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Search results

1000 results found for “NPM”

Name

Description

Product #

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  • View Data Sheet

    Name :

    SNX1 Human

    Description:

    Sorting Nexin 1 Human Recombinant

    HsT17379, SNX1A, Vps5.

    Product # :

    PRO-665

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    SNX1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 415 amino acids (146-522 a.a.) and having a molecular mass of 48 kDa. SNX1 is fused to 38 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNX1 0.25mg/ml solution contains 20mM Tris-HCl buffer pH-8, 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNX1 belongs to the large family of hydrophilic proteins that interact with a range of receptor types that participate in intracellular trafficking. SNX1 and the associated splice variant, SNX1A, bind the EGFR, enable its transport to the lysosome, and thus contribute to the degradation of the receptor. SNX1 is related with cellular membranes, and they, also, associate with EGF, PDGF and the receptor tyrosine kinases.

    • Synonyms

      HsT17379, SNX1A, Vps5.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      SNX1 although stable at 4°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGGSMTV GITDPEKIGD GMNAYVAYKV TTQTSLPLFR SKQFAVKRRF SDFLGLYEKL
      SEKHSQNGFI VPPPPEKSLI GMTKVKVGKE DSSSAEFLEK RRAALERYLQ RIVNHPTMLQ DPDVREFLEK EELPRAVGTQ TLSGAGLLKM
      FNKATDAVSK MTIKMNESDI WFEEKLQEVE CEEQRLRKLH AVVETLVNHR KELALNTAQF AKSLAMLGSS EDNTALSRAL SQLAEVEEKI
      EQLHQEQANN DFFLLAELLS DYIRLLAIVR AAFDQRMKTW QRWQDAQATL QKKREAEARL LWANKPDKLQ QAKDEILEWE SRVTQYERDF
      ERISTVVRKE VIRFEKEKSK DFKNHVIKYL ETLLYSQQQL AKYWEAFLPE AKAIS.

    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.

    Snx1 Human
  • View Data Sheet

    Name :

    NSDHL Human

    Description:

    NAD (P) Dependent Steroid Dehydrogenase-Like Human Recombinant

    H105E3, SDR31E1, XAP104, Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating, Protein H105e3, NSDHL.

    Product # :

    PRO-1800

    Price :

    Quantity :

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    • More Info

    Description

    NSDHL Human Recombinant produced in E. coli is a single polypeptide chain containing 320 amino acids (1-297) and having a molecular mass of 35.5kDa. NSDHL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NSDHL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAD (P) Dependent Steroid Dehydrogenase-Like (NSDHL) takes part in synthesis of cholesterol. NSDHL is involved in one of a few steps which convert lanosterol to cholesterol by removing a carbon atom and three hydrogen atoms (a methyl group). NSDHL is also a vital element of cell membranes and myelin, the fatty covering that insulates nerve cells.

    • Synonyms

      H105E3, SDR31E1, XAP104, Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating, Protein H105e3, NSDHL.

    • 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 MGSMEPAVSE PMRDQVARTH LTEDTPKVNA DIEKVNQNQA KRCTVIGGSG FLGQHMVEQL LARGYAVNVF DIQQGFDNPQ VRFFLGDLCS RQDLYPALKG VNTVFHCASP PPSSNNKELF YRVNYIGTKN VIETCKEAGV QKLILTSSAS VIFEGVDIKN GTEDLPYAMK PIDYYTETKI LQERAVLGAN DPEKNFLTTA IRPHGIFGPR DPQLVPILIE AARNGKMKFV IGNGKNLVDF TFVENVVHGH ILAAEQLSRD STLGGKAFHI TNDEPIPFWT FLSRILTGLN YEAPKYHIPY.

    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.

    Nsdhl Human
  • View Data Sheet

    Name :

    SPIN1 Human

    Description:

    Spindlin-1 Human Recombinant

    Ovarian cancer-related protein, spindlin 1, SPIN, OCR.

    Product # :

    PRO-1184

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    • More Info

    Description

    SPIN1 Human Recombinant produced E. coli is a single polypeptide chain containing 285 amino acids (1-262) and having a molecular mass of 32.0kDa.SPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SPIN1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SPIN1 is a member of the SPIN/STSY family. SPIN1 is localized to nucleus, and expressed in several tissues and cells. SPIN1 takes part in cell-cycle regulation in the course of the transition from gamete to embryo.

    • Synonyms

      Ovarian cancer-related protein, spindlin 1, SPIN, OCR.

