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Search results

1000 results found for “Heparanase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    AMT Human

    Description:

    Aminomethyltransferase Human Recombinant

    GCE, GCST, GCVT, NKH, Aminomethyltransferase, mitochondrial, Glycine cleavage system T protein, GCVT.

    Product # :

    ENZ-900

    Price :

    Quantity :

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    Description

    AMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (29-403 a.a) and having a molecular mass of 43.3kDa.AMT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AMT protein solution (1mg/ml) in Phosphate Buffered Saline, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aminomethyltransferase, mitochondrial isoform 1 (AMT) is a component of the glycine cleavage system termed T-protein. AMT reversibly catalyzes the degradation of the aminomethyl moiety of glycine attached to the lipoate cofactor of H-protein, leading to the production of ammonia, 5,10-methylenetetrahydrofolate, and dihydrolipoate-bearing H-protein in the presence of tetrahydrofolate.

    • Synonyms

      GCE, GCST, GCVT, NKH, Aminomethyltransferase, mitochondrial, Glycine cleavage system T protein, GCVT.

    • 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 MGSAQEVLRR TPLYDFHLAH GGKMVAFAGW SLPVQYRDSH TDSHLHTRQH CSLFDVSHML QTKILGSDRV KLMESLVVGD IAELRPNQGT LSLFTNEAGG ILDDLIVTNT SEGHLYVVSN AGCWEKDLAL MQDKVRELQN QGRDVGLEVL DNALLALQGP TAAQVLQAGV ADDLRKLPFM TSAVMEVFGV SGCRVTRCGY TGEDGVEISV PVAGAVHLAT AILKNPEVKL AGLAARDSLR LEAGLCLYGN DIDEHTTPVE GSLSWTLGKR RRAAMDFPGA KVIVPQLKGR VQRRRVGLMC EGAPMRAHSP ILNMEGTKIG TVTSGCPSPS LKKNVAMGYV PCEYSRPGTM LLVEVRRKQQ MAVVSKMPFV PTNYYTLK.

    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.

    Amt Human
  • View Data Sheet

    Name :

    PLA2G2E Human

    Description:

    Secreted Phospholipase A2-IIE Human Recombinant

    Group IIE secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIIE, GIIE sPLA2, sPLA(2)-IIE, sPLA2-IIE, PLA2G2E.

    Product # :

    ENZ-327

    Price :

    Quantity :

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    Description

    Secreted Phospholipase A2-IIE Human Recombinant manufactured with N-terminal His-Tag. PLA2G2E His-Tagged Fusion Protein is 15.8 kDa protein containing 123 amino acid residues of the human secreted phospholipase A2-IIE and 16 additional amino acid residues – His-Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered 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

      Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
      The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular 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.This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso-PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
      In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.

    • Synonyms

      Group IIE secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIIE, GIIE sPLA2, sPLA(2)-IIE, sPLA2-IIE, PLA2G2E.

    • Physical Appearance

      Sterile Filtered 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 0.2 ml of 0.1M Acetate buffer pH-4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10 μg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMNLVQ FGVMIEKMTG KSALQYNDYG CYCGIGGSHW PVDQTDWCCH AHDCCYGRLE KLGCEPKLEK YLFSVSERGI FCAGRTTCQR LTCECDKRAA LCFRRNLGTY NRKYAHYPNK LCTGPTPPC

    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.

    Pla2G2E Human
  • View Data Sheet

    Name :

    UNG Heat Labile

    Description:

    Recombinant Psychrophilic Marine Bacterium Uracil DNA Glycosylase, Heat Labile

    UDG, b2580, JW2564, EC 3.2.2.27, DGU, UNG15, HIGM5, Uracil-DNA Glycosylase 1, EC 3.2.2, HIGM4, UNG2.

    Product # :

    ENZ-1183

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    UNG psychrophilic marine bacterium Recombinant produced in E.Coli is a single, non-glycosylated polypeptide. UNG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UNG protein solution (1U/ul) 20mM Tris-HCl (25℃, pH 8.0), 100mM KCl, 0.1mM EDTA, 1mM DTT, 0.5% NP-40, 0.5% Tween-20 and 50% glycerol.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      E. coli UDG is a valuable tool in molecular biology research for its ability to remove uracil from DNA templates. This enzyme is widely used in various applications, including site-directed mutagenesis, PCR amplification, and sequencing. UDG can remove uracil from the template strand of a DNA duplex, enabling the introduction of specific mutations or the creation of nicked DNA for downstream applications. Additionally, UDG is used in PCR amplification to prevent the amplification of any residual uracil-containing templates, which can lead to false-positive results. UDG has also been used in sequencing applications to remove uracil from DNA templates before sequencing, improving the accuracy and reliability of the results.

      Conclusion: E. coli UDG is a highly conserved enzyme that plays a crucial role in maintaining genomic integrity by removing uracil from DNA. The crystal structure of E. coli UDG has been extensively studied, revealing the conserved catalytic mechanism and the interaction of the protein with DNA. E. coli UDG is a valuable enzyme with numerous applications in molecular biology research and potential applications in the medical field, such as cancer treatment. More research is needed to fully understand the therapeutic potential of targeting UDG. Overall, E. coli UDG is a valuable enzyme with numerous applications in molecular biology research and potential applications in the medical field.

