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Search results

1000 results found for “Heparanase”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    GOT2 Human

    Description:

    Glutamic-Oxaloacetic Transaminase 2 Human Recombinant

    EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    Product # :

    ENZ-684

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    Description

    GOT2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (30-430 a.a.) and having a molecular mass of 47kDa. The GOT2 fused to a 23 amino acid his tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GOT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 is invloved in amino acid metabolism and the urea and tricarboxylic acid cycles. The 2 enzymes are homodimeric and demonstrate close homology.

    • Synonyms

      EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    • 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 MGSSSWWTHV EMGPPDPILG VTEAFKRDTN SKKMNLGVGA YRDDNGKPYV LPSVRKAEAQ IAAKNLDKEY LPIGGLAEFC KASAELALGE NSEVLKSGRF VTVQTISGTG ALRIGASFLQ RFFKFSRDVF LPKPTWGNHT PIFRDAGMQL QGYRYYDPKT CGFDFTGAVE DISKIPEQSV LLLHACAHNP TGVDPRPEQW KEIATVVKKR NLFAFFDMAY QGFASGDGDK DAWAVRHFIE QGINVCLCQS YAKNMGLYGE RVGAFTMVCK DADEAKRVES QLKILIRPMY SNPPLNGARI AAAILNTPDL RKQWLQEVKV MADRIIGMRT QLVSNLKKEG STHNWQHITD QIGMFCFTGL KPEQVERLIK EFSIYMTKDG RISVAGVTSS NVGYLAHAIH QVTK.

    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.

    Got2 Human
  • View Data Sheet

    Name :

    FAP Human

    Description:

    Fibroblast Activation Protein Alpha Human Recombinant

    Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP,  FAP

    Product # :

    ENZ-1160

    Price :

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    Description

    FAP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 744 amino acids (26-760aa) and having a molecular mass of 86.1 kDa.FAP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The FAP solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 5,000 pmol/min/ug. It is defined by the amount of enzyme that hydrolyzes 1.0 pmole of ZGP-AMC per minute at pH 7.5, at 37˚C.

    More Info

    • Introduction

      DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.

    • Synonyms

      Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP, FAP

    • 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

      ADPLRPSRVH NSEENTMRAL TLKDILNGTF SYKTFFPNWI SGQEYLHQSA DNNIVLYNIE TGQSYTILSN RTMKSVNASN YGLSPDRQFV YLESDYSKLW RYSYTATYYI YDLSNGEFVR GNELPRPIQY LCWSPVGSKL AYVYQNNIYL KQRPGDPPFQ ITFNGRENKI FNGIPDWVYE EEMLATKYAL WWSPNGKFLA YAEFNDTDIP VIAYSYYGDE QYPRTINIPY PKAGAKNPVV RIFIIDTTYP AYVGPQEVPV PAMIASSDYY FSWLTWVTDE RVCLQWLKRV QNVSVLSICD FREDWQTWDC PKTQEHIEES RTGWAGGFFV STPVFSYDAI SYYKIFSDKD GYKHIHYIKD TVENAIQITS GKWEAINIFR VTQDSLFYSS NEFEEYPGRR NIYRISIGSY PPSKKCVTCH LRKERCQYYT ASFSDYAKYY ALVCYGPGIP ISTLHDGRTD QEIKILEENK ELENALKNIQ LPKEEIKKLE VDEITLWYKM ILPPQFDRSK KYPLLIQVYG GPCSQSVRSV FAVNWISYLA SKEGMVIALV DGRGTAFQGD KLLYAVYRKL GVYEVEDQIT AVRKFIEMGF IDEKRIAIWG WSYGGYVSSL ALASGTGLFK CGIAVAPVSS WEYYASVYTE RFMGLPTKDD NLEHYKNSTV MARAEYFRNV DYLLIHGTAD DNVHFQNSAQ IAKALVNAQV DFQAMWYSDQ NHGLSGLSTN HLYTHMTHFL KQCFSLSDHH HHHH

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

    Fap Human
  • View Data Sheet

    Name :

    CTSF Human, Sf9

    Description:

    Cathepsin-F Human Recombinant, Sf9

    CTSF, CATSF, CLN13.

    Product # :

    ENZ-1167

    Price :

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    • More Info

    Description

    CTSF produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 474 amino acids (20-484.a.a) and having a molecular mass of 52.5kDa.CTSF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTSF protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of Z-Phe-ArgAMC to Z-Phe-Arg and AMC per minute at pH 5.0 at 37℃.