    • 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 MGSMKTPFGK TPGQRSRADA GHAGVSANMM KKRTSHKKHR SSVGPSKPVS QPRRNIVGCR IQHGWKEGNG PVTQWKGTVL DQVPVNPSLY LIKYDGFDCV YGLELNKDER VSALEVLPDR VATSRISDAH LADTMIGKAV EHMFETEDGS KDEWRGMVLA RAPVMNTWFY ITYEKDPVLY MYQLLDDYKE GDLRIMPDSN DSPPAEREPG EVVDSLVGKQ VEYAKEDGSK RTGMVIHQVE AKPSVYFIKF DDDFHIYVYD LVKTS

    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.

    Spin1 Human
  • View Data Sheet

    Name :

    CADM1 Human

    Description:

    Cell Adhesion Molecule 1 Human Recombinant

    Cell Adhesion Molecule 1, Tumor Suppressor In Lung Cancer 1, IGSF4, Spermatogenic Immunoglobulin Superfamily, Immunoglobulin Superfamily, Member 4, Immunoglobulin Superfamily Member 4, Synaptic Cell Adhesion Molecule, Nectin-Like Protein 2, Nectin-Like 2, Necl-2, SgIGSF, IGSF4A, SYNCAM, TSLC-1, TSLC1, NECL2, Immunoglobulin Superfamily, Member 4D Variant 1, Immunoglobulin Superfamily, Member 4D Variant 2, TSLC1/Nectin-Like 2/IGSF4, Truncated CADM1 Protein, STSLC-1, SynCAM1, RA175, ST17, BL2, Cell adhesion molecule 1.

    Product # :

    PRO-2098

    Price :

    Quantity :

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    • description
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    Description

    CADM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (45-374 a.a) and having a molecular mass of 39.4 kDa. CADM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CADM1 protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cell Adhesion Molecule 1, also known as CADM1 belongs to the nectin family. CADM1 mediates homophilic cell-cell adhesion in a Ca2+-independent manner as well as mediating heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca2+-independent manner. Furthermore, CADM1 perform as a tumor suppressor in non-small-cell lung cancer, NSCLC, cells. The interaction with CRTAM promotes natural killer (NK) cell cytotoxicity & IFN-gamma secretion by CD8+ cells in vitro over and above NK cell-mediated rejection of tumors expressing CADM3 in vivo.

    • Synonyms

      Cell Adhesion Molecule 1, Tumor Suppressor In Lung Cancer 1, IGSF4, Spermatogenic Immunoglobulin Superfamily, Immunoglobulin Superfamily, Member 4, Immunoglobulin Superfamily Member 4, Synaptic Cell Adhesion Molecule, Nectin-Like Protein 2, Nectin-Like 2, Necl-2, SgIGSF, IGSF4A, SYNCAM, TSLC-1, TSLC1, NECL2, Immunoglobulin Superfamily, Member 4D Variant 1, Immunoglobulin Superfamily, Member 4D Variant 2, TSLC1/Nectin-Like 2/IGSF4, Truncated CADM1 Protein, STSLC-1, SynCAM1, RA175, ST17, BL2, Cell adhesion molecule 1.

    • 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 MGSQNLFTKD VTVIEGEVAT ISCQVNKSDD SVIQLLNPNR QTIYFRDFRP LKDSRFQLLN FSSSELKVSL TNVSISDEGR YFCQLYTDPP QESYTTITVL VPPRNLMIDI QKDTAVEGEE IEVNCTAMAS KPATTIRWFK GNTELKGKSE VEEWSDMYTV TSQLMLKVHK EDDGVPVICQ VEHPAVTGNL QTQRYLEVQY KPQVHIQMTY PLQGLTREGD ALELTCEAIG KPQPVMVTWV RVDDEMPQHA VLSGPNLFIN NLNKTDNGTY RCEASNIVGK AHSDYMLYVY DPPTTIPPPT TTTTTTTTTT TTILTIITDS RAGEEGSIRA VDH.

    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.

    Cadm1 Human
  • View Data Sheet

    Name :

    phrB E.Coli

    Description:

    Deoxyribodipyrimidine photo-lyase E.Coli Recombinant

    800x600 ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    ENZ-362

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    Description

    800x600 800x600 phrB E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 495 amino acids (1-472) and having a molecular mass of 56.1kDa.phrB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The phrB solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Deoxyribodipyrimidine photo-lyase (phrB) is a member of the DNA photolyase class-1 family. phrB takes part in repair of UV radiation-inducedDNA damage. phrB catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidinedimers (in cis-syn configuration), which are formed between closest bases on the same DNA strand uponexposure to ultraviolet radiation.

