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Name :
RHOQ HumanDescription:
Ras Homolog Gene Family Member Q Human Recombinant
ARHQ, RASL7A, TC10, TC10A, Rho-related GTP-binding protein RhoQ, Ras-like protein TC10, Ras-like protein family member 7A, RHOQ.
Product # :
PRO-1451Price :
Quantity :
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Shipped with Ice Packs
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Description
RHOQ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202 a.a) and having a molecular mass of 24.7kDa. RHOQ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RHOQ protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
RHOQ (rho-related GTP-binding protein RhoQ) is a small signaling G protein which cycles between an active GTP-bound and an inactive GDP-bound state. In the active state it binds to a diversity of effector proteins to regulate cellular responses. Ras-like protein belongs to the Rac subfamily of the Rho family of GTPases. RHOQ is involved in epithelial cell polarization processes. In addition, RHOQ plays a role in CFTR trafficking to the plasma membrane. RHOQ causes the formation of thin, actin-rich surface projections called filopodia.
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Synonyms
ARHQ, RASL7A, TC10, TC10A, Rho-related GTP-binding protein RhoQ, Ras-like protein TC10, Ras-like protein family member 7A, RHOQ.
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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 MGSMAHGPGA LMLKCVVVGD GAVGKTCLLM SYANDAFPEE YVPTVFDHYA VSVTVGGKQY LLGLYDTAGQ EDYDRLRPLS YPMTDVFLIC FSVVNPASFQ NVKEEWVPEL KEYAPNVPFL LIGTQIDLRD DPKTLARLND MKEKPICVEQ GQKLAKEIGA CCYVECSALT QKGLKTVFDE AIIAILTPKK HTVKKRIGSR CINCC.
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 :
SERPINA1 HumanDescription:
Alpha 1 Antitrypsin Human Recombinant
Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.
Product # :
PRO-529Price :
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Description
SERPINA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (25-418) and having a molecular mass of 44.4 kDa. The SERPINA1 protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl pH-7.5, 1mM DTT, 10% glycerol, and 2mM EDTA.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. Antral SERPINA1 expression is particularly induced by H. pylori infection. lung and prostate cancers have shown a significant increase in SERPINA1 serum levels compared with healthy controls though breast cancers did not show a significant change. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.
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Synonyms
Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.
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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
MEDPQGDAAQ KTDTSHHDQD HPTFNKITPN LAEFAFSLYR QLAHQSNSTN IFFSPVSIAT AFAMLSLGTK ADTHDEILEG LNFNLTEIPE AQIHEGFQEL LRTLNQPDSQ LQLTTGNGLF LSEGLKLVDK FLEDVKKLYH SEAFTVNFGD TEEAKKQIND YVEKGTQGKI VDLVKELDRD TVFALVNYIF FKGKWERPFE VKDTEEEDFH VDQVTTVKVP MMKRLGMFNI QHCKKLSSWV LLMKYLGNAT AIFFLPDEGK LQHLENELTH DIITKFLENE DRRSASLHLP KLSITGTYDL KSVLGQLGIT KVFSNGADLS GVTEEAPLKL SKAVHKAVLT IDEKGTEAAG AMFLEAIPMS IPPEVKFNKP FVFLMIDQNT KSPLFMGKVV NPTQK.
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 :
STRADA HumanDescription:
STE20-Related Kinase Adaptor Alpha Human Recombinant
LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.
Product # :
PRO-1992Price :
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Description
STRADA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314a.a) and having a molecular mass of 37kDa. STRADA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STRADA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
STE20-Related Kinase Adaptor Alpha (STRADA) is a part of the STE- 20 like kinase family which stimulates MAPK pathways by activating MAPKKK. STRADA is an upstream activator of LKB1 and also leads the sub-cellular localization of LKB1 by fixing it in the cytoplasm. The interaction between STRADA-LKB1 leads to phosphorylation of STRADA and enhanced autophosphorylation of LKB1.
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Synonyms
LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.