    • Synonyms

      UDG, b2580, JW2564, EC 3.2.2.27, DGU, UNG15, HIGM5, Uracil-DNA Glycosylase 1, EC 3.2.2, HIGM4, UNG2.

    • 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.

    • Applications

      Treatment of 0.1μg of uracil containing DNA with 1U UDG for 10 min. at 37℃ renders the DNA incapable of being copied by DNA polymerase. The enzyme can be 95% heat killed by incubation at 95℃ for 10 minutes. Since UDG remains partially active following heat treatment at 95℃, it is recommended that uracil glycosylase inhibitor be added to prevent degradation of product DNA. Alternatively, reaction products can be immediately extracted with phenol/chloroform

    • Unit Definition

      1 unit is defined as the amount of enzyme that releases 1 nmol of uracils from the DNA strand (containing dU) within 1 hour at 37°C in the reaction system containing 70mM TrisHCl, pH-7.5, 10mM NaCl, 1mM EDTA and 0.1mg/ml BSA reaction liquid.

    • Specific Activity

      ≥200,000 U/mg.

    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.

    Ung Heat Labile
  • View Data Sheet

    Name :

    EPHX1 Human, Sf9

    Description:

    Epoxide Hydrolase 1 Microsomal Human Recombinant, sf9

    Epoxide hydrolase 1, Epoxide hydratase, Microsomal epoxide hydrolase, Meh, EPHX1, EPHX, EPOX, Epoxide Hydrolase 1 Microsomal, Microsomal Epoxide Hydrolase, EC 3.3.2.9, HYL1

    Product # :

    ENZ-1076

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    EPHX1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 442 amino acids (21-455 a.a.) and having a molecular mass of 51.5kDaEPHX1 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    EPHX1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 50% glycerol,1mM DTT and 0.1M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Epoxide Hydrolase 1 Microsomal (EPHX1) is a vital biotransformation enzyme which transfers epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase plays a role in both activation and detoxification of epoxides. Mutations in EPHX1 trigger preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.

    • Synonyms

      Epoxide hydrolase 1, Epoxide hydratase, Microsomal epoxide hydrolase, Meh, EPHX1, EPHX, EPOX, Epoxide Hydrolase 1 Microsomal, Microsomal Epoxide Hydrolase,
      EC 3.3.2.9, HYL1

    • 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

      MRDKEETLPL EDGWWGPGTR SAAREDDSIR PFKVETSDEE IHDLHQRIDK FRFTPPLEDS CFHYGFNSNY LKKVISYWRN EFDWKKQVEI LNRYPHFKTK IEGLDIHFIH VKPPQLPAGH TPKPLLMVHG WPGSFYEFYK IIPLLTDPKN HGLSDEHVFE VICPSIPGYG FSEASSKKGF NSVATARIFY KLMLRLGFQE FYIQGGDWGS LICTNMAQLV PSHVKGLHLN MALVLSNFST LTLLLGQRFG RFLGLTERDV ELLYPVKEKV FYSLMRESGY MHIQCTKPDT VGSALNDSPV GLAAYILEKF STWTNTEFRY LEDGGLERKF SLDDLLTNVM LYWTTGTIIS SQRFYKENLG QGWMTQKHER MKVYVPTGFS AFPFELLHTP EKWVRFKYPK LISYSYMVRG GHFAAFEEPE LLAQDIRKFL SVLERQHHHH HH.

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

    Ephx1 Protein
  • View Data Sheet

    Name :

    NFNB E.Coli

    Description:

    Dihydropteridine Reductase E.Coli Recombinant

    DPRA, NFSB, NFSI, NTR.

    Product # :

    ENZ-423

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    Description

    NFNB Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular mass of 26 kDa. The NFNB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.05M NaCl & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NFNB demonstrates the capability to reduce quinines. NFNB enzyme activates prodrugs in antibody directed enzyme prodrug therapy. NFNB reduces nitrofurazone, quinones and anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.

    • Synonyms

      DPRA, NFSB, NFSI, NTR.

    • 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 MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD QEDADGRFAT PEAKAANDKG RKFFADMHRK DLHDDAEWMA KQVYLNVGNF LLGVAALGLD AVPIEGFDAA ILDAEFGLKE KGYTSLVVVP VGHHSVEDFN ATLPKSRLPQ NITLTEV.

    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.

    Nfnb Ecoli
  • View Data Sheet

    Name :

    GNMT Human

    Description:

    Glycine N-methyltransferase Human Recombinant

    Glycine N-methyltransferase, GNMT.

    Product # :

    ENZ-386

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    Description

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

    Source

    Escherichia Coli.

    Formulation

    The GNMT solution contains 20mM Tris pH 8.0 & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine. 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 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.

    • 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
  • View Data Sheet

    Name :

    Cyclophilin B Human

    Description:

    Cyclophilin-B Human Recombinant

    Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.

    Product # :

    ENZ-313

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    Description

    Cyclophilin-B Human Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 192 amino acids (26-216) and having a molecular mass of 21.2 kDa. PPIB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml solution containing 20mM Tris-HCl 8.0, 20mM NaCl, 0.5mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 220 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.

    More Info

    • Introduction

      Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.

    • Synonyms

      Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.

