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Search results

1000 results found for “cathepsin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    FUT7 Human

    Description:

    Fucosyltransferase 7 Human Recombinant

    Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.

    Product # :

    ENZ-784

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    Description

    FUT7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (37-342) and having a molecular mass of 37.9kDa.FUT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FUT7 solution (0.25mg/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

      Fucosyltransferase 7 (FUT7) is a golgi stack membrane protein which is involved in the creation of sialyl-Lewis X antigens. The FUT7 protein leads the synthesis of the E-selectin-binding sialyl-Lewis X moiety. FUT7 catalyzes alpha-1,3 glycosidic linkages involved in the expression of sialyl Lewis X antigens.

    • Synonyms

      Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.

    • 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 MGSPRGTPAP QPTITILVWH WPFTDQPPEL PSDTCTRYGI ARCHLSANRS LLASADAVVF HHRELQTRRS HLPLAQRPRG QPWVWASMES PSHTHGLSHL RGIFNWVLSY RRDSDIFVPY GRLEPHWGPS PPLPAKSRVA AWVVSNFQER QLRARLYRQL APHLRVDVFG RANGRPLCAS CLVPTVAQYR FYLSFENSQH RDYITEKFWR NALVAGTVPV VLGPPRATYE AFVPADAFVH VDDFGSAREL AAFLTGMNES RYQRFFAWRD RLRVRLFTDW RERFCAICDR YPHLPRSQVY EDLEGWFQA.

    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.

    Fut7 Human
  • View Data Sheet

    Name :

    MGLL Human

    Description:

    Monoglyceride Lipase Human Recombinant

    Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.

    Product # :

    ENZ-019

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    Description

    MGLL Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 333 amino acids (1-313 a.a.) and having a molecular mass of 36.4kDa. The MGLL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MGLL solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MGLL is a membrane-associated member of the serine hydrolase superfamily. MGLL is expressed in abundance in skeletal muscle and adipose tissue. MGLL functions jointly with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.

    • Synonyms

      Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.

    • 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 METGPEDPSS MPEESSPRRT PQSIPYQDLP HLVNADGQYL FCRYWKPTGT PKALIFVSHG AGEHSGRYEE LARMLMGLDL LVFAHDHVGH GQSEGERMVV SDFHVFVRDV LQHVDSMQKD YPGLPVFLLG HSMGGAIAIL TAAERPGHFA GMVLISPLVL ANPESATTFK VLAAKVLNLV LPNLSLGPID SSVLSRNKTE VDIYNSDPLI CRAGLKVCFG IQLLNAVSRV ERALPKLTVP FLLLQGSADR LCDSKGAYLL MELAKSQDKT LKIYEGAYHV LHKELPEVTN SVFHEINMWV SQRTATAGTA SPP.

    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.

    Mgll Human
  • View Data Sheet

    Name :

    ADH1C Human, sf9

    Description:

    Alcohol Dehydrogenase 1C, Human Recombinant, sf9

    ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.

    Product # :

    ENZ-1010

    Price :

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    Description

    ADH1C Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 381 amino acids (1-375) and having a molecular mass of 40.6kDa. ADH1C is fused to a 6 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ADH1C protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.

    • Synonyms

      ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.

    • 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

      MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF DLLRSGKSIR
      TVLTFHHHHH H.

    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.

    Adh1C Human Sf9
  • View Data Sheet

    Name :

    DHRS9 Human

    Description:

    Dehydrogenase/Reductase Member 9 Human Recombinant

    Dehydrogenase/reductase SDR family member 9, 3-alpha hydroxysteroid dehydrogenase, 3-alpha-HSD, NADP-dependent retinol dehydrogenase/reductase, RDH-E2, RDHL, Short-chain dehydrogenase/reductase retSDR8, DHRS9, RDH15, RDHTBE, SDR9C4, RETSDR8, 3ALPHA-HSD.

    Product # :

    ENZ-216

    Price :

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    Description

    DHRS9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (18-319) and having a molecular mass of 35.9kDa.DHRS9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DHRS9 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dehydrogenase/reductase SDR family member 9 (DHRS9) functions as a homotetramer, which converts both 3-alpha-tetrahydroprogesterone (allopregnanolone) and 3-alpha-androstanediol to dihydroxyprogesterone and is believed to have a part in retinoic acid biosynthesis.

    • Synonyms

      Dehydrogenase/reductase SDR family member 9, 3-alpha hydroxysteroid dehydrogenase, 3-alpha-HSD, NADP-dependent retinol dehydrogenase/reductase, RDH-E2, RDHL, Short-chain dehydrogenase/reductase retSDR8, DHRS9, RDH15, RDHTBE, SDR9C4, RETSDR8, 3ALPHA-HSD.

