the acetylation of spermidine and spermine, and is involved in the regulation of the intracellular concentration of polyamines and their transport out of cells. Therefore, SAT-1’s role is essential in polyamine homoeostasis, given that acetylated products are either excreted from the cell or oxidized by acetylpolyamine oxidase. Increased SAT1 activity causes variety of other effects which include pancreatic cells death, obstruction of regenerative tissue growth, behavioral changes, keratosis follicularis spinulosa decalvans (KFSD), and hair loss.
Defects in the SAT1 gene are linked to KFSD (keratosis follicularis spinulosa decalvans), which is a rare X-linked disorder affecting the skin and the eye. The KFSD affected men show thickening of the skin of the neck, ears, and extremities, particularly the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration. Even though the majority of the affected families are compatible with an X-linked inheritance, KFSD are found to be clinically and genetically heterogeneous. -
Synonyms
Diamine acetyltransferase 1, Spermidine/spermine N(1)-acetyltransferase 1, Putrescine acetyltransferase, Polyamine N-acetyltransferase 1, SSAT-1, SSAT, SAT1, SAT, DC21, KFSD, KFSDX.
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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 MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP FYHCLVAEVP KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMRC RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMATE 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 :
AKR1B1 HumanDescription:
Aldose Reductase Human Recombinant
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
Product # :
ENZ-390Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AKR1B1 Human Recombinant amino produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids having a molecular mass of 35.8 kDa.The AKR1B1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The 1mg/ml protein solution contains 20mM Tris-HCl buffer pH 8, 10% glycerol, and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 800pmol/min/ug, and is defined as the amount of enzyme that catalyze the reduction of 1.0 pmole DL-glyceraldehyde in the presence of NADPH per minute at pH7.0 at 37°C.More Info
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Introduction
AKR1B1 is part of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. AKR1B1 catalyzes the reduction several aldehydes, including the aldehyde form of glucose, and thus involved in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. AKR1B1 catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Transgenic mice over expressing human aldose reductase show that AKR1B1 is a key player in ischemic injury and impairment of functional and metabolic recovery after ischemia. Aldose Reductase is an obligatory mediator of TNF-alpha signaling leading to an increase in the expression of adhesion molecules and increased binding of monocytes to the endothelium. AKR1B1 is a critical regulator of TNF-alpha-induced apoptotic signaling in endothelial cells.
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Synonyms
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
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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
MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA LLSCTSHKDY PFHEEF.
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 :
DCTN2 (1-403) HumanDescription:
Dynactin 2 (1-403 a.a.) Human Recombinant
Dynactin 2 (P50), 50 KDa Dynein-Associated Polypeptide, Dynactin Complex 50 KDa Subunit, P50 Dynamitin, DCTN50, 50 KD Dynein-Associated Polypeptide, Epididymis Secretory Protein Li 77, Dynactin Complex 50 KD Subunit, DYNAMITIN, HEL-S-77, DCTN-50, RBP50.
Product # :
PRO-2303Price :
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Shipped with Ice Packs
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Description
Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403 a.a) and having a molecular mass of 46.9kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.
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Synonyms
Dynactin 2 (P50), 50 KDa Dynein-Associated Polypeptide, Dynactin Complex 50 KDa Subunit, P50 Dynamitin, DCTN50, 50 KD Dynein-Associated Polypeptide, Epididymis Secretory Protein Li 77, Dynactin Complex 50 KD Subunit, DYNAMITIN, HEL-S-77, DCTN-50, RBP50.
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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 MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAEL EELTSTSVEH IIVNPNAAYD KFKDKRVGTK GLDFSDRIGK TKRTGYESGE YEMLGEGLGV KETPQQKYQR LLHEVQELTT EVEKIKTTVK ESATEEKLTP VLLAKQLAAL KQQLVASHLE KLLGPDAAIN LTDPDGALAK RLLLQLEATK NSKGGSGGKT TGTPPDSSLV TYELHSRPEQ DKFSQAAKVA ELEKRLTELE TAVRCDQDAQ NPLSAGLQGA CLMETVELLQ AKVSALDLAV LDQVEARLQS VLGKVNEIAK HKASVEDADT QSKVHQLYET IQRWSPIAST LPELVQRLVT IKQLHEQAMQ FGQLLTHLDT TQQMIANSLK DNTTLLTQVQ TTMRENLATV EGNFASIDER MKKLGK
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 :
CXCL7 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
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Background
What is the molecular weight/Mw of CXCL7 95 A.A HUMAN Protein?
