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Search results

1000 results found for “Protease”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    CKMB Human

    Description:

    Creatine Kinase MB Human Recombinant

    CKMB, CK-MB 

     

    Product # :

    CKI-286

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    Description

    Recombinant Human Creatine Kinase MB produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.The CKMB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 50mM Tris-HCL, 5mM B-mercaptoethanol, 1mM EDTA, 5mM disodium Succinate, Ph 8.0 and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      CKMB although stable at 10°C for 7 days, should be stored below -18°C.Please prevent 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.

    ckmb-protein
  • View Data Sheet

    Name :

    GPT2 Mouse

    Description:

    Glutamic-Pyruvate Transaminase 2 Mouse Recombinant

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

    Product # :

    ENZ-1096

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    Description

    GPT2 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 522 amino acids (1-522) and having a molecular mass of 60.1 kDa. Mouse GPT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPT2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 7.5), 20% glycerol, and 2mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Biological Activity

    Greater than 50units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH7.5 at 37℃.

    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.

    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.

    Gpt2 Mouse
  • View Data Sheet

    Name :

    PIP Protein

    Description:

    Prolactin-Induced Protein Human Recombinant

    Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.

    Product # :

    CYT-793

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    PIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (29-146 a.a.) and having a molecular mass of 15.9kDa.PIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prolactin-inducible protein (PIP) is a main protein component of benign breast gross cysts. PIP is a famous indicator of breast cancer, since it is found in around 50% of all breast cancer specimens. PIP is expressed in exocrine glands, in pathologic conditions, in breast cysts and breast cancers exhibiting apocrine features. PIP and prostate specific antigen are co-expressed in androgen receptor-positive breast tumours.

    • Synonyms

      Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.

    • 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 MGSQDNTRKI IIKNFDIPKS VRPNDEVTAV LAVQTELKEC MVVKTYLISS IPLQGAFNYK YTACLCDDNP KTFYWDFYTN RTVQIAAVVD VIRELGICPD DAAVIPIKNN RFYTIEILKV E.

    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.

    Human Pip
  • View Data Sheet

    Name :

    PTGDS Human

    Description:

    Prostaglandin D2 Synthase Human Recombinant

    Prostaglandin-H2 D-isomerase, Beta-trace protein, Cerebrin-28, Glutathione-independent PGD synthase, Lipocalin-type prostaglandin-D synthase, Prostaglandin-D2 synthase, PGD2 synthase, PGDS, PGDS2, PTGDS, PDS, PGD2, LPGDS, L-PGDS.

    Product # :

    ENZ-109

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    PTGDS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (23-190 a.a.) and having a molecular mass of 20.9kDa.PTGDS is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTGDS solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 1mM EDTA and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prostaglandin-H2 D-isomerase (PTGDS) is a glutathione-independent prostaglandin D synthase which catalyzes the conversion of prostaglandin H2 (PGH2) to postaglandin D2 (PGD2). PTGDS is may have vital roles in both maturation and maintenance of the central nervous system and male reproductive system. PTGDS is the most abundant protein in the cerebral spinal fluid and recent evidence suggests that PTGDS acts as a beta-amyloid chaperone and may play a role in the deposition of Ab plaques in Alzheimer’s disease.

    • Synonyms

      Prostaglandin-H2 D-isomerase, Beta-trace protein, Cerebrin-28, Glutathione-independent PGD synthase, Lipocalin-type prostaglandin-D synthase, Prostaglandin-D2 synthase, PGD2 synthase, PGDS, PGDS2, PTGDS, PDS, PGD2, LPGDS, L-PGDS.

    • 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 MAPEAQVSVQ PNFQQDKFLG RWFSAGLASN SSWLREKKAA LSMCKSVVAP ATDGGLNLTS TFLRKNQCET RTMLLQPAGS LGSYSYRSPH WGSTYSVSVV ETDYDQYALL YSQGSKGPGE DFRMATLYSR TQTPRAELKE KFTAFCKAQG FTEDTIVFLP QTDKCMTEQ.

