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Search results

1000 results found for “Heparanase”

Name

Description

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  • View Data Sheet

    Name :

    RNGTT Human

    Description:

    RNA Guanylyltransferase And 5'-Phosphatase Human Recombinant

    RNA Guanylyltransferase And 5'-Phosphatase, CAP1A, RNA Guanylyltransferase And 5-Phosphatase, HCAP1, HCE1, HCE, MRNA-Capping Enzyme, HCAP 3, mRNA-capping enzyme.

    Product # :

    ENZ-823

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    Description

    RNGTT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 620 amino acids (1-597a.a) and having a molecular mass of 70.9kDa. RNGTT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNGTT protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 40% glycerol, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RNA Guanylyltransferase And 5'-Phosphatase also known as RNGTT is a bifunctional mRNA-capping enzyme which exhibits RNA 5'-triphosphatase activity in the N-terminal section and mRNA guanylyltransferase activity in the C-terminal section. In addition, RNGTT catalyzes the first two steps of cap formation, through removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and also by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.

    • Synonyms

      RNA Guanylyltransferase And 5'-Phosphatase, CAP1A, RNA Guanylyltransferase And 5-Phosphatase, HCAP1, HCE1, HCE, MRNA-Capping Enzyme, HCAP 3, mRNA-capping enzyme.

    • 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 MGSMAHNKIP PRWLNCPRRG QPVAGRFLPL KTMLGPRYDS QVAEENRFHP SMLSNYLKSL KVKMGLLVDL TNTSRFYDRN DIEKEGIKYI KLQCKGHGEC PTTENTETFI RLCERFNERN PPELIGVHCT HGFNRTGFLI CAFLVEKMDW SIEAAVATFA QARPPGIYKG DYLKELFRRY GDIEEAPPPP LLPDWCFEDD EDEDEDEDGK KESEPGSSAS FGKRRKERLK LGAIFLEGVT VKGVTQVTTQ PKLGEVQQKC HQFCGWEGSG FPGAQPVSMD KQNIKLLDLK PYKVSWKADG TRYMMLIDGT NEVFMIDRDN SVFHVSNLEF PFRKDLRMHL SNTLLDGEMI IDRVNGQAVP RYLIYDIIKF NSQPVGDCDF NVRLQCIERE IISPRHEKMK TGLIDKTQEP FSVRNKPFFD ICTSRKLLEG NFAKEVSHEM DGLIFQPTGK YKPGRCDDIL KWKPPSLNSV DFRLKITRMG GEGLLPQNVG LLYVGGYERP FAQIKVTKEL KQYDNKIIEC KFENNSWVFM RQRTDKSFPN AYNTAMAVCN SISNPVTKEM LFEFIDRCTA ASQGQKRKHH LDPDTELMPP PPPKRPRPLT.

    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.

    Rngtt Human
  • View Data Sheet

    Name :

    SERPINA5 Human

    Description:

    Serpin Peptidase Inhibitor Clade A Member 5 Human Recombinant

    PAI3, PCI, PROCI, PLANH3, Protein-C Inhibitor, Serpin A5, Plasminogen activator inhibitor 3, PAI-3, SERPINA5.

    Product # :

    PRO-749

    Price :

    Quantity :

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    Description

    SERPINA5 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 408 amino acids (20-406 a.a.) and having a molecular mass of 45.9 kDa.The SERPINA5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINA5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SERPINA5 up regulates TAFI activation by inhibiting the protein C activation. SERPINA5 is a significant regulator in the equilibrium between coagulation and fibrinolysis by differentially inhibiting the activation of TAFI and of Protein-C. SERPINA5 belongs to the serpin serine proteinase inhibitor family. SERPINA5 protein inhibits plasminogen activators as well as activated protein C.
      SERPINA5 is secreted in plasma & liver. SERPINA5 is involved in cell inflammation, proliferation, apoptosis, tumour cell migration, invasion, and metastasis. Moreover, SERPINA5 controls the invasive potential of renal cell carcinoma by inhibiting urinary plasminogen activator secreted by the cells. SERPINA5 participtes in regulating key serine proteases which are involved in metastatic prostate disease.

    • Synonyms

      PAI3, PCI, PROCI, PLANH3, Protein-C Inhibitor, Serpin A5, Plasminogen activator inhibitor 3, PAI-3, SERPINA5.

    • 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 MHRHHPREMK KRVEDLHVGA TVAPSSRRDF TFDLYRALAS AAPSQNIFFS PVSISMSLAM LSLGAGSSTK MQILEGLGLN LQKSSEKELH RGFQQLLQEL NQPRDGFQLS LGNALFTDLV VDLQDTFVSA MKTLYLADTF PTNFRDSAGA MKQINDYVAK QTKGKIVDLL KNLDSNAVVI MVNYIFFKAK WETSFNHKGT QEQDFYVTSE TVVRVPMMSR EDQYHYLLDR NLSCRVVGVP YQGNATALFI LPSEGKMQQV ENGLSEKTLR KWLKMFKKRQ LELYLPKFSI EGSYQLEKVL PSLGISNVFT SHADLSGISN HSNIQVSEMV HKAVVEVDES GTRAAAATGT IFTFRSARLN SQRLVFNRPF LMFIVDNNIL FLGKVNRP.