    • 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

      MLLPGPSAAD EKKKGPKVTV KVYFDLRIGD EDVGRVIFGL FGKTVPKTVD NFVALATGEKGFGYKNSKFH RVIKDFMIQG GDFTRGDGTG GKSIYGERFP DENFKLKHYG PGWVSMANAGKDTNGSQFFI TTVKTAWLDG KHVVFGKVLE GMEVVRKVES TKTDSRDKPL KDVIIADCGK IEVEKPFAIA KE.

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    Cyclophilin B Human
  • View Data Sheet

    Name :

    TPST1 Human

    Description:

    Tyrosylprotein Sulfotransferase 1 Human Recombinant

    Tyrosylprotein Sulfotransferase 1, EC 2.8.2.20, TPST-1, Transport And Golgi Organization 13 Homolog A (Drosophila), Transport And Golgi Organization 13 Homolog A, Protein-Tyrosine Sulfotransferase 1, Tyrosylprotein Sulfotransferase-1, TANGO13A, TPST1.

    Product # :

    ENZ-892

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    Description

    TPST1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 369 amino acids (26-370 a.a) and having a molecular mass of 42kDa.TPST1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPST1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosylprotein Sulfotransferase 1, also known as TPST1 is the enzyme which catalyzes the sulfation reaction of protein tyrosines, a post-translational modification of proteins. TPST1 belongs to the protein sulfotransferase family. In addition, TPST1 utilizes 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfonate donor and also binds proteins with target tyrosineresidues to eventually form the tyrosine O-sulfate ester group in addition to the desulfonated 3’-phosphoadenosine-5’-phosphate.

    • Synonyms

      Tyrosylprotein Sulfotransferase 1, EC 2.8.2.20, TPST-1, Transport And Golgi Organization 13 Homolog A (Drosophila), Transport And Golgi Organization 13 Homolog A, Protein-Tyrosine Sulfotransferase 1, Tyrosylprotein Sulfotransferase-1, TANGO13A, TPST1.

    • 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 TGSMQHAMEC HHRIEERSQP VKLESTRTTV RTGLDLKANK TFAYHKDMPL IFIGGVPRSG TTLMRAMLDA HPDIRCGEET RVIPRILALK QMWSRSSKEK IRLDEAGVTD EVLDSAMQAF LLEIIVKHGE PAPYLCNKDP FALKSLTYLS RLFPNAKFLL MVRDGRASVH SMISRKVTIA GFDLNSYRDC LTKWNRAIET MYNQCMEVGY KKCMLVHYEQ LVLHPERWMR TLLKFLQIPW NHSVLHHEEM IGKAGGVSLS KVERSTDQVI KPVNVGALSK WVGKIPPDVL QDMAVIAPML AKLGYDPYAN PPNYGKPDPK IIENTRRVYK GEFQLPDFLK EKPQTEQVE.

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    Tpst1 Human
  • View Data Sheet

    Name :

    PSMA3 Human

    Description:

    Proteasome Subunit Alpha Type 3 Human Recombinant

    proteasome (prosome, macropain) subunit alpha type-3, HC8, Macropain subunit C8, Multicatalytic endopeptidase complex subunit C8, Proteasome component C8, PSC3, PSC8, EC 3.4.25.1.

    Product # :

    ENZ-196

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    Description

    PSMA3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 275 amino acids (1-255) and having a molecular mass of 30.6 kDa.PSMA3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PSMA3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      The proteasome is a multicatalytic proteinase complex which holds an extremely organized 20S core structure shaped like a ring. The central structure is assembled from 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. There is a high concentration of proteasomes all over the eukaryotic cells and their job is to cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway. PSMA3 encodes several of the peptidase T1A family which is a 20S core alpha subunit. Two alternative transcripts encoding diverse isoforms were recognized.

    • Synonyms

      proteasome (prosome, macropain) subunit alpha type-3, HC8, Macropain subunit C8, Multicatalytic endopeptidase complex subunit C8, Proteasome component C8, PSC3, PSC8, EC 3.4.25.1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL QMKEMTCRDI VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA KESLKEEDES DDDNM

    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.

    Psma3 Human
  • View Data Sheet

    Name :

    REXO2 Human

    Description:

    RNA Exonuclease 2 Human Recombinant

    REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.

    Product # :

    ENZ-715

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    Description

    REXO2 Human Recombinant produced in E. coli is a single polypeptide chain containing 235 amino acids (26-237) and having a molecular mass of 26.8kDa. REXO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The REXO2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      EXO2 is a 3'-to-5' exonuclease specific for small (primarily 5 nucleotides or less in length) single-stranded RNA and DNA oligomers. RNA Exonuclease 2 (REXO2) takes part in DNA repair, replication, and recombination, and in RNA processing and degradation. EXO2 is involved in resistance of human cells to UV-C-induced cell death via its part in the DNA repair process.

    • Synonyms

      REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.

    • 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 MGSVREGGAA MAAGESMAQR MVWVDLEMTG LDIEKDQIIE MACLITDSDL NILAEGPNLI IKQPDELLDS MSDWCKEHHG KSGLTKAVKE STITLQQAEY EFLSFVRQQT PPGLCPLAGN SVHEDKKFLD KYMPQFMKHL HYRIIDVSTV KELCRRWYPE EYEFAPKKAA SHRALDDISE SIKELQFYRN NIFKKKIDEK KRKIIENGEN EKTVS.

