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Search results

1000 results found for “protease”

Name

Description

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  • View Data Sheet

    Name :

    PGAM1 Mouse, Active

    Description:

    Phosphoglycerate Mutase 1 Mouse Recombinant, Active

    Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.

    Product # :

    ENZ-980

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
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    • More Info

    Description

    PGAM1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-254) and having a molecular mass of 31.4kDa.PGAM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PGAM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >150units/mg, in which One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37C.

    More Info

    • Introduction

      PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.

    • Synonyms

      Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAAYKL VLIRHGESAW NLENRFSGWY DADLSPAGHE EAKRGGQALR DAGYEFDICF TSVQKRAIRT LWTVLDAIDQ MWLPVVRTWR LNERHYGGLT GLNKAETAAK HGEAQVKIWR RSYDVPPPPM EPDHPFYSNI SKDRRYADLT EDQLPSCESL KDTIARALPF WNEEIVPQIK EGKRVLIAAH GNSLRGIVKH LEGLSEEAIM ELNLPTGIPI VYELDKNLKP IKPMQFLGDE ETVRKAMEAV AAQGKVKK.

    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.

    Pgam1 Mouse Active
  • View Data Sheet

    Name :

    G6PD Human

    Description:

    Glucose-6-Phosphate Dehydrogenase Human Recombinant

    G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    Product # :

    ENZ-608

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
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    Description

    G6PD Human Recombinant produced in Hi-5 cells is a single polypeptide chain containing 535 amino acids (1-515) and having a molecular mass of 61.4kDa.G6PD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Hi-5 cells.

    Formulation

    The G6PD solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF, 2mM EDTA, 2mM DTT, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 45 units/ml obtained by measuring the increase of beta-NADPH in absorbance at 340 nm resulting from the reduction of beta NADP. One unit oxidizes 1.0 umole D-glucose-6-phosphate to 6-phospho-D-gluconate per min in the presence of beta-NADP at pH 7.4 at 25C.

    More Info

    • Introduction

      G6PD is the rate-limiting enzyme of the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells by maintaining the level of NADPH. G6PD converts glucose-6-phosphate into 6-phosphoglucono-?-lactone and at the same time produces NADPH. The NADPH maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. G6PD deficiency causes acute hemolytic anemia, neonatal jaundice or acute hemolysis. G6PD is a cytosolic enzyme encoded by an X-linked gene whose main function is to produce NADPH, a crucial electron donor in the defense against oxidizing agents and in reductive biosynthetic reactions. G6PD produces pentose sugars for nucleic acid synthesis and is a main producer of NADPH reducing power.

    • Synonyms

      G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    • 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 MAEQVALSRT QVCGILREEL FQGDAFHQSD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPENTFIVGY ARSRLTVADI RKQSEPFFKA TPEEKLKLED FFARNSYVAG QYDDAASYQR LNSHMNALHL GSQANRLFYL ALPPTVYEAV TKNIHESCMS QIGWNRIIVE KPFGRDLQSS DRLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVQA NNVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD GVPFILRCGK ALNERKAEVR LQFHDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH QIELEKPKPI PYIYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL

    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.

    G6Pd Human
  • View Data Sheet

    Name :

    IRGM Human

    Description:

    Immunity-Related GTPase Family, M Human Recombinant

    Immunity-related GTPase family M protein, Immunity-related GTPase family M protein1, LPS-stimulated RAW 264.7 macrophage protein 47 homolog, LRG-47, IRGM, IFI1, IRGM1, LRG47.

    Product # :

    PRO-1302

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    IRGM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (23-181) and having a molecular mass of 20.1 kDa. IRGM is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IRGM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Immunity-related GTPase family M protein (IRGM) is essential for clearance of severe protozoan and bacterial infections. IRGM belongs to the p47 immunity-related GTPase family. IRGM serves in innate immune response possibly via regulation of autophagy. IRGM regulates proinflammatory cytokine production and inhibit endotoxemia upon infection and also has a part in macrophages adhesion and motility. Polymorphisms which modify the natural expression of the IRGM gene are associated with a susceptibility to Crohn's disease and tuberculosis.

    • Synonyms

      Immunity-related GTPase family M protein, Immunity-related GTPase family M protein1, LPS-stimulated RAW 264.7 macrophage protein 47 homolog, LRG-47, IRGM, IFI1, IRGM1, LRG47.

    • 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 MKETLKIVSR TPVNITMAGD SGNGMSTFIS ALRNTGHEGK ASPPTELVKA TQRCASYFSS HFSNVVLWDL PGTGSATTTL ENYLMEMQFN RYDFIMVASA QFSMNHVMLA KTAEDMGKKF YIVWTKLDMD LSTGALPEVQ LLQIRENVLE NLQKERVCEY.

    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.

    Irgm Human
  • View Data Sheet

    Name :

    LCAT Human, HEK

    Description:

    Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK

    Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    Product # :

    ENZ-254

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    LCAT Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 429 amino acids (25-440) which includes a 13 amino acid Flag Tag fused at N-terminus and having a total molecular mass of 48.5 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Human Embryonic Kidney 293 cells

    Formulation

    The LCAT protein was lyophilized from 0.4um filtered solution at a concentration of 0.5mg/ml containing 20mM Tris buffer, and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.