    • 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 MGSHMRKGKL KIEDITDKYI FITGCDSGFG NLAARTFDKK GFHVIAACLT ESGSTALKAE TSERLRTVLL DVTDPENVKR TAQWVKNQVG EKGLWGLINN AGVPGVLAPT DWLTLEDYRE PIEVNLFGLI SVTLNMLPLV KKAQGRVINV SSVGGRLAIV GGGYTPSKYA VEGFNDSLRR DMKAFGVHVS CIEPGLFKTN LADPVKVIEK KLAIWEQLSP DIKQQYGEGY IEKSLDKLKG NKSYVNMDLS PVVECMDHAL TSLFPKTHYA AGKDAKIFWI PLSHMPAALQ DFLLLKQKAE LANPKAV.

    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.

    Dhrs9 Human
  • View Data Sheet

    Name :

    HSD17B1 Human

    Description:

    Hydroxysteroid (17-beta) Dehydrogenase 1 Human Recombinant

    E2 17-beta-dehydrogenase 1, EC 1.1.1.62, 17-beta-hydroxysteroid dehydrogenase type 1, 17-beta-HSD 1, 20 alpha-hydroxysteroid dehydrogenase, 20-alpha-HSD, E2DH, Placental 17-beta-hydroxysteroid dehydrogenase, HSD17B1, E17KSR, EDH17B1, EDH17B2, EDHB17, HSD17, SDR28C1.

    Product # :

    ENZ-709

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    Description

    HSD17B1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-328 a.a) and having a molecular mass of 37.5kDa.HSD17B1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HSD17B1 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      E2 17-beta-dehydrogenase 1 (HSD17B1) is a member of the short-chain dehydrogenases/reductases (SDR) family. The HSD17B1 protein advances the reduction of estrogens and androgens. In addition, the HSD17B1 has a 20-alpha-HSD activity. HSD17B1 preferentially uses NADH.

    • Synonyms

      E2 17-beta-dehydrogenase 1, EC 1.1.1.62, 17-beta-hydroxysteroid dehydrogenase type 1, 17-beta-HSD 1, 20 alpha-hydroxysteroid dehydrogenase, 20-alpha-HSD, E2DH, Placental 17-beta-hydroxysteroid dehydrogenase, HSD17B1, E17KSR, EDH17B1, EDH17B2, EDHB17, HSD17, SDR28C1.

    • 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 MGSHMARTVV LITGCSSGIG LHLAVRLASD PSQSFKVYAT LRDLKTQGRL WEAARALACP PGSLETLQLD VRDSKSVAAA RERVTEGRVD VLVCNAGLGL LGPLEALGED AVASVLDVNV VGTVRMLQAF LPDMKRRGSG RVLVTGSVGG LMGLPFNDVY CASKFALEGL CESLAVLLLP FGVHLSLIEC GPVHTAFMEK VLGSPEEVLD RTDIHTFHRF YQYLAHSKQV FREAAQNPEE VAEVFLTALR APKPTLRYFT TERFLPLLRM RLDDPSGSNY VTAMHREVFG DVPAKAEAGA EAGGGAGPGA EDEAGRGAVG DPELGDPPAA PQ.

    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.

    Hsd17B1 Human
  • View Data Sheet

    Name :

    SMS Human

    Description:

    Spermine Synthase Human Recombinant

    Spermine synthase, SPMSY, Spermidine aminopropyltransferase, SMS, SRS, SpS, MRSR.

    Product # :

    ENZ-230

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    Description

    SMS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-366) and having a molecular mass of 43.8kDa.SMS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Spermine synthase (SMS) is amember of the spermidine/spermine synthase family. SMS is an enzyme which converts spermidine into spermine. The SMS enzyme is essential for normal viability, growth and fertility involved in polyamine metabolism. Defects in the SMS gene are the cause of Snyder-Robinson syndrome (SRS), also known as X-linked mental retardation Snyder-Robinson type. SRS is categorized by moderate intellectual deficit, hypotonia, an unsteady gait, osteoporosis, kyphoscoliosis and facial asymmetry, its transmission is X-linked recessive.

    • Synonyms

      Spermine synthase, SPMSY, Spermidine aminopropyltransferase, SMS, SRS, SpS, MRSR.

