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Search results

1000 results found for “deaminase”

Name

Description

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  • View Data Sheet

    Name :

    MSRB E.Coli

    Description:

    Methionine Sulfoxide Reductase B E.Coli Recombinant

    Peptide methionine sulfoxide reductase MsrB, Peptide-methionine (R)-S-oxide reductase, msrB, yeaA, b1778, JW1767.

    Product # :

    ENZ-124

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    Description

    MSRB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids (1-137 a.a.) and having a molecular mass of 17.6kDa.MSRB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Methionine sulfoxide reductase B (MsrB) from Escherichia coli is a member of the msrB Met sulfoxide reductase family. The E.coli msrB carries out the reduction of methionine-R-sulfoxide to methionine. msrB possess a metal binding site composed of 2 CXXC motifs. The bound metal (zinc or iron) may stabilize the conformation of the enzymes.

    • Synonyms

      Peptide methionine sulfoxide reductase MsrB, Peptide-methionine (R)-S-oxide reductase, msrB, yeaA, b1778, JW1767.

    • 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 MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD APLFHSQTKY DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA HLGHVFPDGP QPTGERYCVN SASLRFTDGE NGEEING.

    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.

    Msrb Ecoli
  • 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 :

    ALDOA Human

    Description:

    Aldolase-A Human Recombinant

    Fructose-bisphosphate aldolase A, Muscle-type aldolase, Lung cancer antigen NY-LU-1, ALDOA, ALDA, EC 4.1.2.13, GSD12, MGC10942, MGC17716, MGC17767, Aldolase-A.

    Product # :

    ENZ-486

    Price :

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    Description

    ALDOA Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 384 amino acids (1-364 a.a.) and having a molecular mass of 41.5 kDa. The ALDOA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ALDOA solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aldolase A (ALDOA) is a glycolytic enzyme, which catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. ALDOA is found in the developing embryo and is produced in even greater amounts in adult muscle. ALDOA expression is repressed in the adult liver, kidney and intestine and similar to ALDOC levels in the brain and other nervous tissue. ALDOA deficiency has been linked with myopathy and hemolytic anemia.

    • Synonyms

      Fructose-bisphosphate aldolase A, Muscle-type aldolase, Lung cancer antigen NY-LU-1, ALDOA, ALDA, EC 4.1.2.13, GSD12, MGC10942, MGC17716, MGC17767, Aldolase-A.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKFSHEEIA MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFVS NHAY.

    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.

    Aldoa Human
  • View Data Sheet

    Name :

    NARS Human, Sf9

    Description:

    Asparaginyl-TRNA Synthetase Human Recombinant, Sf9

    Asparagine--tRNA ligase, cytoplasmic, EC 6.1.1.22, Asparaginyl-tRNA synthetase, AsnRS, NARS, NARS1.

    Product # :

    ENZ-716

    Price :

    Quantity :

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    Description

    NARS Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 63,853 Dalton. NARS is expressed with a -6xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    NARS is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

    • Synonyms

      Asparagine--tRNA ligase, cytoplasmic, EC 6.1.1.22, Asparaginyl-tRNA synthetase, AsnRS, NARS, NARS1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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

    Nars Human
  • View Data Sheet

    Name :

    CES2E Mouse

    Description:

    Carboxylesterase 2E Mouse Recombinant

    9030624L02Rik, Ces5, Ces2e.

    Product # :

    ENZ-1141

    Price :

    Quantity :

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    • biological activity
    • More Info

    Description

    CES2E Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids ( 27-559 aa) and having a molecular mass of 60.5kDa.CES2E is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CES2E solution (0.25 mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 30unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0 umole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 25C˚.

    More Info

    • Introduction

      Carboxylesterase 2E or CES2E is an enzyme that hydrolyzes various carboxylic acid esters. This enzyme can be found mainly in mammalian liver cells. CES2E is taking part in chemical reactions, especially in carboxylic ester and water catalyzation to alcohol & carboxylate.

    • Synonyms

      9030624L02Rik, Ces5, Ces2e.