CXCL7 95 A.A HUMAN Protein has a total Mw of 10.3kDa.
What is the source or expression system of CXCL7 95 A.A HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL7 95 A.A HUMAN Protein?
CXCL7 95 A.A HUMAN Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL7 95 A.A HUMAN Protein?
The biological functionality of CXCL7 95 A.A HUMAN Protein will be determined in the future.
What is the amino acid sequence of CXCL7 95 A.A HUMAN Protein?
MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD
What applications can CXCL7 95 A.A HUMAN Protein be used in?
CXCL7 95 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL7 95 A.A HUMAN Protein?
The endotoxin level is minimal, CXCL7 95 A.A HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNUPN HumanDescription:
Snurportin 1 Human Recombinant
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
Product # :
PRO-866Price :
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Shipping Method :
Shipped with Ice Packs
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Description
SNUPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-360 a.a.) and having a molecular mass of 43.3 kDa. The SNUPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SNUPN Human solution containing 20mM Tris pH-8, 2mM DTT, 0.1M NaCl, & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SNUPN is a nuclear import adaptor protein which is part of the Snurportin family.
SNUPN is Localized to the cytoplasm and nucleus and contains an N-terminal IBB domain and a trimethylguanosine (m3G)-cap binding domain. SNUPN binds specifically the terminal 2,2,7-m3G-cap at the 5'' end of U snRNPs and is involved in transport of U snRNPs into the nucleus through an association with Importin β. -
Synonyms
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
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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
MGSSHHHHHH SSGLVPRGSH MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS
TPKLKGSSHS PDHPGCLMEN.
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 :
CXCL5 Human (8-78 a.a)Description:
Epithelial Neutrophil-Activating Protein 78, 8-78 a.a. Human Recombinant (CXCL5)
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
Product # :
CHM-265Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids (8-78 a.a.) and having a molecular mass of 7.8kDa. The CXCL5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity was determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.More Info
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Introduction
Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II interferon IFN-?. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.
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Synonyms
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ENA78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 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
LRELRCVCLQ TTQGVHPKMI SNLQVFAIGP QCSKVEVVAS LKNGKEICLD PEAPFLKKVI QKILDGGNKE N.
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Background
What is the molecular weight/Mw of CXCL5 HUMAN (8-78 A.A) Protein?
CXCL5 HUMAN (8-78 A.A) Protein has a total Mw of 7.8kDa.
What is the source or expression system of CXCL5 HUMAN (8-78 A.A) Protein?
Escherichia Coli.
What is the Purity of CXCL5 HUMAN (8-78 A.A) Protein?
CXCL5 HUMAN (8-78 A.A) Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL5 HUMAN (8-78 A.A) Protein?
The biological activity was determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
What is the amino acid sequence of CXCL5 HUMAN (8-78 A.A) Protein?
LRELRCVCLQ TTQGVHPKMI SNLQVFAIGP QCSKVEVVAS LKNGKEICLD PEAPFLKKVI QKILDGGNKE N.
What applications can CXCL5 HUMAN (8-78 A.A) Protein be used in?
CXCL5 HUMAN (8-78 A.A) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL5 HUMAN (8-78 A.A) Protein?
The endotoxin level is minimal, CXCL5 HUMAN (8-78 A.A) 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 :
Eotaxin Human, HisDescription:
Eotaxin Human Recombinant (CCL11), His Tag
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
Product # :
CHM-344Price :
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Shipped with Ice Packs
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Description
Eotaxin His Tag Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids fragment (24-87) corresponding to the mature Eotaxin protein and having a molecular mass of 8345.9 Dalton with an amino-terminal hexahistidine tag.The Eotaxin-His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Eotaxin-His is supplied liquid In Phosphate Buffered Saline pH7.4 containing 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE
More Info
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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP
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Background
What is the molecular weight/Mw of EOTAXIN HUMAN, HIS Protein?
EOTAXIN HUMAN, HIS Protein has a total Mw of 8.34kDa.
What is the source or expression system of EOTAXIN HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of EOTAXIN HUMAN, HIS Protein?
EOTAXIN HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN HUMAN, HIS Protein?