    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.

    Ptgds Human 2
  • View Data Sheet

    Name :

    HSD17B11 Human

    Description:

    Hydroxysteroid (17-beta) Dehydrogenase 11 Human Recombinant

    17-beta-hydroxysteroid dehydrogenase 11, 17-beta-HSD 11, 17bHSD11, 17betaHSD11, 17-beta-hydroxysteroid dehydrogenase XI, 17-beta-HSD XI, 17betaHSDXI, Cutaneous T-cell lymphoma-associated antigen HD-CL-03, CTCL-associated antigen HD-CL-03, Dehydrogenase/reductase SDR family member 8, Retinal short-chain dehydrogenase/reductase 2, retSDR2, HSD17B11, DHRS8, PAN1B, SDR16C2, 17BHSD11.

    Product # :

    ENZ-049

    Price :

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    • More Info

    Description

    HSD17B11 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 287 amino acids (20-285 a.a.) and having a molecular mass of 31.4kDa. The HSD17B11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSD17B11 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dehydrogenase/reductase SDR family member 8 (HSD17B11) is a member of the HSD17B family of proteins, which regulate the availability of steroids within various tissues throughout the body. HSD17B11 is widely expressed with the highest levels found in the retina, pancreas, kidney, liver, lung, adrenal, small intestine, ovary and heart as well as in steroidogenic cells. HSD17B11 converts androstan-3-?,17-?-diol (3-?-diol) to androsterone, suggesting it may participate in androgen metabolism during steroidogenesis.

    • Synonyms

      17-beta-hydroxysteroid dehydrogenase 11, 17-beta-HSD 11, 17bHSD11, 17betaHSD11, 17-beta-hydroxysteroid dehydrogenase XI, 17-beta-HSD XI, 17betaHSDXI, Cutaneous T-cell lymphoma-associated antigen HD-CL-03, CTCL-associated antigen HD-CL-03, Dehydrogenase/reductase SDR family member 8, Retinal short-chain dehydrogenase/reductase 2, retSDR2, HSD17B11, DHRS8, PAN1B, SDR16C2, 17BHSD11.

    • 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 MESFVKLFIP KRRKSVTGEI VLITGAGHGI GRLTAYEFAK LKSKLVLWDI NKHGLEETAA KCKGLGAKVH TFVVDCSNRE DIYSSAKKVK AEIGDVSILV NNAGVVYTSD LFATQDPQIE KTFEVNVLAH FWTTKAFLPA MTKNNHGHIV TVASAAGHVS VPFLLAYCSS KFAAVGFHKT LTDELAALQI TGVKTTCLCP NFVNTGFIKN PSTSLGPTLE PEEVVNRLMH GILTEQKMIF IPSSIAFLTT LERILPERFL AVLKQKI.

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    Hsd17B11 Human
  • View Data Sheet

    Name :

    ENTPD3 Human, sf9 Bioactive

    Description:

    Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive

    Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.

    Product # :

    ENZ-1020

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    Description

    ENTPD3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 451 amino acids (44-485a.a.) and having a molecular mass of 50.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ENTPD3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ENTPD3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 250,000 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze ATP per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

    • Synonyms

      Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.

    • 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

      ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.

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    Entpd3 Human Sf9 Bioactive
  • View Data Sheet

    Name :

    OTC Human

    Description:

    Ornithine Carbamoyltransferase Human Recombinant

    Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.

    Product # :

    ENZ-596

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    Description

    OTC Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (33-354) and having a molecular mass of 38.9kDa.OTC is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The OTC solution (0.5mg/ml) contains 20mM MES buffer (pH 6.0), 100mM Nacl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      OTC is a member of the ATCase/OTCase family. OTC has a key part in the urea cycle, catalyzing the second step in this pathway: the transformation of L-orthinine and carbamoyl phosphate to L-citrulline. In humans, the urea cycle is a vital pathway to detoxification of ammonia. Alterations in the gene encoding OTC are linked to the X-linked disorder OTCD (ornithine carbamoyltransferase deficiency). OTCD disorder of the urea cycle is characterized by hyperammonemia.

