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Search results

1000 results found for “enolase”

Name

Description

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  • View Data Sheet

    Name :

    PMM1 Human

    Description:

    Phosphomannomutase 1 Human Recombinant

    Phosphomannomutase 1, PMM 1, PMMH-22, PMM1, PMMH22, Sec53.

    Product # :

    ENZ-023

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    Description

    PMM1 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 282 amino acids (1-262 a.a.) and having a molecular mass of 31.9kDa. The PMM1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PMM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 100mM NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphomannomutase 1 (PMM1) is an enzyme involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. PMM1 catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for the synthesis of dolichol-phosphate-mannose, which is crucial for N-linked glycosylation and accordingly the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol (GPI) anchored proteins. Additionally, PMM1 may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.

    • Synonyms

      Phosphomannomutase 1, PMM 1, PMMH-22, PMM1, PMMH22, Sec53.

    • 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 MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV VGGSDYCKIA EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR LPKKRGTFIE FRNGMLNISP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR FSRGGMISFD VFPEGWDKRY CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV VSPQDTVQRC REIFFPETAH EA.

    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.

    Pmm1 Human
  • View Data Sheet

    Name :

    PRSS22 Mouse

    Description:

    Protease Serine 22 Mouse Recombinant

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

    Product # :

    ENZ-964

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Prss22 Mouse
  • View Data Sheet

    Name :

    PRTFDC1 Human

    Description:

    Phosphoribosyl Transferase Domain Containing 1 Human Recombinant

    Phosphoribosyltransferase domain-containing protein 1, PRTFDC1, HHGP.

    Product # :

    ENZ-142

    Price :

    Quantity :

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    Description

    PRTFDC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-225 a.a.) and having a molecular mass of 28.1kDa.PRTFDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRTFDC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphoribosyltransferase domain-containing protein 1 (PRTFDC1) is a member of the purine/pyrimidine phosphoribosyltransferase family. PRTFDC1 has a low, barely measurable phosphoribosyltransferase activity (in vitro). PRTFDC1 can bind GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). PRTFDC1 is not expected to impact purine metabolism or GMP salvage.

    • Synonyms

      Phosphoribosyltransferase domain-containing protein 1, PRTFDC1, HHGP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      PRTFDC1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAGSSEE APDYGRGVVI MDDWPGYDLN LFTYPQHYYG DLEYVLIPHG IIVDRIERLA KDIMKDIGYS DIMVLCVLKG GYKFCADLVE HLKNISRNSD RFVSMKVDFI RLKSYRNDQS MGEMQIIGGD DLSTLAGKNV LIVEDVVGTG RTMKALLSNI EKYKPNMIKV ASLLVKRTSR SDGFRPDYAG FEIPNLFVVG YALDYNEYFR DLNHICVINE HGKEKYRV.

    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.

    Prtfdc1 Human
  • View Data Sheet

    Name :

    UCK1 Human

    Description:

    Uridine-Cytidine Kinase 1 Human Recombinant

    Uridine-cytidine kinase 1, UCK 1, Cytidine monophosphokinase 1, UCK1 Uridine monophosphokinase 1, URK1, FLJ12255, RP11-334J6.5, Uridine-cytidine kinase 1 isoform a.

    Product # :

    PKA-317

    Price :

    Quantity :

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    Description

    UCK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (143-273a.a) and having a molecular mass of 17.5kDa.UCK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UCK1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UCK1 is a uridine-cytidine kinase which catalyzes the phosphorylation of uridine and cytidine to uridine monophosphate and cytidine monophosphate. UCK1 does not phosphorylate deoxyribonucleosides or purine ribonucleosides. UCK1 is also phosphorylates uridine and cytidine analogs and uses ATP and GTP as a phosphate donor.

    • Synonyms

      Uridine-cytidine kinase 1, UCK 1, Cytidine monophosphokinase 1, UCK1 Uridine monophosphokinase 1, URK1, FLJ12255, RP11-334J6.5, Uridine-cytidine kinase 1 isoform a.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MFYSQEIRDM FHLRLFVDTD SDVRLSRRVL RDVRRGRDLE QILTQYTTFV KPAFEEFCLP TKKYADVIIP RGVDNMVAIN LIVQHIQDIL NGDICKWHRG GSNGRSYKRT FSEPGDHPGM LTSGKRSHLE SS.