    More Info

    • Introduction

      Cathepsin F (CTSF) is a member of the peptidase C1 family. Cathepsins are papain family cysteine proteinases which are a main component of the lysosomal proteolytic system. The CTSF gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF plays a role in normal protein catabolism. CTSF is involved in some degradative processes occurring in tumor progression since it is highly expressed in some cancer cell lines.

    • Synonyms

      CTSF, CATSF, CLN13.

    • 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

      ADLAPAQPRA ASFQAWGPPS PELLAPTRFA LEMFNRGRAA GTRAVLGLVR GRVRRAGQGS LYSLEATLEE PPCNDPMVCR LPVSKKTLLC SFQVLDELGR HVLLRKDCGP VDTKVPGAGE PKSAFTQGSA MISSLSQNHP DNRNETFSSV ISLLNEDPLS QDLPVKMASI FKNFVITYNR TYESKEEARW RLSVFVNNMV RAQKIQALDR GTAQYGVTKF SDLTEEEFRT IYLNTLLRKE PGNKMKQAKS VGDLAPPEWD WRSKGAVTKV KDQGMCGSCW AFSVTGNVEG WFLNQGTLL SLSEQELLDC DKMDKACMGG LPSNAYSAIK NLGGLETEDD YSYQGHMQSC NFSAEKAKVY INDSVELSQN EQKLAAWLAK RGPISVAINA FGMQFYRHGI SRPLRPLCSP WLIDHAVLLV GYGNRSDVPF WAIKNSWGTD WGEKGYYYLH RGSGACGVNT MASSAVVDHH HHHH

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

    Ctsf Protein
  • View Data Sheet

    Name :

    KLK11 Human

    Description:

    Kallikrein-11 Human Recombinant

    Kallikrein-11, hK11, Hippostasin, Serine protease 20, Trypsin-like protease, Kallikrein-11 inactive chain 1, Kallikrein-11 inactive chain 2, KLK11, PRSS20, TLSP, UNQ649/PRO1279, Kallikrein 11.

    Product # :

    ENZ-816

    Price :

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    Description

    KLK11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (54-278 a.a) and having a molecular mass of 24.8kDa.

    Source

    Escherichia Coli.

    Formulation

    KLK11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.

    • Synonyms

      Kallikrein-11, hK11, Hippostasin, Serine protease 20, Trypsin-like protease, Kallikrein-11 inactive chain 1, Kallikrein-11 inactive chain 2, KLK11, PRSS20, TLSP, UNQ649/PRO1279, Kallikrein 11.

    • 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

      MIIKGFECKP HSQPWQAALF EKTRLLCGAT LIAPRWLLTA AHCLKPRYIV HLGQHNLQKE EGCEQTRTAT ESFPHPGFNN SLPNKDHRND IMLVKMASPV SITWAVRPLT LSSRCVTAGT SCLISGWGST SSPQLRLPHT LRCANITIIE HQKCENAYPG NITDTMVCAS VQEGGKDSC GDSGGPLVCN QSLQGIISWG QDPCAITRKP GVYTKVCKYV DWIQET.

    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.

    Klk11 Human
  • View Data Sheet

    Name :

    UBE2V2 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2 Variant 2 Human Recombinant

    DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.

    Product # :

    ENZ-550

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    Description

    UBE2V2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145 a.a.) and having a molecular mass of 18.5 kDa. The UBE2V2 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2V2 Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2V2 comprises a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes however require the conserved cysteine residue that is vital for the catalytic activity of E2s. UBE2V2 shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product. UBE2V2 participates in the differentiation of monocytes and enterocytes.

    • Synonyms

      DDVit-1, DDVIT1, EDAF-1, EDPF-1, EDPF1, MMS2, UEV-2, UEV2, Ubiquitin-conjugating enzyme E2 variant 2, Enterocyte differentiation-associated factor 1, Enterocyte differentiation-promoting factor 1, Vitamin D3-inducible protein, UBE2V2.

    • 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 MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ ELRRLMMSKE NMKLPQPPEG QTYNN.

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    Ube2V2 Human
  • View Data Sheet

    Name :

    ENOPH1 Human

    Description:

    Enolase-Phosphatase-1 Human Recombinant

    Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.

