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1000 results found for “HNRNP”
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Name :
TXN2 HumanDescription:
Thioredoxin-2 Human Recombinant
Thioredoxin mitochondrial, Thioredoxin-2, TXN2, MTRX, TRX2, MT-TRX, TRX-2, TXN-2.
Product # :
PRO-625Price :
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Shipped with Ice Packs
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Description
MTRX Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 108 amino acids and having a molecular mass of 11 kDa.
Source
Escherichia Coli.
Formulation
TXN2 protein solution contains 1x PBS pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Specific activity is 3-4 A650/min/mg, obtained by measuring the increase of INS precipitation in absorbance at 650 nm resulting from the reduction of INS.
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Introduction
Thioredoxin-2 is a low molecular weight redox protein. TRX2 contains a redox active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The TXN2 is involved in the regulation of the mitochondrial membrane potential and in protection against oxidant-induced apoptosis. Upon stimulation of Fas, TXN2 mediates denitrosylation of mitochondria-associated caspase-3, a process required for caspase-3 activation, and promoted apoptosis.
TRX2 is important at low oxidative stress conditions.
MTRX is involved in the regulation of the mitochondrial membrane potential and cell death. Mitochondrial thioredoxin plays an important roles in protection against oxidant-induced apoptosis. Thioredoxin1 and thioredoxin2 have opposed regulatory functions on hypoxia-inducible factor-1alpha. -
Synonyms
Thioredoxin mitochondrial, Thioredoxin-2, TXN2, MTRX, TRX2, MT-TRX, TRX-2, TXN-2.
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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
MTTFNIQDGP DFQDRVVNSE TPVVVDFHAQ WCGPCKILGP RLEKMVAKQH GKVVMAKVDI DDHTDLAIEY EVSAVPTVLA MKNGDVVDKF VGIKDEDQLE AFLKKLIG.
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 :
CHP HumanDescription:
Calcium Binding Protein P22 Human Recombinant
CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.
Product # :
PRO-847Price :
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Description
CHP Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-195 a.a.) and having a molecular mass of 24.7 kDa. The CHP is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHP Human solution containing 20mM Tris-HCl pH-7.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Calcium-binding protein P22 is a phosphoprotein that binds to the sodium-hydrogen exchangers (NHEs). CHP is an essential cofactor which maintains the physiological activity of NHE family members. CHP has protein sequence resemblance to calcineurin B and it is also identified to be an endogenous inhibitor of calcineurin activity.CHP is necessary for constitutive membrane traffic. CHP Inhibits GTPase-stimulated Na(+)/H(+) exchange. CHP inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1.
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Synonyms
CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.
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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 MMGSRASTLL RDEELEEIKK ETGFSHSQIT RLYSRFTSLD KGENGTLSRE DFQRIPELAI NPLGDRIINA FFPEGEDQVN FRGFMRTLAH FRPIEDNEKS KDVNGPEPLN SRSNKLHFAF RLYDLDKDEK ISRDELLQVL RMMVGVNISD EQLGSIADRT IQEADQDGDS AISFTEFVKV LEKVDVEQKM SIRFLH.
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 :
MAF1 HumanDescription:
MAF1 Human Recombinant
MAF1 homolog (S. cerevisiae), Repressor of RNA polymerase III transcription MAF1 homolog, homolog of yeast MAF1, MGC20332, MGC31779, MGC39758, DKFZp586G1123.
Product # :
PRO-921Price :
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Description
MAF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 276 amino acids (1-256) and having a molecular mass of 31.0 kDa.The MAF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MAF1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MAF1 resembles Maf1 which is a Saccharomyces cerevisiae – a highly conserved protein in eukaryotic cells, localized to the nucleus. MAF1 Interacts with BRF2, MAF1 and functions as a mediator for signals which explicitly inhibit RNA polymerase III (Pol III) activity by inhibiting the association of TFIIIB to DNA. MAF1 reacts to modifications in the cellular environment and represses pol III transcription.
