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Search results

1000 results found for “hnrnp”

Name

Description

Product #

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  • View Data Sheet

    Name :

    QDPR Human

    Description:

    Quinoid Dihydropteridine Reductase Human Recombinant

    Dihydropteridine reductase, HDHPR, Quinoid dihydropteridine reductase, QDPR, DHPR, PKU2, SDR33C1.

    Product # :

    ENZ-163

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    Description

    QDPR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-244 a.a.) and having a molecular mass of 28.2kDa.QDPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    QDPR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      QDPR belongs to the short-chain dehydrogenases/reductase (SDR) family of enzymes. Operating as a homodimer, QDPR has an imperative role in the recycling of tetrahydrobiopterin (BH4), a vital cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine). More precisely, QDPR catalyzes the regeneration of BH4 from quinonoid dihydrobiopterin (qBH2), the product generated from the hydroxylation reactions. Mutations in the QDPR gene may lead to phenylketonuria II.

    • Synonyms

      Dihydropteridine reductase, HDHPR, Quinoid dihydropteridine reductase, QDPR, DHPR, PKU2, SDR33C1.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMAAAAAA GEARRVLVYG GRGALGSRCV QAFRARNWWV ASVDVVENEE ASASIIVKMT DSFTEQADQV TAEVGKLLGE EKVDAILCVA GGWAGGNAKS KSLFKNCDLM WKQSIWTSTI SSHLATKHLK EGGLLTLAGA KAALDGTPGM IGYGMAKGAV HQLCQSLAGK NSGMPPGAAA IAVLPVTLDT PMNRKSMPEA DFSSWTPLEF LVETFHDWIT GKNRPSSGSL IQVVTTEGRT ELTPAYF.

    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.

    Qdpr Human
  • View Data Sheet

    Name :

    COPS6 Human

    Description:

    COP9 Constitutive Photomorphogenic 6 Human Recombinant

    CSN6, MOV34-34KD, COP9 signalosome complex subunit 6, JAB1-containing signalosome subunit 6, MOV34 homolog, Vpr-interacting protein, hVIP, COPS6.

    Product # :

    PRO-1650

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    Description

    COPS6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 347 amino acids (1-327 a.a.) and having a molecular mass of 38.9kDa.COPS6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COPS6 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COP9 Constitutive Photomorphogenic 6 (COPS6) is a member of the translation initiation factor 3 (eIF3) superfamily,peptidase M67A family and CSN6 subfamily. COPS6 is one of 8 subunits of COP9 signalosome,a highly conserved protein complex which functions as an significant regulator in multiple signaling pathways. COP9's structure and function of signalosome is similar to 19S regulatory particle of 26S proteasome. COP9 signalosome can interact with SCF-type E3 ubiquitin ligases and act as a positive regulator of E3 ubiquitin ligases.COP9 takes part in the regulation of cell cycle and likely to be a cellular cofactor for HIV-1 accessory gene product Vpr.

    • Synonyms

      CSN6, MOV34-34KD, COP9 signalosome complex subunit 6, JAB1-containing signalosome subunit 6, MOV34 homolog, Vpr-interacting protein, hVIP, COPS6.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAAAAAAAAA TNGTGGSSGM EVDAAVVPSV MACGVTGSVS VALHPLVILN ISDHWIRMRS QEGRPVQVIG ALIGKQEGRN IEVMNSFELL SHTVEEKIII DKEYYYTKEE QFKQVFKELE FLGWYTTGGP PDPSDIHVHK QVCEIIESPL FLKLNPMTKH TDLPVSVFES VIDIINGEAT MLFAELTYTL ATEEAERIGV DHVARMTATG SGENSTVAEH LIAQHSAIKM LHSRVKLILE YVKASEAGEV PFNHEILREA YALCHCLPVL STDKFKTDFY DQCNDVGLMA YLGTITKTCN TMNQFVNKFN VLYDRQGIGR RMRGLFF.

    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.

    Cops6 Human
  • View Data Sheet

    Name :

    MED20 Human

    Description:

    Mediator Complex Subunit 20 Human Recombinant

    Mediator of RNA polymerase II transcription subunit 20, Mediator complex subunit 20, TRF-proximal protein homolog, hTRFP, MED20, TRFP, PRO0213.