    • Synonyms

      Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LCAT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCAT 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

      Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. LCAT HEK is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      HVDYKDDDDK PAGFWLLNVL FPPHTTPKAE LSNHTRPVIL VPGCLGNQLE AKLDKPDVVN WMCYRKTEDF FTIWLDLNMF LPLGVDCWID NTRVVYNRSS GLVSNAPGVQ IRVPGFGKTY SVEYLDSSKL AGYLHTLVQN LVNNGYVRDE TVRAAPYDWR LEPGQQEEYY RKLAGLVEEM HAAYGKPVFL IGHSLGCLHL LYFLLRQPQA WKDRFIDGFI SLGAPWGGSI KPMLVLASGD NQGIPIMSSI KLKEEQRITT TSPWMFPSRM AWPEDHVFIS TPSFNYTGRD FQRFFADLHF EEGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPRTYIY DHGFPYTDPV GVLYEDGDDT VATRSTELCG LWQGRQPQPV HLLPLHGIQH LNMVFSNLTL EHINAILLGA YRQGPPASPT ASPEPPPPE

    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.

    Lcat Human Hek
  • View Data Sheet

    Name :

    ENPP1 Mouse

    Description:

    Ectonucleotide Pyrophosphatase Mouse Recombinant

    Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, E-NPP 1, Membrane component chromosome 6 surface marker 1, Phosphodiesterase I/nucleotide pyrophosphatase 1, Plasma-cell membrane glycoprotein PC-1, ENPP1, M6S1, NPPS, PC1, PDNP1, NPP1, PC-1, PCA1, ARHR2, COLED.

    Product # :

    ENZ-1193

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    Description

    ENPP1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing 828 amino acids (Lys85-Glu906) and having a molecular mass of 95.2kDa. ENPP1 Mouse is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    The filtered (0.4µm) concentrated protein solution was lyophilized with PBS, PH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, E-NPP 1, Membrane component chromosome 6 surface marker 1, Phosphodiesterase I/nucleotide pyrophosphatase 1, Plasma-cell membrane glycoprotein PC-1, ENPP1, M6S1, NPPS, PC1, PDNP1, NPP1, PC-1, PCA1, ARHR2, COLED.

    • 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.

    • Solubility

      It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      KEVKSCKGRC FERTFSNCRC DAACVSLGNC CLDFQETCVE PTHIWTCNKF RCGEKRLSRF VCSCADDCKT HNDCCINYSS VCQDKKSWVE ETCESIDTPE CPAEFESPPT LLFSLDGFRA EYLHTWGGLL PVISKLKNCG TYTKNMRPMY PTKTFPNHYS IVTGLYPESH GIIDNKMYDP KMNASFSLKS KEKFNPLWYK GQPIWVTANH QEVKSGTYFW PGSDVEIDGI LPDIYKVYNG SVPFEERILA VLEWLQLPSH ERPHFYTLYL EEPDSSGHSH GPVSSEVIKA LQKVDRLVGM LMDGLKDLGL DKCLNLILIS DHGMEQGSCK KYVYLNKYLG DVNNVKVVYG PAARLRPTDV PETYYSFNYE ALAKNLSCRE PNQHFRPYLK PFLPKRLHFA KSDRIEPLTF YLDPQWQLAL NPSERKYCGS GFHGSDNLFS NMQALFIGYG PAFKHGAEVD SFENIEVYNL MCDLLGLIPA PNNGSHGSLN HLLKKPIYNP SHPKEEGFLS QCPIKSTSND LGCTCDPWIV PIKDFEKQLN LTTEDVDDIY HMTVPYGRPR ILLKQHHVCL LQQQQFLTGY SLDLLMPLWA SYTFLRNDQF SRDDFSNCLY QDLRIPLSPV HKCSYYKSNS KLSYGFLTPP RLNRVSNHIY SEALLTSNIV PMYQSFQVIW HYLHDTLLQR YAHERNGINV VSGPVFDFDY DGRYDSLEIL KQNSRVIRSQ EILIPTHFFI VLTSCKQLSE TPLECSALES SAYILPHRPD NIESCTHGKR ESSWVEELLT LHRARVTDVE LITGLSFYQD RQESVSELLR LKTHLPIFSQ EDHHHHHH.

    • Background

      Ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1) is an enzyme with multifaceted roles in cellular metabolism, bone mineralization, and insulin signaling. Research utilizing mouse models has been pivotal in elucidating the complex biology of ENPP1 and its implications for various physiological processes and disease states. This study aims to provide a comprehensive exploration of ENPP1 in mouse physiology, shedding light on its diverse functions and potential applications in understanding metabolic health and disease mechanisms.

      The primary objective of this research is to elucidate the impact of ENPP1 in mouse models on metabolic health. In vivo experiments using genetically modified mice with altered ENPP1 expression or activity will be conducted to investigate how ENPP1 influences glucose homeostasis, insulin sensitivity, and lipid metabolism. Understanding these mechanisms is fundamental for deciphering the role of ENPP1 in metabolic diseases such as diabetes and obesity.

      The second objective is to assess the clinical relevance of ENPP1 in mouse models of bone health. Mouse models of skeletal disorders will be employed to explore how ENPP1 affects bone mineralization, density, and remodeling. These investigations may provide valuable insights into potential therapeutic strategies targeting ENPP1 in bone-related diseases.

