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Search results

1000 results found for “Hepatitis A”

Name

Description

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  • View Data Sheet

    Name :

    GGCT Human

    Description:

    Gamma-Glutamylcyclotransferase Human Recombinant

    Gamma-Glutamylcyclotransferase, CRF21, C7orf24, MGC3077, Cytochrome c-releasing factor 21, GCTG, Ggc, Chromosome 7 open reading frame 24, FLJ11717, EC 2.3.2.4.

    Product # :

    ENZ-062

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    Description

    GGCT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-188a.a.) and having a molecular mass of 23.2kDa.GGCT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GGCT protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GGCT is a member of the family of transferases, specifically the aminoacyltransferases. GGCT protein catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and takes an important part in glutathione homeostasis. GGCT induces release of cytochrome c from mitochondria with resultant induction of apoptosis.

    • Synonyms

      Gamma-Glutamylcyclotransferase, CRF21, C7orf24, MGC3077, Cytochrome c-releasing factor 21, GCTG, Ggc, Chromosome 7 open reading frame 24, FLJ11717, EC 2.3.2.4.

    • 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

      MGSSHHHHHH SSGLVPRGSHMANSGCKDVT GPDEESFLYF AYGSNLLTER IHLRNPSAAF FCVARLQDFK LDFGNSQGKT SQTWHGGIAT IFQSPGDEVW GVVWKMNKSN LNSLDEQEGV KSGMYVVIEV KVATQEGKEI TCRSYLMTNY ESAPPSPQYK KIICMGAKEN GLPLEYQEKL KAIEPNDYTG KVSEEIEDII KKGETQTL

    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.

    Ggct Human
  • View Data Sheet

    Name :

    TYMS Human

    Description:

    Thymidylate Synthetase Human Recombinant

    TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.

    Product # :

    ENZ-470

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    Description

    Thymidylate synthase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 333 amino acids (1-313 a.a.) and having a molecular mass of 37.8 kDa. The Thymidylate synthase fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymidylate synthase catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5,10-methylenetetrahydrofolate as a cofactor which maintains the dTMP (thymidine-5-prime monophosphate) pool vital for DNA replication and repair. Thymidylate synthase plays an important role as a cancer chemotherapeutic agent. Thymidylate synthase is the primary site of action for 5-fluoro-2-prime-deoxyuridine and several folate analogs.

    • Synonyms

      TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.

    • 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 MPVAGSELPR RPLPPAAQER DAEPRPPHGE LQYLGQIQHI LRCGVRKDDR TGTGTLSVFG MQARYSLRDE FPLLTTKRVF WKGVLEELLW FIKGSTNAKE LSSKGVKIWD ANGSRDFLDS LGFSTREEGD LGPVYGFQWR HFGAEYRDME SDYSGQGVDQ LQRVIDTIKT NPDDRRIIMC AWNPRDLPLM ALPPCHALCQ FYVVNSELSC QLYQRSGDMG LGVPFNIASY ALLTYMIAHI TGLKPGDFIH TLGDAHIYLN HIEPLKIQLQ REPRPFPKLR ILRKVEKIDD FKAEDFQIEG YNPHPTIKME MAV.

    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.

    Tyms Human
  • View Data Sheet

    Name :

    CLTA Human

    Description:

    Clathrin, Light Chain A Human Recombinant

    Clathrin light chain A, Lca, CLTA.

    Product # :

    PRO-1144

    Price :

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    Description

    CLTA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-218 a.a) and having a molecular mass of 26.2kDa (Molecular weight on SDS-PAGE will appear higher).CLTA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLTA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Clathrin, light chain A (CLTA) is a member of the clathrin family. Clathrin, which is a large, soluble protein, is comprised of heavy and light chains. CLTA is one of 2 clathrin light chain proteins which are supposed to function as regulatory elements. CLTA is a key cytosolic coat protein in pits and vesicles originating from the plasma membrane and the trans-Golgi network. In receptor-mediated endocytosis, receptor proteins are encapsulated by Clathrin-coated vesicles.