    • Synonyms

      ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTTHLVW FRQDLRLHDN LALAAACRNS SARVLALYIA TPRQWATHNM SPRQAELINA QLNGLQIALA EKGIPLLFRE VDDFVASVEI VKQVCAENSV THLFYNYQYE VNERARDVEV ERALRNVVCE GFDDSVILPP GAVMTGNHEM YKVFTPFKNA WLKRLREGMP ECVAAPKVRS SGSIEPSPSI TLNYPRQSFD TAHFPVEEKA AIAQLRQFCQ NGAGEYEQQR DFPAVEGTSR LSASLATGGL SPRQCLHRLL AEQPQALDGG AGSVWLNELI WREFYRHLIT YHPSLCKHRP FIAWTDRVQW QSNPAHLQAW QEGKTGYPIV DAAMRQLNST GWMHNRLRMI TASFLVKDLL IDWREGERYF MSQLIDGDLA ANNGGWQWAA STGTDAAPYF RIFNPTTQGE KFDHEGEFIR QWLPELRDVP GKVVHEPWKW AQKAGVTLDY PQPIVEHKEA RVQTLAAYEA ARKGK.

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    Phrb Ecoli
  • View Data Sheet

    Name :

    PPID Mouse

    Description:

    Peptidylprolyl Isomerase D Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, CYP-40, Cyclophilin-related protein, CYP40, CYPD, PPID, Peptidylprolyl Isomerase D.

    Product # :

    ENZ-1069

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    Description

    PPID Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (1-370a.a.) and having a molecular mass of 43.4kDa. PPID is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPID protein solution (1mg/ml) containing 20mM Tris-Hcl buffer (pH8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 700nmol/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-PNA per minute at 37°C in Tris–HCl pH 8.0 using chymotrypsin.

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    • Introduction

      Cyclophilin-D is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-D possess PPIase activity and binds to the immunosuppressant cyclosporin-A. Cyclophilin-D is very well known that its overexpression suppresses the apoptosis in cancer cell. Cyclophilin-D suppresses apoptotic cell death by the use of mitochondrial hexokinase-2 dependent mechanism in cancer cells.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, CYP-40, Cyclophilin-related protein, CYP40, CYPD, PPID, Peptidylprolyl Isomerase D.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFMSHAS PAAKPSNSKN PRVFFDVDIG GERVGRIVLE LFADIVPKTA ENFRALCTGE KGTGSTTGKP LHFKGCPFHR IIKKFMIQGG DFSNQNGTGG ESIYGEKFED ENFHYKHDRE GLLSMANAGP NTNGSQFFIT TVPTPHLDGK HVVFGQVIKG LGVARTLENV EVNGEKPAKL CVIAECGELK EGDDWGIFPK DGSGDSHPDF PEDADIDLKD VDKILLISED LKNIGNTFFK SQNWEMAIKK YAKVLRYVDS SKAVIEKADR SRLQPIALSC VLNIGACKLK MSNWQGAIDS CLEALEMDPS NTKALYRKAQ GWQGLKEYDQ ALADLKKAQE IAPGDKAIQA ELLKVKQMIK AQKDKEKAVY AKMFA.

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    Ppid Mouse
  • View Data Sheet

    Name :

    LASP1 Human

    Description:

    LIM and SH3 Protein 1 Human Recombinant

    LIM and SH3 protein 1, MLN50, Lasp-1, Metastatic lymph node gene 50 protein.

    Product # :

    PRO-1031

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    Description

    LASP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-261) and having a molecular mass of 32.3kDa.LASP1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The LASP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

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    • Introduction

      LASP1 has a vital part in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation can additionally assist in regulation of actin-associated ion transport activities in the parietal cell and in several other F-actin-rich secretory epithelial cell types.

    • Synonyms

      LIM and SH3 protein 1, MLN50, Lasp-1, Metastatic lymph node gene 50 protein.