    Product # :

    PRO-1204

    Price :

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    Description

    MED20 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (1-212 a.a.) and having a molecular mass of 25.6kDa.MED20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    MED20 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mediator Complex Subunit 20 (MED20) is a subunit of the Mediator complex, which is a multiprotein coactivator of RNA transcription that interacts with DNA-bound transcriptional activators, RNA polymerase II, and general initiation factors. The Mediator functions as a link to transmit information from gene-specific regulatory proteins to the basal RNA polymerase II transcription apparatus. Mediator is recruited to promoters by direct interactions with regulatory proteins and functions as a scaffold for the compilation of a functional preinitiation complex with RNA polymerase II and the general transcription factors.

    • Synonyms

      Mediator of RNA polymerase II transcription subunit 20, Mediator complex subunit 20, TRF-proximal protein homolog, hTRFP, MED20, TRFP, PRO0213.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMGVTCVS QMPVAEGKSV QQTVELLTRK LEMLGAEKQG TFCVDCETYH TAASTLGSQG QTGKLMYVMH NSEYPLSCFA LFENGPCLIA DTNFDVLMVK LKGFFQSAKA SKIETRGTRY QYCDFLVKVG TVTMGPSARG ISVEVEYGPC VVASDCWSLL LEFLQSFLGS HTPGAPAVFG NRHDAVYGPA DTMVQYMELF NKIRKQQQVP VAGIR.

    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.

    Med20 Human
  • View Data Sheet

    Name :

    RCHY1 Human

    Description:

    Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant

    ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    Product # :

    PRO-1536

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    Description

    RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RCHY1 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

    • Introduction

      Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.

    • Synonyms

      ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.

    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.

    Rchy1 Human
  • View Data Sheet

    Name :

    RHEB Human

    Description:

    Ras Homolog Enriched in Brain Human Recombinant

    Ras homolog enriched in brain, RHEB2, Ras homolog enriched in brain, GTP-binding protein Rheb, RheB, Ras homolog enriched in brain GTP binding protein Rheb, Ras homolog enriched in brain 2, RHEB 2.

    Product # :

    PRO-308

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    Description

    RHEB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-181 amino acids) and having a molecular mass of 21.7 kDa.The RHEB is fused to T7-tag at N-terminus (16 a.a.) and is purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The RHEB protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RHEB is part of the Ras & GTPase superfamily that was originally identified as an immediate-early gene in brain but is also widely expressed in other tissues. RHEB encodes a lipid-anchored, cell membrane protein with five repeats of the RAS-related GTP-binding region. RHEB is necessary in regulation of growth and cell cycle progression due to its role in the TOR/S6K signaling pathway. RHEB has GTPase activity and shuttles between a GDP-bound form and a GTP-bound form, and farnesylation of the protein is required for this activity. RHEB induces oncogenic transformation. RHEB overexpression accelerates lymphomagenesis and is associated with prostate cancer. RHEB can cytopathologically distinguish between fibroadenoma from malignant breast carcinomas which is considered as a secondary diagnostic tool. RHEB has a central role in the regulation of the Ras/B-Raf/C-Raf/MEK signaling network.

    • Synonyms

      Ras homolog enriched in brain, RHEB2, Ras homolog enriched in brain, GTP-binding protein Rheb, RheB, Ras homolog enriched in brain GTP binding protein Rheb, Ras homolog enriched in brain 2, RHEB 2.

    • 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

      MASMTGGQQM GRGSASMPQS KSRKIAILGY RSVGKSSLTI QFVEGQFVDS YDPTIENTFT KLITVNGQEY HLQLVDTAGQ DEYSIFPQTY SIDINGYILV YSVTSIKSFE VIKVIHGKLL DMVGKVQIPI MLVGNKKDLH MERVISYEEG KALAESWNAA FLESSAKENQ TAVDVFRRII LEAEKMDGAA SQGKSSC.

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    Rheb Human
  • View Data Sheet

    Name :

    RNMTL1 Human

    Description:

    RNA Methyltransferase Like 1 Human Recombinant

    RNA Methyltransferase Like 1, 16S RRNA (Guanosine(1370)-2-O)-Methyltransferase, 16S RRNA [Gm1370] 2-O-Methyltransferase, RNA Methyltransferase-Like Protein 1, HC90, MRM3, RRNA Methyltransferase 3, Mitochondrial, Putative RNA Methyltransferase, EC 2.1.1.-, EC 2.1.1, RMTL1, RNMTL1.

    Product # :

    ENZ-895

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    Description

    RNMTL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 443 amino acids (1-420 a.a) and having a molecular mass of 49.4kDa.RNMTL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNMTL1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RNA methyltransferase-like protein 1, also known as RNMTL1 is a member of the RNA methyltransferase TrmH family. RNMTL1 is probable RNA methyltransferase and expressed at an equal level in normal liver and hepatocarcinoma.