    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.

    Serpina5 Human
  • View Data Sheet

    Name :

    HP-NAP

    Description:

    Neutrophil-activating protein A Helicobacter Pylori Recombinant

    DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.

    Product # :

    PRO-2035

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    HP-NAP Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Ala144) containing 154 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 18.2kDa.

    Source

    Escherichia Coli.

    Formulation

    HP-NAP was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.

    • Synonyms

      DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; 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. HP-NAP is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASMKTFEILKHL QADAIVLFMK VHNFHWNVKG TDFFNVHKAT EEIYEEFADM FDDLAERIVQ LGHHPLVTLS EAIKLTRVKE ETKTSFHSKD IFKEILEDYK YLEKEFKELS NTAEKEGDKV TVTYADDQLA KLQKSIWMLQ AHLA.

    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.

    Hp Nap
  • View Data Sheet

    Name :

    MMP12 Human (1-33)

    Description:

    Matrix Metalloproteinase 12 (1-33 a.a.) Human Recombinant

    Product # :

    ENZ-1201

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    The MMP12 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The MMP12 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 33 amino acid residues of the MMP12 Human, 1-33 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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized MMP12 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.

    • Amino Acid Sequence

      MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFG.

    • Background

      Matrix Metalloproteinase 12 also known as MMP12 is 1 of the main enzymes in the MMP family which is primarily produced by macrophages and neutrophils. MMP12 is implicated in the breakdown of elastin and in the development of chronic inflammatory diseases, such as emphysema, COPD and atherosclerosis. MMP12 is upregulated and contributes to tissue remodeling in inflammatory responses which is essential for wound healing and immune defense. MMP12 catalyzes the cleavage of collagen, elastin and other ECM components. Its activity is regulated in normal tissues to avoid pathological degradation.

    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.

    Mmp12 Enzyme
  • View Data Sheet

    Name :

    DLST Human

    Description:

    Dihydrolipoamide S-Succinyltransferase Human Recombinant

    dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.

    Product # :

    ENZ-083

    Price :

    Quantity :

    Shipping Method :

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    Description

    DLST is a Full-length cDNA coding for the mature form of the human OGDC-E2 protein having a molecular mass of 42,301 Dalton (pH 6.3).DLST protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    DLST (0.74mg/ml) is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    DLST purity was found to be greater than 75% as determined by SDS-PAGE.

    More Info

    • Introduction

      DLST catalyzes the general transformation of 2-oxoglutarate to succinyl-CoA and CO(2). DLST holds multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

    • Synonyms

      dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.

    • Stability

      Store DLST 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. DLST binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.

    • coating concentration

      0.4-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with anti-M2-Antigen autoantibody-positive patient sera or monoclonal
      anti-hexa-His-tag antibody.

    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.

    Dlst Human
  • View Data Sheet

    Name :

    MUG E.Coli

    Description:

    G/U Mismatch-Specific DNA Glycosylase E.Coli Recombinant

    xanthine DNA glycosylase, dug, ECK3058, JW3040, ygjF, G/U mismatch-specific DNA glycosylase, Double-strand-specific uracil glycosylase, Mismatch-specific uracil DNA-glycosylase, mug.

    Product # :

    ENZ-703

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    Description

    MUG Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (1-168) and having a molecular mass of 21.1kDa. MUG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MUG solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      G/U mismatch-specific DNA glycosylase (mug) is a part of the TDG/mug DNA glycosylase family. Mug is necessary for DNA damage lesion repair in stationary-phase cells. Mug protein removes three N4-ethenocytosine and takes away s the uracil base from mismatches in the order of U:G>U:A. The enzyme Uracil-N-Glycosylase removes uracil from the DNA leaving an AP position. Mug is also able to hydrolyzing the carbon-nitrogen bond among the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine plays a role in substrate recognition.

    • Synonyms

      xanthine DNA glycosylase, dug, ECK3058, JW3040, ygjF, G/U mismatch-specific DNA glycosylase, Double-strand-specific uracil glycosylase, Mismatch-specific uracil DNA-glycosylase, mug.

    • 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 MGSMVEDILA PGLRVVFCGI NPGLSSAGTG FPFAHPANRF WKVIYQAGFT DRQLKPQEAQ HLLDYRCGVT KLVDRPTVQA NEVSKQELHA GGRKLIEKIE DYQPQALAIL GKQAYEQGFS QRGAQWGKQT LTIGSTQIWV LPNPSGLSRV SLEKLVEAYR ELDQALVVRG R.

    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.

    Mug Ecoli
  • View Data Sheet

    Name :

    PHOSPHO2 Human

    Description:

    Phosphatase Orphan-2 Human Recombinant

    Pyridoxal phosphate phosphatase PHOSPHO2, PHOSPHO2.