    • 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

      QDSASPIRNT HTGQVRGSLV HVKDTDIAVH TFLGIPFAKP PVGPLRFAPP EAPEPWSGVR DGTSHPNMCL QNDNLMGSED LKMMNLILPP ISMSEDCLYL NIYVPAHAHE GSNLPVMVWI HGGALTVGMA SMYDGSMLAA TEDVVVVAIQ YRLGVLGFFS TGDQHAKGNW GYLDQVAALR WVQQNIVHFG GNPDRVTIFG ESAGGTSVSS HVVSPMSQGL FHGAIMESGV AVLPDLISSS
      SEMVHRIVAN LSGCAAVNSE TLMCCLRGKN EAEMLAINKV FKIIPGVVDG EFLPKHPQEL MASKDFHPVP SIIGINNDEY GWILPTIMDP AQKIEEITRK TLPAVLKSTA LKMMLPPECG DLLMEEYMGD TEDPETLQAQ FREMKGDFMF VIPALQVAHF QRSHAPVYFY EFQHRPSFFK DFRPPYVKAD HGDEIFLVFG YQFGNIKLPY TEEEEQLSRR IMKYWANFAR HGNPNSEGLP YWPVMDHDEQ YLQLDIQPSV GRALKARRLQ FWTKTLPQKI QELKGSQERH KELLEHHHHH 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.

    Ces2E Mouse
  • View Data Sheet

    Name :

    GLYATL2 Human

    Description:

    Glycine-N-Acyltransferase-Like 2 Human Recombinant

    BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.

    Product # :

    ENZ-770

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    Description

    GLYATL2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-294a.a) and having a molecular mass of 36.7kDa. GLYATL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GLYATL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycine-N-Acyltransferase-Like 2 (GLYATL2) is a part of the glycine N-acyltransferase family expressed mainly in salivary gland and trachea. GLYATL2 is a mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL2 conjugates numerous substrates, like arachidonoyl-CoA and saturated medium and longchain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. GLYATL2 also shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor.

    • Synonyms

      BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.

    • 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 MGSMLVLHNS QKLQILYKSL EKSIPESIKV YGAIFNIKDK NPFNMEVLVD AWPDYQIVIT RPQKQEMKDD QDHYTNTYHI FTKAPDKLEE VLSYSNVISW EQTLQIQGCQ EGLDEAIRKV ATSKSVQVDY MKTILFIPEL PKKHKTSSND KMELFEVDDD NKEGNFSNMF LDASHAGLVN EHWAFGKNER SLKYIERCLQ DFLGFGVLGP EGQLVSWIVM EQSCELRMGY TVPKYRHQGN MLQIGYHLEK YLSQKEIPFY FHVADNNEKS LQALNNLGFK ICPCGWHQWK CTPKKYC.

    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.

    Glyatl2 Human
  • View Data Sheet

    Name :

    Cyclophilin F Rat

    Description:

    Cyclophilin F Rat Recombinant

    Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F, Ppif, Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase.

    Product # :

    ENZ-903

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    Description

    Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206a.a.) and having a molecular mass of 21.2kDa.Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidyl-prolyl cis-trans isomerase F, mitochondrial (Cyclophilin-F) accelerates the folding of proteins. Cyclophilin-F catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and involved in regulation of the mitochondrial permeability transition pore (mPTP). Cyclophilin-F, in cooperation with mitochondrial TP53, is involved in activating oxidative stress-induced necrosis. Cyclophilin-F is also involved in modulation of mitochondrial membrane F1F0 ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Furthermore, Cyclophilin-F has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F, Ppif, Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase.

    • 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 MGSCSDGGAR GANSSSQNPL VYLDVGADGQ PLGRVVLELK ADVVPKTAEN FRALCTGEKG FGYKGSTFHR VIPAFMCQAG DFTNHNGTGG KSIYGSRFPD ENFTLKHVGP GVLSMANAGP NTNGSQFFIC TIKTDWLDGK HVVFGHVKEG MDVVKKIESF GSKSGKTSKK IVITDCGQLS.

    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.

    Cyclophilin F Rat
  • View Data Sheet

    Name :

    SETD7 Human

    Description:

    Set7/9 Histone Methyltransferase Human Recombinant

    Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7, EC 2.1.1.43, Histone H3-K4 methyltransferase, H3-K4-HMTase, SET domain-containing protein 7, Set9, SET7/9, SETD7.