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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 MGSMSFLVSK PERIRTNDAS SESIASFSKQ EVMSSFLPEG GCYELLTVIG KGFEDLMTVN LARYKPTGEY VTVRRINLEA CSNEMVTFLQ GELHVSKLFN HPNIVPYRAT FIADNELWVV TSFMAYGSAK DLICTHFMDG MNELAIAYIL QGVLKALDYI HHMGYVHRSV KASHILISVD GKVYLSGLRS NLSMISHGQR QRVVHDFPKY SVKVLPWLSP EVLQQNLQGY DAKSDIYSVG ITACELANGH VPFKDMPATQ MLLEKLNGTV PCLLDTSTIP AEELTMSPSR SVANSGLSDS LTTSTPRPSN GPVPAPS.
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 :
TSSK6 HumanDescription:
Testis Specific Serine Kinase 6 Human Recombinant
TSSK6, Testis-Specific Serine Kinase 6, Cancer/Testis Antigen 72, SSTK, Small Serine/Threonine Kinase, CT72, TSK-6, TSSK4, Serine/Threonine Protein Kinase SSTK, Testis-Specific Serine/Threonine-Protein Kinase 6, EC 2.7.11.1, TSSK-6, Serine/Threonine-Protein Kinase SSTK, Testis-Specific Kinase 6.
Product # :
PKA-220Price :
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Description
TSSK6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273) and having a molecular mass of 32.7kDa.TSSK6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TSSK6 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
Testis-specific serine/threonine-protein kinase 6 (TSSK6) is an intronless gene, which belongs to the CAMK Ser/Thr protein kinase family. The TSSK6 protein contains one protein kinase domain. TSSK6 is highly expressed in the testis and lowly expressed in the colon, prostate, thymus, small intestine, and peripheral blood leukocytes. TSSK6 interacts with the heatshock proteins HSPA8, HSPCB, and HAPA1A; these interactions seem to be essential for TSSK6 kinase activity. TSSK6 plays a role in DNA condensation during postmeiotic chromatin remodeling. In addition, TSSK6 is required for sperm production and function.
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Synonyms
TSSK6, Testis-Specific Serine Kinase 6, Cancer/Testis Antigen 72, SSTK, Small Serine/Threonine Kinase, CT72, TSK-6, TSSK4, Serine/Threonine Protein Kinase SSTK, Testis-Specific Serine/Threonine-Protein Kinase 6, EC 2.7.11.1, TSSK-6, Serine/Threonine-Protein Kinase SSTK, Testis-Specific Kinase 6.
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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 MGSMSGDKLL SELGYKLGRT IGEGSYSKVK VATSKKYKGT VAIKVVDRRR APPDFVNKFL PRELSILRGV RHPHIVHVFE FIEVCNGKLY IVMEAAATDL LQAVQRNGRI PGVQARDLFA QIAGAVRYLH DHHLVHRDLK CENVLLSPDE RRVKLTDFGF GRQAHGYPDL STTYCGSAAY ASPEVLLGIP YDPKKYDVWS MGVVLYVMVT GCMPFDDSDI AGLPRRQKRG VLYPEGLELS ERCKALIAEL LQFSPSARPS AGQVARNCWL RAGDSG.
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 :
CIAPIN1 HumanDescription:
Cytokine Induced Apoptosis Inhibitor 1 Human Recombinant
DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.
Product # :
PRO-024Price :
Quantity :
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Shipped with Ice Packs
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Description
CIAPIN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312 a.a.) and having a molecular mass of 36kDa.CIAPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CIAPIN1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Anamorsin, ( CIAPIN) is a member of anamorsin family. CIAPIN mainly expressed in the cytoplasm of liver, pancreas and heart tissue cells and does not show any homology to known apoptosis regulatory molecules of the Bcl-2 or CASP families, or to signal transduction molecules. CIAPIN1 Expression is reliant on growth factor stimulation. It is a ubiquitously expressed protein, and when it is overexpressed, it grants apoptotic resistance.
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Synonyms
DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.