    Product # :

    ENZ-077

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    Description

    ENOPH1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 281 amino acids (1-261 a.a.) and having a molecular mass of 31kDa. The ENOPH1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ENOPH1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Enolase-phosphatase E1 (ENOPH1) belongs to the MasA family of the HAD (halo-acid dehalogenase)-like hydrolase superfamily. ENOPH1 is a bifunctional enzyme which demonstrates both phosphatase and atypical enolase activities. ENOPH1 has a significant role in the ubiquitous methionine salvage pathway which is a biochemical pathway found in all organisms that regulate methionine levels in the cell.

    • Synonyms

      Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.

    • 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 MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIEENVK EYLQTHWEEE ECQQDVSLLR KQAEEDAHLD GAVPIPAASG NGVDDLQQMI QAVVDNVCWQ MSLDRKTTAL KQLQGHMWRA AFTAGRMKAE FFADVVPAVR KWREAGMKVY IYSSGSVEAQ KLLFGHSTEG DILELVDGHF DTKIGHKVES ESYRKIADSI GCSTNNILFL TDVTREASAA EEADVHVAVV VRPGNAGLTD DEKTYYSLIT SFSELYLPSS T.

    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.

    Enoph1 Human
  • View Data Sheet

    Name :

    RNASE3 Human, Sf9

    Description:

    Ribonuclease 3 Human Recombinant, Sf9

    ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.

    Product # :

    ENZ-1024

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    Description

    RNASE3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (28-160 a.a.) and having a molecular mass of 16.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).RNASE3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RNASE3 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

      Ribonuclease 3 (RNASE3) is cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. RNASE3 possesses a broad diversity of biological activities. RNASE3 protein has shown antibacterial activity such as cytoplasmic membrane depolarization of preferentially Gram-negative and Gram-positive strains and promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.

    • Synonyms

      ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.

    • 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

      ADPRPPQFTR AQWFAIQHIS LNPPRCTIAM RAINNYRWRC KNQNTFLRTT FANVVNVCGN QSIRCPHNRT LNNCHRSRFR VPLLHCDLIN PGAQNISNCR YADRPGRRFY VVACDNRDPR DSPRYPVVPV HLDTTIHHHH HH.

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

    Rnase3 Human Sf9
  • View Data Sheet

    Name :

    SARS Human

    Description:

    Seryl-tRNA Synthetase Human Recombinant

    Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    Product # :

    ENZ-229

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    Description

    SARS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 537 amino acids (1-514) and having a molecular mass of 61.2kDa.SARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SARS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Seryl-tRNA synthetase, cytoplasmic (SARS) is a member of the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases’ role is to catalyze the aminoacylation of tRNAs by their corresponding amino acids, as a result linking amino acids with tRNA-contained nucleotide triplets. The SARS enzyme catalyzes the attachment of serine to tRNA (Ser). SARS enzyme is probably able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be then converted into selenocysteinyl-tRNA (Sec).

    • Synonyms

      Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    • 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 MGSMVLDLDL FRVDKGGDPA LIRETQEKRF KDPGLVDQLV KADSEWRRCR FRADNLNKLK NLCSKTIGEK MKKKEPVGDD ESVPENVLSF DDLTADALAN LKVSQIKKVR LLIDEAILKC DAERIKLEAE RFENLREIGN LLHPSVPISN DEDVDNKVER IWGDCTVRKK YSHVDLVVMV DGFEGEKGAV VAGSRGYFLK GVLVFLEQAL IQYALRTLGS RGYIPIYTPF FMRKEVMQEV AQLSQFDEEL YKVIGKGSEK SDDNSYDEKY LIATSEQPIA ALHRDEWLRP EDLPIKYAGL STCFRQEVGS HGRDTRGIFR VHQFEKIEQF VYSSPHDNKS WEMFEEMITT AEEFYQSLGI PYHIVNIVSG SLNHAASKKL DLEAWFPGSG AFRELVSCSN CTDYQARRLR IRYGQTKKMM DKVEFVHMLN ATMCATTRTI CAILENYQTE KGITVPEKLK EFMPPGLQEL IPFVKPAPIE QEPSKKQKKQ HEGSKKKAAA RDVTLENRLQ NMEVTDA.

    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.

    Sars Human
  • View Data Sheet

    Name :

    HCV NS3, HRP

    Description:

    Hepatitis C Virus NS3, Horseradish Peroxidase Recombinant

    Product # :

    HCV-256

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    Description

    The E.coli derived recombinant HRP Labeled protein contains the HCV NS3 immunodominant regions.

    Formulation

    25mM Tris-HCl pH 8, 1mM EDTA, 1.5M urea and 50% glycerol.