    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.

    Uck1 Human
  • View Data Sheet

    Name :

    CNDP2 Human

    Description:

    CNDP Dipeptidase 2 Human Recombinant

    Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.

    Product # :

    ENZ-681

    Price :

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    Description

    CNDP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 498 amino acids (1-475) and having a molecular mass of 55.3 kDa. CNDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CNDP2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CNDP Dipeptidase 2 (CNDP2), is a cytosolic, non-specific dipeptidase which is a part of the peptidase M20A protein family. CNDP2 is a secreted peptidase homologous to M20 peptidases. CNDP2 expresses through all adult and fetal tissue, though, an isoform missing exons 3 and 4 expresses in all fetal tissue in adult liver. Over expression of CPGL-B in hepatocellular carcinoma cells results in significant inhibition of HC cell viability, colony formation, cell invasiveness and tumor configuration.

    • Synonyms

      Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAALTTL FKYIDENQDR YIKKLAKWVA IQSVSAWPEK RGEIRRMMEV AAADVKQLGG SVELVDIGKQ KLPDGSEIPL PPILLGRLGS DPQKKTVCIY GHLDVQPAAL EDGWDSEPFT LVERDGKLYG RGSTDDKGPV AGWINALEAY QKTGQEIPVN VRFCLEGMEE SGSEGLDELI FARKDTFFKD VDYVCISDNY WLGKKKPCIT YGLRGICYFF IEVECSNKDL HSGVYGGSVH EAMTDLILLM GSLVDKRGNI LIPGINEAVA AVTEEEHKLY DDIDFDIEEF AKDVGAQILL HSHKKDILMH RWRYPSLSLH GIEGAFSGSG AKTVIPRKVV GKFSIRLVPN MTPEVVGEQV TSYLTKKFAE LRSPNEFKVY MGHGGKPWVS DFSHPHYLAG RRAMKTVFGV EPDLTREGGS IPVTLTFQEA TGKNVMLLPV GSADDGAHSQ NEKLNRYNYI EGTKMLAAYL YEVSQLKD.

    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.

    Cndp2 Human
  • View Data Sheet

    Name :

    PYCR2 Human

    Description:

    Pyrroline-5-Carboxylate Reductase 2 Human Recombinant

    P5CR2, Pyrroline-5-carboxylate reductase 2 isoform 1, P5C reductase 2.

    Product # :

    ENZ-118

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    Description

    PYCR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a) and having a molecular mass of 36kDa.PYCR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PYCR2 protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 50% glycerol, 5mM DTT and 1mM EDTA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pyrroline-5-carboxylate reductase 2 isoform 1 (PYCR2) is a member of the pyrroline-5-carboxylate reductase family. PYCR2 protein catalyzes the conversion of pyrroline-5-carboxylate to proline, which is the last step in proline biosynthesis. The three substrates of the PYCR2 enzyme are L-proline, NAD+, and NADP+, while its four products are 1-pyrroline-5-carboxylate, NADH, NADPH, and H+.

    • Synonyms

      P5CR2, Pyrroline-5-carboxylate reductase 2 isoform 1, P5C reductase 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 MGSMSVGFIG AGQLAYALAR GFTAAGILSA HKIIASSPEM NLPTVSALRK MGVNLTRSNK ETVKHSDVLF LAVKPHIIPF ILDEIGADVQ ARHIVVSCAA GVTISSVEKK LMAFQPAPKV IRCMTNTPVV VQEGATVYAT GTHALVEDGQ LLEQLMSSVG FCTEVEEDLI DAVTGLSGSG PAYAFMALDA LADGGVKMGL PRRLAIQLGA QALLGAAKML LDSEQHPCQL KDNVCSPGGA TIHALHFLES GGFRSLLINA VEASCIRTRE LQSMADQEKI SPAALKKTLL DRVKLESPTV STLTPSSPGK LLTRSLALGG KKD.