    • 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 MGSHMAAARH STLDFMLGAK ADGETILKGL QSIFQEQGMA ESVHTWQDHG YLATYTNKNG SFANLRIYPH GLVLLDLQSY DGDAQGKEEI DSILNKVEER MKELSQDSTG RVKRLPPIVR GGAIDRYWPT ADGRLVEYDI DEVVYDEDSP YQNIKILHSK QFGNILILSG DVNLAESDLA YTRAIMGSGK EDYTGKDVLI LGGGDGGILC EIVKLKPKMV TMVEIDQMVI DGCKKYMRKT CGDVLDNLKG DCYQVLIEDC IPVLKRYAKE GREFDYVIND LTAVPISTSP EEDSTWEFLR LILDLSMKVL KQDGKYFTQG NCVNLTEALS LYEEQLGRLY CPVEFSKEIV CVPSYLELWV FYTVWKKAKP.

    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.

    Sms Human
  • View Data Sheet

    Name :

    TKT Human

    Description:

    Transketolase Human Recombinant

    Transketolase, TK, TKT1, EC 2.2.1.1.

    Product # :

    ENZ-588

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    Description

    TKT Human Recombinant produced in E. coli is a single polypeptide chain containing 643 amino acids (1-623) and having a molecular mass of 70.0kDa.TKT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TKT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TKT is a thiamine-dependent enzyme that takes part in the channeling of leftover sugar phosphates to glycolysis in the pentose phosphate pathway. Multiple alternatively spliced variants are known that encode the same protein.

    • Synonyms

      Transketolase, TK, TKT1, EC 2.2.1.1.

    • 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 MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE LLKMFGIDRD AIAQAVRGLI TKA.

    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.

    Tkt Human
  • View Data Sheet

    Name :

    PON2 Human

    Description:

    Paraoxonase-2 Human Recombinant

    Serum paraoxonase, arylesterase 2, EC 3.1.1.2, EC 3.1.8.1, PON 2, Serum aryldialkylphosphatase 2, A-esterase 2, Aromatic esterase 2.

    Product # :

    ENZ-300

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    Description

    Paraoxonase-2 Human Recombinant is expressed in E. coli having a molecular weight of 43.5 kDa and fused to an amino terminal hexahistidine tag.The PON2 purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PON2 is supplied in PBS and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    More Info

    • Introduction

      Paraoxonase 2 (PON2) is a member of a multigene family whose genes share 65% identity at the amino acid level, and is expressed in a variety of tissues, including the pancreas. PON2 overexpression has been shown to lower the intracellular oxidative state and reduce the cells ability to oxidize LDL. PON2 is therefore implicated in the modulation of oxidative stress.

    • Synonyms

      Serum paraoxonase, arylesterase 2, EC 3.1.1.2, EC 3.1.8.1, PON 2, Serum aryldialkylphosphatase 2, A-esterase 2, Aromatic esterase 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • 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.

    • Amino Acid Sequence

      MGRLVAVGLLGIALALLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDID ILPNGLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNP HGISTFIDNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDIT AVGPAHFYATNDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSAN GINISPDDKYIYVADILAHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIW VGCHPNGQKLFVYDPNNPPSSEVLRIQNILSEKPTVTTVYANNGSVLQGSSVASVY DGKLLIGTLYHRALYCELZ.

    • Applications

      Arylesterase 2 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    Pon2 Human
  • View Data Sheet

    Name :

    CNTF Rat, His

    Description:

    Ciliary Neurotrophic Factor Rat Recombinant, His Tag

    Ciliary neurotrophic factor, CNTF, Cntf.

    Product # :

    CYT-926

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    Description

    CNTF Rat Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-200a.a) and having a molecular mass of 25.2kDa.CNTF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNTF protein solution (0.5mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      Ciliary neurotrophic factor, CNTF, Cntf.

    • 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 MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.

    • Background

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 25.2kDa.

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

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

      What is the Biological Activity of CNTF Protein?
      The biological functionality of CNTF Protein will be determined in the future.

      What is the amino acid sequence of CNTF Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
      What applications can CNTF Protein be used in?
      CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Cntf Rat His
  • View Data Sheet

    Name :

    NIT2 Human

    Description:

    Nitrilase Family Member 2 Human Recombinant

    Nitrilase homolog 2, Nitrilase family member 2, omega-amidase NIT2, MGC111199, Nit protein 2, EC 3.5.1.3.

    Product # :

    ENZ-039

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    Description

    NIT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276a.a.) and having a molecular mass of 33kDa.NIT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NIT2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 0.1M NaCl, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      NIT2 is a member of the nitrilase superfamily. NIT2 protein has an omega-amidase activity which removes potentially toxic intermediates by converting alpha-ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively. In addition, Nit2 is widely distributed in nature and is thought to be a tumor suppressor protein.