    Product # :

    ENZ-231

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    Description

    PHOSPHO2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (1-241) and having a molecular mass of 30.3kDa.PHOSPHO2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHOSPHO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pyridoxal phosphate phosphatase PHOSPHO2, orphan 2 (PHOSPHO2) is a member of the haloacid dehalogenase (HAD) superfamily. Phosphatase has an elevated activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). PHOSPHO 1, a phosphoethanolamine/phosphocholine phosphatase, is upregulated in mineralizing cells and is believed to be implicated in the production of inorganic phosphate for bone mineralization. PHOSPHO2 is a recognized phosphatase sharing a 42% sequence identity with PHOSPHO1. PHOSPHO1 and PHOSPHO2 are especially similar, however surprisingly recombinant PHOSPHO2 hydrolyses phosphoethanolamine and phosphocholine comparatively inadequately.

    • Synonyms

      Pyridoxal phosphate phosphatase PHOSPHO2, PHOSPHO2.

    • 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 MGSHMKILLV FDFDNTIIDD NSDTWIVQCA PNKKLPIELR DSYRKGFWTE FMGRVFKYLG DKGVREHEMK RAVTSLPFTP GMVELFNFIR KNKDKFDCII ISDSNSVFID WVLEAASFHD IFDKVFTNPA AFNSNGHLTV ENYHTHSCNR CPKNLCKKVV
      LIEFVDKQLQ QGVNYTQIVY IGDGGNDVCP VTFLKNDDVA MPRKGYTLQK TLSRMSQNLE PMEYSVVVWS SGVDIISHLQ FLIKD.

    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.

    Phospho2 Human
  • View Data Sheet

    Name :

    SERPINI1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade I Member 1 Human Recombinant

    Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    Product # :

    PRO-213

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    Description

    SERPINI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 394 amino acids and having a total molecular mass of 44.7kDa. SERPINI1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of rat C6 cells which is less than 0.5µg/ml, corresponding to a specific activity of >2000IU/mg.

    More Info

    • Introduction

      SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).

    • Synonyms

      Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPINI1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPINI1 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 SERPINI1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG
      STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN
      GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL
      VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM
      MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT
      LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF
      IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL
      YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL.

    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.

    Serpini1 Human
  • View Data Sheet

    Name :

    PPIL1 Human

    Description:

    Peptidylprolyl Isomerase (Cyclophilin)-Like 1 Human Recombinant

    Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIL-1, CYPL1, hCyPX, MGC678, PPIase, CGI-124, PPIL1.

    Product # :

    ENZ-388

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    • sds-page

    Description

    PPIL1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-166) and having a molecular mass of 19.3 kDa. PPIL1 is fused to 8 amino acid His Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPIL1 solution 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 > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    sds-page

    PPIL1 Human SDS-PAGE - Product image 1

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    • Introduction

      PPIL1 belongs to the cyclophilin family of peptidylprolyl isomerases (PPIases).
      The cyclophilins are a well conserved, ubiquitous family, members of which take an significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 protein increases the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. PPIL1 is a novel molecular target for colon-cancer therapy.

    • Synonyms

      Peptidyl-Prolyl Cis-Trans Isomerase-Like 1, PPIL-1, CYPL1, hCyPX, MGC678, PPIase, CGI-124, PPIL1.

    • 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

      MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLEHH HHHH.

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

    Ppil1 Human
  • View Data Sheet

    Name :

    POLR2D Human

    Description:

    Polymerase II Polypeptide D Human Recombinant

    HSRBP4, HSRPB4, RBP4, RPB16, DNA-directed RNA polymerase II subunit RPB4, RNA polymerase II subunit B4, DNA-directed RNA polymerase II subunit D, RNA polymerase II 16 kDa subunit, POLR2D.

    Product # :

    ENZ-739

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    Description

    POLR2D 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 18.7kDa.POLR2D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The POLR2D solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Polymerase II Polypeptide D (POLR2D) is a member of the eukaryotic RPB4 RNA polymerase subunit family. POLR2D is the fourth largest subunit of RNA polymerase II. Pol II is the main element of the basal RNA polymerase II transcription machinery. polymerase is responsible forsynthesizing messenger RNA in eukaryotes. In yeast, POLR2D subunit is connected with the polymeraseunder suboptimal growth conditions and might have a stress protective role. POLR2D catalyzes the transcription of DNA into RNA by the 4 ribonucleoside triphosphates as substrates.

    • Synonyms

      HSRBP4, HSRPB4, RBP4, RPB16, DNA-directed RNA polymerase II subunit RPB4, RNA polymerase II subunit B4, DNA-directed RNA polymerase II subunit D, RNA polymerase II 16 kDa subunit, POLR2D.

    • 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 MGSMAAGGSD PRAGDVEEDA SQLIFPKEFE TAETLLNSEV HMLLEHRKQQ NESAEDEQEL SEVFMKTLNY TARFSRFKNR ETIASVRSLL LQKKLHKFEL ACLANLCPET AEESKALIPS LEGRFEDEEL QQILDDIQTK RSFQY.