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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 MGSMADFGIS AGQFVAVVWD KSSPVEALKG LVDKLQALTG NEGRVSVENI KQLLQSAHKE SSFDIILSGL VPGSTTLHSA EILAEIARIL RPGGCLFLKE PVETAVDNNS KVKTASKLCS ALTLSGLVEV KELQREPLTP EEVQSVREHL GHESDNLLFV QITGKKPNFE VGSSRQLKLS ITKKSSPSVK PAVDPAAAKL WTLSANDMED DSMDLIDSDE LLDPEDLKKP DPASLRAASC GEGKKRKACK NCTCGLAEEL EKEKSREQMS SQPKSACGNC YLGDAFRCAS CPYLGMPAFK PGEKVLLSDS NLHDA.
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 :
RNASEH2A E.ColiDescription:
Ribonuclease H2A E.Coli Recombinant
AGS4, JUNB, RNASEHI, RNHIA, RNHL , Ribonuclease H2 subunit A, Aicardi-Goutieres syndrome 4 protein, RNase H(35), Ribonuclease HI large subunit, RNase HI large subunit, EC=3.1.26.4.
Product # :
ENZ-713Price :
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Shipped with Ice Packs
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Description
RNASEH2A Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.8kDa.RNASEH2A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RNASEH2A solution (0.5mg/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
Ribonuclease H2 subunit A (RNASEH2A) is a member of the RNase HII family and eukaryotic subfamily. RNASEH2A Plays a part in DNA replication, probably by mediating the removal of lagging-strand Okazaki fragment RNA primers throughout DNA replication. RNASEH2A catalyzes the endonucleolytic cleavage of RNA to a 5’-phosphomonoester and is capable to bind magnesium or manganese as cofactors. Aicardi-Goutieres syndrome type 4 (AGS4) caused by defects in RNASEH2A.
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Synonyms
AGS4, JUNB, RNASEHI, RNHIA, RNHL , Ribonuclease H2 subunit A, Aicardi-Goutieres syndrome 4 protein, RNase H(35), Ribonuclease HI large subunit, RNase HI large subunit, EC=3.1.26.4.
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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 MGSMDLSELE RDNTGRCRLS SPVPAVCRKE PCVLGVDEAG RGPVLGPMVY AICYCPLPRL ADLEALKVAD SKTLLESERE RLFAKMEDTD FVGWALDVLS PNLISTSMLG RVKYNLNSLS HDTATGLIQY ALDQGVNVTQ VFVDTVGMPE TYQARLQQSF PGIEVTVKAK ADALYPVVSA ASICAKVARD QAVKKWQFVE KLQDLDTDYG SGYPNDPKTK AWLKEHVEPV FGFPQFVRFS WRTAQTILEK EAEDVIWEDS ASENQEGLRK ITSYFLNEGS QARPRSSHRY FLERGLESAT SL.
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 :
SNRPD2 Human, Sf9Description:
Small Nuclear Ribonucleoprotein Polypeptide D2 Human Recombinant, Sf9
Small nuclear ribonucleoprotein Sm D2, Sm-D2, snRNP core protein D2, SNRPD2, SNRPD1, SMD2.
Product # :
PRO-995Price :
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Description
SNRPD2 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 14,773 Dalton. SNRPD2 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
SNRPD2 is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
SNRPD2 is a member of the small nuclear ribonucleoprotein core protein family. SNRPD2 is a small nuclear ribonucleoprotein (snRNPs) which comprises the spliceosome in eukaryotes. SNRPD2 is required for pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis.
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Synonyms
Small nuclear ribonucleoprotein Sm D2, Sm-D2, snRNP core protein D2, SNRPD2, SNRPD1, SMD2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels including CDC international reference sera).
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coating concentration
0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.
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Applications
Western blot with anti-Sm positive patient sera.
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 :
CD14 Human HEKDescription:
CD14 Human Recombinant HEK
Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein, CD14.