    Purity

    HCV NS3, HRP protein is >95% pure as determined by 10% PAGE (coomassie staining).

    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).

    • Stability

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

    • Applications

      HCV NS3, HRP 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, HRP 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 Hrp
  • View Data Sheet

    Name :

    UBE2E3 Human

    Description:

    Ubiquitin Conjugating Enzyme E2E3 Human Recombinant

    UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.

    Product # :

    ENZ-906

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    Description

    UBE2E3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-207 a.a) and having a molecular mass of 25.3kDa.UBE2E3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2E3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2E3 or Ubiquitin-conjugating enzyme E2 E3 is part of the E2 ubiquitinconjugating enzyme family. UBE2E3 is needed for the destruction of mitotic cyclins and for cell cycle progression. The ubiquitination process covalently attaches to a short protein of 76 amino acids called ubiquitin, to a lysine residue on the target protein. When a protein has been tagged with one ubiquitin molecule, other rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein which grants passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.

    • Synonyms

      UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.

    • 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 MGSMSSDRQR SDDESPSTSS GSSDADQRDP AAPEPEEQEE RKPSATQQKK NTKLSSKTTA KLSTSAKRIQ KELAEITLDP PPNCSAGPKG DNIYEWRSTI LGPPGSVYEG GVFFLDITFS SDYPFKPPKV TFRTRIYHCN INSQGVICLD ILKDNWSPAL TISKVLLSIC SLLTDCNPAD PLVGSIATQY LTNRAEHDRI ARQWTKRYAT.

    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.

    Ube2E3 Human
  • View Data Sheet

    Name :

    OAS1 Human

    Description:

    2’-5’ Oligoadenylate Synthetase 1 Human Recombinant

    2'-5'-oligoadenylate synthetase 1, (2-5')oligo(A) synthetase 1, 2-5A synthetase 1, p46/p42 OAS, E18/E16, OAS1, OIAS, IFI-4, OIASI.

    Product # :

    ENZ-445

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    Description

    OAS1 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 384 amino acids (1-364 a.a.) and having a molecular mass of 43.9kDa.The OAS1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OAS1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      OAS1 enzyme is a member of the 2’,5’-oligoadenylate synthetase family. OAS1 is induced by interferons and uses adenosine triphosphate in 2’-specific nucleotidyl transfer reactions to synthesize 2’,5’-oligoadenylates(2-5As). These molecules in turn activate latent RNase L resulting in viral RNA degradation and the inhibition of viral replication.
      OAS1 may have a role in mediating resistance to virus infection, control of cell growth, differentiation, and apoptosis. OAS1 binds double-stranded RNA and polymerizes ATP into PPP (A2'P5'A)N oligomers, which activate the latent RNase L that, once activated, cleaves single-stranded RNAs.
      OAS1 gene mutations are been linked to host susceptibility to viral infection.
      OSA1 gene polymorphisms are linked to the outcome of hepatitis C virus infection. Furthermore, OAS1 gene polymorphisms are linked to the susceptibility to severe acute respiratory syndrome.

    • Synonyms

      2'-5'-oligoadenylate synthetase 1, (2-5')oligo(A) synthetase 1, 2-5A synthetase 1, p46/p42 OAS, E18/E16, OAS1, OIAS, IFI-4, OIASI.

    • 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 MMDLRNTPAK SLDKFIEDYL LPDTCFRMQI NHAIDIICGF LKERCFRGSS YPVCVSKVVK GGSSGKGTTL RGRSDADLVV FLSPLTTFQD QLNRRGEFIQ EIRRQLEACQ RERAFSVKFE VQAPRWGNPR ALSFVLSSLQ LGEGVEFDVL PAFDALGQLT GSYKPNPQIY VKLIEECTDL QKEGEFSTCF TELQRDFLKQ RPTKLKSLIR LVKHWYQNCK KKLGKLPPQY ALELLTVYAW ERGSMKTHFN TAQGFRTVLE LVINYQQLCI YWTKYYDFKN PIIEKYLRRQ LTKPRPVILD PADPTGNLGG GDPKGWRQLA QEAEAWLNYP CFKNWDGSPV SSWILLVRPP ASSLPFIPAP LHEA.

    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.

    Oas1 Human
  • View Data Sheet

    Name :

    CHST3 Human

    Description:

    Carbohydrate Sulfotransferase 3 Human Recombinant

    Carbohydrate sulfotransferase 3, Chondroitin 6-O-sulfotransferase 1, C6ST-1, Chondroitin 6-sulfotransferase, GST-0, CHST3, CHST-3,C6ST1HSD.