    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.

    Pycr2 Human
  • View Data Sheet

    Name :

    CS Human

    Description:

    Citrate Synthase Human Recombinant

    Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, mitochondrial.

    Product # :

    ENZ-824

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    Description

    CS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (28-466 a.a) and having a molecular mass of 51.4kDa. CS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CS protein 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

      Citrate synthase also known as CS is a Krebs tricarboxylic acid cycle enzyme which catalyzes the synthesis of citrate from oxaloacetate and acetyl coenzyme A. CS is present in almost all cells capable of oxidative metabolism. CS is nuclear encoded and transported into the mitochondrial matrix, where the mature form is found. The diseases related to CS are: critical illness polyneuropathy and mitochondrial cardiomyopathy.

    • Synonyms

      Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, mitochondrial.

    • 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 MGSASSTNLK DILADLIPKE QARIKTFRQQ HGKTVVGQIT VDMMYGGMRG MKGLVYETSV LDPDEGIRFR GFSIPECQKL LPKAKGGEEP LPEGLFWLLV TGHIPTEEQV SWLSKEWAKR AALPSHVVTM LDNFPTNLHP MSQLSAAVTA LNSESNFARA YAQGISRTKY WELIYEDSMD LIAKLPCVAA KIYRNLYREG SGIGAIDSNL DWSHNFTNML GYTDHQFTEL TRLYLTIHSD HEGGNVSAHT SHLVGSALSD PYLSFAAAMN GLAGPLHGLA NQEVLVWLTQ LQKEVGKDVS DEKLRDYIWN TLNSGRVVPG YGHAVLRKTD PRYTCQREFA LKHLPNDPMF KLVAQLYKIV PNVLLEQGKA KNPWPNVDAH SGVLLQYYGM TEMNYYTVLF GVSRALGVLA QLIWSRALGF PLERPKSMST EGLMKFVDSK SG.

    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.

    Cs Human
  • View Data Sheet

    Name :

    CTH Human

    Description:

    Cystathionase Human Recombinant

    Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.

    Product # :

    ENZ-212

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    Description

    CTH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-405) and having a molecular mass of 46.7kDa.CTH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTH solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystathionine gamma-lyase or cystathionase (CTH) is a member of the trans-sulfuration enzymes family. CTH is an enzyme which breaks down cystathionine into cysteine and alpha-ketobutyrate. The CTH catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in the CTH gene cause cystathioninuria.

    • Synonyms

      Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.

    • 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 MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS.

    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.

    Cth Human
  • View Data Sheet

    Name :

    AK1 Human

    Description:

    Adenylate Kinase 1 Human Recombinant

    Adenylate kinase isoenzyme 1, AK 1, ATP-AMP transphosphorylase 1, Myokinase, AK1.

    Product # :

    PKA-316

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    Description

    AK1 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 214 amino acids (1-194 a.a.) and having a molecular mass of 23.7kDa. The AK1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AK1 protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 600 units/mg. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 25°C.

    More Info

    • Introduction

      AK1 is a small ubiquitous enzyme which is essential for maintenance and cell growth. It is involved in the regulation of adenine nucleotide composition within a cell by catalyzing the reversible transfer of the terminal phosphate group between ATP and AMP. The AK1 protein is found in the cytosol of skeletal muscle, brain and erythrocytes. Defects in the AK1 gene are the cause of a form of hemolytic anemia.

    • Synonyms

      Adenylate kinase isoenzyme 1, AK 1, ATP-AMP transphosphorylase 1, Myokinase, AK1.

    • 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 MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG SARGKKLSEI MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ QGEEFERRIG QPTLLLYVDA GPETMTQRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD SVFSQVCTHL DALK.

    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.

    Ak1 Human
  • View Data Sheet

    Name :

    DBH Human

    Description:

    DBH Human Recombinant

    EC 1.14.17.1, DBM, DBH.