    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.

    Polr2D Human
  • View Data Sheet

    Name :

    HEV ORF2 (403-461 a.a.)

    Description:

    Hepatitis E Virus ORF2 (403-461 a.a.) Recombinant

    Product # :

    HEV-272

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    Description

    The e.coli derived HEV protein is fused with beta-galactosidase at the N-Terminus and contains the HEV immunodominant regions from ORF2 403-461 a.a.

    Formulation

    20mM Tris-HCl pH-8, 8M urea and 10mM B-ME.

    Purity

    HEV ORF2 Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      Hepatitis E virus (HEV), the major etiologic agent of enterically transmitted non-A, non-B hepatitis worldwide, is a spherical, non-enveloped, single stranded RNA virus that is approximately 32 to 34 nm in diameter. HEV belongs to a genus of HEV-like viruses (unassigned genus). HEV has a single-stranded polyadenylated RNA genome of approximately 8 kb. Based on its physicochemical properties it is presumed to be a calici-like virus.

    • Stability

      HEV ORF2 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HEV ORF2 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HEV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera HEV-infected individuals.

    • Purification Method

      HEV ORF2 was purified by proprietary chromatographic technique.

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

    Hev Orf2 403 461
  • View Data Sheet

    Name :

    NUDT5 Human

    Description:

    Nudix Type Motif 5 Human Recombinant

    hYSAH1, YSA1, YSA1H, ADP-sugar pyrophosphatase, EC=3.6.1.-, EC=3.6.1.13, Nucleoside diphosphate-linked moiety X motif 5, Nudix motif 5, HSPC115.

    Product # :

    ENZ-547

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    Description

    NUDT5 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (1-219 a.a.) and having a molecular mass of 26.5 kDa. The NUDT5 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUDT5 Human 1mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NUDT5 is part of the nudix hydrolase family which remove toxic nucleotide derivatives from the cell. NUDT5 hydrolyzes ADP-ribose and ADP-mannose in the presence of magnesium, and in addition hydrolyzes nucleotide sugars with decreasing activity such as ADP-glucose and diadenosine diphosphate. As a nudix hydrolase, NUDT5 holds a central nudix motif and functions to eliminate toxic nucleotide metabolites from the cell while maintaining the levels of signaling nucleotides.
      NUDT5 is broadly expressed but is most abundant in liver as a homodimer.

    • Synonyms

      hYSAH1, YSA1, YSA1H, ADP-sugar pyrophosphatase, EC=3.6.1.-, EC=3.6.1.13, Nucleoside diphosphate-linked moiety X motif 5, Nudix motif 5, HSPC115.

    • 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 MESQEPTESS QNGKQYIISE ELISEGKWVK LEKTTYMDPT GKTRTWESVK RTTRKEQTAD GVAVIPVLQR TLHYECIVLV KQFRPPMGGY CIEFPAGLID DGETPEAAAL RELEEETGYK GDIAECSPAV CMDPGLSNCT IHIVTVTING DDAENARPKP KPGDGEFVEV ISLPKNDLLQ RLDALVAEEH LTVDARVYSY ALALKHANAK PFEVPFLKF.

    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.

    Nudt5 Human
  • View Data Sheet

    Name :

    Placental Lactogen Bovine

    Description:

    Placental Lactogen Bovine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    Product # :

    CYT-511

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    Description

    Placental Lactogen Bovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Placental Lactogen Bovine is biologically active as evidenced by inducing proliferation of Nb2 cells.

    More Info

    • Introduction

      Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
      Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Glu-Asp-Tyr-Ala-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.86 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8. This value is calculated by the DNAman computer analysis program of protein sequences.

    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.

    Placental Lactogen Bovine
  • View Data Sheet

    Name :

    BMP 7 Human, HEK

    Description:

    Bone Morphogenetic protein-7 Human Recombinant, HEK

    Osteogenic Protein 1, BMP-7.

    Product # :

    CYT-082

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    Description

    BMP-7 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 30-38kDa due to glycosylation.The BMP7 corresponds to amino acid residues 315 to 431 of the full-length BMP-7 precursor and is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The BMP7 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

    More Info

    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

    • Synonyms

      Osteogenic Protein 1, BMP-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-7 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 BMP-7 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.

    • Background

      BMP-7 Bone Morphogenetic Protein-7 Human Recombinant: A Key Regulator of Osteogenesis and Beyond

      Abstract:

      BMP-7 (Bone Morphogenetic Protein-7), also known as Osteogenic Protein 1 or BMP-7, is a potent growth factor that plays a crucial role in various biological processes, particularly in osteogenesis and tissue regeneration.

      This research paper aims to comprehensively explore the molecular characteristics, signaling pathways, and diverse physiological functions of BMP-7.