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Synonyms
MAF1 homolog (S. cerevisiae), Repressor of RNA polymerase III transcription MAF1 homolog, homolog of yeast MAF1, MGC20332, MGC31779, MGC39758, DKFZp586G1123.
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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 MKLLENSSFE AINSQLTVET GDAHIIGRIE SYSCKMAGDD KHMFKQFCQE GQPHVLEALS PPQTSGLSPS RLSKSQGGEE EGPLSDKCSR KTLFYLIATL NESFRPDYDF STARSHEFSR EPSLSWVVNA VNCSLFSAVR EDFKDLKPQL WNAVDEEICL AECDIYSYNP DLDSDPFGED GSLWSFNYFF YNKRLKRIVF FSCRSISGST YTPSEAGNEL DMELGEEEVE EESRSRGSGA EETSTMEEDR VPVICI
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 :
HARS HumanDescription:
Histidyl-tRNA Synthetase Human Recombinant
Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1, HARS.
Product # :
ENZ-268Price :
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Description
Histidyl-tRNA Synthetase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 55 kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 500mM NaCl and 10mM Tris (pH 8.0) and 6M Urea.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.
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Synonyms
Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1, HARS.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored below -18°C.Please prevent freeze-thaw cycles.
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Applications
Western Blot: Strongly reactive with human anti Histidyl-tRNA Synthetase antisera.
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 :
RBBP9 HumanDescription:
Retinoblastoma Binding Protein 9 Human Recombinant
Retinoblastoma binding protein 9, RBBP-9, Retinoblastoma-binding protein 10, RBBP-10, BOG, B5T-overexpressed gene protein, putative hydrolase RBBP9, retinoma-binding protein 9.
Product # :
PRO-991Price :
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Description
RBBP9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-186 a.a.) and having a molecular mass of 23.1kDa.RBBP9 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RBBP9 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
RBBP9, restricts to the nucleus and cytoplasm, is a retinoblastoma binding protein which takes part in the regulation of cell proliferation and differentiation. RBBP9 cooperates with retinoblastoma (Rb) and offers cellular resistance to the growth-inhibitory effects of TGFbeta1, therefore enabling the cellular transformation process.
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Synonyms
Retinoblastoma binding protein 9, RBBP-9, Retinoblastoma-binding protein 10, RBBP-10, BOG, B5T-overexpressed gene protein, putative hydrolase RBBP9, retinoma-binding protein 9.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASPSKAVIV PGNGGGDVTT HGWYGWVKKE LEKIPGFQCL AKNMPDPITA RESIWLPFME TELHCDEKTI IIGHSSGAIA AMRYAETHRV YAIVLVSAYT SDLGDENERA SGYFTRPWQW EKIKANCPYI VQFGSTDDPF LPWKEQQEVA DRLETKLHKF TDCGHFQNTE FHELITVVKS LLKVPA
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 :
Protein-G HisDescription:
Protein G His Tag Recombinant
Product # :
PRO-1237Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Protein G His Tag Recombinant produced in E.Coli is a 201 amino acids protein which contains amino acid 190-384 of the Streptococcus sp with a C-terminal 6-His tag, and having a molecular mass of 21.6kDa. But it migrates with an apparent molecular mass of 32kDa in SDS-PAGE.The Protein G His Tag is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G 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 Protein G in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Protein G binds to the constant region of many species of immunoglobulin G. It can be used to detect, quantify and purify IgG antibodies and antibody/antigen complexes. Recombinant Protein G contains only IgG binding domains. The albumin-binding domain as well as cell wall and cell membrane binding domains have been removed to ensure the maximum specific IgG binding capacity.
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Specificity
1. Binds with greater affinity to most mammalian immunoglobulins than Protein A, including human IgG3 and rat IgG2a.2. Does not bind to human IgM, IgD and IgA.