    Product # :

    ENZ-891

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    Description

    DBH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 599 amino acids (40-617 a.a) and having a molecular mass of 67.2kDa.DBH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DBH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DBH catalyzes the chemical reaction. DBH is an oxidoreductase which belongs to the copper type II, ascorbate-dependent monooxygenase family, in particular those performing on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated can not be derived from O2 with reduced ascorbate as one donor, as well as incorporation of one ato of oxygen into the other donor.

    • Synonyms

      EC 1.14.17.1, DBM, DBH.

    • 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 MSAPRESPLP YHIPLDPEGS LELSWNVSYT QEAIHFQLLV RRLKAGVLFG MSDRGELENA DLVVLWTDGD TAYFADAWSD QKGQIHLDPQ QDYQLLQVQR TPEGLTLLFK RPFGTCDPKD YLIEDGTVHL VYGILEEPFR SLEAINGSGL QMGLQRVQLL KPNIPEPELP SDACTMEVQA PNIQIPSQET TYWCYIKELP KGFSRHHIIK YEPIVTKGNE ALVHHMEVFQ CAPEMDSVPH FSGPCDSKMK PDRLNYCRHV LAAWALGAKA FYYPEEAGLA FGGPGSSRYL RLEVHYHNPL VIEGRNDSSG IRLYYTAKLR RFNAGIMELG LVYTPVMAIP PRETAFILTG YCTDKCTQLA LPPSGIHIFA SQLHTHLTGR KVVTVLVRDG REWEIVNQDN HYSPHFQEIR MLKKVVSVHP GDVLITSCTY NTEDRELATV GGFGILEEMC VNYVHYYPQT QLELCKSAVD AGFLQKYFHL INRFNNEDVC TCPQASVSQQ FTSVPWNSFN RDVLKALYSF APISMHCNKS SAVRFQGEWN LQPLPKVIST LEEPTPQCPT SQGRSPAGPT VVSIGGGKG

    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.

    Dbh Human
  • View Data Sheet

    Name :

    ALKBH3 Human

    Description:

    ALKB Alkylation Repair Homolog 3 Human Recombinant

    Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3, Alkylated DNA repair protein alkB homolog 3, DEPC-1, Prostate cancer antigen 1, ALKBH3, ABH3, DEPC1, PCA1, FLJ43614, MGC118790, MGC118792, MGC118793.

    Product # :

    ENZ-101

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    Description

    ALKBH3 Human Recombinant fused to 39 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 325 amino acids (1-286 a.a.) and having a molecular mass of 37.9kDa. The ALKBH3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ALKBH3 solution 1mg/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.

    More Info

    • Introduction

      ALKBH3 belongs to the ALKB family of proteins and acts as a dioxygenase with a preference for RNA and single stranded DNA substrates. ALKBH3 protein repairs 1-methyladenine and 3-methylcytosine lesions in alkylated DNA and RNA and its activity is stimulated by ascorbate. ALKBH3 is expressed in a broad array of tissues and localizes to the cytoplasm and the nucleus.

    • Synonyms

      Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3, Alkylated DNA repair protein alkB homolog 3, DEPC-1, Prostate cancer antigen 1, ALKBH3, ABH3, DEPC1, PCA1, FLJ43614, MGC118790, MGC118792, MGC118793.

    • 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 KDRWGSELDM EEKRRRARVQ GAWAAPVKSQ AIAQPATTAK SHLHQKPGQT WKNKEHHLSD REFVFKEPQQ VVRRAPEPRV IDREGVYEIS LSPTGVSRVC LYPGFVDVKE ADWILEQLCQ DVPWKQRTGI REDITYQQPR LTAWYGELPY TYSRITMEPN PHWHPVLRTL KNRIEENTGH TFNSLLCNLY RNEKDSVDWH SDDEPSLGRC PIIASLSFGA TRTFEMRKKP PPEENGDYTY VERVKIPLDH GTLLIMEGAT QADWQHRVPK EYHSREPRVN LTFRTVYPDP RGAPW.

    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.