      The third objective is to explore the broader implications of ENPP1 in mouse physiology, including its effects on vascular health, inflammation, and tissue repair. Research will investigate its roles in vascular calcification, inflammation resolution, and tissue regeneration. Understanding the multifaceted properties of ENPP1 in mouse models may open new avenues for therapeutic interventions in various metabolic and chronic disease contexts.

      By delving into the diverse functions of ENPP1 in mouse physiology, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for metabolic diseases, bone disorders, and other conditions influenced by ENPP1.

    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.

    Enpp1 Mouse
  • View Data Sheet

    Name :

    Protein-A/G, His

    Description:

    Protein A/G Recombinant, His Tag

    Product # :

    PRO-1927

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 3 of protein G (C1-C2-C3) containing 513 amino acids in total and having a molecular mass of 56.9kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 8 IgG-binding domains EDABC-C1C2C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1, C2 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE KLAAALEHHH HHH.

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

    Protein A G His
  • View Data Sheet

    Name :

    GSTA4 Human

    Description:

    Glutathione S-Transferase Alpha 4 Human Recombinant

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

    Product # :

    ENZ-600

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Gsta4 Human
  • View Data Sheet

    Name :

    PON1 Human

    Description:

    Paraoxonase-1 Human Recombinant

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

    Product # :

    ENZ-299

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGL
      AFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNA
      MYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLD
      PYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEK
      HANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILT
      EEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCELEHHHHHH.

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

    Pon1 Human
  • View Data Sheet

    Name :

    TYMP Human

    Description:

    Thymidine Phosphorylase Human Recombinant

    Thymidine phosphorylase, Gliostatin, Platelet-derived endothelial cell growth factor, PD-ECGF, TdRPase, TYMP, ECGF1, TP, MNGIE, MEDPS1, MTDPS1, PDECGF, hPD-ECGF.

    Product # :

    ENZ-005

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    Description

    TYMP Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 493 amino acids (11-482 a.a.) and having a molecular mass of 51.3kDa. The TYMP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymidine phosphorylase precursor (TYMP) is a platelet-derived endothelial cell growth factor that catalyzes the formation of thymine and 2-deoxy-D-ribose-1-phosphate from thymidine and orthophosphate. TYMP is an angiogenic inducer that potently stimulates the growth of endothelial cells and induces chemotaxis. TYMP has a highly restricted target cell specificity acting only on endothelial cells. An increased expression of TYMP is found in a broad array of different solid tumors and inflammatory diseases and is frequently associated with poor prognosis. Mutations in the TYMP gene are linked to mitochondrial neurogastrointestinal encephalomyopathy.

    • Synonyms

      Thymidine phosphorylase, Gliostatin, Platelet-derived endothelial cell growth factor, PD-ECGF, TdRPase, TYMP, ECGF1, TP, MNGIE, MEDPS1, MTDPS1, PDECGF, hPD-ECGF.

    • 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 MAPPAPGDFS GEGSQGLPDP SPEPKQLPEL IRMKRDGGRL SEADIRGFVA AVVNGSAQGA QIGAMLMAIR LRGMDLEETS VLTQALAQSG QQLEWPEAWR QQLVDKHSTG GVGDKVSLVL APALAACGCK VPMISGRGLG HTGGTLDKLE SIPGFNVIQS PEQMQVLLDQ AGCCIVGQSE QLVPADGILY AARDVTATVD SLPLITASIL SKKLVEGLSA LVVDVKFGGA AVFPNQEQAR ELAKTLVGVG ASLGLRVAAA LTAMDKPLGR CVGHALEVEE ALLCMDGAGP PDLRDLVTTL GGALLWLSGH AGTQAQGAAR VAAALDDGSA LGRFERMLAA QGVDPGLARA LCSGSPAERR QLLPRAREQE ELLAPADGTV ELVRALPLAL VLHELGAGRS RAGEPLRLGV GAELLVDVGQ RLRRGTPWLR VHRDGPALSG PQSRALQEAL VLSDRAPFAA PSPFAELVLP PQQ.

    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.

    Tymp Human
  • View Data Sheet

    Name :

    GMPR Human

    Description:

    Guanosine Monophosphate Reductase Human Recombinant

    GMP reductase 1, Guanosine 5'-monophosphate oxidoreductase 1, Guanosine monophosphate reductase 1, GMPR, GMPR1.

    Product # :

    ENZ-570

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    Description

    GMPR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 365 amino acids (1-345) and having a molecular mass of 39.5kDa.GMPR is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GMPR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Guanosine monophosphate reductase (GMPR) catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. GMPR acts in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in upholding the intracellular balance of A and G nucleotides. In addition, the GMPR protein functions in the re-utilization of free intracellular bases and purine nucleosides.

    • Synonyms

      GMP reductase 1, Guanosine 5'-monophosphate oxidoreductase 1, Guanosine monophosphate reductase 1, GMPR, GMPR1.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPRIDADLKL DFKDVLLRPK RSSLKSRAEV DLERTFTFRN SKQTYSGIPI IVANMDTVGT FEMAAVMSQH SMFTAIHKHY SLDDWKLFAT NHPECLQNVA VSSGSGQNDL EKMTSILEAV PQVKFICLDV ANGYSEHFVE FVKLVRAKFP EHTIMAGNVV TGEMVEELIL SGADIIKVGV GPGSVCTTRT KTGVGYPQLS AVIECADSAH GLKGHIISDG GCTCPGDVAK AFGAGADFVM LGGMFSGHTE CAGEVIERNG RKLKLFYGMS SDTAMNKHAG GVAEYRASEG KTVEVPYKGD VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH
      NTVFS.