    Product # :

    ENZ-1166

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    Description

    CHST3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 450 amino acids (39-479.a.a) and having a molecular mass of 51.3kDa. CHST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CHST3 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is greater than 1,000 pmol/min/ug, and is defined as the amount of enzyme that sulfate from PAPS to Chondroitin Sulfate per minute at pH 7.5, at 25C.

    More Info

    • Introduction

      Carbohydrate Sulfotransferase 3 (CHST3) belong to sulfotransferase 1 family which iincludes 14 enzymes that all members are Golgi-localized type II membrane proteins. These enzymes utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. CHST3 can also sulfate Gal residues of keratan sulfate and Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. CHST3 is expressed in heart, placenta, skeletal muscle and pancreas. CHST3 takes part in maintenance of naive T-lymphocytes in the spleen.

    • Synonyms

      Carbohydrate sulfotransferase 3, Chondroitin 6-O-sulfotransferase 1, C6ST-1, Chondroitin 6-sulfotransferase, GST-0, CHST3, CHST-3,C6ST1HSD.

    • 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

      ADLEKENKII SRVSDKLKQI PQALADANST DPALILAENA SLLSLSELDS AFSQLQSRLR NLSLQLGVEP AMEAAGEEEE EQRKEEEPPR PAVAGPRRHV LLMATTRTGS SFVGEFFNQQ GNIFYLFEPL WHIERTVSFE PGGANAAGSA LVYRDVLKQL FLCDLYVLEH FITPLPEDHL TQFMFRRGSS RSLCEDPVCT PFVKKVFEKY HCKNRRCGPL NVTLAAEACR RKEHMALKAV RIRQLEFLQP LAEDPRLDLR VIQLVRDPRA VLASRMVAFA GKYKTWKKWL DDEGQDGLRE EEVQRLRGNC ESIRLSAELG LRQPAWLRGR YMLVRYEDVA RGPLQKAREM YRFAGIPLTP QVEDWIQKNT QAAHDGSGIY STQKNSSEQF EKWRFSMPFK LAQVVQAACG PAMRLFGYKL ARDAAALTNR SVSLLEERGT FWVTHHHHHH.

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    Chst3 Human
  • View Data Sheet

    Name :

    GPC4 511 aa Human

    Description:

    Glypican-4 511 aa Human Recombinant

    Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.

    Product # :

    PRO-2034

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    Description

    Glypican-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala19-Ser529) containing 521 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 58.7kDa.

    Source

    Escherichia Coli.

    Formulation

    Glypican-4 filtered (0.4µm) solution at a concentration of 0.2mg/ml in 20mM Tris buffer, 50mM NaCl, pH 8.0 and 5mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.

    • Synonyms

      Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.

    • Physical Appearance

      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

      MKHHHHHHASALLAAELKSK SCSEVRRLYV SKGFNKNDAP LHEINGDHLK ICPQGSTCCS QEMEEKYSLQ SKDDFKSVVS EQCNHLQAVF ASRYKKFDEF FKELLENAEK SLNDMFVKTY GHLYMQNSEL FKDLFVELKR YYVVGNVNLE EMLNDFWARL LERMFRLVNS QYHFTDEYLE CVSKYTEQLK PFGDVPRKLK LQVTRAFVAA RTFAQGLAVA GDVVSKVSVV NPTAQCTHAL LKMIYCSHCR GLVTVKPCYN YCSNIMRGCL ANQGDLDFEW NNFIDAMLMV AERLEGPFNI ESVMDPIDVK ISDAIMNMQD NSVQVSQKVF QGCGPPKPLP AGRISRSISE SAFSARFRPH HPEERPTTAA GTSLDRLVTD VKEKLKQAKK FWSSLPSNVC NDERMAAGNG NEDDCWNGKG KSRYLFAVTG NGLANQGNNP EVQVDTSKPD ILILRQIMAL RVMTSKMKNA YNGNDVDFFD ISDESSGEGS GSGCEYQQCP SEFDYNATDH AGKSANEKAD S.

    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.

    Gpc4 511 Aa Human
  • View Data Sheet

    Name :

    TH Mouse

    Description:

    Tyrosine Hydroxylase Mouse Recombinant

    Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.