    Alkbh3 Human
  • View Data Sheet

    Name :

    HSD17B11 Human

    Description:

    Hydroxysteroid (17-beta) Dehydrogenase 11 Human Recombinant

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

    Product # :

    ENZ-049

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Hsd17B11 Human
  • View Data Sheet

    Name :

    DIRAS1 Human

    Description:

    DIRAS family, GTP-binding RAS-like 1 Human Recombinant

    GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.

    Product # :

    PRO-256

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    Description

    DIRAS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 215 amino acids (1-195a.a.) and having a molecular mass of 24.1 kDa. DIRAS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    DIRAS1 Human solution (1mg/ml) containing 20mM Tris-HCl buffer(pH 8.0) containing 20% glycerol, 1mM DTT, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      DIRAS1 is a member of a distinct branch of the functionally diverse Ras superfamily of monomeric GTPases. DIRAS1 demonstrates low GTPase activity and exists mainly in the GTP-bound form. Ras proteins operate as binary molecular switches that control intracellular signaling networks. Ras-regulated signal pathways regulate such processes as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. Ras and ras-related proteins are frequently deregulated in cancers, leading to increased invasion and metastasis, and decreased apoptosis.

    • Synonyms

      GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.

    • 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 MPEQSNDYRV VVFGAGGVGK SSLVLRFVKG TFRDTYIPTI EDTYRQVISC DKSVCTLQIT DTTGSHQFPA MQRLSISKGH AFILVFSVTS KQSLEELGPI YKLIVQIKGS VEDIPVMLVG KCDETQREV DTREAQAVAQ EWKCAFMETS AKMNYNVKEL FQELLTLETR RNMSLNIDGK RSGKQKRTDR KGKC.

    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.

    Diras1 Human
  • View Data Sheet

    Name :

    CXCL5 Human

    Description:

    Epithelial Neutrophil-Activating Protein 78 Human Recombinant (CXCL5)

    Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    Product # :

    CHM-331

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    • More Info

    Description

    Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8020 Dalton. The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXCL5 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

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

    Biological Activity

    The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg)  of recombinant human ENA-78.

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    • Introduction

      Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II IFN. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.

    • Synonyms

      Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ENA78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.

    • Background

      What is the molecular weight/Mw of CXCL5 HUMAN Protein?
      CXCL5 HUMAN Protein has a total Mw of 8.02kDa.

      What is the source or expression system of CXCL5 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 HUMAN Protein?
      CXCL5 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 HUMAN Protein?
      The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.

      What is the amino acid sequence of CXCL5 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.

      What applications can CXCL5 HUMAN Protein be used in?
      CXCL5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 HUMAN Protein?
      The endotoxin level is minimal, CXCL5 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.

    Ena 78 Human
  • View Data Sheet

    Name :

    ENTPD6 Mouse

    Description:

    Ectonucleoside Triphosphate Diphosphohydrolase 6 Mouse Recombinant

    ectonucleoside triphosphate diphosphohydrolase 6 isoform1, 2700026H11Rik, Cd39l, Cd39l2, dJ738P15.3, NTPDa, NTPDase-6, Entpd6.

    Product # :

    PRO-2672

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    Description

    ENTPD6 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (33-455 a.a) containing 433 amino acids and having a molecular mass of 47.3 kDa.ENTPD6 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    ENTPD6 protein (0.25mg/ml) contains 20% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 80,000 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze GDP per minute at pH 7.5 at 25C.

    More Info

    • Introduction

      Ectonucleoside Triphosphate Diphosphohydrolase 6 or ENTPD6 is an enzyme, akin to E-type nucleotidases. E-type nucleotidases, for instance CD39, are responsible for extracellular nucleotides catabolism. ENTPD6 has four apyrase-conserved areas like all to E-type nucleotidases. Rather spliced transcript agents that codes various isoforms were discovered for the DNA segment.

    • Synonyms

      ectonucleoside triphosphate diphosphohydrolase 6 isoform1, 2700026H11Rik, Cd39l, Cd39l2, dJ738P15.3, NTPDa, NTPDase-6, Entpd6.