    • 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 MGSHMNPNCA RCGKIVYPTE KVNCLDKFWH KACFHCETCK MTLNMKNYKG YEKKPYCNAH YPKQSFTMVA DTPENLRLKQ QSELQSQVRY KEEFEKNKGK GFSVVADTPE LQRIKKTQDQ ISNIKYHEEF EKSRMGPSGG EGMEPERRDS QDGSSYRRPL EQQQPHHIPT SAPVYQQPQQ QPVAQSYGGY KEPAAPVSIQ RSAPGGGGKR YRAVYDYSAA DEDEVSFQDG DTIVNVQQID DGWMYGTVER TGDTGMLPAN YVEAI

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    Lasp1 Human
  • View Data Sheet

    Name :

    VSTM2L Human

    Description:

    V-Set and Transmembrane Domain Containing 2 Like Human Recombinant

    V-set and transmembrane domain-containing protein 2-like protein, VSTM2L, C20orf102, dJ1118M15.2.

    Product # :

    PRO-1018

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    Description

    VSTM2L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (25-204 a.a.) and having a molecular mass of 22.6kDa. VSTM2L is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    VSTM2L protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl,1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      V-set and transmembrane domain containing 2 (VSTM2L) is a novel modulator of HN neuroprotective activity. VSTM2L colocalizes with HN in distinct brain areas as well as in primary cultured neurons, where it plays a part in the modulation of neuronal viability. When tested in HN neuroprotection bioassays, VSTM2L acts as a potent antagonist of HN neuroprotective activity. The VSTM2L protein is the first example of a secreted antagonist of HN and may have a role in the modulation of HN biological functions.

    • Synonyms

      V-set and transmembrane domain-containing protein 2-like protein, VSTM2L, C20orf102, dJ1118M15.2.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSHMTRPAG HAPWDNHVSG HALFTETPHD MTARTGEDVE MACSFRGSGS PSYSLEIQWW YVRSHRDWTD KQAWASNQLK ASQQEDAGKE ATKISVVKVV GSNISHKLRL SRVKPTDEGS YECRVIDFSD GKARHHKVKA YLRVQPGENS VLHLPEAPPA APAPPPPKPG KELRKRSVDQ EACSL.

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    Vstm2L Human
  • View Data Sheet

    Name :

    HCV NS3 Genotype-1c

    Description:

    Hepatitis C Virus NS3 Genotype-1c, (1192-1459 a.a.) Recombinant

    Product # :

    HCV-208

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    Description

    The E.coli derived recombinant His-Tag fusion protein contains the HCV NS3 immunodominant regions, amino acids 1192-1459.

    Formulation

    1.5M urea, 25mM Tris-HCl pH-8, 0.2% Triton-X & 50% Glycerol.

    Purity

    HCV NS3 Genotype-1c protein is >95% pure as determined by 10% PAGE (coomassie staining).

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    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
      HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

    • Stability

      HCV NS3 Genotype-1c although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HCV NS3 Genotype-1c antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HCV-infected individuals.

    • Purification Method

      HCV NS3 Genotype-1c protein was purified by proprietary chromatographic technique.

    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.

    Hcv Ns3 Genotype 1C
  • View Data Sheet

    Name :

    ProNGF Human

    Description:

    Pro-Nerve Growth Factor Human Recombinant

    Human Pro-NGF, ProNGF, NGFB.

    Product # :

    CYT-426

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    Description

    Pro-NGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 25 kDa.ProNGF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ProNGF was lyophilized from a 0.2 μM filtered solution of 20m Tris-HCL, 0.5M NaCl, 5% Trehalose, 5% Mannitol. 0.01% Tween-80 and 1mM EDTA pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Synonyms

      Human Pro-NGF, ProNGF, NGFB.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ProNGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProNGF 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 ProNGF in distilled water to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
      TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
      SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
      KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
      VCVLSRKAVRRA.

    • Background

      Pro-Nerve Growth Factor Human Recombinant: Unveiling its Potential in Neuroregulation and Disease Pathogenesis

      Abstract:

      Pro-Nerve Growth Factor (Pro-NGF) human recombinant is a crucial precursor protein involved in neuronal development, survival, and degenerative processes. This research paper aims to provide a comprehensive analysis of Pro-NGF, including its characteristics, processing mechanisms, and implications in neuroregulation and disease pathogenesis. Additionally, innovative methodologies for the production and manipulation of Pro-NGF human recombinant are proposed, highlighting its potential as a therapeutic target for neurological disorders and neurodegenerative diseases.

      Introduction:

      Neuroregulation and maintenance of neuronal health are intricate processes governed by a network of signaling molecules. Pro-NGF, the precursor form of Nerve Growth Factor (NGF), acts as a key player in neuronal development, synaptic plasticity, and cell survival. This paper delves into the distinctive features of Pro-NGF and presents novel approaches for the production and manipulation of Pro-NGF human recombinant, aiming to unravel its role in neuroregulation and disease pathogenesis.

