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1000 results found for “ahcy”
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Name :
ARF5 HumanDescription:
ADP-Ribosylation Factor 5 Human Recombinant
ADP-ribosylation factor 5, ARF5.
Product # :
PRO-245Price :
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Shipped with Ice Packs
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Description
ARF5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (1-180 a.a) and having a molecular mass of 22.6kDa.ARF5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARF5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ADP-ribosylation factor 5 (ARF5) is a small guanine nucleotide-binding protein which enhances the enzymatic activities of cholera toxin. ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the connection of actin to the golgi via rho family-dependent G-protein localization and WASP/Arp2/3 complexes. ARF5 is involved in vesicular transport and functioning via phospholipase D activation.
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Synonyms
ADP-ribosylation factor 5, ARF5.
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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 MGLTVSALFS RIFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV QESADELQKM LQEDELRDAV LLVFANKQDM PNAMPVSELT DKLGLQHLRS RTWYVQATCA
TQGTGLYDGL DWLSHELSKR.
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 :
ARF6 HumanDescription:
ADP-Ribosylation Factor 6 Human Recombinant
ADP-ribosylation factor 6, ARF6, DKFZp564M0264.
Product # :
PRO-032Price :
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Description
ARF6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (1-175a.a.) and having a molecular mass of 22.2kDa.ARF6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARF6 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2mM PMSF and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
ARF6 is a part of the ADP ribosylation factor family of GTP-binding proteins. ARF6 is restricted to the plasma membrane, and controls vesicular trafficking, remodeling of membrane lipids, and signaling pathways which lead to actin remodeling. Furthermore, ARF6 is a key player in conservation of organelle integrity, assembly of coat proteins and activation of phospholipase D.
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Synonyms
ADP-ribosylation factor 6, ARF6, DKFZp564M0264.
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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 MGKVLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE TVTYKNVKFN VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR QELHRIINDR EMRDAIILIF ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCATSGD GLYEGLTWLT SNYKS
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 :
CACYBP HumanDescription:
Calcyclin Binding Protein Human Recombinant
S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.
Product # :
PRO-831Price :
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Description
CACYBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids (1-185a.a.) and having a molecular mass of 23.4 kDa. CACYBP protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CACYBP Human solution containing 20mM Tris HCL pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
CACYBP (calcyclin binding protein) participates in calcium-dependent ubiquitination and subsequent proteosomal degradation of target proteins. CACYBP acts as a molecular bridge in ubiquitin E3 complexes. CACYBP is involved in the ubiquitin-mediated degradation of beta-catenin.
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Synonyms
S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.
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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 MQQKSQKKAE LLDNEKPAAV VAPITTGYTV KISNYGWDQS DKFVKIYITL TGVHQVPTEN VQVHFTERSF DLLVKNLNGK SYSMIVNNLL KPISVEGSSK KVKTDTVLIL CRKKVENTRW DYLTQVEKEC KEKEKPSYDT ETDPSEGLMN VLKKIYEDGD DDMKRTINKA WVESREKQAK GDTEF.
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 :
PLEKHF2 HumanDescription:
Pleckstrin Homology Domain Containing Family F Member 2 Human Recombinant
EAPF, PHAFIN2, ZFYVE18, Pleckstrin homology domain-containing family F member 2, PH domain-containing family F member 2, Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains, PH and FYVE domain-containing protein 2, Zinc finger FYVE domain-containing protein 18, PLEKHF2.
Product # :
PRO-1874Price :
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Description
PLEKHF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-249 a.a) and having a molecular mass of 30.2kDa. PLEKHF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PLEKHF2 protein solution (0.25mg/ml) containing 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
Pleckstrin Homology Domain Containing Family F Member 2, also known as PLEKHF2, contains 1 FYVE-type zinc finger and 1 PH domain. PLEKHF2 takes part in early endosome fusion upstream of RAB5, regulates receptor trafficking and fluid-phase transport. PLEKHF2 increases cellular sensitivity to TNF-induced apoptosis.