    Product # :

    ENZ-314

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    Description

    SETD7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids & having a molecular mass of 40.7 kDa. The SETD7 purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein containing 50mM Tris-HCl buffer (pH7.5), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Set 7/9 is a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet). The methylation of lysine residues of histones plays a critical role in the regulation of chromatin structure and gene expression.
      Acetylation, phosphorylation and methylation of the amino-terminal tails of histone are thought to be involved in the regulation of chromatin structure and function. The enzymes identified in the methylation of specific lysine residue on histones belong to the SET family with just one exception. Set7/9, unlike most other SET proteins, is exclusively a mono-methylase.

    • Synonyms

      Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7, EC 2.1.1.43, Histone H3-K4 methyltransferase, H3-K4-HMTase, SET domain-containing protein 7, Set9, SET7/9, SETD7.

    • 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.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MDSDDEMVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK FFFFDGSTLE GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDT DGRLIFKGQY KDNIRHGVCW IYYPDGGSLV GEVNEDGEMT GEKIAYVYPD ERTALYGKFI DGEMIEGKLA TLMSTEEGRP HFELMPGNSV YHFDKSTSSC ISTNALLPDP YESERVYVAE SLISSAGEGL FSKVAVGPNT VMSFYNGVRI THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT PNCIYDMFVH PRFGPIKCIR TLRAVEADEE LTVAYGYDHS PPGKSGPEAP EWYQVELKAF QATQQK

    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.

    Setd7 Human
  • View Data Sheet

    Name :

    TDP1 Human

    Description:

    Tyrosyl-DNA Phosphodiesterase 1 Human Recombinant

    Tyrosyl-DNA phosphodiesterase 1, TDP1 protein, TDP1.

    Product # :

    ENZ-685

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    Description

    TDP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298) and having a molecular mass of 35.8kDa. TDP1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TDP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosyl-DNA phosphodiesterase 1 ( TDP1) is required for repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. TDP1 also detach glycolate from single-stranded DNA having 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks.

    • Synonyms

      Tyrosyl-DNA phosphodiesterase 1, TDP1 protein, TDP1.

    • 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 MSQEGDYGRW TISSSDESEE EKPKPDKPST SSLLCARQGA ANEPRYTCSE AQKAAHKRKI SPVKFSNTDS VLPPKRQKSG SQEDLGWCLS SSDDELQPEM PQKQAEKVVI KKEKDISAPN DGTAQRTENH GAPACHRLKE EEDEYETSGE GQDIWDMLDK GNPFQFYLTR VSGVKPKYNS GALHIKDILS PLFGTLVSSA QFNYCFDVDW LVKQYPPEFR KKPILLVHGD KREAKAHLHA QAKPYENISL CQAKLDIAFG THHTKMMLLL YEEGLRVVIH TSNLIHADWH QKTQGTHL.

    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.

    Tdp1 Human
  • View Data Sheet

    Name :

    CDO1 Human

    Description:

    Cysteine Dioxygenase Human Recombinant

    Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.

    Product # :

    ENZ-449

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    Description

    CDO1 Human Recombinant fused with a 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-170 a.a.) and having a molecular mass of 23.9kDa.The CDO1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDO1 solution contains 20mM Tris buffer(pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDO1 (Cysteine dioxygenase) is a mammalian non-heme iron enzyme that initiates a number of significant metabolic pathways associated with pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate) by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels. CDO1 is highly expressed in the liver and placenta. On the other hand CDO1 has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells.

    • Synonyms

      Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.

    • 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 KDRWGSHMEQ TEVLKPRTLA DLIRILHQLF AGDEVNVEEV QAIMEAYESD PTEWAMYAKF DQYRYTRNLV DQGNGKFNLM ILCWGEGHGS SIHDHTNSHC FLKMLQGNLK ETLFAWPDKK SNEMVKKSER VLRENQCAYI NDSVGLHRVE NISHTEPAVS LHLYSPPFDT CHAFDQR.

    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.

    Cdo1 Human
  • View Data Sheet

    Name :

    UGT8 Human

    Description:

    UDP Glycosyltransferase 8 Human Recombinant

    UDP Glycosyltransferase 8, CGT, UDP-Galactose Ceramide Galactosyltransferase, 2-Hydroxyacylsphingosine 1-Beta-Galactosyltransferase, Ceramide UDP-Galactosyltransferase, Cerebroside Synthase, UGT4, UDP-Galactose-Ceramide Galactosyltransferase, Uridine Diphosphate Glycosyltransferase 8, EC 2.4.1.45, EC 2.4.1.