    • Synonyms

      Nitrilase homolog 2, Nitrilase family member 2, omega-amidase NIT2, MGC111199, Nit protein 2, EC 3.5.1.3.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMTSFRLA LIQLQISSIK SDNVTRACSF IREAATQGAK IVSLPECFNS PYGAKYFPEY AEKIPGESTQ KLSEVAKECS IYLIGGSIPE EDAGKLYNTC AVFGPDGTLL AKYRKIHLFD IDVPGKITFQ ESKTLSPGDS FSTFDTPYCR VGLGICYDMR FAELAQIYAQ RGCQLLVYPG AFNLTTGPAH WELLQRSRAV DNQVYVATAS PARDDKASYV AWGHSTVVNP WGEVLAKAGT EEAIVYSDID LKKLAEIRQQ IPVFRQKRSD LYAVEMKKP

    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.

    Nit2 Human
  • View Data Sheet

    Name :

    PDXP Human

    Description:

    Pyridoxal Phosphatase Human Recombinant

    CIN, PLP, PLPP, EC 3.1.3.74.

    Product # :

    ENZ-551

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    Description

    PDXP Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296 a.a.) and having a molecular mass of 33.8 kDa. The PDXP is fused to 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, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PDXP is the active form of vitamin B6 that functions as a coenzyme in preserving biochemical homeostasis. The desired degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP. PDXP shows activity to pyridoxal 5''-phosphate (PLP), pyridoxine 5''-phosphate (PMP) and Pyridoxine 5''-phosphate (PNP), with a highest activity with PLP followed by PNP.

    • Synonyms

      CIN, PLP, PLPP, EC 3.1.3.74.

    • 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 MARCERLRGA ALRDVLGRAQ GVLFDCDGVL WNGERAVPGA PELLERLARA GKAALFVSNN SRRARPELAL RFARLGFGGL RAEQLFSSAL CAARLLRQRL PGPPDAPGAV FVLGGEGLRA ELRAAGLRLA GDPSAGDGAA PRVRAVLVGY DEHFSFAKLR EACAHLRDPE CLLVATDRDP WHPLSDGSRT PGTGSLAAAV ETASGRQALV VGKPSPYMFE CITENFSIDP ARTLMVGDRL ETDILFGHRC GMTTVLTLTG VSRLEEAQAY LAAGQHDLVP HYYVESIADL TEGLED.

    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.

    Pdxp Human
  • View Data Sheet

    Name :

    CYB5R1 Human

    Description:

    Cytochrome B5 Reductase 1 Human Recombinant

    B5R.1, B5R1, B5R2, humb5R2, NQO3A2, NADH-cytochrome b5 reductase 1, CYB5R1, NAD (P) H: quinone oxidoreductase type 3 polypeptide A2.

    Product # :

    ENZ-727

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    Description

    CYB5R1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 300 amino acids (29-305) and having a molecular mass of 33.8kDa. CYB5R1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CYB5R1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytochrome b5 reductase 1 (CYB5R1) is a part of the flavoprotein pyridine nucleotide cytochrome reductase family. CYB5R1 is engaged in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin decrease.

    • Synonyms

      B5R.1, B5R1, B5R2, humb5R2, NQO3A2, NADH-cytochrome b5 reductase 1, CYB5R1, NAD (P) H: quinone oxidoreductase type 3 polypeptide A2.

    • 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 MGSLVRRSRR PQVTLLDPNE KYLLRLLDKT TVSHNTKRFR FALPTAHHTL GLPVGKHIYL STRIDGSLVI RPYTPVTSDE DQGYVDLVIK VYLKGVHPKF PEGGKMSQYL DSLKVGDVVE FRGPSGLLTY TGKGHFNIQP NKKSPPEPRV AKKLGMIAGG TGITPMLQLI RAILKVPEDP TQCFLLFANQ TEKDIILRED LEELQARYPN RFKLWFTLDH PPKDWAYSKG FVTADMIREH LPAPGDDVLV LLCGPPPMVQ LACHPNLDKL GYSQKMRFTY.

    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.

    Cyb5R1 Human
  • View Data Sheet

    Name :

    CYB5R2 Human

    Description:

    Cytochrome B5 Reductase 2 Human Recombinant

    CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.

    Product # :

    ENZ-799

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    Description

    CYB5R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a.) and having a molecular mass of 33.8kDa. CYB5R2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    CYB5R2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytochrome b5 reductase 2 (CYB5R2) is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. CYB5R2 is responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).