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 :
NRP1 MouseDescription:
Neuropilin 1 Mouse Recombinant
Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.
Product # :
CYT-971Price :
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Description
NRP1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856 a.a.) and having a molecular mass of 94.7kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Neuropilin 1 (Nrp1) is a transmembrane glycoprotein which functions as a co-receptor for several extracellular ligands including class III/IV semaphorins, some isoforms of vascular endothelial growth factor and transforming growth factor beta. Nrp1 binds vascular endothelial growth factor (VEGF)-A and is believed to serve as a coreceptor for kinase insert domain-containing receptor (KDR) by connecting with KDR and enhancing VEGF signaling. Nrp1 is a marker of regulatory T cells.
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Synonyms
Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.
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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
FRSDKCGGTI KIENPGYLTS PGYPHSYHPS EKCEWLIQAP EPYQRIMINF NPHFDLEDRD CKYDYVEVID GENEGGRLWG KFCGKIAPSP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TAPTGVIKSP GFPEKYPNSL ECTYIIFAPK MSEIILEFES FDLEQDSNPP GGMFCRYDRL EIWDGFPEVG PHIGRYCGQK TPGRIRSSSG VLSMVFYTDS AIAKEGFSAN YSVLQSSISE DFKCMEALGM ESGEIHSDQITASSQYGTNW SVERSRLNYP ENGWTPGEDS YKEWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYRVD ISSNGEDWIS LKEGNKAIIF QGNTNPTDVV LGVFSKPLIT RFVRIKPVSW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITASN QADRNWMPEN IRLVTSRTGW ALPPSPHPYT NEWLQVDLGD EKIVRGVIIQ GGKHRENKVF MRKFKIAYSN NGSDWKTIMD DSKRKAKSFE GNNNYDTPEL RTFSPLSTRF IRIYPERATH SGLGLRMELL GCEVEAPTAG PTTPNGNPVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTIIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDSHAQL RWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQSSAHC MTFWYHMSGS HVGTLRVKLR YQKPEEYDQL VWMVVGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PTDLDKKNTE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH
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 :
TSR2 HumanDescription:
TSR2 Human Recombinant
TSR2, 20S RRNA Accumulation, Homolog (S. Cerevisiae), WGG Motif Containing 1, Pre-RRNA-Processing Protein TSR2 Homolog, DT1P1A10, DBA14, WGG1, Pre-rRNA-processing protein TSR2 homolog.
Product # :
PRO-2079Price :
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Shipped with Ice Packs
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Description
TSR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a) and having a molecular mass of 23.2kDa. TSR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TSR2 protein solution (0.5mg/ml) containing PBS buffer (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TSR2 is part of the TSR2 family. TSR2 is involved in 20S pre-rRNA processing. Among the diseases which are associated with TSR2 are blepharospasm and diamond-blackfan anemia.
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Synonyms
TSR2, 20S RRNA Accumulation, Homolog (S. Cerevisiae), WGG Motif Containing 1, Pre-RRNA-Processing Protein TSR2 Homolog, DT1P1A10, DBA14, WGG1, Pre-rRNA-processing protein TSR2 homolog.
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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 MGSMAGAAED ARALFRAGVC AALEAWPALQ IAVENGFGGV HSQEKAKWLG GAVEDYFMRN ADLELDEVED FLGELLTNEF DTVVEDGSLP QVSQQLQTMF HHFQRGDGAA LREMASCITQ RKCKVTATAL KTARETDEDE DDVDSVEEME VTATNDGAAT DGVCPQPEPS DPDAQTIKEE DIVEDGWTIV RRK.
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 :
CHMP5 HumanDescription:
Charged Multivesicular Body Protein 5 Human Recombinant
Charged Multivesicular Body Protein 5, SNF7 Domain-Containing Protein 2, Chromosome 9 Open Reading Frame 83, Chromatin-Modifying Protein 5, Apoptosis-Related Protein PNAS-2, Vacuolar Protein Sorting-Associated Protein 60, Chromatin Modifying Protein 5, HSPC177, PNAS-2, HVps60, SNF7DC2, CGI-34, C9orf83.