    Product # :

    ENZ-754

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    Description

    UGT8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 544 amino acids (21-541 a.a) and having a molecular mass of 61.6kDa.UGT8 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    UGT8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      UDP Glycosyltransferase 8 (UGT8) is a member of the UDP-glycosyltransferase family. UGT8 catalyzes the transfer of galactose to ceramide, a crucial enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.

    • Synonyms

      UDP Glycosyltransferase 8, CGT, UDP-Galactose Ceramide Galactosyltransferase, 2-Hydroxyacylsphingosine 1-Beta-Galactosyltransferase, Ceramide UDP-Galactosyltransferase, Cerebroside Synthase, UGT4, UDP-Galactose-Ceramide Galactosyltransferase, Uridine Diphosphate Glycosyltransferase 8, EC 2.4.1.45, EC 2.4.1.

    • 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 MGSAKIIIVP PIMFESHMYI FKTLASALHE RGHHTVFLLS EGRDIAPSNH YSLQRYPGIF NSTTSDAFLQ SKMRNIFSGR LTAIELFDIL DHYTKNCDLM VGNHALIQGL KKEKFDLLLV DPNDMCGFVI AHLLGVKYAV FSTGLWYPAE VGAPAPLAYV PEFNSLLTDR MNLLQRMKNT GVYLISRLGV SFLVLPKYER IMQKYNLLPE KSMYDLVHGS SLWMLCTDVA LEFPRPTLPN VVYVGGILTK PASPLPEDLQ RWVNGANEHG FVLVSFGAGV KYLSEDIANK LAGALGRLPQ KVIWRFSGPK PKNLGNNTKL IEWLPQNDLL GHSKIKAFLS HGGLNSIFET MYHGVPVVGI PLFGDHYDTM TRVQAKGMGI LLEWKTVTEK ELYEALVKVI NNPSYRQRAQ KLSEIHKDQP GHPVNRTIYW IDYIIRHNGA HHLRAAVHQI SFCQYFLLDI AFVLLLGAAL LYFLLSWVTK FIYRKIKSLW SRNKHSTVNG HYHNGILNGK YKRNGHIKHE KKVK.

    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.

    Ugt8 Human
  • View Data Sheet

    Name :

    UBE2Z Human

    Description:

    Ubiquitin Conjugating Enzyme E2Z Human Recombinant

    HOYS7, USE1, Ubiquitin-conjugating enzyme E2 Z, E2 ubiquitin-conjugating enzyme Z, Uba6-specific E2 conjugating enzyme 1, Ubiquitin carrier protein Z, Ubiquitin-protein ligase Z, UBE2Z.

    Product # :

    ENZ-804

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    Description

    UBE2Z Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-246a.a) and having a molecular mass of 30.5kDa. UBE2Z is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2Z solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin Conjugating Enzyme E2Z, also known as UBE2z, is a protein coding gene which is a part of the ubiquitin-conjugating enzyme family. UBE2z catalyzes the covalent attachment of ubiquitin to various proteins. UBE2z takes part in in apoptosis regulation and is also a specific substrate for UBA6, not charged with ubiquitin by UBE1.

    • Synonyms

      HOYS7, USE1, Ubiquitin-conjugating enzyme E2 Z, E2 ubiquitin-conjugating enzyme Z, Uba6-specific E2 conjugating enzyme 1, Ubiquitin carrier protein Z, Ubiquitin-protein ligase Z, UBE2Z.

    • 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 MGSMSIYKEP PPGMFVVPDT VDMTKIHALI TGPFDTPYEG GFFLFVFRCP PDYPIHPPRV KLMTTGNNTV RFNPNFYRNG KVCLSILGTW TGPAWSPAQS ISSVLISIQS LMTENPYHNE PGFEQERHPG DSKNYNECIR HETIRVAVCD MMEGKCPCPE PLRGVMEKSF LEYYDFYEVA CKDRLHLQGQ TMQDPFGEKR GHFDYQSLLM RLGLIRQKVL ERLHNENAEM DSDSSSSGTE TDLHGSLRV.

    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.

    Ube2Z Human
  • View Data Sheet

    Name :

    NDUFS6 Human

    Description:

    Histidine NADH Dehydrogenase Fe-S Protein 6 Human Recombinant

    NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa (NADH-Coenzyme Q Reductase), Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, CI13KDA.

    Product # :

    ENZ-725

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    Description

    NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa (NADH-Coenzyme Q Reductase), Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, CI13KDA.