    • Synonyms

      Clathrin light chain A, Lca, CLTA.

    • 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 MGSHMAELDP FGAPAGAPGG PALGNGVAGA GEEDPAAAFL AQQESEIAGI ENDEAFAILD GGAPGPQPHG EPPGGPDAVD GVMNGEYYQE SNGPTDSYAA ISQVDRLQSE PESIRKWREE QMERLEALDA NSRKQEAEWK EKAIKELEEW YARQDEQLQK
      TKANNRAAEE AFVNDIDESS PGTEWERVAR LCDFNPKSSK QAKDVSRMRS VLISLKQAPL VH.

    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.

    Clta Human
  • View Data Sheet

    Name :

    GSTA4 Human

    Description:

    Glutathione S-Transferase Alpha 4 Human Recombinant

    Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.

    Product # :

    ENZ-600

    Price :

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    Description

    GSTA4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-222) and having a molecular mass of 28.3kDa.GSTA4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTA4 solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 20% glycerol, 2mM DTT and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutathione S-transferase A4 (GSTA4) is a member of the GST superfamily. The GSTA4 enzyme is involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. GSTA4 shows an especially high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is extremely effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, which is an important product of peroxidative degradation of arachidonic acid and a frequently used biomarker for oxidative damage in tissue. The GSTA4 enzyme is expressed at a high level in the brain, placenta, and skeletal muscle and much lower in the lung and liver.

    • Synonyms

      Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.

    • 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 MGSHMAARPK LHYPNGRGRM ESVRWVLAAA GVEFDEEFLE TKEQLYKLQD GNHLLFQQVP MVEIDGMKLV QTRSILHYIA DKHNLFGKNL KERTLIDMYV EGTLDLLELL IMHPFLKPDD QQKEVVNMAQ KAIIRYFPVF EKILRGHGQS FLVGNQLSLA
      DVILLQTILA LEEKIPNILS AFPFLQEYTV KLSNIPTIKR FLEPGSKKKP PPDEIYVRTV YNIFRP.

    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.

    Gsta4 Human
  • View Data Sheet

    Name :

    GSTM5 Human

    Description:

    Glutathione S-Transferase MU 5 Human Recombinant

    Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.

    Product # :

    ENZ-623

    Price :

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    Description

    GSTM5 Human Recombinant produced in E. coli is a single polypeptide chain containing 242 amino acids (1-218) and having a molecular mass of 28.2 kDa.GSTM5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GSTM5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutathione S-transferase mu 5 (GSTM5) belongs to the glutathione s-transferase (GST) family of proteins. There are 8 families of GST proteins, specifically alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is comprised of proteins which have various functions throughout the cell. GSTM5 belongs to the mu class of enzymes which function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. GSTM5 has an imperative role in detoxification. GSTM5 conjugates reduced glutathione to a large number of exogenous and endogenous hydrophobic electrophiles.

    • Synonyms

      Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.

    • 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 MGSHMPMTLG YWDIRGLAHA IRLLLEYTDS SYVEKKYTLG DAPDYDRSQW LNEKFKLGLD FPNLPYLIDG AHKITQSNAI LRYIARKHNL CGETEEEKIR VDILENQVMD NHMELVRLCY DPDFEKLKPK YLEELPEKLK LYSEFLGKRP WFAGDKITFV DFLAYDVLDM KRIFEPKCLD AFLNLKDFIS RFEGLKKISA YMKSSQFLRG LLFGKSATWN SK

    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.

    Gstm5 Human
  • View Data Sheet

    Name :

    GSTT2 Human

    Description:

    Glutathione S-Transferase Theta-2 Human Recombinant

    Glutathione S-transferase theta 2, GST class-theta-2, GSTT2B, Glutathione S-transferase theta-2B, EC 2.5.1.18.