Product # :
PRO-1232Price :
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Shipped with Ice Packs
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Description
CHMP5 Human Recombinant produced in E. coli is a single polypeptide chain containing 243 amino acids (1-219) and having a molecular mass of 27.0 kDa.CHMP5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CHMP5 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Charged Multivesicular Body Protein 5 (CHMP5) is a member of the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins comprise the ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and development of endocytic multivesicular bodies (MVBs). Certain CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP the CHMP1A, is essential for both MVB formation and regulation of cell cycle progression.
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Synonyms
Charged Multivesicular Body Protein 5, SNF7 Domain-Containing Protein 2, Chromosome 9 Open Reading Frame 83, Chromatin-Modifying Protein 5, Apoptosis-Related Protein PNAS-2, Vacuolar Protein Sorting-Associated Protein 60, Chromatin Modifying Protein 5, HSPC177, PNAS-2, HVps60, SNF7DC2, CGI-34, C9orf83.
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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 MGSH MNRLFG KAKPKAPPPS LTDCIGTVDS RAESIDKKIS RLDAELVKYK DQIKKMREGP AKNMVKQKAL RVLKQKRMYE QQRDNLAQQS FNMEQANYTI QSLKDTKTTV DAMKLGVKEM KKAYKQVKID QIEDLQDQLE DMMEDANEIQ EALSRSYGTP ELDEDDLEAE LDALGDELLA DEDSSYLDEA ASAPAIPEGV PTDTKNKDGV LVDEFGLPQI PAS
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 :
SPP1 Human, HEKDescription:
Osteopontin Human Recombinant, HEK
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
Product # :
CYT-047Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Osteopontin Human Recombinant is a single, glycosylated, polypeptide chain produced in HEK293 cells, is a full length protein (amino acids 17-314) fused with a polyhistidine tag at the C-terminus, having a total calculated molecular mass of 34.5kDa (The actual molecular mass may be approximately 60-65kDa in SDS-PAGE under reducing conditions due to glycosylation).Osteopontin is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
Osteopontin was lyophilized from a 0.2µM filtered solution of 20mM PBS and 150mM NaCl, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases. -
Synonyms
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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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Solubility
It is recommended to reconstitute the lyophilized SPP1 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
IPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETL
PSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDEL
VTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDIT
SHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRK
ANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDS
ASSEVNVDHHHHHH.
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 :
MMP 3 Human, HEKDescription:
Matrix Metalloproteinase-3 Human Recombinant, HEK
Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.
Product # :
ENZ-284Price :
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Shipped with Ice Packs
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- sds-page
Description
MMP-3 Human Recombinant produced in HEK293 cells is a proform of the Human MMP3 [Tyr18-Cys477 (Lys45Glu)] and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa. MMP-3 is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
The MMP-3 is supplied as a 0.2µm filtered solution in 20mM Tris-HCl, 150mM NaCl and 0.05% Brij35, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The activity was measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2. The specific activity is > 150 pmoles/min/µg.
Recombinant Human MMP-3 protein pro form needs to be activated with Chymotrypsin.
Activation Protocol:
1. Dilute MMP3 to 20µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
2. Activate MMP3 by adding Chymotrypsin(Sigma, Catalog#C3142,1mg/ml stock in 1mM HCl) to a final concentration of 5ug/ml.
3. Incubate at 37°C for 30 minutes.
4. Stop activation with 2mM PMSF. Pre-warm the PMSF to 37°C prior to adding to sample.sds-page
More Info
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Introduction
MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.
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Synonyms
Stromelysin-1, EC 3.4.24.17, Matrix metalloproteinase-3, MMP-3, Transin-1, SL-1, STMY, STR1, STMY1, MGC126102, MGC126103, MGC126104.