      Additionally, it investigates the therapeutic implications of BMP-7 in different disorders. Synonyms such as Osteogenic Protein 1 and BMP-7 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a growth factor with multifaceted roles in osteogenesis, tissue regeneration, and disease. This section introduces BMP-7 and its synonyms, highlighting their significance and relevance in scientific research.

      Molecular Characteristics of BMP-7:

      This section explores the molecular characteristics of BMP-7, including its primary amino acid sequence, protein structure, post-translational modifications, and binding partners. The importance of these factors in determining BMP-7's biological activity and receptor specificity is discussed.

      Signaling Pathways Activated by BMP-7 :

      BMP-7 activates specific signaling pathways upon binding to its receptors, leading to diverse cellular responses. This section focuses on the canonical BMP signaling pathway, highlighting the activation of Smad-dependent and Smad-independent pathways. The downstream effectors and transcriptional regulators involved in mediating BMP-7's cellular responses are also discussed.

      Physiological Functions of BMP-7 :

      BMP-7 plays critical roles in various physiological processes, particularly in osteogenesis and tissue regeneration. This section provides an in-depth analysis of BMP-7's contributions to these processes, emphasizing its role in promoting bone formation, cartilage development, renal function, and wound healing.

      Therapeutic Implications of BMP-7 :

      The unique properties of BMP-7 make it a promising therapeutic candidate for various disorders. This section discusses the potential applications of BMP-7 in bone regeneration, cartilage repair, kidney disease, and tissue engineering. The challenges and future directions in utilizing BMP-7 as a therapeutic agent are also explored.

      BMP-7 in Disease Progression:

      BMP-7 is implicated in the progression of certain diseases, including fibrosis, cancer, and cardiovascular disorders. This section examines the role of BMP-7 in tissue fibrosis, tumor progression, angiogenesis, and cardiac remodeling. The therapeutic implications and targeting of BMP-7 in disease management are also discussed.

      Conclusion:

      BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a critical growth factor involved in osteogenesis, tissue regeneration, and disease progression. Understanding the molecular characteristics, signaling pathways, and physiological functions of BMP-7 contributes to the exploration of its therapeutic potential in various disorders.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 38kDa.

      What is the source or expression system of BMP7 Protein?
      HEK.

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

      What is the amino acid sequence of BMP7 Protein?
      DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.


      What applications can BMP7 Protein be used in?
      BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP7 Protein?
      The endotoxin level is minimal, BMP7 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.

    Bmp 7 Human Hek
  • View Data Sheet

    Name :

    MMLV RT

    Description:

    Moloney Murine Leukemia Virus Reverse Trancscriptase Recombinant

    Product # :

    ENZ-310

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    Description

    MMLV (Moloney Murine Leukemia Virus) Reverse Transcriptase is a DNA polymerase that synthesizes a complementary DNA strands from single-stranded RNA, DNA, or an RNA-DNA hybrid as a template. This recombinant enzyme was purified from E.coli, which carried a modified MMLV-RT gene. Compared to AMV Reverse Transcriptase, this enzyme has a much weaker 5' - 3' ribonuclease H activity, which allows the syntesis of longer cDNAs (>7kb).

    Source

    Recombinant E. coli strain.

    Formulation

    50mM Tris-HCl, 0.1M NaCl, 0.1% Triton X-100, 2mM DTT, 0.1mM EDTA and 50% glycerol.

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    • Physical Appearance

      Sterile Filtered clear solution (200 U/µl).

    • Stability

      Stable for 5 days at 10°C, for longer period of time store at -20°C. Please prevent freeze-thaw cycles.

    • Unit Definition

      One unit is defined as the amount of enzyme required to catalyze the incorporation of 1nmol of deoxyribonucleotide into acid-insoluble forms in 10 minutes at 37oC, using poly(A)-oligo(dT)12-18 as the template-primer. Standard cDNA Synthesis Conditions50mM Tris-HCl (pH8.3), 75mM KCl, 3mM MgCl2, 10mM DTT, 1.0mM each dATP, dGTP, dCTP, and dTTP, 0.2 mg radom hexamer,1-5mg RNA, 200units M-MLV RT. The reaction volume was 20ml and the incubation was 45 min at 42oC.

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    M Mlv Reverse Transcriptase
  • View Data Sheet

    Name :

    IDS Antibody

    Description:

    Iduronate 2-Sulfatase, Mouse Anti Human

    Iduronate 2-Sulfatase, Alpha-L-Iduronate Sulfate Sulfatase, Idursulfase, SIDS, Iduronate 2-Sulfatase 14 KDa Chain, Iduronate 2-Sulfatase 42 KDa Chain, Hunter Syndrome, EC 3.1.6.13, MPS2, Iduronate 2-sulfatase, Alpha-L-iduronate sulfate sulfatase, Idursulfase.

    Product # :

    ANT-745

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    Formulation

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

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    • Introduction

      Iduronate 2-Sulfatase also known as IDS, belongs to the highly-conserved sulfatase family of enzymes which catalyze the hydrolysis of O-sulfate and N-salfate esters from a variety of substrates. IDS is essential for the lysosomal degradation of the glycosaminoglycans (GAG) heparan sulfate as well as dermatan sulfate. Furthermore, IDS hydrolyzes the 2-sulfate group of the IDS units of the GAG.