    • Synonyms

      RNA Methyltransferase Like 1, 16S RRNA (Guanosine(1370)-2-O)-Methyltransferase, 16S RRNA [Gm1370] 2-O-Methyltransferase, RNA Methyltransferase-Like Protein 1, HC90, MRM3, RRNA Methyltransferase 3, Mitochondrial, Putative RNA Methyltransferase, EC 2.1.1.-, EC 2.1.1, RMTL1, RNMTL1.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMAALVRP ARFVVRPLLQ VVQAWDLDAR RWVRALRRSP VKVVFPSGEV VEQKRAPGKQ PRKAPSEASA QEQREKQPLE ESASRAPSTW EESGLRYDKA YPGDRRLSSV MTIVKSRPFR EKQGKILLEG RRLISDALKA GAVPKMFFFS RLEYLKELPV DKLKGVSLIK VKFEDIKDWS DLVTPQGIMG IFAKPDHVKM TYPKTQLQHS LPLLLICDNL RDPGNLGTIL RSAAGAGCSK VLLTKGCVDA WEPKVLRAGM GAHFRMPIIN NLEWETVPNY LPPDTRVYVA DNCGLYAQAE MSNKASDHGW VCDQRVMKFH KYEEEEDVET GASQDWLPHV EVQSYDSDWT EAPAAVVIGG ETYGVSLESL QLAESTGGKR LLIPVVPGVD SLNSAMAASI LLFEGKRQLR GRAEDLSRDR SYH

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    Rnmtl1 Human
  • View Data Sheet

    Name :

    RPL11 Human

    Description:

    Ribosomal Protein L11 Human Recombinant

    Ribosomal Protein L11, Cell Growth-Inhibiting Protein 34, CLL-Associated Antigen KW-12, 60S Ribosomal Protein L11, DBA7, GIG34, L11.

    Product # :

    PRO-1561

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    Description

    RPL11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-178) and having a molecular mass of 22.6kDa.RPL11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPL11 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT, 2mM EDTA, 250mM Imidazole and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribosomes are the organelles which catalyze protein synthesis, they’re comprised of a small 40S subunit and a large 60S subunit. Ribosomal Protein L11 (RPL11) is a member of the L5P family of ribosomal proteins. RPL11 is a ribosomal protein which is a component of the 60S subunit. RPL11 is found in the cytoplasm. The RPL11 protein most likely associates with the 5S rRNA.

    • Synonyms

      Ribosomal Protein L11, Cell Growth-Inhibiting Protein 34, CLL-Associated Antigen KW-12, 60S Ribosomal Protein L11, DBA7, GIG34, L11.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAQDQGE KENPMRELRI RKLCLNICVG ESGDRLTRAA KVLEQLTGQT PVFSKARYTV RSFGIRRNEK IAVHCTVRGA KAEEILEKGL KVREYELRKN NFSDTGNFGF GIQEHIDLGI KYDPSIGIYG LDFYVVLGRP GFSIADKKRR TGCIGAKHRI SKEEAMRWFQ QKYDGIILPG K

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    Rpl11 Human
  • View Data Sheet

    Name :

    RPRD1A Human

    Description:

    Regulation Of Nuclear Pre-MRNA Domain Containing 1A Human Recombinant

    Regulation of Nuclear Pre-MRNA Domain Containing 1A, RPRD1A, P15RS, Cyclin-Dependent Kinase 2B-Inhibitor-Related Protein, Cyclin-Dependent Kinase Inhibitor 2B-Related Protein (P15INK4B-Related Protein), P15INK4B-Related Protein, HsT3101, Regulation of Nuclear Pre-MRNA Domain-Containing Protein 1A, Cyclin-Dependent Kinase Inhibitor 2B-Related Protein, FLJ10656.

    Product # :

    PRO-1945

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    Description

    RPRD1A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-312) and having a molecular mass of 38.4 kDa.RPRD1A is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPRD1A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Regulation Of Nuclear Pre-MRNA Domain Containing 1A (RPRD1A) is upregulated in cells overexpressing cyclin-dependent kinase inhibitor p15(INK4b) and may have a part in cell cycle regulation. RPRD1A interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and partakes in dephosphorylation of the CTD. RPRD1A May function as a negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the cell cycle.