    • Synonyms

      CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.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 MGSMNSRRRE PITLQDPEAK YPLPLIEKEK ISHNTRRFRF GLPSPDHVLG LPVGNYVQLL AKIDNELVVR AYTPVSSDDD RGFVDLIIKI YFKNVHPQYP EGGKMTQYLE NMKIGETIFF RGPRGRLFYH GPGNLGIRPD QTSEPKKTLA DHLGMIAGGT GITPMLQLIR HITKDPSDRT RMSLIFANQT EEDILVRKEL EEIARTHPDQ FNLWYTLDRP PIGWKYSSGF VTADMIKEHL PPPAKSTLIL VCGPPPLIQT AAHPNLEKLG YTQDMIFTY.

    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.

    Cyb5R2 Human
  • View Data Sheet

    Name :

    DHFR Mouse

    Description:

    Dihydrofolate Reductase Mouse Recombinant

    Dihydrofolate reductase, DHFR, DHFRP1, AA607882, AI662710, AW555094, 8430436I03Rik.

    Product # :

    ENZ-069

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    Description

    DHFR Mouse Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.8kDa. The DHFR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DHFR solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 0.2 units/mg, in which one unit will convert 1.0 umole of 7,8 –dihydrofloate and beta-NADPH to 5,6,7,8-tetrahydrofloate and beta-NADP per min at pH 6.5 at 25C.

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    • Introduction

      Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes. DHFR deficiency is associated with megaloblastic anemia. DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid. DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.

    • Synonyms

      Dihydrofolate reductase, DHFR, DHFRP1, AA607882, AI662710, AW555094, 8430436I03Rik.

    • 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 MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFKYFQRMTT TSSVEGKQNL VIMGRKTWFS IPEKNRPLKD RINIVLSREL KEPPRGAHFL AKSLDDALRL IEQPELASKV DMVWIVGGSS VYQEAMNQPG HLRLFVTRIM QEFESDTFFP EIDLGKYKLL PEYPGVLSEV QEEKGIKYKF EVYEKKD.

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    Dhfr Mouse
  • View Data Sheet

    Name :

    ASMT Human

    Description:

    Acetylserotonin O-Methyltransferase Human Recombinant

    HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    Product # :

    ENZ-664

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    Description

    ASMT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298 a.a) and having a molecular mass of 35.3kDa.ASMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASMT is a member of the methyltransferase superfamily. ASMT participates in melatonin biosynthesis. ASMT Expressed in brain, retina and pineal gland, ASMT utilities to catalyze the final reaction in the synthesis of melatonin, particularly the conversion of S-adenosyl-L-methionine and N-acetylserotonin to S-adenosyl-Lhomocysteine and melatonin.

    • Synonyms

      HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    • 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 MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGDF FKDPLPEADL YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD EDRRGPLLTQ LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK

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    Asmt Human
  • View Data Sheet

    Name :

    NT5C3B Human

    Description:

    5'-Nucleotidase, Cytosolic IIIB Human Recombinant

    NT5C3L, 7-methylguanosine phosphate-specific 5'-nucleotidase, Cytosolic 5'-nucleotidase 3B, Cytosolic 5'-nucleotidase III-like protein, cN-III-like protein, N(7)-methylguanylate 5'-phosphatase.

    Product # :

    ENZ-836

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    Description

    NT5C3B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a) and having a molecular mass of 36.8kDa.NT5C3B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NT5C3B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      7-methylguanosine phosphate-specific 5'-nucleotidase (NT5C3B) includes transferase activity and nucleotide binding. Among NT5C3B’s related super-pathways are adenosine nucleotides degradation II and Pyrimidine metabolism. NT5C3B hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP guards cells against undesired retrieval of m(7)GMP and its incorporation into nucleic acids. In addition, NT5C3B has weak activity for CMP.

    • Synonyms

      NT5C3L, 7-methylguanosine phosphate-specific 5'-nucleotidase, Cytosolic 5'-nucleotidase 3B, Cytosolic 5'-nucleotidase III-like protein, cN-III-like protein, N(7)-methylguanylate 5'-phosphatase.

    • 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 MGSMAEEVST LMKATVLMRQ PGRVQEIVGA LRKGGGDRLQ VISDFDMTLS RFAYNGKRCP SSYNILDNSK IISEECRKEL TALLHHYYPI EIDPHRTVKE KLPHMVEWWT KAHNLLCQQK IQKFQIAQVV RESNAMLREG YKTFFNTLYH NNIPLFIFSA GIGDILEEII RQMKVFHPNI HIVSNYMDFN EDGFLQGFKG QLIHTYNKNS SACENSGYFQ QLEGKTNVIL LGDSIGDLTM ADGVPGVQNI LKIGFLNDKV EERRERYMDS YDIVLEKDET LDVVNGLLQH ILCQGVQLEM QGP.