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    Rexo2 Human
  • View Data Sheet

    Name :

    TIMP1 Human, HEK

    Description:

    Tissue Inhibitor of Metalloprotease 1 Human Recombinant, HEK

    Metalloproteinase inhibitor 1, Tissue inhibitor of metalloproteinases, TIMP-1, Erythroid-potentiating activity, EPA, TIMP1, CLGI, TIMP, EPO, HCI, FLJ90373.

    Product # :

    ENZ-508

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    Description

    TIMP1 Human Recombinant produced in HEK-293 cells is a secreted protein with the sequence of Human TIMP-1 (amino acids Cys24-Ala207) and fused to a polyhistidine tag at the C-terminus.

    Source

    HEK293 Cells.

    Formulation

    The TIMP1 protein was lyophilized after extensive dialysis against PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The IC50 of 2.5-4 nM is measured by its ability to inhibit recombinant human MMP-2 cleavage of the colorimetric peptide substrate, Mca-PLGL-DpaAR-NH2.

    More Info

    • Introduction

      TIMP1 is a member of the TIMP family. TIMP1 is an inducible glycoprotein produced by various cell types. The TIMP1 glycoprotein is a natural inhibitor of the matrix metalloproteinases, which a group of peptidases involved in degradation of the extracellular matrix. TIMP1 binds in a reversible mode to MMPs, with regions in the N-terminal domain binding to the MMP substrate-binding site. On top of its inhibitory function against most of the known MMPs, TIMP1 is able to promote cell proliferation in a broad range of cell types, and may also have an anti-apoptotic role. Furthermore, TIMP1 has erthyroid-potentiating activity via translocation to the nucleus and also inhibits apoptosis in B-cells. The TIMP1 gene is situated within intron 6 of the synapsin I gene and is transcribed in the opposite direction. TIMP1 activity is dependent on the existence of disulfide bonds. TIMP1 transcription is extremely inducible in reaction to many cytokines and hormones. Increased TIMP1 levels are connecte

    • Synonyms

      Metalloproteinase inhibitor 1, Tissue inhibitor of metalloproteinases, TIMP-1, Erythroid-potentiating activity, EPA, TIMP1, CLGI, TIMP, EPO, HCI, FLJ90373.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TIMP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TIMP1 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 TIMP1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Timp1 Hek
  • View Data Sheet

    Name :

    SERPINB2 Human, His

    Description:

    Serpin Peptidase Inhibitor, Clade B Member 2 Human Recombinant, His Tag

    Plasminogen activator inhibitor 2, PAI-2, Plasminogen activator inhibitor 2, SERPINB2, Serpin Peptidase Inhibitor, Clade B Member 2, His Tag, PLANH2, Monocyte Arg-serpin, Placental plasminogen activator inhibitor, Serpin B2, Urokinase inhibitor, HsT1201, PAI, PAI2.

    Product # :

    PRO-2103

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    Description

    SERPINB2 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 438 amino acids (1-415 a.a.) and having a molecular mass of 49kDa.SERPINB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SERPINB2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

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    • Introduction

      SERPINB2 is an inhibitory serpin produced primarily in keratinocytes, stimulated monocytes, and placental trophoblasts. SERPINB2 is found primarily as a 47 kDa non-glycosylated intracellular protein that is induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated SERPINB2 are similarly effective as inhibitors of urokinase-type plasminogen activator (uPA), the only proven physiological target of SERPINB2.

    • Synonyms

      Plasminogen activator inhibitor 2, PAI-2, Plasminogen activator inhibitor 2, SERPINB2, Serpin Peptidase Inhibitor, Clade B Member 2, His Tag, PLANH2, Monocyte Arg-serpin, Placental plasminogen activator inhibitor, Serpin B2, Urokinase inhibitor, HsT1201, PAI, PAI2.

    • 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 MGSMEDLCVA NTLFALNLFK HLAKASPTQN LFLSPWSISS TMAMVYMGSR GSTEDQMAKV LQFNEVGANA VTPMTPENFT SCGFMQQIQK GSYPDAILQA QAADKIHSSF RSLSSAINAS TGNYLLESVN KLFGEKSASF REEYIRLCQK YYSSEPQAVD FLECAEEARK KINSWVKTQT KGKIPNLLPE GSVDGDTRMV LVNAVYFKGK WKTPFEKKLN GLYPFRVNSA QRTPVQMMYL REKLNIGYIE DLKAQILELP YAGDVSMFLL LPDEIADVST GLELLESEIT YDKLNKWTSK DKMAEDEVEV YIPQFKLEEH YELRSILRSM GMEDAFNKGR ANFSGMSERN DLFLSEVFHQ AMVDVNEEGT EAAAGTGGVM TGRTGHGGPQ FVADHPFLFL IMHKITNCIL FFGRFSSP.

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    Serpinb2 Human His
  • View Data Sheet

    Name :

    GIP Human

    Description:

    Gastric Inhibitory Polypeptide Human Recombinant

    Gastric inhibitory polypeptide, GIP, Incretin hormone.