    • Synonyms

      Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.

    • 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 MGSHMNKVQL KGRDLLTLKN FTGEEIKYML WLSADLKFRI KQKGEYLPLL QGKSLGMIFE KRSTRTRLST ETGFALLGGH PCFLTTQDIH LGVNESLTDT ARVLSSMADA VLARVYKQSD LDTLAKEASI PIINGLSDLY HPIQILADYL TLQEHYSSLK GLTLSWIGDG NNILHSIMMS AAKFGMHLQA ATPKGYEPDA SVTKLAEQYA KENGTKLLLT NDPLEAAHGG NVLITDTWIS MGQEEEKKKR LQAFQGYQVT MKTAKVAASD WTFLHCLPRK PEEVDDEVFY SPRSLVFPEA ENRKWTIMAV MVSLLTDYSP QLQKPKF.

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    Otc Human
  • View Data Sheet

    Name :

    IMPDH1 Human

    Description:

    IMP Dehydrogenase 1 Human Recombinant

    EC 1.1.1.205, IMP (inosine monophosphate) dehydrogenase 1, LCA11, RP10, IMPDH 1, IMPD 1, IMPDH-I, SwSS2608, DKFZp781N0678.

    Product # :

    ENZ-525

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    Description

    IMPDH1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 534 amino acids (1-514 a.a.) and having a molecular mass of 57.5 kDa. The IMPDH1 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IMPDH1 Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IMPDH1 is a rate limiting enzyme in the de novo synthesis of guanine nucleotides and consequently participates in the regulation of cell growth. IMPDH1 takes part in the development of malignancy and the growth progression of some tumors. IMPDH1 performs as a homotetramer to regulate cell growth. IMPDH1 catalyzes the synthesis of xanthine monophosphate (XMP) from inosine-5''-monophosphate (IMP). Defects in this gene are a cause of retinitis pigmentosa type 10 (RP10).

    • Synonyms

      EC 1.1.1.205, IMP (inosine monophosphate) dehydrogenase 1, LCA11, RP10, IMPDH 1, IMPD 1, IMPDH-I, SwSS2608, DKFZp781N0678.

    • 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 MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKMRHGFS GIPITETGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRIELVVAPA GVTLKEANEI LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS QKQLLCGAAV GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGARSLSVLR SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY.

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    Impdh1 Human
  • View Data Sheet

    Name :

    CBR3 Human

    Description:

    Carbonyl Reductase-3 Human Recombinant

    Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.

    Product # :

    ENZ-428

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    Description

    Recombinant Human CBR3 fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (1-277 a.a) and having a molecular mass of 33kDa. CBR3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CBR3 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      CBR3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. CBR3 is one of several monomeric NADPH-dependent oxidoreductases. Furthermore, CBR3 contains 3 exons spanning 11.2 kilobases and is strongly linked to another carbonyl reductase gene, the CBR1. It was suggested that CBR3 mediates 9-cis-retinoic acid-induced cytostatis and is a potential prognostic marker for oral malignancy.
      CBR3 is identified in the ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and the testis.

    • Synonyms

      Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.

    • 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 MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP MPFDIKAEMT LKTNFFATRN MCNELLPIMK PHGRVVNISS LQCLRAFENC SEDLQERFHS ETLTEGDLVD LMKKFVEDTK NEVHEREGWP NSPYGVSKLG VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS IRTVEEGAET PVYLALLPPD ATEPQGQLVH DKVVQNW.

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    Cbr3 Human
  • View Data Sheet

    Name :

    PSMB1 Human

    Description:

    Proteasome Subunit Beta Type 1 Human Recombinant

    HC5, PSC5, PMSB1, FLJ25321, KIAA1838, PSMB1, Proteasome subunit beta type-1, Proteasome component C5, Macropain subunit C5, Multicatalytic endopeptidase complex subunit C5, Proteasome gamma chain.