    Product # :

    ENZ-593

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    Description

    GSTT2 Recombinant produced in E. coli is a single polypeptide chain containing 264 amino acids (1-244) and having a molecular mass of 29.6kDa.GSTT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GSTT2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl,
    1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GSTT2 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The theta type members GSTT1 and GSTT2 have a 55% aa sequence homology and hold a vital role in human carcinogenesis. The theta genes are structurally similar – each has five exons with identical exon/intron boundaries.

    • Synonyms

      Glutathione S-transferase theta 2, GST class-theta-2, GSTT2B, Glutathione S-transferase theta-2B, EC 2.5.1.18.

    • 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 MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS LGKLPTLKDG DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG WHADCIRGTF GIPLWVQVLG PLIGVQVPEE KVERNRTAMD QALQWLEDKF LGDRPFLAGQ QVTLADLMAL EELMQPVALG YELFEGRPRL AAWRGRVEAF LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI ARIP

    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.

    Gstt2 Human
  • View Data Sheet

    Name :

    HBQ1 Human

    Description:

    Hemoglobin Theta 1 Human Recombinant

    Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.

    Product # :

    PRO-1616

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    Description

    HBQ1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-142) and having a molecular mass of 17.9kDa.HBQ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HBQ1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      HBQ1 is a member of the Hemoglobin family. Hemoglobin is a 66.7 kDa protein attached to four iron-binding, methenelinked tetrapyrrole rings (heme). The globin part of Hemoglobin contains 2 alpha chains and 2 beta chains organized as couples creating a tetramer. Every one of the 4 globin chains covalently connects with a heme group. The bonds between alpha and beta chains are frailer than between parallel globin chains, thus creating a cleavage plane which is vital for oxygen binding and release. Relaxation of the alpha1-beta2 cleavage plane results in high affinity for oxygen.

    • Synonyms

      Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.

    • 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 MGSMALSAED RALVRALWKK LGSNVGVYTT EALERTFLAF PATKTYFSHL DLSPGSSQVR AHGQKVADAL SLAVERLDDL PHALSALSHL HACQLRVDPA SFQLLGHCLL VTLARHYPGD FSPALQASLD KFLSHVISAL VSEYR

    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.

    Hbq1 Human
  • View Data Sheet

    Name :

    MDH1 Human

    Description:

    Malate Dehydrogenase 1 Human Recombinant

    MDH-s, MDHA, MOR2.

    Product # :

    ENZ-256

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    Description

    MDH1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-334 a.a.) and having a molecular mass of 37.4 kDa. The MDH1 is fused to an 8 amino acid His tag at C-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The MDH1 1mg/ml protein solution contains 20mM Tris-HCl pH-8, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 250 units/mg, and is defined as the amount of enzyme that cleaves 1umole of oxalacetate and beta-NADH to L-malate and beta-NAD per minute at pH8.0 at 25°C.

    More Info

    • Introduction

      MDH1 catalyzes the reversible oxidation of malate to oxaloacetate, using the NAD/NADH cofactor system in the citric acid cycle. MDH1 is abundantly found in the cytoplasm and is involved in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH1 regulates p53-dependent cell-cycle arrest and apoptosis in response to glucose deprivation.

    • Synonyms

      MDH-s, MDHA, MOR2.

    • 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

      MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC ALPLLKDVIA TDKEDVAFKD LDVAILVGSM PRREGMERKD LLKANVKIFK SQGAALDKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKAQIALK LGVTANDVKN VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFVTTVQQR GAAVIKARKL SSAMSAAKAI CDHVRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV EGLPINDFSR EKMDLTAKEL TEEKESAFEF LSSALEHHHH HH.

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    Mdh1 Human
  • View Data Sheet

    Name :

    RASSF1A Human

    Description:

    Ras association domain-containing protein 1 Human Recombinant

    123F2, NORE2A, RASSF1, RDA32, REH3P21, Ras association domain-containing protein 1.

    Product # :

    PRO-1288

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    Description

    RASSF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (1-340 a.a.) and having a molecular mass of 42.9kDa. RASSF1A is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RASSF1A protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RASSF1A protein is a potential tumor suppressor like the RAS effector proteins. Presence or absence expression of this gene has been related with the pathogenesis of a variety of cancers, which suggests the tumor suppressor function of this RASSF1A gene. The inactivation of RASSF1A was found to be associated with the hypermethylation of its CpG-island promoter region. RASSF1A required for death receptor-dependent apoptosis.