Product # :
PRO-1642Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CD14 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 341 amino acids (20-352). CD14 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
CD14 was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, PH 7.4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CD14 (also known lipopolysaccharide (LPS) receptor) is expressed strongly on monocytes and macrophage and weakly on the surface of neutrophils. CD14 is anchored to cells by linkage to glycosylphosphatidylinositol (GPI) and functions as a high affinity receptor for complexes of LPS and LPS binding protein (LBP). Soluble CD14, also binding to LPS, acts at physiological concentration as an LPS agonist and has, at higher concentrations, an LPS antagonizing effect in cell activation. CD14 has been shown to bind apoptotic cells.
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Synonyms
Monocyte differentiation antigen CD14, Myeloid cell-specific leucine-rich glycoprotein, CD14.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CD14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD14 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 CD14 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
TTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVD
ADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKIT
GTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAF
SCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCA
ALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKL
RVLDLSCNRLNRAPQPDELPEVDNLTLDGNPFLVPGTALPHEGSMNSGVVPACVDHHHHHH
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 :
GST, HisDescription:
Glutathione S-Transferase Recombinant, His Tag
Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.
Product # :
ENZ-451Price :
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Shipped with Ice Packs
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Description
Recombinant Schistosoma japonicum GST full length protein contains a total of 244 amino acids (1-218 a.a.) expressed in E.coli, having a molecular mass of 28.3kDa. The GST protein is fused to a 20 amino acids His-Tag at N-terminus. The GST protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GST is supplied in PBS pH 7.4 & 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
>10 units/mg, & is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH-6.5 at 25C.
More Info
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Introduction
Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions. -
Synonyms
Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.
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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 MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMAIIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALDVVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CTF1 RatDescription:
Cardiotrophin-1 Rat Recombinant
Cardiotrophin-1, CT-1, Ctf1.
Product # :
CYT-199Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.More Info
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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
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Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.
What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 33 RatDescription:
Interleukin-33 Rat Recombinant
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
Product # :
CYT-150Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a molecular mass of 17.4kDa.The IL 33 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine D10S cells is <0.5ng/ml, corresponding to a specific activity of >2,000,000units/mg.More Info
-
Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
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Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL-33 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized IL-33 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SIQGTSLLTE SCALSTYNDQ SVSFVLENGC YVINVEDCGK NQEKDKVLLR YYESSFPAQS GDGVDGKKLM VNMSPIKDTD IWLNANDKDY SVELQKGDVS PPDQAFFVLH KKSSDFVSFE CKNLPGTYIG VKDNQLALVE ENDESCNNIM FKLSKM
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 :
LIF RatDescription:
Leukemia Inhibitory Factor Rat Recombinant
Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.
Product # :
CYT-731Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leukemia Inhibitory Factor (LIF) Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.8 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LIF Rat was lyophilized from 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity of rat LIF is determined by the ability to induce differentiation of M1 myeloid leukemic cells. The minimum detectable concentration of rat LIF in this assay is 0.5ng/mL.More Info
-
Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
-
Synonyms
Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SPLPITPVNA TCAIRHPCHG NLMNQIKSQL AQLNGSANAL FISYYTAQGE PFPNNVDKLC APNMTDFPPF HANGTEKTKL VELYRMVTYL GASLTNITWD QKNLNPTAVS LQIKLNATTD VMRGLLSSVL CRLCNKYHVG HVDVPCVPDN SSKEAFQRKK LGCQLLGTYK QVISVLAQAF .
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 :
MCSF Mouse, Sf9Description:
Macrophage Colony Stimulating Factor Mouse Recombinant, Sf9
M-Csf, Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, C87615, MCSF, op, Processedmacrophage colony-stimulating factor 1.
Product # :
CYT-1141Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MCSF Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 164 amino acids (33-187 aa) and having a molecular mass of 19.1 kDa.MCSF is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The MCSF solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Determined by cell proliferation assay using M-NFS-60 mouse myelogenous leukemia lymphoblast cells. ED50 range for this effect is ≤ 4ng/ml.