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    Gmpr Human
  • View Data Sheet

    Name :

    CKBB Human His

    Description:

    Creatine Kinase Brain Human Recombinant, His Tag

    EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.

    Product # :

    CKI-274

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    Description

    CKBB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-381 a.a.) and having a molecular mass of 44.8 kDa. The CKB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CKBB Human solution containing 20mM Trsi pH-8, 1mM DTT, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      CKB is a cytoplasmic enzyme that takes part in energy homeostasis. CKB enzyme reversibly catalyzes the transfer of phosphate among ATP and various phosphogens such as creatine phosphate. CKB functions as a homodimer in the brain as well as in different tissues, and as a heterodimer with a similar muscle isozyme in heart. Creatine kinases supply the energy of phosphate hydrolysis essential to drive the normal role of many cellular systems including muscle, tumor and cancer cells.

    • Synonyms

      EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD
      RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.

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    Ckb Human
  • View Data Sheet

    Name :

    GPN1 Human

    Description:

    GPN-loop GTPase 1 Human Recombinant

    GPN-loop GTPase 1, XPA binding protein 1 GTPase, RNA polymerase II associated protein 4, MBD2-interacting protein, MBDin, ATP(GTP)-binding protein, XAB1, ATPBD1A, NTPBP, RPAP4.

    Product # :

    PRO-1140

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    Description

    GPN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 398 amino acids (1-374) and having a molecular mass of 44.3 kDa.GPN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPN1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      GPN-loop GTPase 1 (GPN1) is a member of the GPN-loop GTPase family. GPN1 is a guanosine triphosphatase enzyme which has a role in DNA repair and may function in activation of transcription. Small GTPases, which share a biochemical mechanism, act as binary molecular switches and function in the cell is nucleocytoplasmic transport of both proteins and RNA. In addition, GPN1 establishs an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, proposing that it is essential to connect RNA polymerase II to regulators of protein complex formation. GPN1 may also be involved in nuclear localization of XPA.

    • Synonyms

      GPN-loop GTPase 1, XPA binding protein 1 GTPase, RNA polymerase II associated protein 4, MBD2-interacting protein, MBDin, ATP(GTP)-binding protein, XAB1, ATPBD1A, NTPBP, RPAP4.

    • 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 MGSHMAASAA AAELQASGGP RHPVCLLVLG MAGSGKTTFV QRLTGHLHAQ GTPPYVINLD PAVHEVPFPA NIDIRDTVKY KEVMKQYGLG PNGGIVTSLN LFATRFDQVM KFIEKAQNMS KYVLIDTPGQ IEVFTWSASG TIITEALASS FPTVVIYVMD TSRSTNPVTF MSNMLYACSI LYKTKLPFIV VMNKTDIIDH SFAVEWMQDF EAFQDALNQE TTYVSNLTRS MSLVLDEFYS SLRVVGVSAV LGTGLDELFV QVTSAAEEYE REYRPEYERL KKSLANAESQ QQREQLERLR KDMGSVALDA GTAKDSLSPV LHPSDLILTR GTLDEEDEEA DSDTDDIDHR VTEESHEEPA FQNFMQESMA QYWKRNNK

    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.

    Gpn1 Human
  • View Data Sheet

    Name :

    HPD Human

    Description:

    4-Hydroxyphenylpyruvate Dioxygenase Human Recombinant

    4HPPD, GLOD3, 4-HPPD, PPD, HPPDase, Glyoxalase Domain Containing 3, 4-HydroxyphenylpYruvate Dioxygenase.

    Product # :

    ENZ-015

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    Description

    HPD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-393a.a.) and having a molecular mass of 47kDa.HPD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HPD protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 50mM NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      4-Hydroxyphenylpyruvate Dioxygenase Isoform-1 is an Fe-containing enzyme, which catalyzes the second reaction in the catabolism of tyrosine the conversion of 4-hydroxyphenylpyruvate to homogentisate. Present as a homodimer, HPD uses zinc as a cofactor to catalyze the third step in the conversion of L-phenylalanine to fumarate and acetoacetic acid. Flaws in the gene encoding HPD result in tyrosinemia type 3 and hawkinsinuria, two inborn defects of metabolism which are related to a number of symptoms, like mental retardation and seizures and hair and urine abnormalities.

    • Synonyms

      4HPPD, GLOD3, 4-HPPD, PPD, HPPDase, Glyoxalase Domain Containing 3, 4-HydroxyphenylpYruvate Dioxygenase.

    • 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 MTTYSDKGAK PERGRFLHFH SVTFWVGNAK QAASFYCSKM GFEPLAYRGL ETGSREVVSH VIKQGKIVFV LSSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDYIVQKA RERGAKIMRE PWVEQDKFGK VKFAVLQTYG DTTHTLVEKM NYIGQFLPGY EAPAFMDPLL PKLPKCSLEM IDHIVGNQPD QEMVSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVA NYEESIKMPI NEPAPGKKKS QIQEYVDYNG GAGVQHIALK TEDIITAIRH LRERGLEFLS VPSTYYKQLR EKLKTAKIKV KENIDALEEL KILVDYDEKG YLLQIFTKPV QDRPTLFLEV IQRHNHQGFG AGNFNSLFKA FEEEQNLRGN LTNMETNGVV PGM

    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.