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    Nt5C3B Human
  • View Data Sheet

    Name :

    Carbonic Anhydrase II E.coli

    Description:

    Carbonic Anhydrase II E.coli Recombinant

    Carbonic anhydrase 2, Carbonate dehydratase 2, can, cynT2, yadF, b0126, JW0122, Carbonic Anhydrase II.

    Product # :

    ENZ-373

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    Description

    Carbonic anhydrase II is an E.coli Recombinant protein produced in E.Coli containing 240 amino acids (1-220) and having a molecular mass of 27 kDa. Carbonic anhydrase is expressedwith an amino-terminal hexahistidine tag.The Carbonic anhydrase 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Carbonic Anhydrase 2 enzyme is supplied in 20mM Tris pH-8 and 1mM DTT.

    Purity

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

    More Info

    • Introduction

      The enzyme Carbonic anhydrase II having an accession number of NP_414668 is also called carbonate dehydratase which is part of the enzyme family that catalyses rapid inter-conversion of carbon dioxide & water to bicarbonate, carbonic acid and protons (CO2 + H2O ? HCO3? + H+), a reaction that occurs rather slowly in the absence of a catalyst. The majority of carbonic anhydrases enclose a zinc ion in their active site and therefore is classified as metalloenzymes.
      The most important function of Carbonic anhydrase is known to preserve acid-base balance in blood and other tissues, and to help transport carbon dioxide of tissues. Carbonic anhydrases have been found in all kingdoms of life. Carbonic anhydrase has 3 different classes: alpha, beta and gamma which share very little sequence or structural similarity, thus far they all perform the same function and require a zinc ion at the active site. Mammalian carbonic anhydrase is monomeric and belongs to the alpha class. Plant carbonic anhydrase is dimeric and belongs to the beta class.
      Methane-producing bacteria carbonic anhydrase is trimeric and grows in hot springs which forms the gamma class.

    • Synonyms

      Carbonic anhydrase 2, Carbonate dehydratase 2, can, cynT2, yadF, b0126, JW0122, Carbonic Anhydrase II.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKDIDTLISN NALWSKMLVE EDPGFFEKLAQAQKPRFLWI GCSDSRVPAE RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL HIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK.

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    Carbonic Anhydrase Ii
  • View Data Sheet

    Name :

    PLA2G2A Human

    Description:

    Secreted Phospholipase A2-IIA Human Recombinant

    MOM1, PLA2, PLA2B, PLA2L, PLA2S, PLAS1, sPLA2, Phospholipase A2 membrane associated, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IIA phospholipase A2, GIIC sPLA2, Non-pancreatic secretory phospholipase A2, NPS-PLA2, sPLA2-IIA, PLA2G2A.

    Product # :

    ENZ-290

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    Description

    Secreted Phospholipase A2-IIA Human Recombinant is manufactured with N-terminal fusion of HisTag. PLA2G2A His-Tagged Fusion Protein is 15.8 kDa containing 124 amino acid residues of the human secreted phospholipase A2-IIA and 16 additional amino acid residues – HisTag.

    Source

    Escherichia Coli.

    Formulation

    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 lowmolecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
      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.
      sPLA2-IIA can exert beneficial action in the context of infectious diseases since recent studies have shown that this enzyme exhibits potent bactericidal effects. Induction of the synthesis of sPLA2-IIA is generally initiated by endotoxin and a limited number of cytokines via paracrine and/or autocrine processes.

    • Synonyms

      MOM1, PLA2, PLA2B, PLA2L, PLA2S, PLAS1, sPLA2, Phospholipase A2 membrane associated, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IIA phospholipase A2, GIIC sPLA2, Non-pancreatic secretory phospholipase A2, NPS-PLA2, sPLA2-IIA, PLA2G2A.

    • Physical Appearance

      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

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, an intensive dilution by relevant buffer to a concentration of 10μg/ml is recomended. In higher concentrations the solubility of the PLA2G2A antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMNLVN FHRMIKLTTG KEAALSYGFY GCHCGVGGRG SPKDATDRCC VTHDCCYKRL EKRGCGTKFL SYKFSNSGSR ITCAKQDSCR SQLCECDKAA ATCFARNKTT YNKKYQYYSN KHCRGSTPRC.

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    Pla2G2A Human
  • View Data Sheet

    Name :

    LDHB Human, His

    Description:

    Lactate Dehydrogenase B Human Recombinant, His Tag

    LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.

    Product # :

    ENZ-539

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    Description

    LDHB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-334 a.a.) and having a molecular mass of 38.8 kDa. The LDHB is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LDHB Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 6 units/mg. in which one unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C.