More Info
-
Introduction
Macrophage Colony Stimulating Factor (M CSF) or colony stimulating factor 1, is a cytokine, that promoted differentiation in hematopoietic stem cells to macrophages. Another role of M CSF is to bind to its receptor (colony stimulating factor 1 receptor) and to take part in placenta growth and development.
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Synonyms
M-Csf, Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, C87615, MCSF, op, Processedmacrophage colony-stimulating factor 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.
-
Amino Acid Sequence
ADPKEVSEHC SHMIGNGHLK VLQQLIDSQM ETSCQIAFEF VDQEQLDDPV CYLKKAFFLV
QDIIDETMRF KDNTPNANAT ERLQELSNNL NSCFTKDYEE QNKACVRTFH ETPLQLLEKI
KNFFNETKNL LEKDWNIFTK NCNNSFAKCS SRDVVTKPHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Treponema p17 16.4kDaDescription:
Treponema pallidum p17, 16.4kDa Recombinant
Product # :
TRP-252Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
- formulation
- purity
- More Info
Description
Recombinant Treponema p17 produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 16.4kDa and fused to a His tag at N-terminus.
Source
Escherichia Coli.
Formulation
Lyophilized from 1mg/ml in 20mM sodium carbonate pH-10.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Treponema p17 although stable at room temperature for 4 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Treponema p17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PTPS HumanDescription:
6-Pyruvoyltetrahydropterin Synthase Human Recombinant
PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.
Product # :
ENZ-471Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
6-PyruvoylTetrahydropterin Synthase Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145) and having a molecular mass of 18.5kDa. 6-PyruvoylTetrahydropterin Synthase is fused to a 20 amino acid His Tag at N-terminus and purified using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
6-PyruvoylTetrahydropterin Synthase is formulated in 20mM Tris-HCl buffer pH-8, 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
-
Introduction
6-PyruvoylTetrahydropterin Synthase is part of the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. 6-PyruvoylTetrahydropterin Synthase catalyzes the elimination of inorganic triphosphate from dihydroneopterin triphosphate, which is the second and irreversible step in the biosynthesis of tetrahydrobiopterin from GTP. Tetrahydrobiopterin, is a necessary cofactor and regulator of a range of enzyme activities, including enzymes involved in serotonin biosynthesis and NO synthase activity. Mutations in 6-PyruvoylTetrahydropterin Synthase gene result in hyperphenylalaninemia.
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Synonyms
PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.
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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 MSTEGGGRRC QAQVSRRISF SASHRLYSKF LSDEENLKLF GKCNNPNGHG HNYKVVVTVH GEIDPATGMV MNLADLKKYM EEAIMQPLDH KNLDMDVPYF ADVVSTTENV AVYIWDNLQK VLPVGVLYKV KVYETDNNIV VYKGE.
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 :
TNFR2 HumanDescription:
Tumor Necrosis Factor Receptor Type 2 Human Recombinant
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, TNFRSF1B, TNFBR, TNFR2.
Product # :
CYT-769Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNFR2 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 20kDa. The TNFR2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFR2 was Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to inhibit the TNF-a mediated cytotoxicity in the L-929 cells is less than 0.2µg/ml, corresponding to a specific activity of > 5000IU/mg in the presence of 0.25ng/mL of rHuTNF-a.More Info
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Introduction
TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury. -
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, TNF-RII, TNFR-II, p75, p80 TNF-alpha receptor, TNFRSF1B, TNFBR, TNFR2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TNFR2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TNFR2 should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized TNFR2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MPAQVAFTPY APEPGSTCRL REYYDQTAQM CCSKCSPGQH AKVFCTKTSD TVCDSCEDST YTQLWNWVPE CLSCGSRCSS DQVETQACTR EQNRICTCRP GWYCALSKQE GCRLCAPLRK CRPGFGVARP GTETSDVVCK PCAPGTFSNT TSSTDICRPH QICNVVAIPG NASMDAVCTS TSPT.
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 :
S100A7A HumanDescription:
S100 Calcium Binding Protein A7A Human Recombinant
NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.