    Hpd Human
  • View Data Sheet

    Name :

    NDUFB9 Human

    Description:

    NADH Dehydrogenase 1 Beta Subcomplex 9 Human Recombinant

    NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 9, B22, LYRM3, UQOR22, Complex I-B22, CI-B22, LYR motif-containing protein 3, NADH-ubiquinone oxidoreductase B22 subunit, NDUFB9.

    Product # :

    ENZ-740

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    Description

    NDUFB9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-179) and having a molecular mass of 24.2kDa.NDUFB9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFB9 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 9 (NDUFB9) which is a part of the complex I LYR family is localized to the internal mitochondrial membrane, as well as to the matrix side of the peripheral membrane. NDUFB9 serves as an accessory subunit of the multi-subunit mitochondrial membrane respiratory chain NADH dehydrogenase complex I. Complex I takes a crucial part in the transfer of electrons from NADH to the respiratory chain, a process which is vital for cellular respiration.

    • Synonyms

      NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 9, B22, LYRM3, UQOR22, Complex I-B22, CI-B22, LYR motif-containing protein 3, NADH-ubiquinone oxidoreductase B22 subunit, NDUFB9.

    • 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 MGSMAFLASG PYLTHQQKVL RLYKRALRHL ESWCVQRDKY RYFACLMRAR FEEHKNEKDM AKATQLLKEA EEEFWYRQHP QPYIFPDSPG GTSYERYDCY KVPEWCLDDW HPSEKAMYPD YFAKREQWKK LRRESWEREV KQLQEETPPG GPLTEALPPA RKEGDLPPLW WYIVTRPRER PM.

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    Ndufb9 Human
  • View Data Sheet

    Name :

    HNMT Human, Active

    Description:

    Histamine N-Methyltransferase Human Recombinant, Active

     HMT, HNMT-S1, HNMT-S2, MRT51.

    Product # :

    ENZ-1071

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    Description

    HNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-292 a.a) and having a molecular mass of 37.4kDa. HNMT is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HNMT protein solution (1mg/ml) containing 20mM, Tris-Hcl (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 200 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37°C.

    More Info

    • Introduction

      Histamine N-Methyltransferase or HNMT, is located in the cell cytosol. Sadenosyl-L-methionine acts as a methyl donor for HNMT which inactivates histamine. By inactivation of histamine, it affects the immune system’s response. HNMT acts on histamine in body tissues such as kidney, central nervous system and bronchus. The protein has a crucial part in the airway response to histamine & histamine degradation process and regulation.

    • Synonyms

      HMT, HNMT-S1, HNMT-S2, MRT51.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASS MRSLFSDHGK YVESFRRFLN HSTEHQCMQE FMDKKLPGII GRIGDTKSEI KILSIGGGAG EIDLQILSKV QAQYPGVCIN NEVVEPSAEQ IAKYKELVAK TSNLENVKFA WHKETSSEYQ SRMLEKKELQ KWDFIHMIQM LYYVKDIPAT LKFFHSLLGT NAKMLIIVVS GSSGWDKLWK KYGSRFPQDD LCQYITSDDL TQMLDNLGLK YECYDLLSTM DISDCFIDGD ENGDLLWDFL TETCNFNATA PPDLRAELGK DLQEPEFSAK KEGKVLFNNT LSFIVIEA.

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    Hnmt Protein
  • View Data Sheet

    Name :

    UBA2 Human

    Description:

    Ubiquitin-Like Modifier Activating Enzyme 2 Human Recombinant

    SAE2, UBA-2, SAE-2, SUMO-1 Activating Enzyme Subunit 2.

    Product # :

    ENZ-959

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    Description

    UBA2 Human Recombinant produced in in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 649 amino acids (1-640a.a) and having a molecular mass of 72.3kDa. UBA2 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    UBA2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SUMO-activating enzyme subunit 2 (UBA2) belongs to a family of small and related proteins which can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. UBA2 is conjugated to various molecules in the presence of the SAE1/UBA2 SUMO-activating(E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating(E2) enzyme. UBA2 represents a vital mechanism to protect neurons during episodes of cerebral ischemia.