      Characteristics and Processing Mechanisms:

      Pro-NGF is initially synthesized as an inactive precursor, requiring proteolytic cleavage for conversion into mature NGF. The processing of Pro-NGF involves the action of proteases, such as furin, and the formation of distinct protein complexes. The balance between Pro-NGF and mature NGF levels plays a critical role in modulating neuronal function and fate, influencing processes such as neuronal survival, axonal growth, and synaptic plasticity.

      Production and Manipulation of Pro-NGF Human Recombinant:

      Efficient production methodologies and manipulation strategies are crucial for studying the role of Pro-NGF in neuroregulation and disease pathogenesis. Recombinant protein expression systems, including mammalian cell culture and bacterial expression systems, have been employed to produce functional Pro-NGF human recombinant. Techniques such as mutagenesis, protein purification, and specific inhibitors targeting Pro-NGF processing pathways enable the manipulation of Pro-NGF levels and investigation of its downstream effects.

      Implications in Neuroregulation and Disease Pathogenesis:

      Pro-NGF human recombinant holds significant potential in understanding the intricate mechanisms underlying neuroregulation and disease pathogenesis. Dysregulation of Pro-NGF processing and altered Pro-NGF/mature NGF ratios have been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and ischemic stroke. Manipulating Pro-NGF levels and the balance between its mature form may offer therapeutic strategies for modulating neurotrophic signaling and promoting neuronal health in these conditions.

      Conclusion:

      Pro-NGF human recombinant emerges as a key regulator in neuroregulation and disease pathogenesis, offering promising avenues for therapeutic intervention. Enhancing our understanding of Pro-NGF processing mechanisms and its downstream signaling cascades will provide valuable insights into neurodevelopment, neurodegeneration, and potential therapeutic strategies. Targeting Pro-NGF as a therapeutic intervention may hold immense promise in treating neurological disorders and promoting neuronal health.

      What is the molecular weight / Mw of ProNGF Protein?
      ProNGF Protein has a total Mw of 25kDa.

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

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


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

      What is the amino acid sequence of ProNGF Protein?
      MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
      TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
      SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
      KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
      VCVLSRKAVRRA

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

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

    Pro Ngf Human
  • View Data Sheet

    Name :

    DCTPP1 Human

    Description:

    dCTP Pyrophosphatase 1 Human Recombinant

    dCTP pyrophosphatase 1, RS21C6, XTP3TPA, Deoxycytidine-triphosphatase 1, dCTPase 1, XTP3-transactivated gene A protein, CDA03, MGC5627, XTP3-transactivated protein A, EC 3.6.1.12.

    Product # :

    ENZ-234

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    Description

    DCTPP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 194 amino acids (1-170) and having a molecular mass of 21.2kDa.DCTPP1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DCTPP1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      DCTPP1, also known as dCTP pyrophosphatase 1, contains an epilepsy-associated repeat (EAR) domain that is predicted to participate in protein-protein interactions, most likely involved in ligand recognition. This protein functions to hydrolyze abnormal nucleotide triphosphates (NTPs) in cancer cells that, if unregulated, could be incorporated into nascent DNA or RNA.

    • Synonyms

      dCTP pyrophosphatase 1, RS21C6, XTP3TPA, Deoxycytidine-triphosphatase 1, dCTPase 1, XTP3-transactivated gene A protein, CDA03, MGC5627, XTP3-transactivated protein A, EC 3.6.1.12.

    • 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 MGSHMSVAGG EIRGDTGGED TAAPGRFSFS PEPTLEDIRR LHAEFAAERD WEQFHQPRNL LLALVGEVGE LAELFQWKTD GEPGPQGWSP RERAALQEEL SDVLIYLVAL AARCRVDLPL AVLSKMDINR RRYPAHLARS SSRKYTELPH GAISEDQAVG PADIPCDSTG QTST.

    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.

    Dctpp1 Human
  • View Data Sheet

    Name :

    CRP Rat

    Description:

    C-Reactive Protein Rat Recombinant

    Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.

    Product # :

    PRO-1421

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    Description

    CRP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 217 amino acids (20-230 a.a.) and having a molecular mass of 24.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa).CRP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CRP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.

    • Synonyms

      Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.