    Product # :

    PRO-1438

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    Description

    GIP Human Recombinant produced in E. coli is a single polypeptide chain containing 155 amino acids (22-153) and having a molecular mass of 17.3kDa. GIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GIP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Gastric Inhibitory Polypeptide (GIP) which is a significant hormone of the enteroinsular axis has a functional profile of possible therapeutic value for type 2 diabetes. GIP is an important incretin hormone released into the circulation from endocrine K-cells of the duodenum and jejunum after ingestion of food1. GIP was evaluated for his ability to elevate cellular cAMP production. GIP promotes plasma triglyceride clearance in response to oral fat loading.

    • Synonyms

      Gastric inhibitory polypeptide, GIP, Incretin hormone.

    • 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 MGSEKKEGHF SALPSLPVGS HAKVSSPQPR GPRYAEGTFI SDYSIAMDKI HQQDFVNWLL AQKGKKNDWK HNITQREARA LELAGQANRK EEEAVEPQSS PAKNPSDEDL LRDLLIQELL ACLLDQTNLC RLRSR.

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    Gip Human
  • View Data Sheet

    Name :

    HK1 Antibody

    Description:

    Hexokinase-1, Mouse Anti Human

    Hexokinase-1, EC 2.7.1.1, Hexokinase type I, HK I, Brain form hexokinase, HK1-ta, HK1-tb, HXK1, HK1.

    Product # :

    ANT-375

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase1 encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of HXK1 results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein.

    • Synonyms

      Hexokinase-1, EC 2.7.1.1, Hexokinase type I, HK I, Brain form hexokinase, HK1-ta, HK1-tb, HXK1, HK1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human Hexokinase-1 mAb is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Hexokinase-1 amino acids 1-917 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and κ light chain.

    • Clone

      P4D7AT.

    • Applications

      Hexokinase-1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.

    • 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

      Hexokinase-1 antibody was purified from mouse ascitic fluids by protein-G 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.

    Hk1 Antibody
  • View Data Sheet

    Name :

    ACE Human

    Description:

    Angiotensin Converting Enzyme Human Recombinant

    Angiotensin-converting enzyme, ACE, Dipeptidyl carboxypeptidase I, Kininase II, CD_antigen: CD143, DCP, DCP1, ACE1, CD143

    Product # :

    ENZ-1156

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    Description

    ACE Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1235 amino acids (30-1256 a.a.) and having a molecular mass of 142kDa. ACE is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACE protein solution (0.25mg/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 > 1,000 pmol/min/mg. Defined by the amount of enzyme that cleaves 1pmol of McaRPPGFSAFK(Dnp)-OH per minute at 25C˚.

    More Info

    • Introduction

      Angiotensin Converting Enzyme (ACE) is a zinc metallopeptidase vital for blood pressure control and salt and water metabolism.ACE converts angiotensin I to angiotensin II by release of the terminal His-Leu which causes the vasoconstrictor activity of angiotensin to increase.ACE inactivates bradykinin, a potent vasodilator and has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.

    • Synonyms

      Angiotensin-converting enzyme, ACE, Dipeptidyl carboxypeptidase I, Kininase II, CD_antigen: CD143, DCP, DCP1, ACE1, CD143

    • 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

      LDPGLQPGNF SADEAGAQLF AQSYNSSAEQ VLFQSVAASW AHDTNITAEN ARRQEEAALL SQEFAEAWGQ KAKELYEPIW QNFTDPQLRR IIGAVRTLGS ANLPLAKRQQ YNALLSNMSR IYSTAKVCLP NKTATCWSLD PDLTNILASS RSYAMLLFAW EGWHNAAGIP LKPLYEDFTA LSNEAYKQDG FTDTGAYWRS WYNSPTFEDD LEHLYQQLEP LYLNLHAFVR RALHRRYGDR YINLRGPIPA HLLGDMWAQS WENIYDMVVP FPDKPNLDVT STMLQQGWNA THMFRVAEEF FTSLELSPMP PEFWEGSMLE KPADGREVVC HASAWDFYNR KDFRIKQCTR VTMDQLSTVH HEMGHIQYYL QYKDLPVSLR RGANPGFHEA IGDVLALSVS TPEHLHKIGL LDRVTNDTES DINYLLKMAL EKIAFLPFGY LVDQWRWGVF SGRTPPSRYN FDWWYLRTKY QGICPPVTRN ETHFDAGAKF HVPNVTPYIR YFVSFVLQFQ FHEALCKEAG YEGPLHQCDI YRSTKAGAKL RKVLQAGSSR PWQEVLKDMV GLDALDAQPL LKYFQPVTQW LQEQNQQNGE VLGWPEYQWH PPLPDNYPEG IDLVTDEAEA SKFVEEYDRT SQVVWNEYAE ANWNYNTNIT TETSKILLQK NMQIANHTLK YGTQARKFDV NQLQNTTIKR IIKKVQDLER AALPAQELEE YNKILLDMET TYSVATVCHP NGSCLQLEPD LTNVMATSRK YEDLLWAWEG WRDKAGRAIL QFYPKYVELI NQAARLNGYV DAGDSWRSMY ETPSLEQDLE RLFQELQPLY LNLHAYVRRA LHRHYGAQHI NLEGPIPAHL LGNMWAQTWS NIYDLVVPFP SAPSMDTTEA MLKQGWTPRR MFKEADDFFT SLGLLPVPPE FWNKSMLEKP TDGREVVCHA SAWDFYNGKD FRIKQCTTVN LEDLVVAHHE MGHIQYFMQY KDLPVALREG ANPGFHEAIG DVLALSVSTP KHLHSLNLLS SEGGSDEHDI NFLMKMALDK IAFIPFSYLV DQWRWRVFDG SITKENYNQE WWSLRLKYQG LCPPVPRTQG DFDPGAKFHI PSSVPYIRYF VSFIIQFQFH EALCQAAGHT GPLHKCDIYQ SKEAGQRLAT AMKLGFSRPW PEAMQLITGQ PNMSASAMLS YFKPLLDWLR TENELHGEKL GWPQYNWTPN SARSEGPLPD SGRVSFLGLD LDAQQARVEH HHHHH

    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.