    • 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

      DGSMKWHRAS AAQAFFTIAG AASGARWTQQ AFSSPGSAAR GHEVFYGIMF DAGSTGTRIH VFQFARPPGE TPTLTHETFK ALKPGLSAYA DDVEKSAQGI QELLNVAKQH IPYDFWKATP LVLKATAGLR LLPGEKAQKL LQKVKEVFKA SPFLVGDDCV SIMNGTDEGV SAWITVNFLT GSLKTPGSSS VGMLDLGGGS TQITFLPRVE GTLQASPPGH LTALQMFNRT
      YKLYSYSYLG LGLMSARLAI LGGVEGKPAE NDKELVSPCL SPRFRGEWEH AEVTYRISGQ KAVGLYELCA SRVSEVLRNK VHRTEEAQHV DFYAFSYYYD LAASFGLIDA EKGGSLVVGD FEIAAKYVCR TLETQPPSSP FACMDLTYIS LLLHEFGFPG DKVLKLARKI DNVETSWALG AIFHYIDSLK RQKVPALHHH HHH

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    Entpd6 Mouse
  • View Data Sheet

    Name :

    BLMH Human

    Description:

    BLM Hydrolase Human Recombinant

    BMH, BH, BLM hydrolase.

    Product # :

    ENZ-018

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    Description

    BLMH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 475 amino acids (1-455a.a.) and having a molecular mass of 54.7kDa.BLMH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BLMH protein solution (1mg/1ml) is formulated in 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 1,000 pmole/min/ug. Measured by the hydrolysis of Met-AMC at pH 7.5, at 37C.

    More Info

    • Introduction

      BLMH is affiliate to the papain superfamily of the cysteine protease and the peptidase C1 family. BLMH is a cytoplasmic cysteinepeptidase usually found as a homohexamer. The standard physiological role of BLMH has not been determined, but it shields normal and malignant cells from the glycopeptide antitumor drug BLM. BLMH catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and in addition demonstrates general aminopeptidase activity.

    • Synonyms

      BMH, BH, BLM hydrolase.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSSGLNSEK VAALIQKLNS DPQFVLAQNV GTTHDLLDIC LKRATVQRAQ HVFQHAVPQE GKPITNQKSS GRCWIFSCLN VMRLPFMKKL NIEEFEFSQS YLFFWDKVER CYFFLSAFVD TAQRKEPEDG RLVQFLLMNP ANDGGQWDML VNIVEKYGVI PKKCFPESYT TEATRRMNDI LNHKMREFCI RLRNLVHSGA TKGEISATQD VMMEEIFRVV CICLGNPPET FTWEYRDKDK NYQKIGPITP LEFYREHVKP LFNMEDKICL VNDPRPQHKY NKLYTVEYLS NMVGGRKTLY NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNSKLGLSD MNLYDHELVF GVSLKNMNKA ERLTFGESLM THAMTFTAVS EKDDQDGAFT KWRVENSWGE DHGHKGYLCM TDEWFSEYVY EVVVDRKHVP EEVLAVLEQE PIILPAWDPM GALAE

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    Blmh Human
  • View Data Sheet

    Name :

    CASP3 Human

    Description:

    Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant

    Caspase 3 Apoptosis-Related Cysteine Peptidase, CPP32 Caspase 3 Apoptosis-Related Cysteine Protease, Cysteine Protease CPP32, Protein Yama, CASP-3, CPP-32, SCA-1, SREBP Cleavage Activity 1, EC 3.4.22.56, CPP32B, caspase-3, PARP Cleavage Protease, procaspase3, Apopain, EC 3.4.22, CASP3.

    Product # :

    ENZ-791

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    Description

    CASP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 103 amino acids (176-277) and having a molecular mass of 12kDa.CASP3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CASP3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Caspase 3 Apoptosis-Related Cysteine Peptidase (CASP3) belongs to the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a key role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to generate 2 subunits, large and small, that dimerize to create the active enzyme. CASP3 protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. CASP3 is the leading caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is linked with neuronal death in Alzheimer's disease. In addition, CASP3 is involved in the cleavage of huntingtin. CASP3 also cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. CASP3 initiates cell adhesion in sympathetic neurons through RET cleavage.