    • Synonyms

      123F2, NORE2A, RASSF1, RDA32, REH3P21, Ras association domain-containing protein 1.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMSGE PELIELRELA PAGRAGKGRT RLERANALRI ARGTACNPTR QLVPGRGHRF QPAGPATHTW CDLCGDFIWG VVRKGLQCAH CKFTCHYRCR ALVCLDCCGP RDLGWEPAVE RDTNVDEPVE WETPDLSQAE IEQKIKEYNA QINSNLFMSL NKDGSYTGFI KVQLKLVRPV SVPSSKKPPS LQDARRGPGR GTSVRRRTSF YLPKDAVKHL HVLSRTRARE VIEALLRKFL VVDDPRKFAL FERAERHGQV YLRKLLDDEQ PLRLRLLAGP SDKALSFVLK ENDSGEVNWD AFSMPELHNF LRILQREEEE HLRQILQKYS YCRQKIQEAL HACPLG.

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    Rassf1A Human
  • View Data Sheet

    Name :

    Borrelia Garinii DbpA

    Description:

    Borrelia Garinii Decorin Binding Protein A Recombinant

    Product # :

    BOR-025

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    Description

    Recombinant Borrelia Garinii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19kDa. Borrelia Garinii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Garinii DbpA 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 is a part of the 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. Borreliella garinii DbpA demonstrates the typical lipid anchor and decorin/glycoaminoglycon binding properties of a DbpA protein.

    • 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.

    • 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 Garinii Dbpa
  • View Data Sheet

    Name :

    Borrelia p45

    Description:

    Borrelia Burgdorferi p45 Recombinant

    Product # :

    BOR-018

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    Description

    Recombinant Borrelia Burgdorferi p45 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 45,259.3 Dalton. Borrelia p45 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Borrelia p45 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.Immunodot test with Lyme disease positive/negative plasma, suitable for LTT (lymphocyte transformation test). 2.T cell stimulation assays. 3.ELISPOT (enzyme-linked immunospot).

    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 P45
  • View Data Sheet

    Name :

    DIMT1 Human

    Description:

    DIM1 Dimethyladenosine Transferase 1 Human Recombinant

    Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.

    Product # :

    ENZ-628

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    Description

    DIMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-313) and having a molecular mass of 37.5kDa.DIMT1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DIMT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 30% glycerol, 2mM DTT, 200mM NaCl and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.

    • Synonyms

      Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.

    • 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 MMPKVKSGAI GRRRGRQEQR RELKSAGGLM FNTGIGQHIL KNPLIINSII DKAALRPTDV VLEVGPGTGN MTVKLLEKAK KVVACELDPR LVAELHKRVQ GTPVASKLQV LVGDVLKTDL PFFDTCVANL PYQISSPFVF KLLLHRPFFR CAILMFQREF ALRLVAKPGD KLYCRLSINT QLLARVDHLM KVGKNNFRPP PKVESSVVRI EPKNPPPPIN FQEWDGLVRI TFVRKNKTLS AAFKSSAVQQ LLEKNYRIHC SVHNIIIPED FSIADKIQQI LTSTGFSDKR ARSMDIDDFI RLLHGFNAEG IHFS.

    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.

    Dimt1 Human
  • View Data Sheet

    Name :

    MGAT2 Human, Sf9

    Description:

    Mannoside Acetylglucosaminyltransferase 2 Human Recombinant, Sf9

    Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II.

    Product # :

    ENZ-1077

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    Description

    MGAT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 427 amino acids (30-447a.a.) and having a molecular mass of 49.3kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MGAT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MGAT2 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 7.5), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.

    • Synonyms

      Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II.