    • Synonyms

      Iduronate 2-Sulfatase, Alpha-L-Iduronate Sulfate Sulfatase, Idursulfase, SIDS, Iduronate 2-Sulfatase 14 KDa Chain, Iduronate 2-Sulfatase 42 KDa Chain, Hunter Syndrome, EC 3.1.6.13, MPS2, Iduronate 2-sulfatase, Alpha-L-iduronate sulfate sulfatase, Idursulfase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human IDS mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IDS protein 26-550 amino acids purified from insect cell.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT6H4AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis and FACS analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

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

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

    Ids Antibody
  • View Data Sheet

    Name :

    GAPDH Mouse

    Description:

    GAPDH Mouse Recombinant

    Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, Gapdh, Gapd, Glyceraldehyde-3-phosphate dehydrogenase isoform 2, G3PD, GAPD, HEL-S-162eP.

    Product # :

    ENZ-860

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    Description

    GAPDH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 356 amino acids (1-333a.a.) and having a molecular mass of 38.2kDa.GAPDH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GAPDH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GAPDH is a catalytic enzyme normally known to play a role in glycolysis. GAPDH exists as a tetramer composed of 36-kDa subunits and has a range of intracellular functions. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Besides functioning as a glycolytic enzyme in cytoplasm, GAPDH has function in intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and DNA repair. GAPDH catalyzes a vital energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains.

    • Synonyms

      Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, Gapdh, Gapd, Glyceraldehyde-3-phosphate dehydrogenase isoform 2, G3PD, GAPD, HEL-S-162eP.

    • 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 MGSMVKVGVN GFGRIGRLVT RAAICSGKVE IVAINDPFID LNYMVYMFQY DSTHGKFNGT VKAENGKLVI NGKPITIFQE RDPTNIKWGE AGAEYVVEST GVFTTMEKAG AHLKGGAKRV IISAPSADAP MFVMGVNHEK YDNSLKIVSN ASCTTNCLAP LAKVIHDNFG IVEGLMTTVH AITATQKTVD GPSGKLWRDG RGAAQNIIPA STGAAKAVGK VIPELNGKLT GMAFRVPTPN VSVVDLTCRL EKPAKYDDIK KVVKQASEGP LKGILGYTED QVVSCDFNSN SHSSTFDAGA GIALNDNFVK LISWYDNEYG YSNRVVDLMA YMASKE.

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    Gapdh Mouse
  • View Data Sheet

    Name :

    Flavokinase Human

    Description:

    Riboflavin Kinase Human Recombinant

    Riboflavin kinase, ATP:riboflavin 5'-phosphotransferase, Flavokinase, RFK, RIFK, FLJ11149, RP11-422N19.2.

    Product # :

    PKA-352

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    Description

    Flavokinase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids (1-162 a.a.) and having a molecular mass of 20.5kDa. Flavokinase is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Flavokinase solution containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Flavokinase is a transferases family member, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. Flavokinase is an enzyme that catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), which is an obligatory step in vitamin B2 utilization and flavin cofactor synthesis. It has been proposed that TNF, through the activation of the RFK gene, enhances the incorporation of FAD in NADPH oxidase enzymes, which is a critical step for the assembly and activation of NADPH oxidase.

    • Synonyms

      Riboflavin kinase, ATP:riboflavin 5'-phosphotransferase, Flavokinase, RFK, RIFK, FLJ11149, RP11-422N19.2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Flavokinase although stable at 4°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPRADCIMRH LPYFCRGQVV RGFGRGSKQL GIPTANFPEQ VVDNLPADIS TGIYYGWASV GSGDVHKMVV SIGWNPYYKN TKKSMETHIM HTFKEDFYGE ILNVAIVGYL RPEKNFDSLE SLISAIQGDI EEAKKRLELP EHLKIKEDNF FQVSKSKIMNGH.

    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.

    Flavokinase Human
  • View Data Sheet

    Name :

    Uricase

    Description:

    Urate Oxidase Recombinant

    Urate Oxidase, Uricase, Urate Oxygen, Oxidoreductase, UOX, UO, EC 1.7.3.

    Product # :

    ENZ-312

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    Description

    Urate Oxidase Recombinant produced in E.Coli is a tetrameric, non-glycosylated polypeptide chain containing 302 amino acids, having a molecular formula of C1523H2383N417O462S7 and a molecular mass of 34,247 Dalton.The cDNA coding for urate-oxidase was cloned from a strain of Aspergillus flavus . The monomer protein has no intra- or inter-disulfide bridges.

    Source

    Escherichia Coli.

    Formulation

    Each 1.5mg Uricase contains 5mg sucrose, 25mg glycine, 0.1mg Tween-80, 13.6 mg Na2HPO4*12H20 and 0.33 mg NaH2PO4*2H20.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 10U/mg.
    One Unit oxidizes one micromole of uric acid per minute at 25°C, at pH 8.5.