    Ace Human
  • View Data Sheet

    Name :

    DDT Mouse

    Description:

    D-Dopachrome Tautomerase Mouse Recombinant

    D-dopachrome decarboxylase (EC:4.1.1.84), D-dopachrome tautomerase, Ddt.

    Product # :

    ENZ-1073

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    Description

    DDT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (1-118 a.a) and having a molecular mass of 15.5kDa. DDT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DDT protein solution (1mg/ml) contains 20mM Tris-Hcl buffer (pH8.0) & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DDT is an enzyme that catayzes the tautomerization of D-dopachrome to give 5,6-dihydroxyindole (DHI). DDT is part of the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. DDT shares a homologous amino acid sequence (33% identical) with MIF and has similar tautomerase activity. DDT functions a proinflammatory cytokine.

    • Synonyms

      D-dopachrome decarboxylase (EC:4.1.1.84), D-dopachrome tautomerase, Ddt.

    • 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 MGSMPFVELE TNLPASRIPA GLENRLCAAT ATILDKPEDR VSVTIRPGMT LLMNKSTEPC AHLLVSSIGV VGTAEQNRTH SASFFKFLTE ELSLDQDRIV IRFFPLEAWQ IGKKGTVMTF L

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

    Ddt Mouse
  • View Data Sheet

    Name :

    C.Albicans Enolase

    Description:

    Candida Albicans Enolase Recombinant

    Product # :

    PRO-2297

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    Description

    Recombinant Candida Albicans Enolase produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. C.Albicans Enolase is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    C.Albicans Enolase is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Candida albicans is a diploid fungus, which grows both as yeast and filamentous cells and a contributory agent of opportunistic oral and genital infections in humans, and candidal onychomycosis (an infection of the nail plate). Systemic fungal infections (fungemias) including those by C. albicans are regarded as key causes of morbidity and mortality in immunocompromised patients (e.g., AIDS, cancer chemotherapy, organ or bone marrow transplantation). C. albicans biofilms may develop on the surface of implantable medical devices. C. albicans is commensal and a constituent of the normal gut flora containing microorganisms which live in the human mouth and gastrointestinal tract. Overgrowth of the fungus leads to in candidiasis (candidosis). Candidiasis is frequently detected in immunocompromised persons, including HIV-infected patients. To infect host tissue, the habitual unicellular yeast-like form of C. albicans reacts to environmental signals and changes into an invasive, multicellular filamentous form, a phenomenon which is known as dimorphism.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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

    Calbicans Enolase
  • View Data Sheet

    Name :

    FGF20 Human

    Description:

    Fibroblast Growth Factor-20 Human Recombinant

    Fibroblast Growth Factor 20, FGF-20, RHDA2, FGF20.

    Product # :

    CYT-875

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    Description

    FGF20 Human Recombinant (1-211) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids and having a molecular mass of 24kDa.The FGF-20 is fused to a 6 amino acid His tag [HHHHHH] at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in MOPS, (NH4)2SO4, DTT and EDTA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 2.5ng/ml.

    More Info

    • Introduction

      Fibroblast growth factor 20 (FGF20) belongs to the FGF gene family and member of FGF-9 subfamily (based upon its structure). Human FGF20 has several receptors which include FGF R1c, FGF R2c, FGF R3b, FGF R3c and FGF R4. FGF20 is expressed a various cells, including dopaminergic neurons, fibroblasts, keratinocytes and breast epithelium, and numerous sites in the fetus.

    • Synonyms

      Fibroblast Growth Factor 20, FGF-20, RHDA2, FGF20.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-20 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 FGF-20 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHAPL AEVGGFLGGL EGLGQQVGSH FLLPPAGERP PLLGERRSAA ERSARGGPGA AQLAHLHGIL RRRQLYCRTG FHLQILPDGS VQGTRQDHSL FGILEFISVA VGLVSIRGVD SGLYLGMNDK GELYGSEKLT SECIFREQFE ENWYNTYSSN IYKHGDTGRR YFVALNKDGT PRDGARSKRH QKFTHFLPRP VDPERVPELY KDLLMYT.

    • Background

      What is the molecular weight/Mw of FGF20 Protein?
      FGF20 Protein has a total Mw of 24kDa.

      What is the source or expression system of FGF20 Protein?
      Escherichia Coli.

      What is the Purity of FGF20 Protein?
      FGF20 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF20 Protein?
      The ED50, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 2.5ng/ml.