    • Synonyms

      Caspase 3 Apoptosis-Related Cysteine Peptidase, CPP32 Caspase 3 Apoptosis-Related Cysteine Protease, Cysteine Protease CPP32, Protein Yama, CASP-3, CPP-32, SCA-1, SREBP Cleavage Activity 1, EC 3.4.22.56, CPP32B, caspase-3, PARP Cleavage Protease, procaspase3, Apopain, EC 3.4.22, CASP3.

    • 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

      MSGVDDDMAC HKIPVEADFL YAYSTAPGYY SWRNSKDGSW FIQSLCAMLK QYADKLEFMH ILTRVNRKVA TEFESFSFDA TFHAKKQIPC IVSMLTKELY FYH.

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    Casp3 Human
  • View Data Sheet

    Name :

    Placental Lactogen Ovine

    Description:

    Placental Lactogen Ovine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    Product # :

    CYT-512

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis gel filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Gln-His-Pro-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.85 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Placental Lactogen Ovine
  • View Data Sheet

    Name :

    GCAT Human

    Description:

    Glycine C-Acetyltransferase Human Recombinant

    2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

    Product # :

    ENZ-705

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    Description

    GCAT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (22-419 a.a) and having a molecular mass of 45kDa.GCAT is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GCAT protein solution (1mg/ml) containing 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

      L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.

    • Synonyms

      2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

    • 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 MSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP.

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    Gcat Human
  • View Data Sheet

    Name :

    GMDS Human

    Description:

    GDP-Mannose 4,6-Dehydratase Human Recombinant

    GDP-mannose 4,6-dehydratase, GMD, SDR3E1, short chain dehydrogenase/reductase family 3E member 1, GDP-D-mannose dehydratase, EC 4.2.1.47.

    Product # :

    ENZ-191

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    Description

    GMDS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 392 amino acids (1-372) and having a molecular mass of 44.1 kDa.GMDS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GMDS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl, 0.1mM PMSF and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GMDS is a member of the GDP-mannose 4,6-dehydratase family. GMDS uses NADP as a cofactor to catalyze the conversion of GDP-mannose to GDP-4-keto-6-deoxymannose. Defects in the gene encoding GMDS cause TRAIL (tumor necrosis factor-related apoptosis-inducing ligand)-induced apoptosis.

    • Synonyms

      GDP-mannose 4,6-dehydratase, GMD, SDR3E1, short chain dehydrogenase/reductase family 3E member 1, GDP-D-mannose dehydratase, EC 4.2.1.47.

    • 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 MAHAPARCPS ARGSGDGEMG KPRNVALITG ITGQDGSYLA EFLLEKGYEV HGIVRRSSSF NTGRIEHLYK NPQAHIEGNM KLHYGDLTDS TCLVKIINEV KPTEIYNLGA QSHVKISFDL AEYTADVDGV GTLRLLDAVK TCGLINSVKF YQASTSELYG KVQEIPQKET TPFYPRSPYG AAKLYAYWIV VNFREAYNLF AVNGILFNHE SPRRGANFVT RKISRSVAKI YLGQLECFSL GNLDAKRDWG HAKDYVEAMW LMLQNDEPED FVIATGEVHS VREFVEKSFL HIGKTIVWEG KNENEVGRCK ETGKVHVTVD LKYYRPTEVD FLQGDCTKAK QKLNWKPRVA FDELVREMVH ADVELMRTNP NA.

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    Gmds 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.