    More Info

    • Introduction

      LDHB is part of the lactate dehydrogenase family. LDHB is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LDHB catalyzes the oxidation of hydroxybutyrate, and frequently called Hydroxybutyrate Dehydrogenase (HBD). The LDH family consists of three members, LDH-A, LDH-B and LDH-C. LDHs function as powerful markers for germ cell tumors.

    • Synonyms

      LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.

    • 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 MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL.

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    Ldhb Human
  • View Data Sheet

    Name :

    TYMS Human

    Description:

    Thymidylate Synthetase Human Recombinant

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

    Product # :

    ENZ-470

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Tyms Human
  • View Data Sheet

    Name :

    PRPS2 Human

    Description:

    Phosphoribosyl Pyrophosphate Synthetase 2 Human Recombinant

    Phosphoribosyl Pyrophosphate Synthetase 2, Phosphoribosyl Pyrophosphate Synthase II, Ribose-Phosphate Diphosphokinase 2, EC 2.7.6.1, PRS-II, Ribose-Phosphate Pyrophosphokinase 2, PPRibP Synthetase , PRS II, PPRibP, PRSII, Ribose-phosphate pyrophosphokinase 2.

    Product # :

    PKA-009

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    Description

    PRPS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a) and having a molecular mass of 37.4kDa. PRPS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    PRPS2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoribosyl Pyrophosphate Synthetase 2, also known as PRPS2 is a member of the ribose-phosphate pyrophosphokinase family. PRPS2 catalyzes the synthesis of 5-phosphoribosyl 1-pyrophosphate from ATP and D-ribose 5-phosphate.

    • Synonyms

      Phosphoribosyl Pyrophosphate Synthetase 2, Phosphoribosyl Pyrophosphate Synthase II, Ribose-Phosphate Diphosphokinase 2, EC 2.7.6.1, PRS-II, Ribose-Phosphate Pyrophosphokinase 2, PPRibP Synthetase , PRS II, PPRibP, PRSII, Ribose-phosphate pyrophosphokinase 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 MGSMPNIVLF SGSSHQDLSQ RVADRLGLEL GKVVTKKFSN QETSVEIGES VRGEDVYIIQ SGCGEINDNL MELLIMINAC KIASSSRVTA VIPCFPYARQ DKKDKVGESR APISAKLVAN MLSVAGADHI ITMDLHASQI QGFFDIPVDN LYAEPAVLQW IRENIAEWKN CIIVSPDAGG AKRVTSIADR LNVEFALIHK ERKKANEVDR MVLVGDVKDR VAILVDDMAD TCGTICHAAD KLLSAGATKV YAILTHGIFS GPAISRINNA AFEAVVVTNT IPQEDKMKHC TKIQVIDISM ILAEAIRRTH NGESVSYLFS HVPL.

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    Prps2 Human
  • View Data Sheet

    Name :

    GPT Rat

    Description:

    Glutamic-Pyruvate Transaminase Rat Recombinant

    Alanine aminotransferase 1 (EC:2.6.1.2), ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, Gpt, Aat1, Gpt1.

    Product # :

    ENZ-918

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    Description

    GPT Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 57.5kDa. GPT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GPT protein solution (1mg/ml) containing Phosphate Buffered Saline pH 7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 60units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.

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    • Introduction

      GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

    • Synonyms

      Alanine aminotransferase 1 (EC:2.6.1.2), ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, Gpt, Aat1, Gpt1.

    • 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 MGSMASRVND QSQASRNGLK GKVLTLDTMN PCVRRVEYAV RGPIVQRALE LEQELRQGVK KPFTEVIRAN IGDAQAMGQR PITFFRQVLA LCVYPNLLSS PDFPEDAKRR AERILQACGG HSLGAYSISS GIQPIREDVA QYIERRDGGI PADPNNIFLS TGASDAIVTM LKLLVSGEGR ARTGVLIPIP QYPLYSAALA ELDAVQVDYY LDEERAWALD IAELRRALCQ ARDRCCPRVL CVINPGNPTG QVQTRECIEA VIRFAFKEGL FLMADEVYQD NVYAEGSQFH SFKKVLMEMG PPYSTQQELA SFHSVSKGYM GECGFRGGYV EVVNMDAEVQ KQMGKLMSVR LCPPVPGQAL MDMVVSPPTP SEPSFKQFQA ERQEVLAELA AKAKLTEQVF NEAPGIRCNP VQGAMYSFPQ VQLPLKAVQR AQELGLAPDM FFCLCLLEET GICVVPGSGF GQQEGTYHFR MTILPPMEKL RLLLEKLSHF HAKFTHEYS.