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Synonyms
EAPF, PHAFIN2, ZFYVE18, Pleckstrin homology domain-containing family F member 2, PH domain-containing family F member 2, Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains, PH and FYVE domain-containing protein 2, Zinc finger FYVE domain-containing protein 18, PLEKHF2.
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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 MGSMVDRLAN SEANTRRISI VENCFGAAGQ PLTIPGRVLI GEGVLTKLCR KKPKARQFFL FNDILVYGNI VIQKKKYNKQ HIIPLENVTI DSIKDEGDLR NGWLIKTPTK SFAVYAATAT EKSEWMNHIN KCVTDLLSKS GKTPSNEHAA VWVPDSEATV CMRCQKAKFT PVNRRHHCRK CGFVVCGPCS EKRFLLPSQS SKPVRICDFC YDLLSAGDMA TCQPARSDSY SQSLKSPLND MSDDDDDDDS SD.
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 :
TNFRSF6B HumanDescription:
Tumor Necrosis Factor Receptor Superfamily, Member 6b Human Recombinant
Tumor Necrosis Factor Receptor Superfamily, Member 6b Decoy, Decoy Receptor For Fas Ligand, Decoy Receptor 3, DCR3, M68E, M68, TR6, DJ583P15.1.1, DcR3.
Product # :
CYT-799Price :
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Shipped with Ice Packs
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Description
TNFRSF6B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (30-300aa) and having a molecular mass of 32.1kDa.TNFRSF6B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFRSF6B 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
TNFRSF6B is a member of the Tumor necrosis factor receptor superfamily. TNFRSF6B performs as a decoy receptor which races against death receptors for ligand binding. TNFRSF6B has a regulatory role in suppressing FasL- and LIGHT-mediated cell death and T cell activation in addition to inducing angiogenesis via neutralization of TL1A.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily, Member 6b Decoy, Decoy Receptor For Fas Ligand, Decoy Receptor 3, DCR3, M68E, M68, TR6, DJ583P15.1.1, DcR3.
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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 MGSVAETPTY PWRDAETGER LVCAQCPPGT FVQRPCRRDS PTTCGPCPPR HYTQFWNYLE RCRYCNVLCG EREEEARACH ATHNRACRCR TGFFAHAGFC LEHASCPPGA GVIAPGTPSQ NTQCQPCPPG TFSASSSSSE QCQPHRNCTA LGLALNVPGS SSHDTLCTSC TGFPLSTRVP GAEECERAVI DFVAFQDISI KRLQRLLQAL EAPEGWGPTP RAGRAALQLK LRRRLTELLG AQDGALLVRL LQALRVARMP GLERSVRERF LPVH.
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 :
PRDX3 HumanDescription:
Peroxiredoxin-3 Human Recombinant
AOP1, MER5, AOP-1, SP-22, PRO1748, MGC24293, MGC104387, PRDX3, Thioredoxin-dependent peroxide reductase mitochondrial, Peroxiredoxin-3, PRX III, Antioxidant protein 1, Protein MER5 homolog, HBC189.
Product # :
ENZ-419Price :
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Description
PRDX3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids (63-256 a.a.) and having a molecular mass of 21.5 kDa.The PRDX3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PRDX3 solution contains 20mM Tris-HCl pH-8, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be approximately 82-83 pmole/min/µg.
The enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX3 and peroxide for 20 min at room temperature. Specific activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25°C for 1 minute.More Info
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Introduction
PRDX3 is part of the peroxiredoxin family of antioxidant enzymes, that reduces hydrogen peroxide and alkyl hydroperoxides. PRDX3 is particularly located in the mitochondria and involved in the regulation of cellular redox status by serving as a primary line of defense against H2O2 produced during respiration. PRDX3 is a significant regulator of the abundance of mitochondrial H(2)O(2), which itself promotes apoptosis in cooperation with other mediators of apoptotic signaling. PRDX3 mitochondrial protein is significantly decreased in Alzheimer Disease and Down Syndrome.