      What is the amino acid sequence of FGF20 Protein?
      MHHHHHHAPL AEVGGFLGGL EGLGQQVGSH FLLPPAGERP PLLGERRSAA ERSARGGPGA AQLAHLHGIL RRRQLYCRTG FHLQILPDGS VQGTRQDHSL FGILEFISVA VGLVSIRGVD SGLYLGMNDK GELYGSEKLT SECIFREQFE ENWYNTYSSN IYKHGDTGRR YFVALNKDGT PRDGARSKRH QKFTHFLPRP VDPERVPELY KDLLMYT.

      What applications can FGF20 Protein be used in?
      FGF20 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF20 Protein?
      The endotoxin level is minimal, FGF20 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.

    Fgf20 Human
  • View Data Sheet

    Name :

    KLK7 Human, sf9

    Description:

    Kallikrein-7 Human Recombinant, sf9

    Kallikrein Related Peptidase 7, Kallikrein 7 (Chymotryptic, Stratum Corneum), Stratum Corneum Chymotryptic Enzyme, Serine Protease 6, PRSS6, SCCE, HK7, Kallikrein-Related Peptidase 7, Signal Protein, EC 3.4.21.117, EC 3.4.21, HSCCE.

    Product # :

    ENZ-962

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    Description

    KLK7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (1-181 a.a.) and having a molecular mass of 20.9kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). KLK7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK7 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 cleaves insulin B chain at ''6-Leu- -Cys-7'', ''16-Tyr- -Leu-17'', ''25-Phe- -Tyr-26'' and ''26-Tyr--Thr-27''. KLK7 is involved in the activation of precursors to inflammatory cytokines.

    • Synonyms

      Kallikrein Related Peptidase 7, Kallikrein 7 (Chymotryptic, Stratum Corneum), Stratum Corneum Chymotryptic Enzyme, Serine Protease 6, PRSS6, SCCE, HK7, Kallikrein-Related Peptidase 7, Signal Protein, EC 3.4.21.117, EC 3.4.21, HSCCE.

    • 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

      ADPMNEYTVH LGSDTLGDRR AQRIKASKSF RHPGYSTQTH VNDLMLVKLN SQARLSSMVK KVRLPSRCEP PGTTCTVSGW GTTTSPDVTF PSDLMCVDVK LISPQDCTKV YKDLLENSML CAGIPDSKKN ACNGDSGGPL VCRGTLQGLV SWGTFPCGQP NDPGVYTQVC KFTKWINDTM KKHRHHHHHH.

    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.

    Klk7 Human Sf9
  • View Data Sheet

    Name :

    VCAM1 Human, HEK

    Description:

    Vascular cell adhesion molecule 1 Human Recombinant, HEK

    Vascular cell adhesion protein 1, V-CAM 1, INCAM-100, CD106, VCAM1, L1CAM, MGC99561, DKFZp779G2333.

    Product # :

    PRO-1641

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    Description

    VCAM1 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 682 amino acids (25-698). VCAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    VCAM1 was lyophilized from a 0.2 µM filtered solution of 20mM PB, 150mM NaCl, 2mM CaCl2, 2mM MgCl2 and 5%Threhalose, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).

    • Synonyms

      Vascular cell adhesion protein 1, V-CAM 1, INCAM-100, CD106, VCAM1, L1CAM, MGC99561, DKFZp779G2333.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized VCAM1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VCAM1 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 VCAM1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      FKIETTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPLNGKVTNEGTTS
      TLTMNPVSFGNEHSYLCTATCESRKLEKGIQVEIYSFPKDPEIHLSGPLEAGKP
      ITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIE
      DIGKVLVCRAKLHIDEMDSVPTVRQAVKELQVYISPKNTVISVNPSTKLQEGGSVT
      MTCSSEGLPAPEIFWSKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEV
      ELIVQEKPFTVEISPGPRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGKVRSEGTN
      STLTLSPVSFENEHSYLCTVTCGHKKLEKGIQVELYSFPRDPEIEMSGGLVNGSSVTVSCKV
      PSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVCQAKLHID
      DMEFEPKQRQSTQTLYVNVAPRDTTVLVSPSSILEEGSSVNMTCLSQGFPAPKILWSRQLPNGE
      LQPLSENATLTLISTKMEDSGVYLCEGINQIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRE
      NNKDYFSPEVDHHHHHHAGRSRKEVELIIQVTPKDIKLTAFPSESVKEGDTVIISCTCGNVPETW
      IILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRENNKDYFSPE
      VDHHHHHH.

    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.

    Vcam1 Human Hek
  • View Data Sheet

    Name :

    ART4 Human

    Description:

    ADP-Ribosyltransferase 4 Human Recombinant

    ARTC4, DOK1, CD297 Antigen, Dombrock Blood Group, ADP-Ribosyltransferase 4, Ecto-ADP-Ribosyltransferase 4.

    Product # :

    ENZ-1072

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    Description

    ART4 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 248 amino acids (47-285 a.a.) and having a molecular mass of 28.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). ART4 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ART4 protein solution (0.25mg/ml) contains Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ecto-ADP-Ribosyltransferase 4 or ART4 is typed as a glycosylphosphatidylinositol (GPI)-linked membrane protein which carries Dombrock blood group antigens. The development of this protein takes place at the highest levels in the fetal liver. the process of the ART4 development is regulated while the erythroid differentiation process occurs. ART4 is a is part of the Ribosyltransferase family.