    • Synonyms

      SAE2, UBA-2, SAE-2, SUMO-1 Activating Enzyme Subunit 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

      ADLMALSRGL PRELAEAVAG GRVLVVGAGG IGCELLKNLV LTGFSHIDLI DLDTIDVSNL NRQFLFQKKH VGRSKAQVAK ESVLQFYPKA NIVAYHDSIM NPDYNVEFFR QFILVMNALD NRAARNHVNR MCLAADVPLI ESGTAGYLGQ VTTIKKGVTE CYECHPKPTQ RTFPGCTIRN TPSEPIHCIV WAKYLFNQLF GEEDADQEVS PDRADPEAAW EPTEAEARAR ASNEDGDIKR ISTKEWAKST GYDPVKLFTK LFKDDIRYLL TMDKLWRKRK PPVPLDWAEV QSQGEETNAS DQQNEPQLGL KDQQVLDVKS YARLFSKSIE TLRVHLAEKG DGAELIWDKD DPSAMDFVTS AANLRMHIFS MNMKSRFDIK SMAGNIIPAI ATTNAVIAGL IVLEGLKILS GKIDQCRTIF LNKQPNPRKK LLVPCALDPP NPNCYVCASK PEVTVRLNVH KVTVLTLQDK IVKEKFAMVA PDVQIEDGKG TILISSEEGE TEANNHKKLS EFGIRNGSRL QADDFLQDYT LLINILHSED LGKDVEFEVV GDAPEKVGPK QAEDAAKSIT NGSDDGAQPS TSTAQEQDDV LIVDSDEEDS SNNADVSEEE RSRKRKLDEK ENLSAKRSRI EQKEELDDVI ALDHHHHHH

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    Uba2 Human
  • View Data Sheet

    Name :

    PPM1A Human

    Description:

    Protein Phosphatase 1A Alpha Isoform Human Recombinant

    Protein phosphatase 1A, EC 3.1.3.16, Protein phosphatase 2C isoform alpha, PP2C-alpha, IA, PPM1A, PP2CA, MGC9201.

    Product # :

    PKA-222

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    Description

    PPM1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (1-382a.a) and having a molecular mass of 46.6kDa. PPM1A is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPM1A protein solution (1mg/ml) contains 10mM Tris-HCl, pH7.5, 50mM NaCl, 2mM DTT, 1mM MnCl2 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein Phosphatase 2C alpha is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding two distinct isoforms have been described.
      Protein phosphatase 2C(PP2C?) is a Mn2+- or Mg2+-dependent protein serine/threonine phosphatase that is essential for regulating cellular stress response in eukaryotes.

    • Synonyms

      Protein phosphatase 1A, EC 3.1.3.16, Protein phosphatase 2C isoform alpha, PP2C-alpha, IA, PPM1A, PP2CA, MGC9201.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWILMGAF LDKPKMEKHN AQGQGNGLRY GLSSMQGWRV EMEDAHTAVI GLPSGLESWS FFAVYDGHAG SQVAKYCCEH LLDHITNNQD FKGSAGAPSV ENVKNGIRTG FLEIDEHMRV MSEKKHGADR SGSTAVGVLI SPQHTYFINC GDSRGLLCRN RKVHFFTQDH KPSNPLEKER IQNAGGSVMI QRVNGSLAVS RALGDFDYKC VHGKGPTEQL VSPEPEVHDI ERSEEDDQFI ILACDGIWDV MGNEELCDFV RSRLEVTDDL EKVCNEVVDT CLYKGSRDNM SVILICFPNA PKVSPEAVKK EAELDKYLEC RVEEIIKKQG EGVPDLVHVM RTLASENIPS LPPGGELASK RNVIEAVYNR LNPYKNDDTD STSTDDMW.

    • Unit Definition

      One unit will hydrolyze 1 nanomole of p-nitrophenyl phosphatate (pNPP) per minute at pH 7.5 at 37°C.

    • Specific Activity

      >1,400 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.

    Ppm1A Human
  • View Data Sheet

    Name :

    LCMT1 Human

    Description:

    Leucine Carboxyl Methyltransferase 1 Human Recombinant

    Leucine carboxyl methyltransferase 1, LCMT1, LCMT, PPMT1, CGI-68.

    Product # :

    ENZ-219

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    Description

    LCMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-334) and having a molecular mass of 41kDa.LCMT1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LCMT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      LCMT1 is a member of the LCMT family, methyltransferase superfamily. LCMT1 catalyzes the methylation of the carboxyl group of the C-terminal leucine residue (leu309) of the catalytic subunit of protein phosphatase-2A to form alpha-leucine ester residues.

    • Synonyms

      Leucine carboxyl methyltransferase 1, LCMT1, LCMT, PPMT1, CGI-68.

    • 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 MGSHMATRQR ESSITSCCST SSCDADDEGV RGTCEDASLC KRFAVSIGYW HDPYIQHFVR LSKERKAPEI NRGYFARVHG VSQLIKAFLR KTECHCQIVN LGAGMDTTFW RLKDEDLLPS KYFEVDFPMI VTRKLHSIKC KPPLSSPILE LHSEDTLQMD GHILDSKRYA VIGADLRDLS ELEEKLKKCN MNTQLPTLLI AECVLVYMTP EQSANLLKWA ANSFERAMFI NYEQVNMGDR FGQIMIENLR RRQCDLAGVE TCKSLESQKE RLLSNGWETA SAVDMMELYN RLPRAEVSRI ESLEFLDEME LLEQLMRHYC LCWATKGGNE LGLKEITY.

    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.

    Lcmt1 Human
  • View Data Sheet

    Name :

    PRMT3 Human

    Description:

    Protein Arginine Methyltransferase 3 Human Recombinant

    Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.

    Product # :

    ENZ-848

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    Description

    PRMT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 554 amino acids (1-531 a.a) and having a molecular mass of 62.3kDa.PRMT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRMT3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol, 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRMT3, also known as protein arginine N-methyltransferase 3, is a member of the protein arginine methyltransferase family. PRMT3 catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. PRMT3 operates on 40S ribosomal protein S2 ,rpS2, which is the major in-vivo substrate, additionally PRMT3 is also involved in the proper maturation of the 80S ribosome.