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Synonyms
AOP1, MER5, AOP-1, SP-22, PRO1748, MGC24293, MGC104387, PRDX3, Thioredoxin-dependent peroxide reductase mitochondrial, Peroxiredoxin-3, PRX III, Antioxidant protein 1, Protein MER5 homolog, HBC189.
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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
MPAVTQHAPY FKGTAVVNGE FKDLSLDDFK GKYLVLFFYP LDFTFVCPTE IVAFSDKANE FHDVNCEVVA VSVDSHFSHL AWINTPRKNG GLGHMNIALL SDLTKQISRD YGVLLEGSGL ALRGLFIIDP NGVIKHLSVN DLPVGRSVEE TLRLVKAFQY VETHGEVCPA NWTPDSPTIK PSPAASKEYF QKVNQ.
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 :
PROCR HumanDescription:
Protein-c Receptor Human Recombinant
Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA
Product # :
PRO-1938Price :
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Shipped with Ice Packs
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Description
PROCR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (18-210) and having a molecular mass of 24.4 kDa.PROCR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PROCR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein-c Receptor (PROCR) is a receptor for activated protein C, a serine protease activated by and involved in the blood coagulation pathway. The PROCR protein is an N-glycosylated type I membrane protein which enhances the activation of protein C. PROCR gene mutations are linked with venous thromboembolism and myocardial infarction, as well as with late fetal loss during pregnancy. In addition, PROCR may have a role in malarial infection and has been linked with cancer.
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Synonyms
Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA
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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 MGSSQDASDG LQRLHMLQIS YFRDPYHVWY QGNASLGGHL THVLEGPDTN TTIIQLQPLQ EPESWARTQS GLQSYLLQFH GLVRLVHQER TLAFPLTIRC FLGCELPPEG SRAHVFFEVA VNGSSFVSFR PERALWQADT QVTSGVVTFT LQQLNAYNRT RYELREFLED TCVQYVQKHI SAENTKGSQT SRSYTS.
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 :
GNAI2 HumanDescription:
Guanine Nucleotide Binding Protein-G Alpha Inhibiting Activity Polypeptide 2 Human Recombinant
Guanine Nucleotide Binding Protein (G Protein), Alpha Inhibiting Activity Polypeptide 2, GTP-Binding Regulatory Protein Gi Alpha-2 Chain, Guanine Nucleotide-Binding Protein G(I), Alpha-2 Subunit, Adenylate Cyclase-Inhibiting G Alpha Protein, GNAI2B, H_LUCA16.1, GIP.
Product # :
PRO-1310Price :
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Shipped with Ice Packs
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Description
GNAI2 Human Recombinant produced in E. coli is a single polypeptide chain containing 375 amino acids (1-355) and having a molecular mass of 42.0 kDa.GNAI2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GNAI2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GNAI2 is an alpha subunit of guanine nucleotide binding proteins (G proteins) and holds a guanine nucleotide binding site. GNAI2 takes part in the hormonal regulation of adenylate cyclase. GNAI2 has varies transcript variants encoding different isoforms yet only two full-length isoforms were identified up to date.
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Synonyms
Guanine Nucleotide Binding Protein (G Protein), Alpha Inhibiting Activity Polypeptide 2, GTP-Binding Regulatory Protein Gi Alpha-2 Chain, Guanine Nucleotide-Binding Protein G(I), Alpha-2 Subunit, Adenylate Cyclase-Inhibiting G Alpha Protein, GNAI2B, H_LUCA16.1, GIP.
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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 MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPSR ADDARQLFAL SCTAEEQGVL PDDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT HSPLTICFPE YTGANKYDEA ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF.
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 :
UBE2L3 Human HisDescription:
Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant, His Tag
Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.