    • 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

      ADPRQRKNEA LAPPLLDAEP ARGAGGRGGD HPSVAVGIRR VSNVSAASLV PAVPQPEADN LTLRYRSLVY QLNFDQTLRN VDKAGTWAPR ELVLVVQVHN RPEYLRLLLD SLRKAQGIDN VLVIFSHDFW STEINQLIAG VNFCPVLQVF FPFSIQLYPN EFPGSDPRDC PRDLPKNAAL
      KLGCINAEYP DSFGHYREAK FSQTKHHWWW KLHFVWERVK ILRDYAGLIL FLEEDHYLAP DFYHVFKKMW KLKQQECPEC DVLSLGTYSA SRSFYGMADK VDVKTWKSTE HNMGLALTRN AYQKLIECTD TFCTYDDYNW DWTLQYLTVS CLPKFWKVLV PQIPRIFHAG DCGMHHKKTC
      RPSTQSAQIE SLLNNNKQYM FPETLTISEK FTVVAISPPR KNGGWGDIRD HELCKSYRRL QHHHHHH.

    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.

    Mgat2 Protein
  • View Data Sheet

    Name :

    ADAM10 Human, Sf9

    Description:

    A Disintegrin and Metalloproteinase Domain 10 Human Recombinant, Sf9

    Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.

    Product # :

    PRO-2359

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    Description

    ADAM10 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 467 amino acids (214-672 aa) and having a molecular mass of 51.6kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).ADAM10 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ADAM10 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADAM10 is part of the ADAM family which are cell surface proteins with a distinctive structure possessing both potential adhesion and protease domains. ADAM10 cleaves many proteins including TNF-alpha and E-cadherin. ADAM10 cleaves the membrane-bound precursor of tnf-alpha at 76- ala-|-val-77 to its mature soluble form. ADAM10 is in charge for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-a2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein ADAM10 is involved in the normal cleavage of the cellular prion protein. ADAM10 is involved in the cleavage of the adhesion molecule l1 at the cell surface and in the release of membrane vesicles, suggesting a vesicle-based protease activity. ADAM10 controls the proteolytic processing of notch and mediates lateral inhibition during neurogenesis.

    • Synonyms

      Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.

    • 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

      TTSAEKNTCQ LYIQTDHLFF KYYGTREAVI AQISSHVKAI DTIYQTTDFS GIRNISFMVK RIRINTTADE KDPTNPFRFP NIGVEKFLEL NSEQNHDDYC LAYVFTDRDF DDGVLGLAWV GAPSGSSGGI CEKSKLYSDG KKKSLNTGII TVQNYGSHVP PKVSHITFAH EVGHNFGSPH DSGTECTPGE SKNLGQKENG NYIMYARATS GDKLNNNKFS LCSIRNISQV LEKKRNNCFV ESGQPICGNG MVEQGEECDC GYSDQCKDEC CFDANQPEGR KCKLKPGKQC SPSQGPCCTA QCAFKSKSEK CRDDSDCARE GICNGFTALC PASDPKPNFT DCNRHTQVCI NGQCAGSICE KYGLEECTCA SSDGKDDKEL CHVCCMKKMD PSTCASTGSV QWSRHFSGRT ITLQPGSPCN DFRGYCDVFM RCRLVDADGP LARLKKAIFS PELYENIAEL EHHHHHH

    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.

    Adam10 Human Sf9
  • View Data Sheet

    Name :

    ADK Mouse

    Description:

    Adenosine Kinase Mouse Recombinant

    AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase.

    Product # :

    PKA-105

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    Description

    ADK produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-361a.a.) and having a molecular mass of 42.5kDa.ADK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ADK protein solution (1mg/ml) contains 20% glycerol, 20mM Tris-HCl buffer (pH8.0), 1mM EDTA & 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100 pmol/min/ug and is defined as the amount of enzyme that convert 1.0 pmole of adenosine to AMP per minute at pH 7.5 at 37C in a couple system with PK and LDH. 

    More Info

    • Introduction

      Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.

    • Synonyms

      AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase.