    • Synonyms

      Protein Arginine Methyltransferase 3, Heterogeneous Nuclear Ribonucleoprotein, Methyltransferase-Like Protein 3, HRMT1L3, HMT1 HnRNP Methyltransferase-Like 3 (S. Cerevisiae), Protein Arginine N-Methyltransferase 3, HMT1 HnRNP Methyltransferase-Like 3, EC 2.1.1.- ,EC 2.1.1, PRMT3.

    • 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 MGSMCSLASG ATGGRGAVEN EEDLPELSDS GDEAAWEDED DADLPHGKQQ TPCLFCNRLF TSAEETFSHC KSEHQFNIDS MVHKHGLEFY GYIKLINFIR LKNPTVEYMN SIYNPVPWEK EEYLKPVLED DLLLQFDVED LYEPVSVPFS YPNGLSENTS VVEKLKHMEA RALSAEAALA RAREDLQKMK QFAQDFVMHT DVRTCSSSTS VIADLQEDED GVYFSSYGHY GIHEEMLKDK IRTESYRDFI YQNPHIFKDK VVLDVGCGTG ILSMFAAKAG AKKVLGVDQS EILYQAMDII RLNKLEDTIT LIKGKIEEVH LPVEKVDVII SEWMGYFLLF ESMLDSVLYA KNKYLAKGGS VYPDICTISL VAVSDVNKHA DRIAFWDDVY GFKMSCMKKA VIPEAVVEVL DPKTLISEPC GIKHIDCHTT SISDLEFSSD FTLKITRTSM CTAIAGYFDI YFEKNCHNRV VFSTGPQSTK THWKQTVFLL EKPFSVKAGE ALKGKVTVHK NKKDPRSLTV TLTLNNSTQT YGLQ

    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.

    Prmt3 Human
  • View Data Sheet

    Name :

    PAPSS1 Human

    Description:

    3'-Phosphoadenosine 5'-Phosphosulfate Synthase 1 Human Recombinant

    3'-phosphoadenosine 5'-phosphosulfate synthase 1, ATPSK1, PAPSS 1, SK 1, 3-prime-phosphoadenosine 5-prime-phosphosulfate synthase 1, bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1, PAPS synthase 1, Sulfurylase kinase 1, EC 2.7.1.25.

    Product # :

    ENZ-236

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    Description

    PAPSS1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 626 amino acids (24-624) and having a molecular mass of 70.9kDa.PAPSS1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PAPSS1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      PAPSS1 is a bifunctional enzyme with APS kinase and ATP sulfurylase activity. PAPSS1 facilitates two stages in the sulfate activation pathway, yielding 3'-phosphoadenylylsulfate (PAPS). Additionally, PAPSS1 takes part in the biosynthesis of sulfated L-selectin ligands in endothelial cells.

    • Synonyms

      3'-phosphoadenosine 5'-phosphosulfate synthase 1, ATPSK1, PAPSS 1, SK 1, 3-prime-phosphoadenosine 5-prime-phosphosulfate synthase 1, bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1, PAPS synthase 1, Sulfurylase kinase 1, EC 2.7.1.25.

    • 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 MGSHMRATNV TYQAHHVSRN KRGQVVGTRG GFRGCTVWLT GLSGAGKTTV SMALEEYLVC HGIPCYTLDG DNIRQGLNKN LGFSPEDREE NVRRIAEVAK LFADAGLVCI TSFISPYTQD RNNARQIHEG ASLPFFEVFV DAPLHVCEQR DVKGLYKKAR AGEIKGFTGI DSEYEKPEAP ELVLKTDSCD VNDCVQQVVE LLQERDIVPV DASYEVKELY VPENKLHLAK TDAETLPALK INKVDMQWVQ VLAEGWATPL NGFMREREYL QCLHFDCLLD GGVINLSVPI VLTATHEDKE RLDGCTAFAL MYEGRRVAIL RNPEFFEHRK EERCARQWGT TCKNHPYIKM VMEQGDWLIG GDLQVLDRVY WNDGLDQYRL TPTELKQKFK DMNADAVFAF QLRNPVHNGH ALLMQDTHKQ LLERGYRRPV LLLHPLGGWT KDDDVPLMWR MKQHAAVLEE GVLNPETTVV AIFPSPMMYA GPTEVQWHCR ARMVAGANFY IVGRDPAGMP HPETGKDLYE PSHGAKVLTM APGLITLEIV PFRVAAYNKK KKRMDYYDSE HHEDFEFISG TRMRKLAREG QKPPEGFMAP KAWTVLTEYY KSLEKA.

    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.

    Papss1 Human
  • View Data Sheet

    Name :

    SSU72 Human

    Description:

    SSU72 RNA Polymerase II CTD Phosphatase Human Recombinant

    SSU72 RNA polymerase II CTD phosphatase homolog (S. cerevisiae), HSPC182, CTD phosphatase SSU72, Ssu72 RNA polymerase II CTD phosphatase homolog (yeast), PNAS-120, RNA polymerase II subunit A C-terminal domain phosphatase SSU72, EC 3.1.3.16.