Product # :
ENZ-344Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.coli is an 18.9 kDa protein containing 162 amino acids.The UBE2L3 protein contains 6xHis tag and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated (1 mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Human Ubquitin Conjugating Enzyme 7 (UbcH7) is a class I enzyme which functions in the stress response and the control of transcription factors. The enzyme is ubiquitously expressed with high levels of expression seen in adult muscle. UbcH7 mediates the selective degradation of short-lived and abnormal proteins and is highly homologous to UbcH5. It has been demonstrated to participate in the ubiquitinylation of p53, c-Fos and NF-?B. UbcH7 is one of two E2s (UbcH5 being the other) with which HECT domain proteins interact with UbcH7 being able to efficiently substitute for UbcH5 in E6-AP-dependent ubiquitinylation.
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Synonyms
Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized UBE2L3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2L3 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 UBE2L3 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHHHHHHAMAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVP
DNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAEN
WKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFT
KKYGEKRPVD.
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 :
CXCL1 HumanDescription:
GRO-Alpha Human Recombinant (CXCL1)
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
Product # :
CHM-329Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human 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 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
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Synonyms
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 CXCL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
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Background
What is the molecular weight/Mw of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein has a total Mw of 7.81kDa.
What is the source or expression system of CXCL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL1 HUMAN Protein?
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 CXCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
What applications can CXCL1 HUMAN Protein be used in?
CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL1 HUMAN Protein?
The endotoxin level is minimal, CXCL1 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 :
CLIC2 HumanDescription:
Chloride Intracellular Channel 2 Human Recombinant
Chloride intracellular channel protein 2, XAP121, CLIC2, CLIC2b, XAP121.
Product # :
PRO-198Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CLIC2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-247 a.a.) and having a molecular mass of 30.5kDa.CLIC2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CLIC2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Chloride intracellular channel protein 2 (CLIC2) regulates cellular traffic of chloride ions, which is a critical component of all living cells. CLIC2 is involved in membrane potential stabilization, signal transduction, cell volume regulation and organic solute transport. CLIC2 is identified in the fetal liver and adult skeletal muscle tissue. CLIC2 is a likely candidate for one of the many diseases linked to Xq28.
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Synonyms
Chloride intracellular channel protein 2, XAP121, CLIC2, CLIC2b, XAP121.
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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 MSGLRPGTQV DPEIELFVKA GSDGESIGNC PFCQRLFMIL WLKGVKFNVT TVDMTRKPEE LKDLAPGTNP PFLVYNKELK TDFIKIEEFL EQTLAPPRYP HLSPKYKESF DVGCNLFAKF SAYIKNTQKE ANKNFEKSLL KEFKRLDDYL NTPLLDEIDP
DSAEEPPVSR RLFLDGDQLT LADCSLLPKL NIIKVAAKKY RDFDIPAEFS GVWRYLHNAY AREEFTHTCP EDKEIENTYA NVAKQKS.
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 :
RAB5C HumanDescription:
RAB5C, Member RAS Oncogene Family Human Recombinant
L1880, RAB5CL, RAB5L, RABL, Ras-related protein Rab-5C, RAB5C.
Product # :
PRO-1427Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
RAB5C Human Recombinant produced in E. coli is a single polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 25.9kDa. RAB5C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RAB5C solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
RAB5C is a part of the Ras-related protein family. Members of the Rab protein family are small GTPases of the Ras superfamily guarantee reliability in the process of docking and fusion of vesicles with their right acceptor compartment.
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Synonyms
L1880, RAB5CL, RAB5L, RABL, Ras-related protein Rab-5C, RAB5C.
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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 MGSMAGRGGA ARPNGPAAGN KICQFKLVLL GESAVGKSSL VLRFVKGQFH EYQESTIGAA FLTQTVCLDD TTVKFEIWDT AGQERYHSLA PMYYRGAQAA IVVYDITNTD TFARAKNWVK ELQRQASPNI VIALAGNKAD LASKRAVEFQ EAQAYADDNS LLFMETSAKT AMNVNEIFMA IAKKLPKNEP QNATGAPGRN RGVDLQENNP ASRSQCCSN.