Product # :
PRO-756Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The S100A7A Human Recombinant is manufactured with N-terminal fusion of 9 amino acids His Tag. The S100A7A His -Tagged Fusion Protein is a 12.3kDa protein containing 109 amino acid residues and 9 additional amino acid residues - His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
S100A7A takes part in epidermal differentiation and inflammation thus is significant for the pathogenesis of psoriasis and other diseases.
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Synonyms
NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.
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Stability
Store lyophilized S100A7A Human recombinant at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted S100A7A can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
Add pyrogen free water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MMKHHHHHHASNTQAERSIIG MIDMFHKYTG RDGKIEKPSL LTMMKENFPN FLSACDKKGI HYLATVFEKK DKNEDKKIDF SEFLSLLGDI AADYHKQSHG AAPCSGGSQ.
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 :
SOST Human, HEKDescription:
Sclerostin Human Recombinant, HEK
Sclerostin, SOST, CDD, VBCH.
Product # :
PRO-2481Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SOST Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-213) containing 196 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 22.4kDa (calculated).
Source
HEK293 Cells.
Formulation
SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
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Synonyms
Sclerostin, SOST, CDD, VBCH.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SOST is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
QGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SPINT2 Human, Sf9Description:
Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant, Sf9
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
Product # :
PRO-2219Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPINT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 176 amino acids (28-197 a.a.) and having a molecular mass of 20kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SPINT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SPINT2 protein solution (0.2mg/ml) contains phosphate buffered saline (pH 7.4) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
SPINT2 is a transmembrane protein acts as an inhibitor of HGF activator. SPINT2 inhibits plasmin, plasma and tissue kallikrein, and factor XIa. SPINT2 has two extracellular Kunitz domains that inhibit few serine proteases. SPINT2 is assumed tumor suppressor, mutations in SPINT2 leads to a congenital sodium diarrhea.
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Synonyms
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADRERSIHDF CLVSKVVGRC RASMPRWWYN VTDGSCQLFV YGGCDGNSNN YLTKEECLKK CATVTENATG DLATSRNAAD SSVPSAPRRQ DSEDHSSDMF NYEEYCTANA VTGPCRASFP RWYFDVERNS CNNFIYGGCR GNKNSYRSEE ACMLRCFRQQ ENPPLPLGSK HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
OSCAR Human, Sf9Description:
Osteoclast Associated, Immunoglobulin-Like Receptor Human Recombinant, Sf9
OSCAR, PIgR-3, PIGR3, hOSCAR, PIgR-3, Poly-Ig Receptor 3.
Product # :
PRO-2546Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
OSCAR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-282 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 270 amino acids and having a molecular mass of 29.2kDa.OSCAR shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
OSCAR protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Osteoclast-associated immunoglobulin-like receptor isoform 6 or OSCAR, is a receptor for surfactant protein D that can be found on human myeloid cells. OSCAR is part of the TNF-α release from human CCR2+ inflammatory monocytes process. The protein is involved in antigen presentation and activation of dendritic cells. Preosteoclasts or mature osteoclasts express the OSCAR protein. Patients that suffer from RA (rheumatoid arthritis) has upregulations on monocytes which present increased proosteoclastogenic potential.
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Synonyms
OSCAR, PIgR-3, PIGR3, hOSCAR, PIgR-3, Poly-Ig Receptor 3.
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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.
-
Amino Acid Sequence
DITPSVPPAS YHPKPWLGAQ PATVVTPGVN VTLRCRAPQP AWRFGLFKPG EIAPLLFRDV SSELAEFFLE EVTPAQGGSY RCCYRRPDWG PGVWSQPSDV LELLVTEELP RPSLVALPGP VVGPGANVSL RCAGRLRNMS FVLYREGVAA PLQYRHSAQP WADFTLLGAR APGTYSCYYH TPSAPYVLSQ RSEVLVISWE GEGPEARPAS SAPGMQAPGP PPSDPGAQAP SLSSFRPRGL VLQPLLPQTQ DSWDPAPPPS DPGVHHHHHH.