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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.
- View Data Sheet
Name :
DCN MouseDescription:
Decorin Mouse Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
Product # :
PRO-2234Price :
Quantity :
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Shipped with Ice Packs
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Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
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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
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH 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 :
NAT1 HumanDescription:
N-Acetyltransferase 1 Human Recombinant
N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.
Product # :
ENZ-144Price :
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Description
NAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-290) and having a molecular mass of 36.1 kDa.The NAT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAT1 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 2mM DTT and 10% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
NAT1 is a member of the arylamine N-acetyltransferase family. NAT1 catalyzes N- or O-acetylation of heterocyclic and arylamine substrates in the detoxification of a large number of drugs. Several alleles triggering high levels of N-acetyltransferase activity were linked to colon and urinary bladder cancers, since NAT1 also bioactivate numerous known carcinogens. NAT1 aids metabolize drugs and other xenobiotics, and takes part in the detoxification of a plethora of hydrazine and arylamine drugs.
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Synonyms
N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.
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Physical Appearance
NAT1 is supplied as a sterile filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDIEAYLERI GYKKSRNKLD LETLTDILQH QIRAVPFENL NIHCGDAMDL GLEAIFDQVV RRNRGGWCLQ VNHLLYWALT TIGFETTMLG GYVYSTPAKK YSTGMIHLLL QVTIDGRNYI VDAGFGRSYQ MWQPLELISG KDQPQVPCIF RLTEENGFWY LDQIRREQYI PNEEFLHSDL LEDSKYRKIY SFTLKPRTIE DFESMNTYLQ TSPASVFTSK SFCSLQTPDG VHCLVGFTLT HRRFNYKDNT DLIEFKTLSE EEIEKVLKNI FNISLQRKLV PKHGDRFFTI
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 :
SNURF HumanDescription:
SNRPN Upstream Reading Frame Human Recombinant
SNRPN Upstream Reading Frame Protein.
Product # :
PRO-1849Price :
Quantity :
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Description
SNURF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (1-71) and having a molecular mass of 10.8 kDa. SNURF is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The SNURF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SNURF is an extremely basic protein restricted to the nucleus. The evolutionarily reserved open reading frame is located on a bicistronic transcript which has a downstream ORF encoding the small nuclear ribonucleoprotein polypeptide N. The first three exons of the transcript are exploited by the upstream coding region which is known as an imprinting center. The full-length nature of these transcripts is yet to be determined but multiple transcription initiation sites have been identified and large scale alternative splicing takes place in the 5' untranslated region. An alternate exon which substitutes for exon 4 and leads to a truncated, monocistronic transcript was identified. Deletion or alternative splicing produced by a translocation event in the 5' UTR or coding region of this gene results in Prader-Willi syndrome or Angelman syndrome because of parental imprint switch failure.
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Synonyms
SNRPN Upstream Reading Frame Protein.
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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 MGSMERARDR LHLRRTTEQH VPEVEVQVKR RRTASLSNQE CQLYPRRSQQ QQVPVVDFQA ELRQAFLAET PRGG
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 :
PCNA Human, Sf9Description:
Proliferating Cell Antigen Human Recombinant, Sf9
Proliferating cell nuclear antigen, PCNA, Cyclin, MGC8367.
Product # :
PRO-303Price :
Quantity :
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Description
PCNA Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 35 kDa. PCNA is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Recombinant Human PCNA is supplied in16mM HEPES buffer pH-8, 400mM NaCl, and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Proliferating cell nuclear antigen (PCNA), a protein of 30 kDa molecular weight also known as cyclin, forms a trimer ring around a DNA double-helix. It binds to a variety of other nuclear proteins and thereby organises biochemical processes at the DNA replication fork. PCNA thereby assumes important functions in DNA synthesis, repair and processing, the regulation of cell cycle and even apoptosis.