The biological functionality of EOTAXIN HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of EOTAXIN HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP
What applications can EOTAXIN HUMAN, HIS Protein be used in?
EOTAXIN HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN HUMAN, HIS Protein?
The endotoxin level is minimal, EOTAXIN HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
STMN1 HumanDescription:
Stathmin-1 Human Recombinant
Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.
Product # :
PRO-676Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Human Stathmin-1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-149 a.a) and having a molecular mass of 19.4 kDa. STMN1 is fused to 20 amino acid His Tga at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STMN1 protein solution contains 20mM Tris-HCl, pH-8 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
STMN1 takes part in the regulation of the microtubule filament structure by destabilizing microtubules. STMN1 promotes the disassembly of microtubules and prevents assembly. STMN1 is a ubiquitous cytosolic phosphoprotein which functions as an intracellular relay integrating regulatory signals of the cellular environment. Stathmin functions as an Oncoprotein in regulation of the cell cycle. Stathmin mutation results in uncontrolled cell proliferation. Stathmin expression associates with cervical carcinogenesis and tumor progression, thus Stathmin is an important prognostic marker in cervical carcinoma. STMN1, takes part in the prevenative progression of ER-positive primary in breast cancer. Somatic mutation in STMN1 effects cell homeostasis that leads to tumorigenicity.
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Synonyms
Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.
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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 MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL ERLREKDKHI EEVRKNKESK DPADETEAD.
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 :
Streptavidin (37-159), HisDescription:
Streptavidin (37-159 a.a) Recombinant, His Tag
Product # :
PRO-1495Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Streptavidin Recombinant produced in E. coli is a single polypeptide chain containing 148 amino acids (37-159) and having a molecular mass of 15.6kDa. Streptavidin is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The Streptavidin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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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
MGSSHHHHHH SSGLVPRGSH MGSHMAEAGI TGTWYNQLGS TFIVTAGADG ALTGTYESAV GNAESRYVLT GRYDSAPATD GSGTALGWTV AWKNNYRNAH SATTWSGQYV GGAEARINTQ WLLTSGTTEA NAWKSTLVGH DTFTKVKP.
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 :
SULT2B1 HumanDescription:
Sulfotransferase Family, Cytosolic, 2B, Member 1 Human Recombinant
SULT2B1, HSST2, EC 2.8.2.2, Sulfotransferase 2B1, Hydroxysteroid sulfotransferase 2, ST2B1, Sulfotransferase family cytosolic 2B member 1.
Product # :
ENZ-512Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SULT2B1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 365 amino acids (1-365 a.a.) and having a molecular mass of 41.3 kDa. SULT2B1 protein is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
SULT2B1 Human solution containing 20mM Tris-HCl pH-7.5, & 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
SULT2B1 catalyzes the sulfate conjugation of numerous hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation enhances the water solubility of molecules, and therefore their renal excretion, however it can also result in bioactivation to form active metabolites. SULT2B1b is localized in the cytosol and nuclei of human cells. SULT2B1b is selective for the sulfation of 3beta-hydroxysteroids such as dehydroepiandrosterone and pregnenolone, and participates in cholesterol sulfation in human skin.
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Synonyms
SULT2B1, HSST2, EC 2.8.2.2, Sulfotransferase 2B1, Hydroxysteroid sulfotransferase 2, ST2B1, Sulfotransferase family cytosolic 2B member 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
MDGPAEPQIP GLWDTYEDDI SEISQKLPGE YFRYKGVPFP VGLYSLESIS LAENTQDVRD DDIFIITYPK SGTTWMIEII CLILKEGDPS WIRSVPIWER APWCETIVGA FSLPDQYSPR LMSSHLPIQI FTKAFFSSKA KVIYMGRNPR DVVVSLYHYS KIAGQLKDPG TPDQFLRDFL KGEVQFGSWF DHIKGWLRMK GKDNFLFITY EELQQDLQGS VERICGFLGR PLGKEALGSV VAHSTFSAMK ANTMSNYTLL PPSLLDHRRG AFLRKGVCGD WKNHFTVAQS EAFDRAYRKQ MRGMPTFPWD EDPEEDGSPD PEPSPEPEPK PSLEPNTSLE REPRPNSSPS PSPGQASETP HPRPS.