    Source

    Escherichia Coli.

    Formulation

    The NDUFS6 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NADH Dehydrogenase Fe-S Protein 6 (NDUFS6) is a subunit of the NADH: ubiquinone oxidoreductase (complex I), which is the 1st enzyme complex in the electron transport chain of the mitochondria. This complex operates in the transfer of electrons from NADH to the respiratory chain. NDUFS6 is one of seven subunits in the iron-sulfur protein segment. DNA alterations in NDUFS6 are the cause for mitochondrial complex I deficiency, a disease which results in an extensive assortment of clinical disorders, like adult-onset neurodegenerative disorders and neonatal disease.

    • Synonyms

      NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa (NADH-Coenzyme Q Reductase), Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, CI13KDA.

    • 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 MGSFGVRVSP TGEKVTHTGQ VYDDKDYRRI RFVGRQKEVN ENFAIDLIAE QPVSEVETRV IACDGGGGAL GHPKVYINLD KETKTGTCGY CGLQFRQHHH

    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.

    Ndufs6 Human
  • View Data Sheet

    Name :

    CDK5 Human

    Description:

    Cyclin-dependent Kinase 5 Human Recombinant

    Cyclin-dependent kinase 5, Cell division protein kinase 5, Serine/threonine-protein kinase PSSALRE, Tau protein kinase II catalytic subunit, CDK5, CDKN5, TPKII catalytic subunit, cyclin dependent kinase 5.

    Product # :

    PKA-047

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    Description

    CDK5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-292) and having a molecular mass of 35.8kDa. CDK5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDK5 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Cell division protein kinase 5 (CDK5) belongs to the cyclin-dependent kinase family. CDK5 is essential for appropriate development of the brain and in order to be activated CDK5 must link to CDK5R1 or CDK5R2. CDK5 doesn't need phosphorylation on the T loop so that binding with the activator is enough to activate the kinase. CDK5 is engaged in the processes of neuronal maturation and migration, phosphorylating the central intracellular adaptor of the reeling signaling chain.

    • Synonyms

      Cyclin-dependent kinase 5, Cell division protein kinase 5, Serine/threonine-protein kinase PSSALRE, Tau protein kinase II catalytic subunit, CDK5, CDKN5, TPKII catalytic subunit, cyclin dependent kinase 5.

    • 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 MGSHMQKYEK LEKIGEGTYG TVFKAKNRET HEIVALKRVR LDDDDEGVPS SALREICLLK ELKHKNIVRL HDVLHSDKKL TLVFEFCDQD LKKYFDSCNG DLDPEIVKSF LFQLLKGLGF CHSRNVLHRD LKPQNLLINR NGELKLADFG LARAFGIPVR CYSAEVVTLW YRPPDVLFGA KLYSTSIDMW SAGCIFAELA NAGRPLFPGN DVDDQLKRIF RLLGTPTEEQ WPSMTKLPDY KPYPMYPATT SLVNVVPKLN ATGRDLLQNL LKCNPVQRIS AEEALQHPYF SDFCPP.

    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.

    Cdk5 Human
  • View Data Sheet

    Name :

    UBE2A Human

    Description:

    Ubiquitin Conjugating Enzyme E2A Human Recombinant

    HHR6A, HR6A, RAD6A, UBC2, UBE2A, EC=6.3.2.19, Ubiquitin-conjugating enzyme E2 A, Ubiquitin-protein ligase A, Ubiquitin carrier protein A, RAD6 homolog A.

    Product # :

    ENZ-514

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    Description

    UBE2A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids (1-152 a.a.) and having a molecular mass of 19.4 kDa. UBE2A protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    UBE2A Human solution containing 20mM Tris HCl pH-8, 1mM DTT, 1mM EDTA and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      The alteration of proteins with ubiquitin is a vital cellular mechanism for targeting atypical or short-lived proteins for degradation. Ubiquitination involves noT less than three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. UBE2A is part of the E2 ubiquitin-conjugating enzyme family. UBE2A is necessary for post-replicative DNA damage repair. UBE2A catalyzes the covalent attachment of ubiquitin to other proteins. UBE2A is necessary for postreplication repair of UV-damaged DNA.