    • 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 MGSMAAADEP KPKKLKVEAP QALSENVLFG MGNPLLDISA VVDKDFLDKY SLKPNDQILA EDKHKELFDE LVKKFKVEYH AGGSTQNSMK VAQWLIQEPH KAATFFGCIG IDKFGEILKR KAADAHVDAH YYEQNEQPTG TCAACITGGN RSLVANLAAA NCYKKEKHLD LERNWVLVEK ARVYYIAGFF LTVSPESVLK VARYAAENNR VFTLNLSAPF ISQFFKEALM DVMPYVDILF GNETEAATFA REQGFETKDI KEIAKKAQAL PKVNSKRQRT VIFTQGRDDT IVAAENDVTA FPVLDQNQEE IIDTNGAGDA FVGGFLSQLV SDKPLTECIR AGHYAASVII RRTGCTFPEK PDFH.

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    Adenosine Kinase Mouse
  • View Data Sheet

    Name :

    SDF 1a Mouse, His

    Description:

    Stromal Cell-Derived Factor-1 alpha (CXCL12), Mouse Recombinant, His Tag

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.

    Product # :

    CHM-323

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    Description

    SDF 1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (22-89 a.a) and having a molecular mass of 10.4kDa. SDF 1a is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SDF 1a protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
      The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.

    • 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 MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.

    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.

    Sdf 1A Mouse His
  • View Data Sheet

    Name :

    NDUFS3 Human

    Description:

    Histidine NADH Dehydrogenase Fe-S Protein 3 Human Recombinant

    CI-30, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondria, Complex I-30kD, CI-30kD, NADH-ubiquinone oxidoreductase 30 kDa subunit.

    Product # :

    ENZ-662

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    Description

    Recombinant Human NDUFS3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 249amino acids (37-264 a.a.) and having a molecular mass of 28.7 kDa. NDUFS3 is fused to a 21 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFS3 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 (NDUFS3) is a member of the complex I 30 kDa subunit family. NDUFS3 is one of the iron-sulfur protein (IP) components of mitochondrial NADH:ubiquinone oxidoreductase (complex I). This complex is the first enzyme complex in the electron transport chain of mitochondria. The iron-sulfur protein (IP) fraction of complex I consists of seven subunits. NDUFS3 gene mutations are linked with Leigh syndrome resulting from mitochondrial complex indefficiency.

    • Synonyms

      CI-30, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondria, Complex I-30kD, CI-30kD, NADH-ubiquinone oxidoreductase 30 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 MESAGADTRP TVRPRNDVAH KQLSAFGEYV AEILPKYVQQ VQVSCFNELE VCIHPDGVIP VLTFLRDHTN AQFKSLVDLT AVDVPTRQNR FEIVYNLLSL RFNSRIRVKT YTDELTPIES AVSVFKAANW YEREIWDMFG VFFANHPDLR RILTDYGFEG HPFRKDFPLS GYVELRYDDE VKRVVAEPVE LAQEFRKFDL NSPWEAFPVY RQPPESLKLE AGDKKPDAK

    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.

    Ndufs3 Human
  • View Data Sheet

    Name :

    SIRPA Human, HEK

    Description:

    Signal-Regulatory Protein Alpha Human Recombinant, HEK

    Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptorSHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR.

    Product # :

    PRO-2755

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    Description

    SIRPA Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-373a.a) containing 356 amino acids and having a molecular mass of 39kDa.SIRPA is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The SIRPA solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human CD47.

    More Info

    • Introduction

      Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as the immunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which are involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.
      SIRPA can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part in signal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA.

    • Synonyms

      Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptor
      SHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR.

    • 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

      DGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY HHHHHH.

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

    Cd172A Human
  • View Data Sheet

    Name :

    HTF Bovine

    Description:

    Holo Transferrin Bovine

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    Product # :

    PRO-510

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    Description

    Bovine Holo Transferrin is a glycoprotein of approximately 80 kDa.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by Cellulose Acetate.

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

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

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG, HBc, ALT and Syphilis.Viral inactivation by pasteurization (60°C for 10 hours) has been validated using three different test viruses, with removal of 8-14.5 logs of virus documented. The purification process has also been found to remove significant additional quantities of virus.