    Product # :

    ENZ-405

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    Description

    PSMB1 Human Recombinant fused to a 37 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids (30-241) and having a molecular mass of 27.7 kDa. The PSMB1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PSMB1 solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PSMB1 is part of the proteasome B-type family, also identified as the T1B family, that is a 20S core beta subunit. PSMB1 is tightly linked to the TBP (TATA-binding protein) gene in human and in mouse, and is transcribed in the opposite orientation in both species.The main function of PSMB1 is its degradation activity of unnecessary or damaged proteins by proteolysis. PSMB1 is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with arg, phe, tyr, leu, and glu adjacent to the leaving group at neutral or slightly basic ph. the proteasome has an atp-dependent proteolytic activity.

    • Synonyms

      HC5, PSC5, PMSB1, FLJ25321, KIAA1838, PSMB1, Proteasome subunit beta type-1, Proteasome component C5, Macropain subunit C5, Multicatalytic endopeptidase complex subunit C5, Proteasome gamma chain.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMFS PYVFNGGTIL AIAGEDFAIV ASDTRLSEGF SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK MYKHSNNKAM TTGAIAAMLS TILYSRRFFP YYVYNIIGGL DEEGKGAVYS FDPVGSYQRD SFKAGGSASA MLQPLLDNQV GFKNMQNVEH VPLSLDRAMR LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVSLRKD.

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    Psmb1 Human
  • View Data Sheet

    Name :

    PSME1 Human

    Description:

    Proteasome Activator Subunit 1 Human Recombinant

    REG-alpha, PA28alpha, PA28a, Proteasome Activator subunit-1, Proteasome Activator 28 subunit alpha.

    Product # :

    PRO-266

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    Description

    PSME1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-249a.a.) and having a molecular mass of 30.8kDa.PSME1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PSME1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PSME1 is a Proteasome Activator 28 subunit alpha essential for presentation of certain major histocompatibility (MHC) class I antigens. The PSME1 complex is an alternate proteasome activator which operates with no use of ubiquitin. The PSME1 complex is made out of two homologous subunits, alpha and beta, that functions in similar catalytic properties and is connected to a hexameric ring.

    • Synonyms

      REG-alpha, PA28alpha, PA28a, Proteasome Activator subunit-1, Proteasome Activator 28 subunit alpha.

    • 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 SSGLVPRGSH MAMLRVQPEA QAKVDVFRED LCTKTENLLG SYFPKKISEL DAFLKEPALN EANLSNLKAP LDIPVPDPVK EKEKEERKKQ QEKEDKDEKK KGEDEDKGPP CGPVNCNEKI VVLLQRLKPE IKDVIEQLNL VTTWLQLQIP RIEDGNNFGV AVQEKVFELM TSLHTKLEGF HTQISKYFSE RGDAVTKAAK QPHVGDYRQL VHELDEAEYR DIRLMVMEIR NAYAVLYDII LKNFEKLKKP RGETKGMIY

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    Psme1 Human
  • View Data Sheet

    Name :

    KLK8 Mouse

    Description:

    Kallikrein-8 Mouse Recombinant

    Ovasin, PRSS19, TADG14, NRPN, NP, Kallikrein 8 (Neuropsin/Ovasin) 2 EC 3.4.21.118, Kallikrein-8, Neuropsin, EC 3.4.21 61, HNP, HK8

    Product # :

    ENZ-1014

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    Description

    KLK8 Mouse Recombinant produced in Sf9 is a single, glycosylated polypeptide chain containing 240 amino acids (29-260) and having a molecular mass of 26.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). The KLK8 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK8 protein 0.5mg/ml is supplied in PBS, pH-7.4, and 10% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikrein-8 is a serine protease which degrades various proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Kallikrein-8 takes part in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is essential for memory acquisition and synaptic plasticity. Kallikrein-8 participates in the secondary phase of pathogenesis following spinal cord injury and also takes part in skin desquamation and keratinocyte proliferation.