    • Synonyms

      Regulation of Nuclear Pre-MRNA Domain Containing 1A, RPRD1A, P15RS, Cyclin-Dependent Kinase 2B-Inhibitor-Related Protein, Cyclin-Dependent Kinase Inhibitor 2B-Related Protein (P15INK4B-Related Protein), P15INK4B-Related Protein, HsT3101, Regulation of Nuclear Pre-MRNA Domain-Containing Protein 1A, Cyclin-Dependent Kinase Inhibitor 2B-Related Protein, FLJ10656.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFMSAFS EAALEKKLSE LSNSQQSVQT LSLWLIHHRK HSRPIVTVWE RELRKAKPNR KLTFLYLAND VIQNSKRKGP EFTKDFAPVI VEAFKHVSSE TDESCKKHLG RVLSIWEERS VYENDVLEQL KQALYGDKKP RKRTYEQIKV DENENCSSLG SPSEPPQTLD LVRALQDLEN AASGDAAVHQ RIASLPVEVQ EVSLLDKITD KESGERLSKM VEDACMLLAD YNGRLAAEID DRKQLTRMLA DFLRCQKEAL AEKEHKLEEY KRKLARVSLV RKELRSRIQS LPDLSRLPNV TGSHMHLPFA GDIYSED.

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    Rprd1A Human
  • View Data Sheet

    Name :

    Darbepoetin

    Description:

    Darbepoetin-Alpha Human Recombinant

    Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    Product # :

    CYT-1263

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    Description

    Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells(CHO).

    Formulation

    Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

    More Info

    • Introduction

      Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.

    • Synonyms

      NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Darbepoetin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Darbepoetin 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 Darbepoetin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.

    • Background

      What is the molecular weight/Mw of DARBEPOETIN Protein?
      DARBEPOETIN Protein has a total Mw of 38.5kDa.

      What is the source or expression system of DARBEPOETIN Protein?
      Chinese Hamster Ovary Cells(CHO).

      What is the Purity of DARBEPOETIN Protein?
      DARBEPOETIN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of DARBEPOETIN Protein?
      The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

      What is the amino acid sequence of DARBEPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD

      What applications can DARBEPOETIN Protein be used in?
      DARBEPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for DARBEPOETIN Protein?
      The endotoxin level is minimal, DARBEPOETIN 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.

    Darbepoetin
  • View Data Sheet

    Name :

    ANGPTL3 Human, HEK

    Description:

    Angiopoietin Like Protein 3 Human Recombinant, HEK

    Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.

    Product # :

    CYT-766

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    Description

    ANGPTL3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 17-460) containing a total of 450 amino acids, having a molecular mass of 52.6kDa (calculated) and fused to a 6 aa His tag at C-Terminus.The Human ANGPTL3 is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.

    • Synonyms

      Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.

    • 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.

    • Solubility

      It is recommended to add deionized 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

      SRIDQDNSSF DSLSPEPKSR FAMLDDVKIL ANGLLQLGHG LKDFVHKTKG QINDIFQKLN IFDQSFYDLS LQTSEIKEEE KELRRTTYKL QVKNEEVKNM SLELNSKLES LLEEKILLQQ KVKYLEEQLT NLIQNQPETP EHPEVTSLKT FVEKQDNSIK DLLQTVEDQY KQLNQQHSQI KEIENQLRRT SIQEPTEISL SSKPRAPRTT PFLQLNEIRN VKHDGIPAEC TTIYNRGEHT SGMYAIRPSN SQVFHVYCDV ISGSPWTLIQ HRIDGSQNFN ETWENYKYGF GRLDGEFWLG LEKIYSIVKQ SNYVLRIELE DWKDNKHYIE YSFYLGNHET NYTLHLVAIT GNVPNAIPEN KDLVFSTWDH KAKGHFNCPE GYSGGWWWHD ECGENNLNGK YNKPRAKSKP ERRRGLSWKS QNGRLYSIKS TKMLIHPTDS ESFEHHHHHH.

    • Background

      What is the molecular weight/Mw of ANGPTL3 Protein?
      ANGPTL3 Protein has a total Mw of 52.6kDa.

      What is the source or expression system of ANGPTL3 Protein?
      HEK 293.

      What is the Purity of ANGPTL3 Protein?
      ANGPTL3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of ANGPTL3 Protein?
      The biological functionality of ANGPTL3 Protein will be determined in the future.