    Product # :

    ENZ-243

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    Description

    SSU72 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (1-194) and having a molecular mass of 25.0kDa.SSU72 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SSU72 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SSU72 is an extremely conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. SSU72 interacts with TFIIB, Rb and DNAM-1 and operates to catalyze the dephosphorylation of target proteins, and taking part in RNA processing and termination via dephosphorylation of Pol II. SSU72 is found in multiple alternatively spliced isoforms.

    • Synonyms

      SSU72 RNA polymerase II CTD phosphatase homolog (S. cerevisiae), HSPC182, CTD phosphatase SSU72, Ssu72 RNA polymerase II CTD phosphatase homolog (yeast), PNAS-120, RNA polymerase II subunit A C-terminal domain phosphatase SSU72, EC 3.1.3.16.

    • 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 MGSMPSSPLR VAVVCSSNQN RSMEAHNILS KRGFSVRSFG TGTHVKLPGP APDKPNVYDF KTTYDQMYND LLRKDKELYT QNGILHMLDR NKRIKPRPER FQNCKDLFDL ILTCEERVYD QVVEDLNSRE QETCQPVHVV NVDIQDNHEE ATLGAFLICE LCQCIQHTED MENEIDELLQ EFEEKSGRTF LHTVCFY

    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.

    Ssu72 Human
  • View Data Sheet

    Name :

    GST, His

    Description:

    Glutathione S-Transferase Recombinant, His Tag

    Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    Product # :

    ENZ-451

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    Description

    Recombinant Schistosoma japonicum GST full length protein contains a total of 244 amino acids (1-218 a.a.) expressed in E.coli, having a molecular mass of 28.3kDa. The GST protein is fused to a 20 amino acids His-Tag at N-terminus. The GST protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GST is supplied in PBS pH 7.4 & 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    >10 units/mg, & 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

      Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
      The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions.

    • Synonyms

      Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    • 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 MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMAIIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALDVVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.

    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.

    Glutathione S Transferase His
  • View Data Sheet

    Name :

    ALDOC Mouse

    Description:

    Aldolase C Fructose-Bisphosphate Mouse Recombinant

    Aldolase 3, Brain-type aldolase, Scrapie-responsive protein 2, Zebrin II, Aldo3, Scrg2, Fructose-bisphosphate aldolase C, ALDOC.

    Product # :

    ENZ-868

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    Description

    ALDOC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-363 a.a) and having a molecular mass of 41.9kDa.ALDOC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.

    • Synonyms

      Aldolase 3, Brain-type aldolase, Scrapie-responsive protein 2, Zebrin II, Aldo3, Scrg2, Fructose-bisphosphate aldolase C, ALDOC.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMPHSYP ALSAEQKKEL SDIALRIVTP GKGILAADES VGSMAKRLSQ IGVENTEENR RLYRQVLFSA DDRVKKCIGG VIFFHETLYQ KDDNGVPFVR TIQDKGILVG IKVDKGVVPL AGTDGETTTQ GLDGLLERCA QYKKDGADFA KWRCVLKISD RTPSALAILE NANVLARYAS ICQQNGIVPI VEPEILPDGD HDLKRCQYVT EKVLAAVYKA LSDHHVYLEG TLLKPNMVTP GHACPIKYSP EEIAMATVTA LRRTVPPAVP GVTFLSGGQS EEEASLNLNA INRCPLPRPW ALTFSYGRAL QASALNAWRG QRDNAGAATE EFIKRAEMNG LAAQGRYEGS GDGGAAAQSL YIANHAY

    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.

    Aldoc Mouse
  • View Data Sheet

    Name :

    UBE2G2 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2G2 Human Recombinant

    Ubiquitin-conjugating enzyme E2 G2, E2 ubiquitin-conjugating enzyme G2, Ubiquitin carrier protein G2, Ubiquitin-protein ligase G2, UBE2G2, Ubiquitin-Conjugating Enzyme E2G2, Ubiquitin-conjugating enzyme E2 G2 isoform 1, UBC7.

    Product # :

    ENZ-884

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    Description

    UBE2G2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165a.a.) and having a molecular mass of 21kDa.UBE2G2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2G2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-Conjugating Enzyme E2G2 (UBE2G2) is a protein coding gene which is a part of the E2 ubiquitin-conjugating enzyme family. UBE2G2 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to various proteins. UBE2G2 is ubiquitously expressed mainly in adult muscle. UBE2G2 also takes part in endoplasmic reticulum-associated degradation (ERAD).

    • Synonyms

      Ubiquitin-conjugating enzyme E2 G2, E2 ubiquitin-conjugating enzyme G2, Ubiquitin carrier protein G2, Ubiquitin-protein ligase G2, UBE2G2, Ubiquitin-Conjugating Enzyme E2G2, Ubiquitin-conjugating enzyme E2 G2 isoform 1, UBC7.

    • 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 MGSMAGTALK RLMAEYKQLT LNPPEGIVAG PMNEENFFEW EALIMGPEDT CFEFGVFPAI LSFPLDYPLS PPKMRFTCEM FHPNIYPDGR VCISILHAPG DDPMGYESSA ERWSPVQSVE KILLSVVSML AEPNDESGAN VDASKMWRDD REQFYKIAKQ IVQKSLGL.

    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.

    Ube2G2 Human
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