    Product # :

    ENZ-988

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    Description

    TH Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 507 amino acids (1-498a.a.) and having a molecular mass of 57.0kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). TH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosine 3-monooxygenase (Th), is a rate-limiting enzyme in catecholamine synthesis. Th utilizes tetrahydrobiopterin as well as molecular oxygen to convert tyrosine to DOPA. Th regulates dopamine (DA) neurotransmission at the biosynthesis and reuptake steps. Th takes a vital part in the physiology of adrenergic neurons. Furthermore, Th effects overexpression in lymphocytes on the differentiation as well as function of T helper cells.

    • Synonyms

      Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.

    • 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

      ADPMPTPSAS SPQPKGFRRA VSEQDTKQAE AVTSPRFIGR RQSLIEDARK EREAAAAAAA AAVASAEPGN PLEAVVFEER DGNAVLNLLF SLRGTKPSSL SRALKVFETF EAKIHHLETR PAQRPLAGSP HLEYFVRFEV PSGDLAALLS SVRRVSDDVR SAREDKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD QAYRQRRKLI AEIAFQYKQG EPIPHVEYTK EEIATWKEVY ATLKGLYATH ACREHLEAFQ LLERYCGYRE DSIPQLEDVS HFLKERTGFQ LRPVAGLLSA RDFLASLAFR VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADRTFAQ FSQDIGLASL GASDEEIEKL STVYWFTVEF GLCKQNGELK AYGAGLLSSY GELLHSLSEE PEVRAFDPDT AAVQPYQDQT YQPVYFVSES FSDAKDKLRN YASRIQRPFS VKFDPYTLAI DVLDSPHTIR RSLEGVQDEL HTLTQALSAI SHHHHHH.

    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.

    Th Mouse
  • View Data Sheet

    Name :

    IFIH1 Human

    Description:

    Interferon Induced With Helicase C Domain 1 Human Recombinant

    Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

    Product # :

    PRO-1505

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    Description

    IFIH1 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 152,000 Dalton. IFIH1 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    IFIH1 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.

    • Synonyms

      Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

    • 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.

    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.

    Ifih1 Human
  • View Data Sheet

    Name :

    GAD2 Human

    Description:

    Glutamate Decarboxylase 2 Human Recombinant

    Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kDa), Glutamate Decarboxylase 65 KDa Isoform, 65 KDa Glutamic Acid Decarboxylase, EC 4.1.1.15, GAD-65, GAD65, Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kD), Glutamate Decarboxylase-2 (Pancreas), EC 4.1.1, GAD2.

    Product # :

    ENZ-937

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    Description

    Recombinant Human GAD2 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 61 kDa. GAD2 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    GAD2 protein solution is supplied in 20mM Sodium phosphate pH-7.4, 150mM NaCl, 0.016mM Pyridoxal-5’-Phosphate, 0.05% Tergitol 15-S-9 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamate Decarboxylase 2 (GAD2) is one of several forms of glutamic acid decarboxylase, identified as a main autoantigen in type II diabetes. The GAD2 enzyme is responsible for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. A pathogenic role for the GAD2 enzyme has been characterized in the human pancreas since it has been identified as an autoantibody and an autoreactive T cell target in type II diabetes. GAD2 gene may also have a role in the stiff man syndrome. In addition, GAD2 catalyzes the production of GABA.

    • Synonyms

      Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kDa), Glutamate Decarboxylase 65 KDa Isoform, 65 KDa Glutamic Acid Decarboxylase, EC 4.1.1.15, GAD-65, GAD65, Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kD), Glutamate Decarboxylase-2 (Pancreas), EC 4.1.1, GAD2.

    • 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.

    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.

    Gad2 Human
  • View Data Sheet

    Name :

    Collagen-I Goat

    Description:

    Goat Collagen-I

    Product # :

    PRO-2682

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    Description

    Goat Collagen-I is a natural protein purified from Goat tissues. Collagen-I is purified by proprietary chromatographic techniques.

    Source

    Goat tissues.

    Formulation

    Collagen-I was lyophilized without additives.

    Purity

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

    More Info

    • Introduction

      Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to Add 0.5 M acetic acid, pH 2.5 to prepare a working stock solution not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Collagen I Goat
  • View Data Sheet

    Name :

    PI16 Human

    Description:

    Peptidase Inhibitor 16 Human Recombinant

    Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

    Product # :

    ENZ-113

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    Description

    The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.

    • Synonyms

      Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized PI16 Human recombinant at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution 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

      LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.

    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.