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    Gpt Rat
  • View Data Sheet

    Name :

    CKMT1A Human

    Description:

    Creatine Kinase, Mitochondrial 1A Human Recombinant

    Creatine kinase mitochondrial 1A, creatine kinase mitochondrial 1 (ubiquitous), creatine kinase U-type mitochondrial, Acidic-type mitochondrial creatine kinase, Ubiquitous mitochondrial creatine kinase, CKMT1, U-MtCK, mia-CK, EC 2.7.3, EC 2.7.3.2.

    Product # :

    CKI-275

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    • description
    • source
    • formulation
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    Description

    CKMT1A Human Recombinant produced in E. coli is a single polypeptide chain containing 403 amino acids (40-417) and having a molecular mass of 45.0 kDa.CKMT1A is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CKMT1A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is greater than 50unit/mg and is defined as the amount of enzyme that convert 1.0 umole of phosphate from phosphocreatine to ADP per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      CKMT1A is in charge of the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. CKMT1A is a member of the creatine kinase isoenzyme family and exists as two isoenzymes, sarcomeric MtCK and ubiquitous MtCK, encoded by separate genes. Mitochondrial creatine kinase arises in two different oligomeric forms: dimers and octamers, unlike the exclusively dimeric cytosolic creatine kinase isoenzymes. Numerous malignant cancers with poor prognosis have displayed overexpression of ubiquitous mitochondrial creatine kinase which is linked to high energy turnover and inability to remove cancer cells through apoptosis.

    • Synonyms

      Creatine kinase mitochondrial 1A, creatine kinase mitochondrial 1 (ubiquitous), creatine kinase U-type mitochondrial, Acidic-type mitochondrial creatine kinase, Ubiquitous mitochondrial creatine kinase, CKMT1, U-MtCK, mia-CK, EC 2.7.3, EC 2.7.3.2.

    • 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 MGSHMASERR RLYPPSAEYP DLRKHNNCMA SHLTPAVYAR LCDKTTPTGW TLDQCIQTGV DNPGHPFIKT VGMVAGDEET YEVFADLFDP VIQERHNGYD PRTMKHTTDL DASKIRSGYF DERYVLSSRV RTGRSIRGLS LPPACTRAER REVERVVVDA LSGLKGDLAG RYYRLSEMTE AEQQQLIDDH FLFDKPVSPL LTAAGMARDW PDARGIWHNN EKSFLIWVNE EDHTRVISME KGGNMKRVFE RFCRGLKEVE RLIQERGWEF MWNERLGYIL TCPSNLGTGL RAGVHIKLPL LSKDSRFPKI LENLRLQKRG TGGVDTAATG GVFDISNLDR LGKSEVELVQ LVIDGVNYLI DCERRLERGQ DIRIPTPVIH TKH

    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.

    Ckmt1A Human
  • View Data Sheet

    Name :

    CXCL6 Human

    Description:

    Granulocyte Chemotactic Protein 2 (CXCL6) Human Recombinant

    C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.

    Product # :

    CHM-025

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    Shipped at Room temp

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    Description

    GCP-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9kDa.

    Source

    Escherichia Coli.

    Formulation

    GCP-2 protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-50 ng/ml corresponding to a specific activity of 20,000-100,000 IU/mg.

    More Info

    • Introduction

      Granulocyte Chemotactic Protein 2 (CXCL6), also known as GCP-2, is a Chemotactic for neutrophil granulocytes. GCP-2 signals through binding and activation of its receptors (CXCR1 and CXCR2). GCP-2 has strong antibacterial activity against Gram-positive and Gram-negative bacteria In addition to its chemotactic and angiogenic property.

    • Synonyms

      C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VLTELRCTCL RVTLRVNPKT IGKLQVFPAG PQCSKVEVVA SLKNGKQVCL DPEAPFLKKV IQKILDSGNK KN.

    • Background

      What is the molecular weight/Mw of CXCL6 HUMAN Protein?
      CXCL6 HUMAN Protein has a total Mw of 7.9kDa.

      What is the source or expression system of CXCL6 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL6 HUMAN Protein?
      CXCL6 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL6 HUMAN Protein?
      Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-50 ng/ml corresponding to a specific activity of 20,000-100,000 IU/mg.

      What is the amino acid sequence of CXCL6 HUMAN Protein?
      VLTELRCTCL RVTLRVNPKT IGKLQVFPAG PQCSKVEVVA SLKNGKQVCL DPEAPFLKKV IQKILDSGNK KN.

      What applications can CXCL6 HUMAN Protein be used in?
      CXCL6 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL6 HUMAN Protein?
      The endotoxin level is minimal, CXCL6 HUMAN Protein was purified using conventional chromatography techniques.


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

    Gcp 2 Human
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