    • 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

      HEDMSKQAFV FPGVSATAYV SLEAESKKPL EAFTVCLYAH ADVSRSFSIF SYATKTSFNE ILLFWTRGQG FSIAVGGPEI LFSASEIPEV PTHICATWES ATGIVELWLD GKPRVRKSLQ KGYIVGTNAS IILGQEQDSY GGGFDANQSL VGDIGDVNMW DFVLSPEQIN AVYVGRVFSP NVLNWRALKY ETHGDVFIKP QLWPLTDCCE SHHHHHH.

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    Crp Rat
  • View Data Sheet

    Name :

    ELOB Mouse

    Description:

    Elongin B Mouse Recombinant

    Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.

    Product # :

    PRO-2550

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    Description

    ELOB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 141 amino acids ( 1-118 a.a.) having a molecular mass of 15.6 kDa. The Recombinant Mouse ELOB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains PBS pH-7.4 containing 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Elongin B (Elob) is a subunit of the transcription factor B (SIII) complex. SIII complex is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. The SIII complex comprised of a transcriptionally active subunit (A) and 2 regulatory subunits (B and C). Subunit A is transcriptionally active and its transcription activity is enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C. The von Hippel-Lindau tumor suppressor protein binds to elongin B and C and inhibits transcription elongation.

    • Synonyms

      Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.

    • 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 MGSMDVFLMI RRHKTTIFTD AKESSTVFEL KRIVEGILKR PPEEQRLYKD DQLLDDGKTL GECGFTSQTA RPQAPATVGL AFRADDTFEA LRIEPFSSPP ELPDVMKPQD SGGSANEQAV Q

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    Elongin B Human
  • View Data Sheet

    Name :

    Borrelia Afzelii BmpA

    Description:

    Borrelia Afzelii Basic Membrane Protein A Recombinant

    Product # :

    BOR-012

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    Description

    Recombinant Borrelia Afzelii Basic Membrane Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 36,227 Dalton. Borrelia Afzelii BmpA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Afzelii BmpA 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

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • 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-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma; suitable for LTT (lymphocyte transformation test).

    • Applications

      Western blot with Lyme positive plasma.

    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.

    Borrelia Afzelii Bmpa
  • View Data Sheet

    Name :

    BPNT1 Human

    Description:

    3(2) 5-Bisphosphate Nucleotidase 1 Human Recombinant

    3'(2'), 5'-bisphosphate nucleotidase 1, Bisphosphate 3'-nucleotidase 1, PAP-inositol-1,4-phosphatase, PIP, EC 3.1.3.7, BPntase.

    Product # :

    ENZ-061

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    Description

    BPNT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-308a.a.) and having a molecular mass of 37.5kDa.BPNT1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BPNT1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 5mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      BPNT1 belongs to the magnesium-dependent, lithium-sensitive phosphomono-esterase superfamily. BPNT1 catalyzes the conversion of PAPS (adenosine 3'-phosphate 5' phosphosulfate) to APS (adenosine 5'-phosphosulfate) and the conversion of PAP (3'(2')-phosphoadenosine 5' phosphate) to AMP (adenosine 5'-phosphate) using magnesium as a cofactor. BPNT1 is expressed everywhere but at maximum levels in brain and kidney. BPNT1 is potently inhibited by lithium, a drug used for the treatment of manic depression and bipolar affective disorder, which suggests that BPNT1 has a possible role in the etiology of mood disorders.

    • Synonyms

      3'(2'), 5'-bisphosphate nucleotidase 1, Bisphosphate 3'-nucleotidase 1, PAP-inositol-1,4-phosphatase, PIP, EC 3.1.3.7, BPntase.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASS NTVLMRLVAS AYSIAQKAGM IVRRVIAEGD LGIVEKTCAT DLQTKADRLA QMSICSSLAR KFPKLTIIGE EDLPSEEVDQ ELIEDSQWEE ILKQPCPSQY SAIKEEDLVV WVDPLDGTKE YTEGLLDNVT VLIGIAYEGK AIAGVINQPY YNYEAGPDAV LGRTIWGVLG LGAFGFQLKE VPAGKHIITT TRSHSNKLVT DCVAAMNPDA VLRVGGAGNK IIQLIEGKAS AYVFASPGCK KWDTCAPEVI LHAVGGKLTD IHGNVLQYHK DVKHMNSAGV LATLRNYDYY ASRVPESIKN ALVP

    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.

    Bpnt1 Human
  • View Data Sheet

    Name :

    Borrelia Garinii OspC

    Description:

    Borrelia Garinii OspC Recombinant

    Product # :

    BOR-021

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    Description

    Recombinant Borrelia Garinii Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 22kDa.Borrelia Garinii OspC is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Garinii OspC is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • 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-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.