    Pi16 Human
  • View Data Sheet

    Name :

    RNASE7 Human

    Description:

    Ribonuclease 7 Human Recombinant

    Ribonuclease, RNase A Family, 7, Skin-Derived Antimicrobial Protein 2, RNase 7, SAP-2, EC 3.1.27.5, EC 3.1.27., EC 3.1.27, Ribonuclease 7.

    Product # :

    ENZ-704

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    Description

    RNASE7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (29-156 a.a) and having a molecular mass of 16.9kDa. RNASE7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNASE7 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribonuclease 7 (RNASE7) is one of the final RNase A superfamily ribonucleases. RNASE7 was isolated from skin-derived stratum corneum. RNASE7 protein demonstrated potent ribonuclease activity and hence may contribute to the well-known ribonuclease activity of human skin. RNASE7 has revealed a broad spectrum antimicrobial activity against many pathogenic microorganisms and extraordinarily potent activity.

    • Synonyms

      Ribonuclease, RNase A Family, 7, Skin-Derived Antimicrobial Protein 2, RNase 7, SAP-2, EC 3.1.27.5, EC 3.1.27., EC 3.1.27, Ribonuclease 7.

    • 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 MGSKPKGMTS SQWFKIQHMQ PSPQACNSAM KNINKHTKRC KDLNTFLHEP FSSVAATCQT PKIACKNGDK NCHQSHGPVS LTMCKLTSGK YPNCRYKEKR QNKSYVVACK PPQKKDSQQF HLVPVHLDRV L.

    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.

    Rnase7 Human
  • View Data Sheet

    Name :

    CTSZ Mouse

    Description:

    Cathepsin-Z Mouse Recombinant

    Cathepsin Z, CTSZ.

    Product # :

    ENZ-934

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    Description

    CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (23-306a.a.) and having a molecular mass of 32.8kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, CTSZ.

    • 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

      ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH HH.

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

    Ctsz Mouse
  • View Data Sheet

    Name :

    MGMT Human

    Description:

    O-6-Methylguanine-DNA Methyltransferase Human Recombinant

    Methylated-DNA--protein-cysteine methyltransferase, 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase, MGMT.

    Product # :

    ENZ-389

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    Description

    MGMT Human Recombinant fused to a 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 227 amino acids (1-207) and having a molecular mass of 23.8 kDa. The MGMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MGMT solution contains 20mM Tris-HCl pH-7.5, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MGMT is an enzyme that repairs O-6-methylguanine, a mutagenic DNA base damaged by endogenous and environmental alkylating agents and takes part in the cellular defense against the biological effects of O-6-methylguanine in DNA. MGMT repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. abnormal MGMT expression correlates with the prognosis in human solid cancers. MGMT decrease of expression is correlated with methylation. The human MGMT is a negative regulator of estrogen receptor-mediated transcription upon alkylation DNA damage. MGMT promoter hypermethylation plays an important role in the early steps of colorectal carcinogenesis. Abnormal promoter hypermethylation of MGMT gene is associated with oral squamous cell carcinomas.

    • Synonyms

      Methylated-DNA--protein-cysteine methyltransferase, 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase, MGMT.

    • Physical Appearance

      Sterile Filtered clear 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 MDKDCEMKRT TLDSPLGKLE LSGCEQGLHE IKLLGKGTSA ADAVEVPAPA AVLGGPEPLM QCTAWLNAYF HQPEAIEEFP VPAFHHPVFQ QESFTRQVLW KLLKVVKFGE VISYQQLAAL AGNPKAARAV GGAMRGNPVP ILIPCHRVVC SSGAVGNYSG GLAVKEWLLA HEGHRLGKPG LGGSSGLAGA WLKGAGATSG SPPAGRN.

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

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  • View Data Sheet

    Name :

    MMP14 Human

    Description:

    Matrix Metalloproteinase-14 Recombinant Human

    Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 1.

    Product # :

    ENZ-1101

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    Description

    Matrix Metalloproteinase-14 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 264 amino acids and having a molecular mass of 29.6kDa. MMP14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MMP14 is supplied as a 0.2 μm filtered solution conteining 20mM Tris-HCl, pH 7.4, 30 % glycerol, 300mM NaCl, 3mM CaCl2 and 10μM ZnCl2.

    Purity

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

    More Info

    • Introduction

      Matrix metalloproteinase-14 (MMP14), is a membrane-anchored zinc-binding endopeptidase which is expressed at the leading edge of different invasive carcinomas and also promotes tumor cell invasion through degradation of the extracellular matrix. MMP14 takes a vital part in extracellular matrix, ECM, remodeling by having the capability to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules for instance CD44 and integrin alpha V. MMP14 is a key enzyme in many physiological as well as pathological processes for example angiogenesis & tumor invasion.