    • Synonyms

      ARTC4, DOK1, CD297 Antigen, Dombrock Blood Group, ADP-Ribosyltransferase 4, Ecto-ADP-Ribosyltransferase 4.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPSEVAIKI DFDFAPGSFD DQYQGCSKQV MEKLTQGDYF TKDIEAQKNY FRMWQKAHLA WLNQGKVLPQ NMTTTHAVAI LFYTLNSNVH SDFTRAMASV ARTPQQYERS FHFKYLHYYL TSAIQLLRKD SIMENGTLCY EVHYRTKDVH FNAYTGATIR FGQFLSTSLL KEEAQEFGNQ TLFTIFTCLG APVQYFSLKK EVLIPPYELF KVINMSYHPR GDWLQLRSTG NLSTYNCQLL KAHHHHHH.

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    Art4 Human
  • View Data Sheet

    Name :

    PARP2 Human

    Description:

    Poly (ADP-Ribose) Polymerase 2 Human Recombinant

    ADPRT2, ADPRTL2, ADPRTL3, ARTD2, pADPRT-2, PARP-2, Poly [ADP-ribose] polymerase 2, hPARP-2, ADP-ribosyltransferase diphtheria toxin-like 2, NAD (+) ADP-ribosyltransferase 2, Poly [ADP-ribose] synthase 2.

    Product # :

    ENZ-694

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    Description

    PARP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (233-583a.a) and having a molecular mass of 42.5kDa. PARP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PARP2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Poly (ADP-Ribose) Polymerase 2 (PARP2) contains a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. PARP2 is capable of catalyzing a poly (ADP-ribosyl)ation reaction. The basic residues within the N-terminal area of this protein can bear potential DNA-binding properties, and can be engaged in the nuclear and/or nucleolar targeting of the protein. There has been found two alternatively spliced transcript variants encoding distinct isoforms.

    • Synonyms

      ADPRT2, ADPRTL2, ADPRTL3, ARTD2, pADPRT-2, PARP-2, Poly [ADP-ribose] polymerase 2, hPARP-2, ADP-ribosyltransferase diphtheria toxin-like 2, NAD (+) ADP-ribosyltransferase 2, Poly [ADP-ribose] synthase 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 MGSHMQLDLR VQELIKLICN VQAMEEMMME MKYNTKKAPL GKLTVAQIKA GYQSLKKIED CIRAGQHGRA LMEACNEFYT RIPHDFGLRT PPLIRTQKEL SEKIQLLEAL GDIEIAIKLV KTELQSPEHP LDQHYRNLHC ALRPLDHESY EFKVISQYLQ STHAPTHSDY TMTLLDLFEV EKDGEKEAFR EDLHNRMLLW HGSRMSNWVG ILSHGLRIAP PEAPITGYMF GKGIYFADMS SKSANYCFAS RLKNTGLLLL SEVALGQCNE LLEANPKAEG LLQGKHSTKG LGKMAPSSAH FVTLNGSTVP LGPASDTGIL NPDGYTLNYN EYIVYNPNQV RMRYLLKVQF NFLQLW.

    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.

    Parp2 Human
  • View Data Sheet

    Name :

    CTSB Mouse, Active

    Description:

    Cathepsin-B Mouse Recombinant, Active

    Cathepsin B, Cathepsin B1, CTSB.

    Product # :

    PRO-2377

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    CTSB Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 330 amino acids (18-339a.a.) and having a molecular mass of 36.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTSB is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of Z-Arg-Arg-AMC to Z-Arg-Arg and AMC per minute at pH 6.0 at 37C.

    More Info

    • Introduction

      Cathepsin B preproprotein (CTSB) is a papain-family cysteine protease which is normally located in lysosomes. CTSB is able to degrade several extracellular matrix components at both neutral and acidic pH and has been implicated in the progression of some human and rodent tumors progression and arthritis.

    • Synonyms

      Cathepsin B, Cathepsin B1, CTSB.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      HDKPSFHPLS DDLINYINKQ NTTWQAGRNF YNVDISYLKK LCGTVLGGPK LPGRVAFGED IDLPETFDAR EQWSNCPTIG QIRDQGSCGS CWAFGAVEAI SDRTCIHTNG RVNVEVSAED LLTCCGIQCG DGCNGGYPSG AWSFWTKKGL VSGGVYNSHV GCLPYTIPPC EHHVNGSRPP CTGEGDTPRC NKSCEAGYSP SYKEDKHFGY TSYSVSNSVK EIMAEIYKNG PVEGAFTVFS DFLTYKSGVY KHEAGDMMGG HAIRILGWGV ENGVPYWLAA NSWNLDWGDN GFFKILRGEN HCGIESEIVA GIPRTDQYWG RFLEHHHHHH.

    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.

    Ctsb Mouse Active
  • View Data Sheet

    Name :

    GSTM1 Mouse, His

    Description:

    Glutathione S-Transferase M1 Mouse Recombinant, His Tag

    GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.

    Product # :

    ENZ-456

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    Description

    GSTM1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 28.1kDa. The GTM1 is fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM1 solution contains 20 mM Tris-HCl buffer ( pH8.0), 1mM DTT and 10% glycerol

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is < 11 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

    More Info

    • Introduction

      Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

    • Synonyms

      GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK.

    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.

    Gstm1 Mouse His
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