    More Info

    • Introduction

      Urate oxidase catalyzes the enzymatic oxidation (degrades) of uric acid into allantoin, an inactive and soluble metabolite, which is 5 to 10 fold more soluble than uric acid . Urate oxidase is an enzyme of the purine breakdown pathway that catalyses the oxidation of uric acid to allantoin. Uricase is present in numerous diverse organisms, but not in higher primates including human. Hyperuricaemia is most commonly associated with gout and also occurs in mammalians with malignancy, especially those with lymphoid malignancies due to rapid cell turnover and an increased rate of purine metabolism. Uricase is effective in the prevention and treatment of hyperuricaemia in mammalians with malignancy and in those who have undergone transplantation. It appears to act rapidly, safely and induces a more dramatic decrease in plasma levels of uric acid.

    • Synonyms

      Urate Oxidase, Uricase, Urate Oxygen, Oxidoreductase, UOX, UO, EC 1.7.3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Urate Oxidase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Uricase should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      We highly recommend reconstituting the lyophilized Uricase in 50mM borate buffer containing 0.001%Triton X-100 and 1.0mM EDTA, pH 8.5 for activity assay.

    • Amino Acid Sequence

      msavkaaryg kdnvrvykvh kdektgvqtv yemtvcvlle geietsytka dnsvivatds ikntiyitak qnpvtppelf gsilgthfie kynhihaahv nivchrwtrm didgkphphs firdseekrn vqvdvvegkg idiksslsgl tvlkstnsqf wgflrdeytt lketwdrils tdvdatwqwk nfsglqevrs hvpkfdatwa tarevtlktf aednsasvqa tmykmaeqil arqqlietve yslpnkhyfe idlswhkglq ntgknaevfa pqsdpnglik ctvgrsslks kl.

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    Urate Oxidase
  • View Data Sheet

    Name :

    PRSS22 Mouse

    Description:

    Protease Serine 22 Mouse Recombinant

    Brain-specific serine protease 4, Prss22, 4733401N09Rik, BSSP-4, SP001LA, Serine protease 22, Serine protease 26, Tryptase epsilon, Bssp4, Prss26.

    Product # :

    ENZ-964

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    Description

    PRSS22 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 283 amino acids (33-307) and having a molecular mass of 31.1kDa.PRSS22 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PRSS22 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protease Serine 22 also known as Prss22 is identified brain-specific expression gene which is expressed mainly in epitheliumrich tissues such as the lung and eye. Prss22 encodes to a serine protease which called BSSP-4 or BSP-2.

    • Synonyms

      Brain-specific serine protease 4, Prss22, 4733401N09Rik, BSSP-4, SP001LA, Serine protease 22, Serine protease 26, Tryptase epsilon, Bssp4, Prss26.

    • 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

      ATIRVSPDCG KPQQLNRIVG GEDSMDAQWP WIVSILKNGS HHCAGSLLTN RWVVTAAHCF KSNMDKPSLF SVLLGAWKLG SPGPRSQKVG IAWVLPHPRY SWKEGTHADI ALVRLEHSIQ FSERILPICL PDSSVRLPPK TDCWIAGWGS IQDGVPLPHP QTLQKLKVPI IDSELCKSLY WRGAGQEAIT EGMLCAGYLE GERDACLGDS GGPLMCQVDD HWLLTGIISW GEGCAERNRP GVYTSLLAHR SWVQRIVQGV QLRGYLADSG DTGSSLEHHH HHH.

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    Prss22 Mouse
  • View Data Sheet

    Name :

    MAOA Human

    Description:

    Monoamine Oxidase A Human Recombinant

    Monoamine Oxidase A, Monoamine Oxidase Type A, EC 1.4.3.4, MAO-A, Amine Oxidase [Flavin-Containing] A, EC 1.4.3, Amine oxidase [flavin-containing] A, Monoamine oxidase type A.

    Product # :

    ENZ-866

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    Description

    MAOA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 520 amino acids (1-497 a.a) and having a molecular mass of 58.8kDa. MAOA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 80% as determined by SDS-PAGE.

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    • Introduction

      Monoamine Oxidase A, also known as MAOA catalyzes the oxidative deamination of biogenic as well as xenobiotic amines and has significant functions in the metabolism of neuroactive and vasoactive amines in the central nervous system as well as peripheral tissues. Mutation in MAOA results in Brunner syndrome; in addition MAOA has also been linked with a diversity of other psychiatric disorders, which includes antisocial behavior. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT).

    • Synonyms

      Monoamine Oxidase A, Monoamine Oxidase Type A, EC 1.4.3.4, MAO-A, Amine Oxidase [Flavin-Containing] A, EC 1.4.3, Amine oxidase [flavin-containing] A, Monoamine oxidase type A.