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 :
MCEE HumanDescription:
Methylmalonyl CoA Epimerase Human Recombinant
GLOD2, Methylmalonyl CoA Epimerase, Glyoxalase Domain Containing 2, DL-methylmalonyl-CoA Racemase.
Product # :
ENZ-013Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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- More Info
Description
MCEE produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (37-176a.a.) and having a molecular mass of 17.3kDa.MCEE is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MCEE protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
MCEE catalyzes the interconversion of D- and L-methylmalonyl-CoA throughout the degradation of branched chain amino acids, odd chain-length fatty acids, and other metabolites. MCEE protein deficiency is an autosomal recessive inborn error of amino acid metabolism, involving valine, threonine, isoleucine and methionine. This organic aciduria can appear in the neonatal period with life-threatening metabolic acidosis, hyperammonemia, feeding difficulties, pancytopenia and coma.
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Synonyms
GLOD2, Methylmalonyl CoA Epimerase, Glyoxalase Domain Containing 2, DL-methylmalonyl-CoA Racemase.
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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
MGSSHHHHHH SSGLVPRGSH MQVTGSVWNL GRLNHVAIAV PDLEKAAAFY KNILGAQVSE AVPLPEHGVS VVFVNLGNTK MELLHPLGRD SPIAGFLQKN KAGGMHHICI EVDNINAAVM DLKKKKIRSL SEEVKIGAHG KPVIFLHPKD CGGVLVELEQ A
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 :
YWHAG HumanDescription:
Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.
Product # :
PKA-238Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 247 amino acids (1-247) and having a molecular mass of 28 kDa. YWHAG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
YWHAG solution containing 20mM Tris 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.
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Synonyms
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.
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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
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN.
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 :
IL 17 A/F MouseDescription:
Interleukin-17 A/F Heterodimer Mouse Recombinant
IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.
Product # :
CYT-640Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
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- More Info
Description
Interleukin-17 A/F Mouse Recombinant produced in E.Coli is a heterodimeric, non-glycosylated polypeptide comprised of IL17A monomeric subunit & and IL17F monomeric subunit containing a total of 266 amino acids and having a total molecular mass of 29.8kDa. The IL-17 A/F is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 97.0% as determined by SDS-PAGE.
More Info
-
Introduction
Human IL-17A/F is a 40kDa glycoprotein which is secreted as a disulfide-linked heterodimer. IL-17A/F consists of two proteins of the IL-17 family, IL-17A and IL17F. Proteins of the 6 homodimeric IL17 family show a cysteine knot motif that contains two disulfide-bonds. Human IL17A is produced as a 155 a.a precursor that includes a 23 amino acids signal sequence and a 132 amino acid chain that includes an N-linked glycosylation site. Human IL17F is produced as a 153 amino acid precursor with a 20 amino acid signal sequence and a 133 amino acid region. Similar to IL17A, IL17F also has an N-linked glycosylation site. Both proteins (IL17A & IL17F) share 50% amino acid sequence identity. Human IL17A & IL17F show approximately 60% homology in their amino acid sequence to mouse IL-17A and IL-17F. Interleukin-17A/F and IL17A, IL17F homodimers are manufactured by activted CD4+ T cells, called Th17. IL-23 causes Th17 lymphocytes to manufacture IL-17A/F. IL17RA and IL17RC form a heterodimer for the binding of IL17A and IL17F. IL-17A/F binds IL-17RA. Interleukin-17A/F induces chemokine production and airway neutrophilia with intermediate potency between IL17A (most potent) and IL17F (least potent).