Anti-PCNA antibodies occur in systemic lupus, where they represent a rare specificity (< 10 % of SLE patients). However, their presence alone or in combination with other autoantibodies should alert the clinician to the presence of defined or evolving SLE. -
Synonyms
Proliferating cell nuclear antigen, PCNA, Cyclin, MGC8367.
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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. 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, immuno-dot analysis with validated SLE patient sera.
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coating concentration
0.5-1.1 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 monoclonal anti-hexa-His-tag antibody & Scleroderma 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.
- View Data Sheet
Name :
ACP5 Human, HisDescription:
Acid Phosphatase-5 Human Recombinant, His Tag
Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, EC 3.1.3.2, TrATPase, SPENCDI, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TR-AP, TRAP, ACP5.
Product # :
ENZ-913Price :
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Description
ACP5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (22-325 a.a) and having a molecular mass of 35.1kDa.ACP5 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ACP5 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 5,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37C.More Info
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Introduction
Acid Phosphatase-5, also known as ACP5 is a member of the Purple acid phosphatase family. ACP5 is implicated in osteopontin as well as bone sialoprotein dephosphorylation. ACP5 expression appears to increase in certain pathological states for instance Gaucher & Hodgkin diseases, the hairy cell, the B-cell, as well as the T-cell leukemias.
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Synonyms
Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, EC 3.1.3.2, TrATPase, SPENCDI, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TR-AP, TRAP, ACP5.
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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
ATPALRFVAV GDWGGVPNAP FHTAREMANA KEIARTVQIL GADFILSLGD NFYFTGVQDI NDKRFQETFE DVFSDRSLRK VPWYVLAGNH DHLGNVSAQI AYSKISKRWN FPSPFYRLHF KIPQTNVSVA IFMLDTVTLC GNSDDFLSQQ PERPRDVKLA RTQLSWLKKQ LAAAREDYVL VAGHYPVWSI AEHGPTHCLV KQLRPLLATY GVTAYLCGHD HNLQYLQDEN GVGYVLSGAG NFMDPSKRHQ RKVPNGYLRF HYGTEDSLGG FAYVEISSKE MTVTYIEASG KSLFKTRLPR RARPHHHHHH.
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 MouseDescription:
Adiponectin Mouse Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-1168Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Acrp30 Mouse Recombinant is a single, glycosylated polypeptide chain containing 230 amino acids (18-247a.a) and having a molecular mass of 24.9kDa (calculated).
Source
HEK293 cells.
Formulation
Acrp30 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris 50mM NaCl and 1mM CaCl2, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit proliferation of mouse 3T3 fibroblasts stimulated by PDGF. The ED50 for the effect is typically 5-15 μg/mL.
More Info
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Introduction
Adiponectin, also known as Acrp30, AdipoQ and GBP-28, is a 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). Adiponectin is a part of the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYVYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.9kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293 cells.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological activity Measured by its ability to inhibit proliferation of mouse 3T3 fibroblasts stimulated by PDGF. The ED50 for the effect is typically 5-15 μg/mL.
What is the amino acid sequence of ADIPONECTIN Protein?
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYVYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN.
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 :
DCPS HumanDescription:
Decapping Enzyme, Scavenger Human Recombinant
Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.
Product # :
ENZ-159Price :
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Description
DCPS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-337 a.a.) and having a molecular mass of 40.7kDa.DCPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCPS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Scavenger mRNA-decapping enzyme (DCPS) is a member of the HIT family. DCPS is required for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It was shown that DCPS hydrolyzes the residual m7GpppN cap structure after the complete 3'–5' degradation of the mRNA by the exosome. Furthermore, DCPS releases m7GMP and is incapable of cleaving cap structures attached to a long RNA chain.
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Synonyms
Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.
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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 MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ KVLRESARDK IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP PRQLNDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL LRNILHQGQE AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS.
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 :
SERPINI1 Human, HisDescription:
Serpin Peptidase Inhibitor, Clade I Member 1 Human Recombinant, His Tag
Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.