      What is the amino acid sequence of ANGPTL3 Protein?
      SRIDQDNSSF DSLSPEPKSR FAMLDDVKIL ANGLLQLGHG LKDFVHKTKG QINDIFQKLN IFDQSFYDLS LQTSEIKEEE KELRRTTYKL QVKNEEVKNM SLELNSKLES LLEEKILLQQ KVKYLEEQLT NLIQNQPETP EHPEVTSLKT FVEKQDNSIK DLLQTVEDQY KQLNQQHSQI KEIENQLRRT SIQEPTEISL SSKPRAPRTT PFLQLNEIRN VKHDGIPAEC TTIYNRGEHT SGMYAIRPSN SQVFHVYCDV ISGSPWTLIQ HRIDGSQNFN ETWENYKYGF GRLDGEFWLG LEKIYSIVKQ SNYVLRIELE DWKDNKHYIE YSFYLGNHET NYTLHLVAIT GNVPNAIPEN KDLVFSTWDH KAKGHFNCPE GYSGGWWWHD ECGENNLNGK YNKPRAKSKP ERRRGLSWKS QNGRLYSIKS TKMLIHPTDS ESFEHHHHHH.

      What applications can ANGPTL3 Protein be used in?
      ANGPTL3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ANGPTL3 Protein?
      The endotoxin level is minimal, ANGPTL3 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.

    Angptl3 Human Hek
  • View Data Sheet

    Name :

    JSRP1 Human

    Description:

    Junctional Sarcoplasmic Reticulum Protein 1 Human Recombinant

    Junctional Sarcoplasmic Reticulum Protein 1, Homolog of Mouse Skeletal Muscle Sarcoplasmic Reticulum Protein JP-45, Junctional-Face Membrane Protein Of 45 KDa Homolog, JP45, 2310032K21Rik, Skeletal Muscle Sarcoplasmic Reticulum Protein JP-45.

    Product # :

    PRO-1707

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    Description

    JSRP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-331) and having a molecular mass of 38.0kDa.JSRP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The JSRP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      JSRP1 takes part in excitation-contraction connection at the sarcoplasmic reticulum. JSRP1 is able to cooperate with CACNA1S, CACNB1 and calsequestrin to assist in regulating calcium influx and efflux in skeletal muscle.

    • Synonyms

      Junctional Sarcoplasmic Reticulum Protein 1, Homolog of Mouse Skeletal Muscle Sarcoplasmic Reticulum Protein JP-45, Junctional-Face Membrane Protein Of 45 KDa Homolog, JP45, 2310032K21Rik, Skeletal Muscle Sarcoplasmic Reticulum Protein JP-45.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSMTTRA WEELDGGLGS CQALEDHSAL AETQEDRASA TPRLADSGSV PHDSQVAEGP SVDTRPKKME KEPAARGTPG TGKERLKAGA SPRSVPARKK AQTAPPLQPP PPPPALSEEL PWGDLSLNKC LVLASLVALL GSAFQLCRDA VPGEAALQAR VPEPWVPPSS APREPSSPLP KFEAQAPPSA PPAPRAEAEV RPKIPGSREA AENDEEEPGE ATGEAVREDR VTLADRGPKE RPRREGKPRK EKPRKEERPK KERPRKEERP RAAREPREAL PQRWESREGG HRPWARDSRD AEPRKKQAWV SPRRPDEEQR PGSRQKLRAG KGRD

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    Jsrp1 Human
  • View Data Sheet

    Name :

    CDKN2AIPNL Human

    Description:

    CDKN2A Interacting Protein N-Terminal Like Human Recombinant

    CDKN2AIP N-terminal-like protein, CDKN2A-interacting protein N-terminal-like protein, CDKN2AIPNL.

    Product # :

    PRO-1865

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    Description

    CDKN2AIPNL Human Recombinant produced in E. coli is. a single polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 15.6kDa. CDKN2AIPNL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDKN2AIPNL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDKN2A Interacting Protein N-Terminal Like (CDKN2AIPNL) is a part of the CARF family.

    • Synonyms

      CDKN2AIP N-terminal-like protein, CDKN2A-interacting protein N-terminal-like protein, CDKN2AIPNL.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMVGGEAA AAVEELVSGV RQAADFAEQF RSYSESEKQW KARMEFILRH LPDYRDPPDG SGRLDQLLSL SMVWANHLFL GCSYNKDLLD KVMEMADGIE VEDLPQFTTR SELMKKHQS.

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    Cdkn2Aipnl Human
  • View Data Sheet

    Name :

    TSR2 Human

    Description:

    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-2079

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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

    • 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.

    • 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.

    • 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

      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.

    Tsr2 Human
  • View Data Sheet

    Name :

    CNDP1 Human, Active

    Description:

    CNDP Dipeptidase 1 Human Recombinant, Active

    Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.