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 :
Procalcitonin RatDescription:
Procalcitonin Rat Recombinant
Calcitonin, Calca, Calc.
Product # :
HOR-019Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
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- formulation
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Description
Procalcitonin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val26-Asn136) containing 121 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 13.6kDa.
Source
Escherichia Coli.
Formulation
Procalcitonin was filtered (0.4µm) and lyophilized in 20mM TRIS and 50mM NaCl, pH 8.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
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Synonyms
Calcitonin, Calca, Calc.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASVPLRSTLESS PGMATLSEEE ARLLAALVQN YMQMKVRELE QEEEQEAEGS SLDSPRSKRC GNLSTCMLGT YTQDLNKFHT FPQTSIGVGA PGKKRDMAKD LETNHHPYFG N.
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 :
Pen a 1.0101Description:
Tropomyosin Pen a 1.0101 Recombinant
Product # :
ALR-024Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Tropomyosin Pen a 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 38kDa.Pen a 1.0101 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Pen a 1.0101 is supplied in 20mM HEPES buffer pH-7.9 200mM NaCl and 6M Urea.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Pen a 1.0101 is a Tropomyosin and the only major allergen in brown shrimp Penaeus aztecus. The panallergen is highly conserved and soluble muscle protein. Pen a 1.0101 is has an alpha-helical homodimeric, coiled-coil structure.
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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.Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
S100A5 HumanDescription:
S100 Calcium Binding Protein A5 Human Recombinant
Protein S100-A5, Protein S-100D, S100 calcium-binding protein A5, S100A5, S100D.
Product # :
PRO-147Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A5 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 112 amino acids (1-92 a.a.) and having a molecular mass of 12.9kDa. The S100A5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The S100A5 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
S100 calcium binding protein A5 (S100A5) belongs to the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 family members are localized in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A5 has a Ca2+ affinity 20-100 fold higher than the other S100 proteins investigated under identical conditions. Furthermore, S100A5 protein binds Zn2+ and Cu2+, and Cu2+ strongly which harms the binding of Ca2+. S100A5 is expressed in very limited regions of the adult brain.
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Synonyms
Protein S100-A5, Protein S-100D, S100 calcium-binding protein A5, S100A5, S100D.
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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 METPLEKALT TMVTTFHKYS GREGSKLTLS RKELKELIKK ELCLGEMKES SIDDLMKSLD KNSDQEIDFK EYSVFLTMLC MAYNDFFLED NK.
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 :
SAP18 HumanDescription:
Sin3A-Associated Protein 18kDa Human Recombinant
Histone deacetylase complex subunit SAP18, Sin3-associated polypeptide 18 kDa, Sin3-associated polypeptide p18, Cell growth-inhibiting protein 38, 2HOR0202, SAP18, GIG38.
Product # :
PRO-707Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
- purity
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Description
SAP18 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 173 amino acids (20- 172 a.a.) and having a molecular mass of 19.7 kDa.The SAP18 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SAP18 solution contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 30% glycerol, 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SAP18 is a component of the histone deacetylase complex which has a significant role in the regulation of eukaryotic gene expression. SAP18 directly interacts with SIN3 and enhances SIN3-mediated transcriptional repression once bound to the promoter. SAP18 plays an important part in gene-specific recruitment of the HDAC complex by a number of transcription factors including Gli, GAGA, and Bicoid. Histone acetylation is significant in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation is catalyzed by multisubunit complexes. SAP18 is a component of the histone deacetylase complex, which includes SIN3, SAP30, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. SAP18 is a component of a splicing-dependent multiprotein EJC (exon junction complex) placed at splice junction on mRNAs.
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Synonyms
Histone deacetylase complex subunit SAP18, Sin3-associated polypeptide 18 kDa, Sin3-associated polypeptide p18, Cell growth-inhibiting protein 38, 2HOR0202, SAP18, GIG38.
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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 MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN VPSSELQIYT WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFTDVKRPG YRVKEIGSTM SGRKGTDDSM TLQSQKFQIG DYLDIAITPP NRAPPPSGRM RPY.
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.