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Synonyms
IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Mouse IL17 A/F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse IL17 A/F 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 Mouse IL17 A/F 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
RKNPKAGVPALQKAGNCPPLEDNTVRVDIRIFNQNQGISVPREFQNRSSSP
WDYNITRDPHRFPSEIAEAQCRHSGCINAQGQEDSTMNSVAIQQEILVLRR
EPQGCSNSFRLEKMLLKVGCTCVKPIVHQAAAAIIPQSSACPNTEAKDFLQ
NVKVNLKVFNSLGAKVSSRRPSDYLNRSTSPWTLHRNEDPDRYPSVIWE
AQCRHQRCVNAEGKLDHHMNSVLIQQEILVLKREPESCPFTFRVEKMLV
GVGCTCVASIVRQAA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TGFB2 Human, HEKDescription:
Transforming Growth Factor-Beta 2 Human Recombinant, HEK
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Product # :
CYT-112Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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- biological activity
- More Info
Description
TGF-b 2 Human Recombinant produced in HEK cells is a non-glycosylated homodimer, having a total molecular weight of 25kDa.The TGF-b 2 is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
TGF-b 2 was lyophilized from a 0.2µm filtered solution containing 50mM sodium acetate pH 4.5.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2), the ED50 is 0.16ng/ml.More Info
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Introduction
TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-beta (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.
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Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TGF-b 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized TGF-b 2 in sterile solution containing 20% ethanol, 50mM sodium acetate and 75mM acetic acid.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Adiponectin Human, Sf9Description:
Adiponectin Human Recombinant, Sf9
Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.
Product # :
CYT-1002Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Acrp30 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.
sds-page
More Info
-
Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules. -
Synonyms
Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.
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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
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.9kDa.
What is the source or expression system of ADIPONECTIN Protein?
Sf9, Baculovirus cells.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.
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.
- View Data Sheet
Name :
AIMP1 HumanDescription:
Aminoacyl tRNA Synthetase Complex-Interacting Multifunctional Protein 1 Human Recombinant
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.
Product # :
CYT-021Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
AIMP1 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 356 amino acids (1-336 a.a.) and having a molecular mass of 39.2kDa (Molecular size on SDS-PAGE will appear higher). The AIMP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AIMP1 solution (0.25mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
AIMP1 (EMPA2 or p43) is a cytokine that is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of the AIMP1 cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. Furthermore, AIMP1 is involved in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
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Synonyms
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
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Background
What is the molecular weight/Mw of AIMP1 HUMAN Protein?
AIMP1 HUMAN Protein has a total Mw of 39.2kDa.
What is the source or expression system of AIMP1 HUMAN Protein?
Escherichia Coli.
What is the Purity of AIMP1 HUMAN Protein?
AIMP1 HUMAN Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of AIMP1 HUMAN Protein?
The biological functionality of AIMP1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of AIMP1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
What applications can AIMP1 HUMAN Protein be used in?
AIMP1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for AIMP1 HUMAN Protein?
The endotoxin level is minimal, AIMP1 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.
- View Data Sheet
Name :
ANKRD1 HumanDescription:
Ankyrin Repeat Domain 1 Human Recombinant
Ankyrin Repeat Domain 1 (Cardiac Muscle), Cardiac Ankyrin Repeat Protein, Cytokine-Inducible Gene C-193 Protein, Ankyrin Repeat Domain-Containing Protein 1, Cytokine-Inducible Nuclear Protein, Liver Ankyrin Repeat Domain 1, BA320F15.2, CARP, ALRP, CVARP, MCARP, HA1A2, C193.
Product # :
PRO-1219Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANKRD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 342 amino acids (1-319) and having a molecular mass of 38.6 kDa.ANKRD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ANKRD1 solution contains 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 5mM DTT and 50% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
ANKRD1 takes part in endothelial cell activation and performs as a nuclear transcription factor which negatively controls the expression of cardiac genes.