    • Synonyms

      Ovasin, PRSS19, TADG14, NRPN, NP, Kallikrein 8 (Neuropsin/Ovasin) 2 EC 3.4.21.118, Kallikrein-8, Neuropsin, EC 3.4.21 61, HNP, HK8

    • 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

      QGSKILEGRE CIPHSQPWQA ALFQGERLIC GGVLVGDRWV LTAAHCKKQK YSVRLGDHSL QSRDQPEQEI QVAQSIQHPC YNNSNPEDHS HDIMLIRLQN SANLGDKVKP VQLANLCPKV GQKCIISGWG TVTSPQENFP NTLNCAEVKI YSQNKCERAY PGKITEGMVC AGSSNGADTC QGDSGGPLVC DGMLQGITSW GSDPCGKPEK PGVYTKICRY TTWIKKTMDN RDLEHHHHHH.

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    Klk8 Mouse
  • View Data Sheet

    Name :

    Streptavidin Protein

    Description:

    Streptavidin

    Product # :

    PRO-283

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    Description

    Streptavidin is a protein produced by Streptomyces avidinii and isolated by purification from fermentation broth. The pure, homogeneous protein shows predominantly one single band in SDS PAGE. Streptavidin consists of 4 identical subunits, each bearing an active binding site for biotin. Streptavidin has a molecular weight of 55kDa.

    Source

    Bacterium Streptomyces avidinii.

    Formulation

    The Streptavidin was lyophilized from a 25mg/ml solution in 10 mM potassium phosphate buffer pH 6.5

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Streptavidin although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. For longer storage in dissolved form add 1mM EDTA and/or 0.02 % NaN3 or pass the solution through a sterile filter.Please prevent freeze-thaw cycles.

    • Solubility

      Gives a clear solution at 10mg/ml in 4.0 mM potassium phosphate pH 6.5

    • Specific Activity

      The biological activity is 16.8 U/mg, 1 unit binds 1µg biotin.

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    Streptavidin
  • View Data Sheet

    Name :

    Protein-L Cys

    Description:

    Protein L Cys Recombinant

    Product # :

    PRO-1931

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    Description

    Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-L was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    sds-page, HPLC

    Protein-L Cys SDS-PAGE - Product image 1
    Protein-L cys HPLC - Product image 2

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.

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

    Protein L Cys
  • View Data Sheet

    Name :

    GPT Human, Active

    Description:

    Glutamic-Pyruvate Transaminase Human Recombinant, Active

    Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.

    Product # :

    ENZ-280

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    Description

    Alanine Aminotransferase Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 495a.a and having a molecular mass of 54,479 Dalton. The amino acid sequence is the same as that of native form of human liver ALT.The ALT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was dialyzed against 40mM sodium acetate buffer (pH 5.5), 1mM DTT,1mM EDTA, 5mM 2-oxoglutarate and 0.1mM pyridoxal-5'-phosphate.

    Purity

    Greater than 95.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 839 U/mg.

    More Info

    • Introduction

      Alanine transaminase or ALT is a transaminaseenzyme.
      ALT is found in serumand in various bodily tissues, but is most commonly associated with the liver; It catalyzes the transfer of an aminogroup from alanineto a-ketoglutarate, the products of this reversible transaminationreaction being pyruvateand glutamatealanine+ a-ketoglutarate= pyruvate+ glutamate
      It is commonly measured clinically as a part of a diagnostic liver function test, to determine liver health. It is also called serum glutamate pyruvate transaminase (SGPT) or alanine aminotransferase (ALAT). Diagnostically, it is almost always measured in units/litre (U/L).

    • Synonyms

      Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.

    • Physical Appearance

      Sterile liquid formulation.

    • Stability

      AAT1 although stable at 10°C for 5 days, should be stored below -18°C.Please prevent 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.

    Alanine Aminotransferase Human
  • View Data Sheet

    Name :

    PON1 Human

    Description:

    Paraoxonase-1 Human Recombinant

    Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1, Serum aryldialkylphosphatase 1, A-esterase 1, Aromatic esterase 1, K-45, ESA, PON.