    • Applications

      Bovine Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    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.

    Holo Transferrin Bovine
  • View Data Sheet

    Name :

    IFNA2C Human

    Description:

    Interferon-alpha 2c Human Recombinant

    Interferon alpha-2, IFN-alpha-2, Interferon alpha-A, LeIF A, IFNA2, IFNA2A, IFNA2B, IFNA2C.

    Product # :

    CYT-1117

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    Description

    Interferon-alpha 2c Recombinant Human produced in yeast is a single, glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 19.3kDa. The IFNA2C is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4 and 0.02 % Tween-20.

    Purity

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

    Biological Activity

    The activity is determined by the cytopathic effect inhibition assay. 

    More Info

    • Introduction

      IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

    • Synonyms

      Interferon alpha-2, IFN-alpha-2, Interferon alpha-A, LeIF A, IFNA2, IFNA2A, IFNA2B, IFNA2C.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFNA2C although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interferon-alpha 2c 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 Interferon-alpha 2c in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.

    • Background

      What is the molecular weight/Mw of IFNA2C HUMAN Protein?
      IFNA2C HUMAN Protein has a total Mw of 19.3kDa.

      What is the source or expression system of IFNA2C HUMAN Protein?
      Saccharomyces cerevisiae.

      What is the Purity of IFNA2C HUMAN Protein?
      IFNA2C HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNA2C HUMAN Protein?
      The activity is determined by the cytopathic effect inhibition assay.

      What is the amino acid sequence of IFNA2C HUMAN Protein?
      CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.

      What applications can IFNA2C HUMAN Protein be used in?
      IFNA2C HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNA2C HUMAN Protein?
      The endotoxin level is minimal, IFNA2C HUMAN 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.

    Ifna2C Human
  • View Data Sheet

    Name :

    FGF1 Human, 154 a.a.

    Description:

    Fibroblast Growth Factor-acidic (154 a.a.) Human Recombinant

    HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

    Product # :

    CYT-1112

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    Description

    Fibroblast Growth Factor-acidic Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids and having a molecular mass of 17.3kDa. The FGF1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4, with 0.5mM DTT, 2mM EDTA, and 5 % Trehalose.

    Purity

    Greater than 97.0% as determined by:

    (a) Analysis by RP-HPLC.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×106 IU/mg in the presence of 10µg/ml Heparin.

    More Info

    • Introduction

      Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF1 functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor.FGF1 acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-acidic 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 Fibroblast Growth Factor-acidic Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.

    • Background

      What is the molecular weight/Mw of FGF 1 Protein?
      FGF 1 Protein has a total Mw of 17.3kDa.

      What is the source or expression system of FGF 1 Protein?
      Escherichia Coli.

      What is the Purity of FGF 1 Protein?
      FGF 1 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 1 Protein?
      The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×106 IU/mg in the presence of 10µg/ml Heparin.

      What is the amino acid sequence of FGF 1 Protein?
      AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.

      What applications can FGF 1 Protein be used in?
      FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF 1 Protein?
      The endotoxin level is minimal, FGF 1 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.

    Fgf1 Protein
  • View Data Sheet

    Name :

    GPT2 Mouse, Active

    Description:

    Glutamic-Pyruvate Transaminase 2, Active Mouse Recombinant

    ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.

    Product # :

    ENZ-1110

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    Description

    GPT2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 542 amino acids (1-522 aa) and having a molecular mass of 60.1kDa.GPT2 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GPT2 solution (1 mg/ml) contains 2mM DTT, 20% Glycerol and 20mM Tris-HCl (pH7.5).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 50 units/mg. Measured by the amount of enzyme that cleaves 1umole of L-Alanineto L-Glutamate per minute at pH7.5 at 37C˚.

    More Info

    • Introduction

      Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.