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 :
CXCL14 HumanDescription:
BRAK (CXCL14) Human Recombinant
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
Product # :
CHM-001Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 was lyophilized after extensive dialysis against 20mM Tris-HCl, pH 8.5 and 1M NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 of CXCL14 as determined by its ability to induce calcium flux of prostaglandin E2 treated THP1 human acute monocytic leukemia cells was 1.0-10.0 ng/ml.More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Cys-Lys-Cys.
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Background
What is the molecular weight/Mw of CXCL14 HUMAN Protein?
CXCL14 HUMAN Protein has a total Mw of 9.4kDa.
What is the source or expression system of CXCL14 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL14 HUMAN Protein?
CXCL14 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 HUMAN Protein?
The ED50 of CXCL14 as determined by its ability to induce calcium flux of prostaglandin E2 treated THP1 human acute monocytic leukemia cells was 1.0-10.0 ng/ml.
What is the amino acid sequence of CXCL14 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Cys-Lys-Cys.
What applications can CXCL14 HUMAN Protein be used in?
CXCL14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 HUMAN Protein?
The endotoxin level is minimal, CXCL14 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL8 Human, HisDescription:
Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8), His Tag
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-345Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
- purity
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Description
Interleukin-8 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (23-99) and having a total molecular mass of 13.7kDa with an amino-terminal hexahistidine tag. The IL-8 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL8 His is supplied in 10mM Tris-HCl pH 8, 250mM NaCl and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein has a total Mw of 13.7kDa.
What is the source or expression system of CXCL8 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, HIS Protein?
The biological functionality of CXCL8 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein is composed from 77 amino acids.
What applications can CXCL8 HUMAN, HIS Protein be used in?
CXCL8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL8 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TECK Human, HisDescription:
Thymus Expressed Chemokine (CCL25) Human Recombinant, His Tag
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Product # :
CHM-032Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TECK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (24-150 a.a.) and having a molecular mass of 16.8kDa.TECK is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TECK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils. -
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
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Physical Appearance
Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMQGVFE DCCLAYHYPI GWAVLRRAWT YRIQEVSGSC NLPAAIFYLP KRHRKVCGNP KSREVQRAMK LLDARNKVFA KLHHNTQTFQ AGPHAVKKLS SGNSKLSSSK FSNPISSSKR NVSLLISANS GL.
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 :
ING1 HumanDescription:
Inhibitor of Growth Family, Member 1 Human Recombinant
Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .
Product # :
PRO-2130Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279 a.a) and having a molecular mass of 34.3kDa.ING1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ING1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Inhibitor of Growth Family Member 1, also known as ING1 is a tumor suppressor protein which is able to induce cell growth arrest and apoptosis. ING1 is a nuclear protein which physically act together with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. In addition, Reduced expression and rearrangement of ING1 have been identified in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described for ING1.
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Synonyms
Inhibitor Of Growth Family, Member 1, Growth Inhibitory Protein ING1, Tumor Suppressor ING1, Growth Inhibitor ING1, Inhibitor Of Growth Protein 1, Inhibitor Of Growth 1, P24ING1c,P33ING1b, P47ING1a, P33ING1, P33, P47, ING1 .
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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 MGSMLSPANG EQLHLVNYVE DYLDSIESLP FDLQRNVSLM REIDAKYQEI LKELDECYER FSRETDGAQK RRMLHCVQRA LIRSQELGDE KIQIVSQMVE LVENRTRQVD SHVELFEAQQ ELGDTAGNSG KAGADRPKGE AAAQADKPNS KRSRRQRNNE NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE ASPADLPIDP NEPTYCLCNQ VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR GENEKTMDKA LEKSKKERAY NR.
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 :
Frataxin HumanDescription:
Frataxin Human Recombinant
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
Product # :
PRO-761Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Frataxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids (42-210 a.a.) and having a molecular mass of 21.1 kDa. The Frataxin is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Frataxin solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Frataxin is a mitochondrial iron binding protein that is part of the FRATAXIN family. Frataxin functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Frataxin plays a role in iron homeostasis. Frataxin is an anti-apoptotic protein which prevents mitochondrial damage and reactive oxygen species (ROS) production.
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Synonyms
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
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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 MLRTDIDATC TPRRASSNQR GLNQIWNVKK QSVYLMNLRK SGTLGHPGSL DETTYERLAE ETLDSLAEFF EDLADKPYTF EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDWTG KNWVYSHDGV SLHELLAAEL TKALKTKLDL SSLAYSGKDA.
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.