    Product # :

    ENZ-299

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    Description

    Paraoxonase-1 Isoform Human Recombinant is expressed in E. coli, fused to a 7 amino acid c- terminal hexahistidine tag, containing 362 amino acids and ( 1-355 a.a.) having a total molecular weight of 40.68kDa. The PON1 purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    lyophilized from 0.5 mg/mL in 20mM Tris buffer, 50 mM NaCl, pH 7.5

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Paraoxonase 1 also called Esterase-A is involved in the detoxification of organophosphate insecticides such as parathion. Paraoxonase 1 may also confer protection against coronary artery disease by destroying proinflammatory oxidized lipids present in oxidized low-density lipoproteins (LDLs).

    • Synonyms

      Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1, Serum aryldialkylphosphatase 1, A-esterase 1, Aromatic esterase 1, K-45, ESA, PON.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized PON1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGL
      AFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNA
      MYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLD
      PYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEK
      HANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILT
      EEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCELEHHHHHH.

    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.

    Pon1 Human
  • View Data Sheet

    Name :

    Streptolysin-O

    Description:

    Streptolysin-O Streptococcus Pyogenes Recombinant

    Streptolysin O, Thiol-activated cytolysin, slo.

    Product # :

    PRO-2302

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    Description

    Recombinant Streptococcus Pyogenes Streptolysin-O produced in E.coli is a single, non-glycosylated, polypeptide chain containing 538 amino acids and having a molecular mass of 60.1kDa.The Streptolysin-O is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Streptolysin-O protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Streptolysin-O is a sulfhydryl-activated toxin which causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the Streptolysin-O protein undergoes a major conformation change, leading to its insertion in the host membrane and creation of an oligomeric pore complex. Cholesterol may be needed for binding to host membranes, membrane insertion and pore formation. Streptolysin-O can be reversibly inactivated by oxidation.

    • Synonyms

      Streptolysin O, Thiol-activated cytolysin, slo.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

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

    • Amino Acid Sequence

      NKQNTASTET TTTNEQPKPE SSELTTEKAG QKTDDMLNSN DMIKLAPKEM PLESAEKEEK KSEDKKKSEE DHTEEINDKI YSLNYNELEV LAKNGETIEN FVPKEGVKKA DKFIVIERKK KNINTTPVDI SIIDSVTDRT YPAALQLANK GFTENKPDAV VTKRNPQKIH IDLPGMGDKA TVEVNDPTYA NVSTAIDNLV NQWHDNYSGG NTLPARTQYT ESMVYSKSQI EAALNVNSKI LDGTLGIDFK SISKGEKKVM IAAYKQIFYT VSANLPNNPA DVFDKSVTFK ELQRKGVSNE APPLFVSNVA YGRTVFVKLE TSSKSNDVEA AFSAALKGTD VKTNGKYSDI LENSSFTAVV LGGDAAEHNK VVTKDFDVIR NVIKDNATFS RKNPAYPISY TSVFLKNNKI AGVNNRTEYV ETTSTEYTSG KINLSHQGAY VAQYEILWDE INYDDKGKEV ITKRRWDNNW YSKTSPFSTV IPLGANSRNI RIMARECTGL AWEWWRKVID ERDVKLSKEI NVNISGSTLS PYGSITYK.

    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.

    Streptolysin O
  • View Data Sheet

    Name :

    Luciferase Firefly, Active

    Description:

    Luciferin 4-Monooxygenase Firefly Recombinant, Active

    Luciferase-like monooxygenase, LUC, EC 1.13.12.7.

    Product # :

    ENZ-1035

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    Description

    Luciferase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-311 a.a) and having a molecular mass of 38.5kDa. Luciferase is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Luciferase solution (0.5mg/ml) contains 20mM Tris-HCl (pH8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >1x109 light units/mg. One luciferase enzyme units will produce one Relative Light Unit (RLU) at pH7.5 at 25°C. 

    More Info

    • Introduction

      Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.