    • Synonyms

      ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 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 MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE
      RSPRDRILTL ESMNPQVKAV EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA
      MGQQPITFLR QVMALCTYPN LLNSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR
      EDVAAFITRR DGVPADPDNI YLTTGASDGI STILKLLVSG GGKSRTGVMI PIPQYPLYSA
      VISELDAVQV NYYLDEENCW ALNVDELRRA LRQAKDHCDP KVLCIINPGN PTGQVQSRKC
      IEDVIHFAWE EKLFLLADEV YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK
      GYMGECGYRG GYMEVINLHP EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ
      FSREKEFVLG NLAKKAKLTE DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA VEAAQSHKMA
      PDMFYCMKLL EETGICVVPG SGFGQREGTY HFRMTILPPV DKLKTVLHKV KDFHLKFLEQ YS

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    Gpt 2 Mouse
  • View Data Sheet

    Name :

    HIV-1 nef, Clade B

    Description:

    HIV-1 nef Clade B Recombinant

    Product # :

    HIV-156

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    Description

    The E.coli derived 27 kDa recombinant HIV-1 Nef Clade-B protein is a single non-glycosylated polypeptide chain.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized with 1% glycerol.

    Purity

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

    More Info

    • Introduction

      HIV-1 Nef is a 27kDa protein highly produced after a very short time after virus infection. HIV-1 Nef is an essential factor for efficient viral replication and phatogenesis.
      HIV-1 Nef facilitates virus replication and improves virions infectivity. HIV-1 Nef exerts pleiotropic effect. HIV-1 Nef down-modulates surface MHC-I molecules, decreases cell surface CD4 antigen by interacting with the Src family kinase LCK thereby inducing LCK-CD4 dissociation and by increasing clathrindependent endocytosis of this antigen to target it to lysosomial degradation. HIV-1 Nef guards the infected cell from apoptosis in order to keep it alive until the next virus generation is ready to strike. HIV-1 Nef protein bypasses host Tcell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation.

    • Physical Appearance

      Sterile Filtered and lyophilized, though might appear as a solution as a result of the glycerol content.

    • Stability

      Lyophilized HIV-1 nef although stable at room temperature for 1 week, should be stored desiccated below -18°C. Upon reconstitution HIV-1 nef 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 HIV-1 nef in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Hiv 1 Nef Clade B
  • View Data Sheet

    Name :

    MutY E.Coli

    Description:

    Adenine DNA Glycosylase E.Coli Recombinant

    ECK2956, JW2928, mica, mutB, mutY.

    Product # :

    ENZ-702

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    MutY Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 373 amino acids (1-350) and having a molecular mass of 41.5kDa. MutY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MutY solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adenine DNA glycosylase (mutY) is an adenine DNA glycosylase active on DNA substrates including A/G, A/8-oxoG, or A/C mismatches and also has a weak guanine glycosylase activity on G/8- oxoG-containing DNA. mutY is essential for the prevention of mutations resulting from oxidative DNA impairment. Rising levels of mutY in A549 cells exposed to oxygen and infrared radiation leads to improvements in cell survival. mutY is common in neurons where mitochondrial genomes exposed to reactive oxygen species that damage DNA must uphold integrity over the whole mammalian life span.

    • Synonyms

      ECK2956, JW2928, mica, mutB, mutY.

    • 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 MGSMQASQFS AQVLDWYDKY GRKTLPWQID KTPYKVWLSE VMLQQTQVAT VIPYFERFMA RFPTVTDLAN APLDEVLHLW TGLGYYARAR NLHKAAQQVA TLHGGKFPET FEEVAALPGV GRSTAGAILS LSLGKHFPIL DGNVKRVLAR CYAVSGWPGK KEVENKLWSL SEQVTPAVGV ERFNQAMMDL GAMICTRSKP KCSLCPLQNG CIAAANNSWA LYPGKKPKQT LPERTGYFLL LQHEDEVLLA QRPPSGLWGG LYCFPQFADE ESLRQWLAQR QIAADNLTQL TAFRHTFSHF HLDIVPMWLP VSSFTGCMDE GNALWYNLAQ PPSVGLAAPV ERLLQQLRTG APV.

    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.

    Muty Ecoli
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