    Product # :

    ENZ-1022

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    Description

    CNDP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 489 amino acids (27-507 a.a.) and having a molecular mass of 54.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).CNDP1 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >3,000 pmol/min/ug, and as measured by the hydrolysis of carnosine per minute at pH6.8 at 25°C.

    More Info

    • Introduction

      CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.

    • Synonyms

      Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.

    • 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

      SPSPPPALLE KVFQYIDLHQ DEFVQTLKEW VAIESDSVQP VPRFRQELFR MMAVAADTLQ RLGARVASVD MGPQQLPDGQ SLPIPPVILA ELGSDPTKGT VCFYGHLDVQ PADRGDGWLT DPYVLTEVDG KLYGRGATDN KGPVLAWINA VSAFRALEQD LPVNIKFIIE GMEEAGSVAL EELVEKEKDR FFSGVDYIVI SDNLWISQRK PAITYGTRGN SYFMVEVKCR DQDFHSGTFG GILHEPMADL VALLGSLVDS SGHILVPGIY DEVVPLTEEE INTYKAIHLD LEEYRNSSRV EKFLFDTKEE ILMHLWRYPS LSIHGIEGAF DEPGTKTVIP GRVIGKFSIR LVPHMNVSAV EKQVTRHLED VFSKRNSSNK MVVSMTLGLH PWIANIDDTQ YLAAKRAIRT VFGTEPDMIR DGSTIPIAKM FQEIVHKSVV LIPLGAVDDG EHSQNEKINR WNYIEGTKLF AAFFLEMAQL HLEHHHHHH.

    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.

    Cndp1 Human Active
  • View Data Sheet

    Name :

    YWHAB Human, His

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein, Beta, Human Recombinant, His Tag

    14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054,  YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.

    Product # :

    PKA-096

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    Description

    YWHAB Human Recombinant produced in E. coli is a single polypeptide chain containing 270 amino acids (1-246) and having a molecular mass of 30.6kDa. YWHAB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YWHAB solution (1mg/1ml) contains phosphate buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

    • Synonyms

      14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSHMTMDKS ELVQKAKLAE QAERYDDMAA AMKAVTEQGH ELSNEERNLL SVAYKNVVGA RRSSWRVISS IEQKTERNEK KQQMGKEYRE KIEAELQDIC NDVLELLDKY LIPNATQPES KVFYLKMKGD YFRYLSEVAS GDNKQTTVSN SQQAYQEAFE ISKKEMQPTH PIRLGLALNF SVFYYEILNS PEKACSLAKT AFDEAIAELD TLNEESYKDS TLIMQLLRDN LTLWTSENQG DEGDAGEGEN.

    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.

    Ywhab Human His
  • View Data Sheet

    Name :

    REN Mouse

    Description:

    Renin Mouse Recombinant

    Renin-1, Angiotensinogenase, Kidney renin, Ren1, Ren, Ren-A, Ren1c, Ren1d, Rn-1, Rnr.

    Product # :

    PRO-2251

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    Description

    REN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 387 amino acids (22-402 a.a.) and having a molecular mass of 42.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).REN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    REN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.

    • Synonyms

      Renin-1, Angiotensinogenase, Kidney renin, Ren1, Ren, Ren-A, Ren1c, Ren1d, Rn-1, Rnr.

    • 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

      LPTRTATFER IPLKKMPSVR EILEERGVDM TRLSAEWGVF TKRPSLTNLT SPVVLTNYLN TQYYGEIGIG TPPQTFKVIF DTGSANLWVP STKCSRLYLA CGIHSLYESS DSSSYMENGS DFTIHYGSGR VKGFLSQDSV TVGGITVTQT FGEVTELPLI PFMLAKFDGV LGMGFPAQAV GGVTPVFDHI LSQGVLKEEV FSVYYNRGSH LLGGEVVLGG SDPQHYQGNF HYVSISKTDS WQITMKGVSV GSSTLLCEEG CAVVVDTGSS FISAPTSSLK LIMQALGAKE KRIEEYVVNC SQVPTLPDIS FDLGGRAYTL SSTDYVLQYP NRRDKLCTLA LHAMDIPPPT GPVWVLGATF IRKFYTEFDR HNNRIGFALA RHHHHHH.

    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.

    Ren Mouse
  • View Data Sheet

    Name :

    Protein-L, His

    Description:

    Protein L Recombinant, His Tag

    Product # :

    PRO-1930

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    Description

    Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 372 amino acids in total and having a molecular mass of 41.5kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-L was lyophilized without any additives.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHKEE TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AG.

    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.