Product # :
PRO-1595Price :
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Shipped at Room temp
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Description
SERPINI1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 17-410) containing 404 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 45.9kDa (calculated).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.025M phosphate buffer and 0.035M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).
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Synonyms
Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SERPINI1 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
MKHHHHHHASTGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL.
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 :
SIRPA RatDescription:
Signal-Regulatory Protein Alpha Rat Recombinant
Tyrosine-protein phosphatase non-receptor type substrate 1, SHP substrate, SHPS-1, Brain Ig-like molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, Inhibitory receptor SHPS-1, Macrophage fusion receptor, Macrophage membrane protein MFP150, Signal-regulatory protein alpha-1, Sirp-alpha-1, CD172a, Sirpa, Bit, Mfr, Ptpns1, Shps1, Sirp.
Product # :
PRO-2258Price :
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Description
SIRPA Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 350 amino acids (32-373a.a) and having a molecular mass of 38.5kDa. (Migrates at 57-70kDa on SDS-PAGE under reducing conditions). SIRPA is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SIRPA protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as theimmunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which areinvolved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRPA can bephosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part insignal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand forSIRPA.
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Synonyms
Tyrosine-protein phosphatase non-receptor type substrate 1, SHP substrate, SHPS-1, Brain Ig-like molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, Inhibitory receptor SHPS-1, Macrophage fusion receptor, Macrophage membrane protein MFP150, Signal-regulatory protein alpha-1, Sirp-alpha-1, CD172a, Sirpa, Bit, Mfr, Ptpns1, Shps1, Sirp.
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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
KELKVTQADK SVSVAAGDSA TLNCTVSSLT PVGPIKWFKG EGQNRSPIYS FIGGEHFPRI TNVSDATKRN NMDFSICISN VTPEDAGTYY CVKFQKGIVE PDTEIKSGGG TTLYVLAKPS SPEVSGPDSR GSPGQTVNFT CKSYGFSPRN ITLKWLKNGK ELSHLETTIS SKSNVSYNIS STVSVKLSPE DIHSRVICEV AHVTLEGRPL NGTANFSNII RVSPTLKITQ QPLTPASQVN LTCQVQKFYP KALQLNWLEN GNLSRTDKPE HFTDNRDGTY NYTSLFLVNS SAHREDVVFT CQVEHDSQPA ITENHTVRAF AHSSSGGSME TIPDNNAYYN WNVEHHHHHH.
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 :
TARC Human, HisDescription:
Thymus and Activation Regulated Chemokine Human Recombinant (CCL17), His Tag
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
Product # :
CHM-359Price :
Quantity :
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Shipped with Ice Packs
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Description
TARC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 92 amino acids (24-94 a.a.) and having a molecular mass of 10.3 kDa. The TARC is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TARC protein contains 1xPBS (pH7.4) and 10% glycerol.
Purity
Greater than 95% as determined by Analysis by SDS-PAGE.
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Introduction
TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.
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Synonyms
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
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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 MARGTNVGRE CCLEYFKGAI PLRKLKTWYQ TSEDCSRDAI VFVTVQGRAI CSDPNNKRVK NAVKYLQSLE RS.
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 :
THAP11 HumanDescription:
THAP Domain Containing, Apoptosis Associated Protein 11 Human Recombinant
THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.
Product # :
PRO-2009Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
THAP11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 36.8kDa.THAP11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The THAP11 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
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Introduction
THAP Domain Containing, Apoptosis Associated Protein 11 (THAP11) is a part of the thanatos-associated protein family. THAP11 plays a role as a transcriptional repressor and interacts with HCF1 through a coiled coil domain. THAP11 which is localized to the nucleus and cytoplasm takes part in embryogenesis and pluripotency of embryonic stem cells by recruiting epigenetic modifiers.
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Synonyms
THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.