    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.

    Borrelia Garinii Ospc
  • View Data Sheet

    Name :

    AMTN Human

    Description:

    Amelotin Human Recombinant

    UNQ689, Amelotin, PRO1329.

    Product # :

    PRO-1301

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    Description

    AMTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (17-209 a.a.) and having a molecular mass of 22.2kDa.AMTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AMTN protein solution (0.5mg/ml) contains mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AMTN is a member of the amelotin family. AMTN is a lately discovered secreted enamel protein. AMTN mainly expressed during the maturation stage of enamel formation. AMTN gathers in a basal lamina-like structure at the interface between ameloblasts and enamel mineral and it co-localizes with one more lately described enamel protein, odontogenic ameloblast- related protein (ODAM(.

    • Synonyms

      UNQ689, Amelotin, PRO1329.

    • 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 MGSLPQLKPA LGLPPTKLAP DQGTLPNQQQ SNQVFPSLSL IPLTQMLTLG PDLHLLNPAA GMTPGTQTHP LTLGGLNVQQ QLHPHVLPIF VTQLGAQGTI LSSEELPQIF TSLIIHSLFP GGILPTSQAG ANPDVQDGSL PAGGAGVNPA TQGTPAGRLP TPSGTDDDFA VTTPAGIQRS THAIEEATTE SANGIQ.

    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.

    Amtn Human
  • View Data Sheet

    Name :

    BNP Human, His

    Description:

    B-type Natriuretic Peptide Human Recombinant, His Tag

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    Product # :

    CYT-605

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    Description

    BNP Recombinant Human fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids (27-134 a.a) and having a molecular mass of 14 kDa. BNP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BNP 0.5mg/ml is formulated with 1X PBS pH-7.4, 2mM DTT, 0.1mM PMSF, 1mM EDTA and 40% glycerol.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    sds-page

    BNP Human sds-page - Product image 1

    More Info

    • Introduction

      Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MHPLGSPGSA SDLETSGLQE QRNHLQGKLSELQVEQTSLE PLQESPRPTG VWKSREVATE GIRGHRKMVL YTLRAPRSPK MVQGSGCFGR KMDRISSSSG LGCKVLRRH.

    • Background

      What is the molecular weight / Mw of BNP His Protein?
      BNP Protein has a total Mw of 14kDa.

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

      What is the Purity of BNP His Protein?

      BNP Protein is >95% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of BNP His Protein?
      MGSSHHHHHH SSGLVPRGSH MHPLGSPGSA SDLETSGLQE QRNHLQGKLSELQVEQTSLE PLQESPRPTG VWKSREVATE GIRGHRKMVL YTLRAPRSPK MVQGSGCFGR KMDRISSSSG LGCKVLRRH

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

      What is the endotoxin level for BNP His Protein?
      The endotoxin level is minimal, BNP His Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nppb Human His
  • View Data Sheet

    Name :

    Midkine Rat

    Description:

    Midkine Rat Recombinant

    Midkine, MK, Mdk.

    Product # :

    CYT-747

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    Description

    Midkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a molecular mass of 13.2kDa.The Midkine Rat is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-100 ng/ml.

    More Info

    • Introduction

      Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
      Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
      The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
      Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
      Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
      Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

    • Synonyms

      Midkine, MK, Mdk.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAKKKDKVKK GSECSEWTWG PCTPSSKDCG MGFREGTCGA QTQRIHCKVP CNWKKEFGAD CKYKFESWGA CDGSTGTKAR QGTLKKARYN AQCQETIRVT KPCTSKTKSK AKAKKGKGKD.

    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.

    Midkine Rat
  • View Data Sheet

    Name :

    TNF a Rat

    Description:

    Tumor Necrosis Factor-Alpha Rat Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-393

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    Description

    Tumor Necrosis Factor-a Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17339.44 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The concentrated protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 IU/mg.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MLRSSSQNSS DKPVVHVVAN HQAEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLIY SQVLFKGQGC PDYVLLTHTV SRFATSYQEK VSLLSAIKSP CPKDTPEGAE LKPWYEPMYL GGVSQLEKGD LLSAEVNLPK YLDITESGQV YFGVIAL.

    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.

    Tnf Alpha Rat
  • View Data Sheet

    Name :

    CNRIP1 Human

    Description:

    Cannabinoid Receptor Interacting Protein 1 Human Recombinant

    Cannabinoid Receptor Interacting Protein 1, Cannabinoid Receptor CB1-Interacting Protein 1, Chromosome 2 Open Reading Frame 32, C2orf32, CRIP1, CRIP1a, CRIP1b, DKFZP566K1924.