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Synonyms
Ankyrin Repeat Domain 1 (Cardiac Muscle), Cardiac Ankyrin Repeat Protein, Cytokine-Inducible Gene C-193 Protein, Ankyrin Repeat Domain-Containing Protein 1, Cytokine-Inducible Nuclear Protein, Liver Ankyrin Repeat Domain 1, BA320F15.2, CARP, ALRP, CVARP, MCARP, HA1A2, C193.
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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 MGS MMVLKVE ELVTGKKNGN GEAGEFLPED FRDGEYEAAV TLEKQEDLKT LLAHPVTLGE QQWKSEKQRE AELKKKKLEQ RSKLENLEDL EIIIQLKKRK KYRKTKVPVV KEPEPEIITE PVDVPTFLKA ALENKLPVVE KFLSDKNNPD VCDEYKRTAL HRACLEGHLA IVEKLMEAGA QIEFRDMLES TAIHWASRGG NLDVLKLLLN KGAKISARDK LLSTALHVAV RTGHYECAEH LIACEADLNA KDREGDTPLH DAVRLNRYKM IRLLIMYGAD LNIKNCAGKT PMDLVLHWQN GTKAIFDSLR ENSYKTSRIA TF
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 :
NEUROG3 HumanDescription:
Neurogenin 3 Human Recombinant
Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.
Product # :
CYT-811Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NEUROG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-214) and having a molecular mass of 25.1 kDa. NEUROG3 is fused to a 20 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The NEUROG3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
NEUROG3 is a common helix-loop-helix (bHLH) transcription factor which takes part in neurogenesis. NEUROG3 functions as a heterodimer with another bHLH protein. Mutations in this gene can result in congenital malabsorptive diarrhea 4 (DIAR4).
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Synonyms
Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.
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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 MTPQPSGAPT VQVTRETERS FPRASEDEVT CPTSAPPSPT RTRGNCAEAE EGGCRGAPRK LRARRGGRSR PKSELALSKQ RRSRRKKAND RERNRMHNLN SALDALRGVL PTFPDDAKLT KIETLRFAHN YIWALTQTLR IADHSLYALE PPAPHCGELG SPGGSPGDWG SLYSPVSQAG SLSPAASLEE RPGLLGATSS ACLSPGSLAF SDFL
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HBsAg ayw, 31kDaDescription:
Hepatitis B Surface Antigen ayw Recombinant
Product # :
HBS-877Price :
Quantity :
Shipping Method :
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Description
Recombinant HbsAg ayw full length is a 31kDa proteincloned from HBV 320 genome and fused to 6xHis Tag.
Source
Escherichia Coli.
Formulation
Sterile Filtered solution (1mg/ml) contains 7.5mM phosphate buffer pH-7.2, 75mM NaCl and 50% glycerol.
Purity
Greater than 99.0% as determined by SDS-PAGE.
More Info
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Introduction
HBsAg is the surface antigen of the Hepatitis-B-Virus (HBV). The capsid of a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
HBsAg Should be stored at 4°C between 3-4 weeks and for future use should be stored below -18°C.
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Amino Acid Sequence
MGQNLSTSNP LGFFPDHQLD PAFRANTANP DWDFNPNKDT WPDANKVGAG AFGLGFTPPH
GGLLGWSPQA QGILQTLPTN PPPASTNRQS GRQPTPLSPP LRNTHPQAMQ WNSTTFHQTL
QDPRVRGLYF PAGGSSSGTV NPVPTTVSPI SSIFSRIGDP TRILTIPQSL DSWWTSLNFL
GGTTVCLGQN SQSPTSNHSP TSCPPTCGYR WMCLMLPVCP LIPGSSTTTG PCRTCTTPAQ
GTMYPSCCCT KPSDGNCTCP IPSSWAFGKF LWEWASHHHH 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 :
IL31 Canine, HEKDescription:
Interleukin-31 Canine Recombinant, HEK
IL-31, Interleukin 31, IL31.