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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 MGSMPGFTCC VPGCYNNSHR DKALHFYTFP KDAELRRLWL KNVSRAGVSG CFSTFQPTTG HRLCSVHFQG GRKTYTVRVP TIFPLRGVNE RKVARRPAGA AAARRRQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQSSPSA STAQTAQLQP NLVSASAAVL LTLQATVDSS QAPGSVQPAP ITPTGEDVKP IDLTVQVEFA AAEGAAAAAA ASELQAATAG LEAAECPMGP QLVVVGEEGF PDTGSDHSYS LSSGTTEEEL LRKLNEQRDI LALMEVKMKE MKGSIRHLRL TEAKLREELR EKDRLLAMAV IRKKHGM.
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 :
TSLP Human, HisDescription:
Thymic Stromal Lymphopoietin Human Recombinant, His Tag
Thymic Stromal Lymphopoietin, TSLP.
Product # :
CYT-836Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
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Description
TSLP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Tyr29-Gln159) containing 141 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 16.2kDa.
Source
Escherichia Coli.
Formulation
TSLP was filtered (0.4µm) and lyophilized in phosphate buffered saline.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
TSLP protein is a hemopoietic cytokine which signals throughout a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor & the Interleukin-7 receptor alpha chain. TSLP impacts myeloid cells thus induces the discharge of T cell-attracting chemokines from monocytes & increases the growth of CD11c(+) dendritic cells. TSLP is mainly expressed in the heart, liver and prostate. TSLP is related in its biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the Interleukin-7 receptor alpha chain & the TSLPR. Similar to IL-7, TSLP enhances phosphorylation of STAT3 and STAT5, though uses kinases excluding JAKs for its activation. TSLP induces the release of T cell-attracting chemokines such asTARC & MDC from monocytes & triggers CD11c(+) dendritic cells. TSLP activated dendritic cells primes naive T cells to manufacture pro-allergic cytokines such as Iinterleukin-4, Interleukin-5, Interleukin-13 and TNF-alpha whereas down-regulating Interleukin-10 and IFN-gamma play a role in the initiation of allergic inflammation.
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Synonyms
Thymic Stromal Lymphopoietin, TSLP.
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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.
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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. TSLP 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
MKHHHHHHASYDFTNCDFEK IKAAYLSTIS KDLITYMSGT KSTEFNNTVS CSNRPHCLTE IQSLTFNPTA GCASLAKEMF AMKTKAALAI WCPGYSETQI NATQAMKKRR KRKVTTNKCL EQVSQLQGLW RRFNRPLLKQ Q.
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 :
LRRC59 HumanDescription:
Leucine Rich Repeat Containing 59 Human Recombinant
Leucine Rich Repeat Containing 59, Ribosome-Binding Protein P34, p34, Leucine-Rich Repeat-Containing Protein 59.
Product # :
PRO-1714Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LRRC59 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-244) and having a molecular mass of 30.3kDa.LRRC59 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LRRC59 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
LRRC59 controls nuclear import of exogenous FGF1 by enabling interaction with the nuclear import mechanism and by transporting cytosolic FGF1 to and through the nuclear pores. LRRC59 is essential for nuclear import of FGF1, but not that of FGF2.
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Synonyms
Leucine Rich Repeat Containing 59, Ribosome-Binding Protein P34, p34, Leucine-Rich Repeat-Containing Protein 59.
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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 MGSMTKAGSK GGNLRDKLDG NELDLSLSDL NEVPVKELAA LPKATILDLS CNKLTTLPSD FCGLTHLVKL DLSKNKLQQL PADFGRLVNL QHLDLLNNKL VTLPVSFAQL KNLKWLDLKD NPLDPVLAKV AGDCLDEKQC KQCANKVLQH MKAVQADQER ERQRRLEVER EAEKKREAKQ RAKEAQEREL RKREKAEEKE RRRKEYDALK AAKREQEKKP KKEANQAPKS KSGSRPRKPP PRKHTRS
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.