    Protein L His
  • View Data Sheet

    Name :

    PDPN P56F7AT Antibody

    Description:

    Podoplanin clone P56F7AT, Mouse Anti Human

    Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.

    Product # :

    ANT-641

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
      PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
      Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors.

    • Synonyms

      Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PDPN mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PDPN amino acids 99-207 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      P56F7AT.

    • Applications

      PDPN antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      PDPN antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Pdpn P56F7At Antibody
  • View Data Sheet

    Name :

    CCN1 Human

    Description:

    Cysteine-Rich Angiogenic Inducer 61 Human Recombinant

    CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.

    Product # :

    CYT-164

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    Description

    CYR61 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids and having a molecular mass of 39.5kDa.The CYR61 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2m 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 proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.

    More Info

    • Introduction

      CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.

    • Synonyms

      CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 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 CYR61 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
      PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD

    • Background

      Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis

      Abstract:


      Cysteine-rich angiogenic inducer 61 (CYR61) is an important extracellular matrix-associated protein that plays a significant role in angiogenesis and cell adhesion. This research paper provides a comprehensive analysis of human recombinant CYR61, focusing on its production, characterization, and potential applications in regulating angiogenesis. The paper discusses the significance of CYR61 in physiological and pathological angiogenesis, including wound healing, tumor development, and cardiovascular diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYR61 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYR61 and its utility as a research tool and a potential regulator of angiogenesis.

      Introduction:


      Cysteine-rich angiogenic inducer 61 (CYR61) is an extracellular matrix-associated protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. Human recombinant CYR61, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.

      Production and Characterization:


      Recombinant CYR61 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYR61.

      Role in Angiogenesis:


      CYR61 is involved in various aspects of angiogenesis, including endothelial cell proliferation, migration, and tube formation. It interacts with integrins and other cell surface receptors to modulate signaling pathways involved in angiogenic processes. Recombinant CYR61 serves as a valuable tool for studying the mechanisms underlying angiogenesis and exploring its potential as a therapeutic target.

      Therapeutic Implications:


      The dysregulation of angiogenesis is associated with several pathological conditions, including cancer, cardiovascular diseases, and chronic wounds. Recombinant CYR61 has shown promise as a potential regulator of angiogenesis and a therapeutic agent. It can be used to promote or inhibit angiogenesis, depending on the specific context. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYR61 in various diseases, including cancer and ischemic disorders.

      Conclusion:


      Human recombinant CYR61 is a valuable research tool and a potential regulator of angiogenesis. Its production, characterization, and applications in modulating angiogenic processes contribute to our understanding of angiogenesis and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYR61 offer promising prospects for improving outcomes in cancer, cardiovascular diseases, and wound healing.

      What is the molecular weight/Mw of CCN1 Protein?
      CCN1 Protein has a total Mw of 39.5kDa.

      What is the source or expression system of CCN1 Protein?
      Escherichia Coli.

      What is the Purity of CCN1 Protein?
      CCN1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCN1 Protein?
      The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.

      What is the amino acid sequence of CCN1 Protein?
      TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
      PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD

      What applications can CCN1 Protein be used in?
      CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCN1 Protein?
      The endotoxin level is minimal, CCN1 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.

    Cyr61 Human
  • View Data Sheet

    Name :

    HB-EGF Human

    Description:

    HB-EGF Human Recombinant

    HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    Product # :

    CYT-119

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    • More Info

    Description

    HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

    More Info

    • Introduction

      HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

    • Synonyms

      HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF 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 Human HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC

      KYVKELRAPS CICHPGYHGE RCHGLSL.

    • Background

      What is the molecular weight/Mw of HB-EGF Protein?
      HB-EGF Protein has a total Mw of 9.9kDa.

      What is the source or expression system of HB-EGF Protein?
      Escherichia Coli.

      What is the Purity of HB-EGF Protein?
      HB-EGF Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of HB-EGF Protein?
      The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

      What is the amino acid sequence of HB-EGF Protein?
      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
      KYVKELRAPS CICHPGYHGE RCHGLSL.

      What applications can HB-EGF Protein be used in?
      HB-EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HB-EGF Protein?
      The endotoxin level is minimal, HB-EGF 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.

    Hb Egf Human
  • View Data Sheet

    Name :

    GH Porcine

    Description:

    Growth Hormone Porcine Recombinant

    GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin, pST.