Product # :
CYT-1215Price :
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Description
IL31 Canine Recombinant is a single, glycosylated, polypeptide chain (24-159 a.a) containing a total of 136 amino acids, having a molecular mass of 25.2 kDa. IL31 is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IL31 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Synonyms
IL-31, Interleukin 31, IL31.
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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
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQ.
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Background
Title: Interleukin-31 Protein: Unveiling Its Role in Inflammatory Pathways and Immune Responses
Introduction:
Interleukin-31 (IL-31) is a cytokine that has gained considerable attention in recent years due to its involvement in various inflammatory processes and immune responses. Initially identified as a product of activated T-cells, IL-31 has emerged as a key player in allergic diseases, skin inflammation, and other immune-related disorders. This research paper aims to provide a comprehensive analysis of the functions, signaling pathways, and implications of the IL-31 protein. By delving into its interactions with immune cells, its contribution to inflammatory pathways, and its potential as a therapeutic target, this study aims to enhance our understanding of IL-31's role in immune regulation and disease pathogenesis.
Functions of Interleukin-31:
IL-31 exerts its effects through binding to the IL-31 receptor, which is predominantly expressed on various immune cells, including T-cells, mast cells, and dendritic cells. Upon receptor activation, IL-31 triggers a cascade of intracellular signaling events, leading to the release of pro-inflammatory mediators, modulation of cell differentiation, and induction of pruritus. Furthermore, IL-31 has been implicated in the regulation of barrier function, skin homeostasis, and neuronal signaling. Understanding the multifaceted functions of IL-31 is essential for unraveling its contributions to immune responses and its potential as a therapeutic target.
Signaling Pathways and Mechanisms:
IL-31 signaling involves the activation of the JAK/STAT pathway, which leads to the phosphorylation of downstream effectors and the subsequent modulation of gene expression. Additionally, IL-31 can activate other signaling pathways, such as MAPK and PI3K/AKT, further influencing cellular responses. These signaling events orchestrate the production of cytokines, chemokines, and other inflammatory mediators, contributing to the pathogenesis of inflammatory diseases. Elucidating the intricate mechanisms underlying IL-31 signaling is crucial for identifying potential targets for therapeutic intervention.
Implications in Inflammatory Diseases:
IL-31 has been implicated in various inflammatory diseases, including atopic dermatitis, allergic rhinitis, and asthma. Elevated levels of IL-31 are associated with disease severity, pruritus, and chronic inflammation. Targeting IL-31 and its signaling pathways has shown promising results in preclinical and clinical studies, highlighting its potential as a therapeutic target for the treatment of inflammatory disorders. Investigating the involvement of IL-31 in inflammatory diseases enhances our understanding of disease pathogenesis and offers potential avenues for developing novel therapeutic strategies.
Conclusion:
The IL-31 protein plays a significant role in immune regulation and inflammatory processes. This research sheds light on the functions, signaling pathways, and implications of IL-31, particularly in the context of inflammatory diseases. Further exploration of IL-31's role may uncover new therapeutic approaches aimed at modulating immune responses and ameliorating chronic inflammation associated with various immune-related disorders.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on IL-31 for a comprehensive list of references and sources.
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 :
IL8 Canine, HEKDescription:
Interleukin-8, HEK Canine Recombinant
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
Product # :
CHM-045Price :
Quantity :
Shipping Method :
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Description
IL8 Canine, HEK Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 80 amino acids (28-101 a.a) and having a molecular mass of 9.4 kDa.IL8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IL8 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.
Purity
Greater than 90.0% 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. IL8 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
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
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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
VSSELRCQCI KTHSTPFHPK YIKELRVIDS GPHCENSEII VKLFNGNEVC LDPKEKWVQK VVQIFLKKAE KQDPHHHHHH
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 :
MINA HumanDescription:
MYC Induced Nuclear Antigen Human Recombinant
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
Product # :
PRO-2078Price :
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Description
MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MINA protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.
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Synonyms
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
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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 MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.
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.