    • Synonyms

      Luciferase-like monooxygenase, LUC, EC 1.13.12.7.

    • 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 MGSHMTSKVY DPEQRKRMIT GPQWWARCKQ MNVLDSFINY YDSEKHAENA VIFLHGNAAS SYLWRHVVPH IEPVARCIIP DLIGMGKSGK SGNGSYRLLD HYKYLTAWFE LLNLPKKIIF VGHDWGACLA FHYSYEHQDK IKAIVHAESV VDVIESWDEW PDIEEDIALI KSEEGEKMVL ENNFFVETML PSKIMRKLEP EEFAAYLEPF KEKGEVRRPT LSWPREIPLV KGGKPDVVQI VRNYNAYLRA SDDLPKMFIE SDPGFFSNAI VEGAKKFPNT EFVKVKGLHF SQEDAPDEMG KYIKSFVERV LKNEQ.

    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.

    Luciferase Firefly Active
  • View Data Sheet

    Name :

    TrxR Yeast

    Description:

    Thioredoxin Reductase (NADPH) Yeast Recombinant

    Thioredoxin Reductase (NADPH), NTR, TrxR.

    Product # :

    ENZ-278

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    Description

    Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 20mM phosphate buffer pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 5.8 IU/mg.

    More Info

    • Introduction

      Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.

    • Synonyms

      Thioredoxin Reductase (NADPH), NTR, TrxR.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NTR in sterile 18MΩ-cm H2O.

    • Unit Definition

      One unit equals the change in absorbance at 412 nm per minute at 25°C using 0.2mM NADPH containing 5mM DTNB (pH 7.0).

    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.

    Thioredoxin Reductase Yeast
  • View Data Sheet

    Name :

    GNMT Human, Active

    Description:

    Glycine N-Methyltransferase Human Recombinant , Active

    Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP.

    Product # :

    ENZ-1059

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    Description

    GNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295 a.a) and having a molecular mass of 34.9kDa.GNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37C.

    More Info

    • Introduction

      GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine and sarcosine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine (sarcosine) with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

    • Synonyms

      Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20
      Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP.

    • 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 MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD.

    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.

    Gnmt Human Active
  • View Data Sheet

    Name :

    Cystatin-C Protein

    Description:

    Cystatin-C Human Recombinant

    Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    Product # :

    PRO-2601

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    Description

    Cystatin-C Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13.3kDa. Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cystatin-C is supplied as a 0.2 μm filtered solution containing 20mM Tris-HCl, 50 % glycerol, pH 8.0 and 300mM NaCl.

    Purity

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

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    • 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

      SSPGKPPRLV GGPMDASVEE EGVRRALDFA VGEYNKASND MYHSRALQVV RARKQIVAGV NYFLDVELGR TTCTKTQPNL DNCPFHDQPH LKRKAFCSFQ IYAVPWQGTM TLSKSTCQDA.

    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.

    Cystatin C
  • View Data Sheet

    Name :

    UCHL1 (1-126) Human

    Description:

    Ubiquitin Carboxyl-Terminal Hydrolase L1 (1-126) Human Recombinant

    PGP 9.5, UCHL1, PGP9.5, PARK5.

    Product # :

    PRO-2823

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    Description

    The UCHL1 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCHL1 His-Tagged Fusion Protein, produced in E. coli, is a 19kDa protein containing 126 amino acid residues of the UCHL1 Human, 1-126 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      PGP 9.5, UCHL1, PGP9.5, PARK5.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized UCHL1 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 approximately 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 on cell culture.

    • Background

      Human Ubiquitin Carboxyl-Terminal Hydrolase L1 (UCH-L1) is an important enzyme involved in the ubiquitin-proteasome system, which regulates protein degradation and turnover in cells.

      UCHL1 Function:

      UCHL1 mainly removes ubiquitin molecules from proteins, thereby recycling ubiquitin and regulating protein stability. This action is important for controlling various cellular processes and maintaining cellular homeostasis and.