    Product # :

    CYT-519

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    Description

    Porcine-Somatotropin Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids and having a molecular mass of 21730 Dalton. Growth Hormone is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Growth-hormone (1 mg/ml) was lyophilized after extensive dialyses against 0.34 mg sodium phosphate buffer (0.02 mg sodium phosphate monobasic & 0.32 mg sodium phosphate dibasic).

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Somatotropin contains 3 units/mg.

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin, pST.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Somatotropin 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 pST in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Phe-Pro-Ala-Met-Pro.

    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.

    Growth Hormone Porcine
  • View Data Sheet

    Name :

    ARTN Human

    Description:

    Artemin Human Recombinant

    ART, ARTN , EVN, NBN.

    Product # :

    CYT-306

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    • description
    • source
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    • More Info

    Description

    Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

    More Info

    • Introduction

      The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.

    • Synonyms

      ART, ARTN , EVN, NBN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Artemin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Artemin Human Recombinant 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 Artemin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

    • Background

      Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications

      Abstract:

      Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.

      Introduction:

      Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.

      Artemin Signaling and Mechanisms:

      Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.

      Artemin in Neurological Disorders:

      Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.

      Therapeutic Potential of Artemin Human Recombinant:

      Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.

      Challenges and Future Directions:

      While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.

      Conclusion:

      Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.

      What is the molecular weight/Mw of ARTN Protein?
      ARTN Protein has a total Mw of 24.2kDa.

      What is the source or expression system of ARTN Protein?
      Escherichia Coli.

      What is the Purity of ARTN Protein?
      ARTN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of ARTN Protein?
      The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

      What is the amino acid sequence of ARTN Protein?
      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

      What applications can ARTN Protein be used in?
      ARTN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ARTN Protein?
      The endotoxin level is minimal, ARTN 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.

    Artemin Human
  • View Data Sheet

    Name :

    WISP2 Human

    Description:

    WNT1 Inducible Signaling Pathway Protein 2 Human Recombinant

    WNT1 Inducible Signaling Pathway Protein 2, Connective Tissue Growth Factor-Related Protein 58, Connective Tissue Growth Factor-Like Protein, CCN Family Member 5, CTGF-L, CT58, CCN5, WISP-2, CTGFL, WISP2.

    Product # :

    CYT-970

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    Description

    WISP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 24.4kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WNT1-inducible-signaling pathway protein 2 (WISP2) belongs to the WNT1 inducible signaling pathway (WISP) protein subfamily, which belongs to the connective tissue growth factor (CTGF) family. The CTGF family members are characterized by 4 conserved cysteine-rich domains: insulin-like growth factor-binding domain, von Willebrand factor type C module, thrombospondin domain and C-terminal cystine knot-like (CT) domain. WISP2 protein lacks the CT domain which is implicated in dimerization binding. WISP2 is possibly involved in bone remodeling. WISP2 is expressed in primary osteoblasts and fibroblasts. WISP2 stimulates osteoblast adhesion and inhibits osteocalcin production. WISP2 expression in colon tumors is reduced while the other 2 WISP members are overexpressed in colon tumors. WISP2 may play an imperative role in modulating bone turnover.

    • Synonyms

      WNT1 Inducible Signaling Pathway Protein 2, Connective Tissue Growth Factor-Related Protein 58, Connective Tissue Growth Factor-Like Protein, CCN Family Member 5, CTGF-L, CT58, CCN5, WISP-2, CTGFL, WISP2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized WISP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution WISP-2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized WISP-2 in sterile 10mM acetic acidnot less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQLCPTPCTC PWPPPRCPLG VPLVLDGCGC CRVCARRLGE PCDQLHVCDA SQGLVCQPGA GPGGRGALCL LAEDDSSCEV NGRLYREGET FQPHCSIRCR CEDGGFTCVP LCSEDVRLPS WDCPHPRRVE VLGKCCPEWV CGQGGGLGTQ PLPAQGPQFS GLVSSLPPGV PCPEWSTAWG PCSTTCGLGM ATRVSNQNRF CRLETQRRLC LSRPCPPSRG RSPQNSAF.

    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.

    Wisp2 Human
  • View Data Sheet

    Name :

    Y.Enterocolitica (O:9) LcrV

    Description:

    Yersinia Enterocolitica (O:9) LcrV Recombinant

    Product # :

    PRO-2277

    Price :

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    Shipped with Ice Packs

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    • description
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    Description

    Recombinant Yersinia Enterocolitica (O:9) LcrV produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 38,668 Dalton. Y.Enterocolitica (O:9) LcrV is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Y.Enterocolitica (O:9) LcrV is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG- and IgM- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.

    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.

    Yenterocolitica O 9 Lcrv
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