    • Synonyms

      Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 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

      ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYG.

    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.

    Mmp14 Protein
  • View Data Sheet

    Name :

    ADA Human

    Description:

    Adenosine Deaminase Human Recombinant

    Adenosine deaminase, Adenosine aminohydrolase, ADA1, EC 3.5.4.4.

    Product # :

    ENZ-147

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    • More Info

    Description

    ADA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 383 amino acids (1-363) and having a molecular mass of 42.9 kDa.The ADA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ADA protein 0.5mg/ml is supplied in 20mM Tris-HCL, pH-8, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately >25 units/mg. Enzymatic activity was confirmed by measuring the amount of enzyme that deaminates 1.0 umol of adenosine to inosine per minute at pH 7.5 at 25C.

    More Info

    • Introduction

      ADA catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. ADA has a vital part in purine metabolism and in adenosine homeostasis. ADA performs as a positive regulator of T-cell coactivation, by binding DPP4 which regulates lymphocyte-epithelial cell adhesion.

    • Synonyms

      Adenosine deaminase, Adenosine aminohydrolase, ADA1, EC 3.5.4.4.

    • Physical Appearance

      ADA is supplied as a 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 MAQTPAFDKP KVELHVHLDG SIKPETILYY GRRRGIALPA NTAEGLLNVI GMDKPLTLPD FLAKFDYYMP AIAGCREAIK RIAYEFVEMK AKEGVVYVEV RYSPHLLANS KVEPIPWNQA EGDLTPDEVV ALVGQGLQEG ERDFGVKARS ILCCMRHQPN WSPKVVELCK KYQQQTVVAI DLAGDETIPG SSLLPGHVQA YQEAVKSGIH RTVHAGEVGS AEVVKEAVDI LKTERLGHGY HTLEDQALYN RLRQENMHFE ICPWSSYLTG AWKPDTEHAV IRLKNDQANY SLNTDDPLIF KSTLDTDYQM TKRDMGFTEE EFKRLNINAA KSSFLPEDEK RELLDLLYKA YGMPPSASAG QNL

    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.

    Ada Human
  • View Data Sheet

    Name :

    RNASEH2A E.Coli

    Description:

    Ribonuclease H2A E.Coli Recombinant

    AGS4, JUNB, RNASEHI, RNHIA, RNHL , Ribonuclease H2 subunit A, Aicardi-Goutieres syndrome 4 protein, RNase H(35), Ribonuclease HI large subunit, RNase HI large subunit, EC=3.1.26.4.

    Product # :

    ENZ-713

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    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    RNASEH2A Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.8kDa.RNASEH2A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RNASEH2A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribonuclease H2 subunit A (RNASEH2A) is a member of the RNase HII family and eukaryotic subfamily. RNASEH2A Plays a part in DNA replication, probably by mediating the removal of lagging-strand Okazaki fragment RNA primers throughout DNA replication. RNASEH2A catalyzes the endonucleolytic cleavage of RNA to a 5’-phosphomonoester and is capable to bind magnesium or manganese as cofactors. Aicardi-Goutieres syndrome type 4 (AGS4) caused by defects in RNASEH2A.

    • Synonyms

      AGS4, JUNB, RNASEHI, RNHIA, RNHL , Ribonuclease H2 subunit A, Aicardi-Goutieres syndrome 4 protein, RNase H(35), Ribonuclease HI large subunit, RNase HI large subunit, EC=3.1.26.4.

    • 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 MGSMDLSELE RDNTGRCRLS SPVPAVCRKE PCVLGVDEAG RGPVLGPMVY AICYCPLPRL ADLEALKVAD SKTLLESERE RLFAKMEDTD FVGWALDVLS PNLISTSMLG RVKYNLNSLS HDTATGLIQY ALDQGVNVTQ VFVDTVGMPE TYQARLQQSF PGIEVTVKAK ADALYPVVSA ASICAKVARD QAVKKWQFVE KLQDLDTDYG SGYPNDPKTK AWLKEHVEPV FGFPQFVRFS WRTAQTILEK EAEDVIWEDS ASENQEGLRK ITSYFLNEGS QARPRSSHRY FLERGLESAT SL.

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

    Rnaseh2A Human
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