      UCHL1 Structure

      UCHL1 is characterized by a catalytic domain which facilitates its hydrolase activity, allowing it to cleave ubiquitin from substrates.

      UCHL1 Role in Neurodegeneration

      UCHL1 has been implicated in neurodegenerative diseases, such as Parkinson’s and Alzheimer's disease. Its expression levels and activity can affect neuronal survival and function.

      UCH-L1 is also studied in the context of cancer. Altered levels of UCHL1 may affect on tumour progression and response to therapy.

      UCHL1 Biomarker Potential

      UCHL1 is being investigated as a potential biomarker for diseases, especially neurodegenerative disorders due to its involvement in various pathologies.

      UCHL1 Research

      Ongoing studies focus on understanding its role in various cellular contexts, its regulation, and its potential as a therapeutic target.

      In conclusion, UCHL1 is a very important component of cellular regulation, with implications in health and disease.

    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.

    Uchl1 Protein
  • View Data Sheet

    Name :

    PLA2G1B Human

    Description:

    Secreted Phospholipase A2-IB Human Recombinant

    Phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IB phospholipase A2, PLA2, PLA2A, PPLA2, sPLA2-IB,MGC119834, MGC119835, PLA2G1B.

    Product # :

    ENZ-325

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    Description

    Secreted Phospholipase A2-IB Human Recombinant is manufactured with N-terminal fusionf HisTag. PLA2G1B His-Tagged Fusion Protein is 16 kDa containing 126 amino acid residues of the human secreted phospholipase A2-IB and 16 additional amino acid residues - HisTag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Group IB secretory phospholipase A2 (sPLA2-IB) mediates cell proliferation, cell migration, hormone release and eicosanoid production via its receptor in peripheral tissues. In the CNS, high-affinity binding sites of sPLA2-IB have been documented. sPLA2-IB induced neuronal cell death in a concentrationdependent manner depending on PGD2 metabolites, especially Delta12-PGJ2 that might mediate sPLA2-IB-induced apoptosis. The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of lowmolecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.

    • Synonyms

      Phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IB phospholipase A2, PLA2, PLA2A, PPLA2, sPLA2-IB,MGC119834, MGC119835, PLA2G1B.

    • Physical Appearance

      Lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMAVWQ FRKMIKCVIP GSDPFLEYNN YGCYCGLGGS GTPVDELDKC CQTHDNCYDQ AKKLDSCKFL LDNPYTHTYS YSCSGSAITC SSKNKECEAF ICNCDRNAAI CFSKAPYNKA HKNLDTKKYC QS.

    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.

    Pla2G1B Human
  • View Data Sheet

    Name :

    PPP1CC Human, Active

    Description:

    Protein Phosphatase 1, Catalytic Subunit Gamma Human Recombinant, Active

    Protein phosphatase 1 catalytic subunit gamma isozyme/isoform, Protein phosphatase 1C catalytic subunit, serine/threonine phosphatase 1 gamma, serine/threonine-protein phosphatase PP1-gamma catalytic subunit, PP1gamma, PPP1G, EC 3.1.3.16.

    Product # :

    ENZ-1042

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    • More Info

    Description

    PPP1CC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-323a.a.) and having a molecular mass of 39.1kDa.PPP1CC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPP1CC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 700 units/mg, and is defined as the amount of enzyme that hydrolyzes 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37°C.

    More Info

    • Introduction

      PPP1CC is vital for cell division and takes part in the regulation of protein synthesis, muscle contractility and glycogen metabolism. Additionally, PPP1CC has a role in long-term synaptic plasticity and regulation of ionic conductance, and has a significant role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II.

    • Synonyms

      Protein phosphatase 1 catalytic subunit gamma isozyme/isoform, Protein phosphatase 1C catalytic subunit, serine/threonine phosphatase 1 gamma, serine/threonine-protein phosphatase PP1-gamma catalytic subunit, PP1gamma, PPP1G, EC 3.1.3.16.

    • 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 MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE KKKPNATRPV TPPRGMITKQ AKK.

    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.

    Ppp1Cc Human Active
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