    Product # :

    PRO-1214

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    Description

    CNRIP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 187 amino acids (1-164) and having a molecular mass of 21.0 kDa.CNRIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CNRIP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.

    • Synonyms

      Cannabinoid Receptor Interacting Protein 1, Cannabinoid Receptor CB1-Interacting Protein 1, Chromosome 2 Open Reading Frame 32, C2orf32, CRIP1, CRIP1a, CRIP1b, DKFZP566K1924.

    • 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 MGSMGDLPGL VRLSIALRIQ PNDGPVFYKV DGQRFGQNRT IKLLTGSSYK VEVKIKPSTL QVENISIGGV LVPLELKSKE PDGDRVVYTG TYDTEGVTPT KSGERQPIQI TMPFTDIGTF ETVWQVKFYN YHKRDHCQWG SPFSVIEYEC KPNETRSLMW VNKESFL

    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.

    Cnrip1 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 :

    HCV NS5B (2634-2752 a.a)

    Description:

    Hepatitis C Virus NS5B (2634-2752 a.a) Recombinant

    Product # :

    HCV-003

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    Description

    Recombinant Hepatitis C Virus NS5B produced in E. coli is a single polypeptide chain containing 155 amino acids (aa 2634-2752) and having a molecular mass of 17kDa (NCBI Accession # NP_671491).Recombinant HCV NS5B is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HCV NS5B protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae. HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPMGF SYDTRCFDST VTESDIRTEE AIYQCCDLDP QARVAIKSLT ERLYVGGPLT NSRGENCGYR RCRASGVLTT SCGNTLTCYI KARAACRAAG LQDCTMLVCG DDLVVICESA GVQED.

    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.

    Hcv Ns5B 2634 2752 Aa
  • View Data Sheet

    Name :

    MMP1 Human, sf9

    Description:

    Matrix Metalloproteinase-1 Human Recombinant, sf9

    Matrix Metallopeptidase 1, Interstitial Collagenase, Fibroblast Collagenase, EC 3.4.24.7, CLG, Matrix Metalloproteinase 1 (Interstitial Collagenase), Matrix Metallopeptidase 1 (Interstitial Collagenase), Matrix Metalloproteinase 1, Matrix Metalloproteinase-1, Matrix Metalloprotease 1, EC 3.4.24, MMP-1, CLGN, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1.

    Product # :

    ENZ-989

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    • description
    • source
    • formulation
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    • More Info

    Description

    MMP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 460 amino acids (18-469a.a) and having a molecular mass of 53.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). MMP1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MMP1 protein solution (0.25mg/ml) containing 20mM MES buffer (pH 5.5), 10mM CaCl2, 100 mM NaCl, 0.05% Brij35 and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

    • Synonyms

      Matrix Metallopeptidase 1, Interstitial Collagenase, Fibroblast Collagenase, EC 3.4.24.7, CLG, Matrix Metalloproteinase 1 (Interstitial Collagenase), Matrix Metallopeptidase 1 (Interstitial Collagenase), Matrix Metalloproteinase 1, Matrix Metalloproteinase-1, Matrix Metalloprotease 1, EC 3.4.24, MMP-1, CLGN, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1.

    • 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

      HSFPATLETQ EQDVDLVQKY LEKYYNLKND GRQVEKRRNS GPVVEKLKQM QEFFGLKVTG KPDAETLKVM KQPRCGVPDV AQFVLTEGNP RWEQTHLTYR IENYTPDLPR ADVDHAIEKA FQLWSNVTPL TFTKVSEGQA DIMISFVRGD HRDNSPFDGP GGNLAHAFQP GPGIGGDAHF DEDERWTNNF REYNLHRVAA HELGHSLGLS HSTDIGALMY PSYTFSGDVQ LAQDDIDGIQ AIYGRSQNPV QPIGPQTPKA CDSKLTFDAI TTIRGEVMFF KDRFYMRTNP FYPEVELNFI SVFWPQLPNG LEAAYEFADR DEVRFFKGNK YWAVQGQNVL HGYPKDIYSS FGFPRTVKHI DAALSEENTG KTYFFVANKY WRYDEYKRSM DPGYPKMIAH DFPGIGHKVD AVFMKDGFFY FFHGTRQYKF DPKTKRILTL QKANSWFNCR KNLEHHHHHH.

    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.

    Mmp1 Human Sf9
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