    • 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 MGSMENQEKA SIAGHMFDVV VIGGGISGLS AAKLLTEYGV SVLVLEARDR VGGRTYTIRN EHVDYVDVGG AYVGPTQNRI LRLSKELGIE TYKVNVSERL VQYVKGKTYP FRGAFPPVWN PIAYLDYNNL WRTIDNMGKE IPTDAPWEAQ HADKWDKMTM KELIDKICWT KTARRFAYLF VNINVTSEPH EVSALWFLWY VKQCGGTTRI FSVTNGGQER KFVGGSGQVS ERIMDLLGDQ VKLNHPVTHV DQSSDNIIIE TLNHEHYECK YVINAIPPTL TAKIHFRPEL PAERNQLIQR LPMGAVIKCM MYYKEAFWKK KDYCGCMIIE DEDAPISITL DDTKPDGSLP AIMGFILARK ADRLAKLHKE IRKKKICELY AKVLGSQEAL HPVHYEEKNW CEEQYSGGCY TAYFPPGIMT QYGRVIRQPV GRIFFAGTET ATKWSGYMEG AVEAGERAAR EVLNGLGKVT EKDIWVQEPE SKDVPAVEIT HTFWERNLPS.

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    Maoa Human
  • View Data Sheet

    Name :

    SPINK1 Human

    Description:

    Serine Peptidase Inhibitor Kazal Type 1 Human Recombinant

    Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.

    Product # :

    ENZ-724

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    Description

    SPINK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 79 amino acids (24-79) and having a molecular mass of 8.6kDa.SPINK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPINK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Trypsin inhibitor SPINK1 is secreted from pancreatic acinar cells into pancreatic fluid. SPINK1 has a role in inhibition of trypsin-catalyzed premature initiation of zymogens in the pancreas and the pancreatic duct. Alterations in SPINK1 gene are the cause for tropical calcific and pancreatitis hereditary pancreatitis.

    • Synonyms

      Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.

    • 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 MGSDSLGREA KCYNELNGCT KIYDPVCGTD GNTYPNECVL CFENRKRQTS ILIQKSGPC.

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    Spink1 Human
  • View Data Sheet

    Name :

    HBsAgA Antibody

    Description:

    Hepatitis B surface Antigen A, Polyclonal Goat Antibody

    Product # :

    ANT-163

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    Description

    Affinity-purified Goat antibodies against the Native Ad/AyHBsAg antigens.1mg/ml in PBS, was passed through a 0.2um Filter into a 50ml sterile conic Tube.

    Formulation

    (1ml) PBS.

    More Info

    • Introduction

      Hepatitis B is one of a few known non-retroviralviruses which employ reverse transcriptionas a part of its replication process. (HIV, a completely unrelated virus, also uses reverse transcription, but it is a retrovirus.) HBV invades the cell by binding to surface receptor and become internalized. The viral core particles then migrate to the hepatocyte nucleus and the partially double-stranded, relaxed circular genomes (RC-DNA) are repaired to form a covalently closed circular DNA (cccDNA), which is the template for viral genomic and sub-genomic RNAs by cellular RNA polymerase II. Of these, the pregenomic RNA (pgRNA is selectively packaged into progeny capsids and is then reverse-transcribed into new RC-DNA. The core can either bud into the endoplasmic reticulum to be enveloped or exported from the cell or recycled back into the genome for conversion to cccDNA.

    • Physical Appearance

      Sterile Filtered solution.

    • Host

      Rabbit.

    • Specificity

      Immunoreactive with all HBsAg A antigens. Direct ELISA shows signal above cut-off at antibody levels of 100ng/test and above.

    • Type

      Polyclonal Goat Antibody.

    • Storage Procedures

      Store at -20°C.

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    HBsAgA Antibody
  • View Data Sheet

    Name :

    Myc-HRP Antibody

    Description:

    Myc, Mouse Antibody Peroxidase Conjugated

    MYC, CMYC, C-MYS, V-MYC, P64.

    Product # :

    ANT-224

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    Description

    Monoclonal antibodies are produced by immunizing mouse with synthetic peptide (EQKLISEEDL) coupled to KLH.

    Formulation

    1×PBS & 50% glycerol.

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    • Introduction

      c-Myc is a multifunctional, nuclear phosphoprotein that plays a role in cell cycle progression, apoptosis and cellular transformation. It functions as a transcription factor that regulates transcription of specific target genes. Mutations, overexpression, rearrangement and translocation of c-Myc have been associated with a variety of hematopoietic tumors, leukemias and lymphomas, including Burkitt lymphoma. There is evidence to show that alternative translation initiations from an upstream, in-frame non-AUG (CUG) and a downstream AUG start site result in the production of two isoforms with distinct N-termini. The synthesis of non-AUG initiated protein is suppressed in Burkitt's lymphomas, suggesting its importance in the normal function of this gene.

    • Synonyms

      MYC, CMYC, C-MYS, V-MYC, P64.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      PMYCHRPSHG.

    • Applications

      Western Blot.

    • Titer

      Western Blotting, 1:1000.

    • Type

      Mouse Antibody Monoclonal.

    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.

    Myc Hrp Antibody
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