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    Tymp Human
  • View Data Sheet

    Name :

    GPT2 Human

    Description:

    Glutamic-Pyruvate Transaminase 2 Human Recombinant

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

    Product # :

    ENZ-680

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    Description

    GPT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 546 amino acids (1-523) and having a molecular mass of 60.3 kDa. GPT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPT2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 7.5), 30% glycerol, 0.2M NaCl and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMQRAAAL VRRGCGPRTP SSWGRSQSSA AAEASAVLKV RPERSRRERI LTLESMNPQV KAVEYAVRGP IVLKAGEIEL ELQRGIKKPF TEVIRANIGD AQAMGQQPIT FLRQVMALCT YPNLLDSPSF PEDAKKRARR ILQACGGNSL GSYSASQGVN CIREDVAAYI TRRDGGVPAD PDNIYLTTGA SDGISTILKI LVSGGGKSRT GVMIPIPQYP LYSAVISELD AIQVNYYLDE ENCWALNVNE LRRAVQEAKD HCDPKVLCII NPGNPTGQVQ SRKCIEDVIH FAWEEKLFLL ADEVYQDNVY SPDCRFHSFK KVLYEMGPEY SSNVELASFH STSKGYMGEC GYRGGYMEVI NLHPEIKGQL VKLLSVRLCP PVSGQAAMDI VVNPPVAGEE SFEQFSREKE SVLGNLAKKA KLTEDLFNQV PGIHCNPLQG AMYAFPRIFI PAKAVEAAQA HQMAPDMFYC MKLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPVEKLKTV LQKVKDFHIN FLEKYA.

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    Gpt2 Human
  • View Data Sheet

    Name :

    RELM a Mouse, His

    Description:

    RELM-Alpha Mouse Recombinant, His Tag

    Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.

    Product # :

    CYT-453

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    Description

    RELM-alpha Mouse Recombinant is manufactured with a signal sequence of phage fd (20aa) and C-terminal fusion of flagTag (10aa). The RELM-alpha Flag-Tagged Fusion Protein is a 13.3 kDa protein containing 91 amino acid residues with 30 additional amino acid residues - signal sequence of phage fd, flagTag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered and lyophilized from 0.5 mg/ml in 5mM Tris pH 7.5, 25mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Bronchoalveolar lavage fluid from mice with experimentally induced allergic pulmonary inflammation contains a novel 9.4 kDa cysteine-rich secreted protein, RELM-alpha (FIZZ1, found in inflammatory zone). RELM-alpha is a secreted protein that has a restricted tissue distribution with highest levels in adipose tissue stroma. Murine RELM-alpha (FIZZ1) is the founding member of a new gene family including two other murine genes expressed, respectively, in intestinal crypt epithelium (RELM-beta) and white adipose tissue (Resistin), and two related human genes.
      RELMalpha inhibits the differentiation of 3T3-L1 preadipocytes into adipocytes but has no effect on proliferation of 3T3-L1 preadipocytes. RELMalpha is able to form heterooligomers with resistin but not RELMbeta. Since RELMalpha is expressed by adipose tissue and it is a secreted factor, our findings suggest that RELMalpha may be involved in the control of the adipogenesis as well as in the process of muscle differentiation.
      In the lung, RELM-alpha is induced by hypoxia and was renamed as hypoxia-induced mitogenic factor (HIMF). HIMF strongly activated Akt phosphorylation. The phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 (10 micromol/L) inhibited HIMF-activated Akt phosphorylation. It also inhibited HIMFstimulated RPSM proliferation. Thus, the PI3K/Akt pathway, at least in part, mediates the proliferative effect of HIMF. Further studies showed that HIMF had angiogenic and vasoconstrictive properties. HIMF increased pulmonary arterial pressure and vascular resistance. Further studies suggest that HIMF regulates apoptosis and may participate in lung alveolarization and maturation.

    • Synonyms

      Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add deionized H2O and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKKLLFAIPL VVPFYSHSTM VNTDETIEII VENKVKELLA NPANYPSTVT TLSCTSVKT MNRWASCPAG MTATGCACGF ACGSWEIQSG DTCNCLCLLV DWTTARCCQL SLEDYKDDDD K.

    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.

    Relm Alpha Mouse His
  • View Data Sheet

    Name :

    GLUL Antibody

    Description:

    Glutamine Synthetase, Mouse Anti Human

    GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    Product # :

    ANT-705

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

    • Synonyms

      GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human GLUL mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GLUL amino acids 1-373 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT8D7AT.

    • Applications

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

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

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

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

    Glul Antibody
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