    • Synonyms

      HHR6A, HR6A, RAD6A, UBC2, UBE2A, EC=6.3.2.19, Ubiquitin-conjugating enzyme E2 A, Ubiquitin-protein ligase A, Ubiquitin carrier protein A, RAD6 homolog 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 MSTPARRRLM RDFKRLQEDP PAGVSGAPSE NNIMVWNAVI FGPEGTPFED GTFKLTIEFT EEYPNKPPTV RFVSKMFHPN VYADGSICLD ILQNRWSPTY DVSSILTSIQ SLLDEPNPNS PANSQAAQLY QENKREYEKR VSAIVEQSWR DC.

    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.

    Ube2A Human
  • View Data Sheet

    Name :

    AARS Human

    Description:

    Alanyl-tRNA Synthetase Human Recombinant

    Alanyl-tRNA synthetase cytoplasmic, EC 6.1.1.7, Alanine-tRNA ligase, AlaRS, Renal carcinoma antigen NY-REN-42, PL-12, AARS.

    Product # :

    ENZ-305

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    Description

    Alanyl-tRNA synthetase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 110 kDa. PL-12 is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    AARS is supplied in 20mM HEPES buffer pH-8, 250mM sodium chloride, and 20% glycerol.

    Purity

    AARS purity is greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alanyl-tRNA synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge tRNA molecules with the respective amino acids. This 108 kDa protein is an autoantigen recognized by PL-12 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that epitope spreading occurs in the autoimmune PL-12 response such that even antibodies to an isolated alanyl-tRNA molecule can develop.

    • Synonyms

      Alanyl-tRNA synthetase cytoplasmic, EC 6.1.1.7, Alanine-tRNA ligase, AlaRS, Renal carcinoma antigen NY-REN-42, PL-12, AARS.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sampels).

    • coating concentration

      0.3-0.8 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for labeling of functional groups.

    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.

    Alanyl T Rna Synthetase Human
  • View Data Sheet

    Name :

    MSRA E.Coli

    Description:

    Methionine Sulfoxide Reductase A E.Coli Recombinant

    Peptide methionine sulfoxide reductase MsrA, Protein-methionine-S-oxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, msrA, pms, b4219, JW4178.

    Product # :

    ENZ-129

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    Description

    MSRA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212 a.a.) and having a molecular mass of 25.4kDa.MSRA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MSRA protein solution (0.5mg/ml) 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptide methionine sulfoxide reductase A (msrA) is an enzyme which catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. MSRA may have a significant function as a repair enzyme for proteins which have been inactivated by oxidation.

    • Synonyms

      Peptide methionine sulfoxide reductase MsrA, Protein-methionine-S-oxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, msrA, pms, b4219, JW4178.

    • 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 MSLFDKKHLV SPADALPGRN TPMPVATLHA VNGHSMTNVP DGMEIAIFAM GCFWGVERLF WQLPGVYSTA AGYTGGYTPN PTYREVCSGD TGHAEAVRIV YDPSVISYEQ LLQVFWENHD PAQGMRQGND HGTQYRSAIY PLTPEQDAAA RASLERFQAA
      MLAADDDRHI TTEIANATPF YYAEDDHQQY LHKNPYGYCG IGGIGVCLPP 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.

    Msra Ecoli
  • View Data Sheet

    Name :

    CES1 Human

    Description:

    Carboxylesterase 1 Human Recombinant

    Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.

    Product # :

    ENZ-1099

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    Description

    CES1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 559 amino acids (19-568 a.a.) and having a molecular mass of 61.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1 protein solution (0.5mg/ml) contains 25mM Sodium Acetate (pH 4.0), 10% glycerol, 0.1M NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CES1 is a part of the alpha/beta fold hydrolase familyand participates in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. CES1hydrolyzes aromatic and aliphatic esters, although it has no catalytic activity toward amides or a fatty acyl-CoA ester. CES1hydrolyzes the methyl ester group of cocaine to form benzoylecgonine and catalyzes the transesterification of cocaine to form cocaethylene. CES1also plays a role in detoxification in the lung and protection of the central nervous system from ester or amide compounds.CES1 is found in most tissues, mainly in the liver.

    • Synonyms

      Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.

    • 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

      ADLGHPSSPP VVDTVHGKVL GKFVSLEGFA QPVAIFLGIP FAKPPLGPLR FTPPQPAEPW
      SFVKNATSYP PMCTQDPKAG QLLSELFTNR KENIPLKLSE DCLYLNIYTP ADLTKKNRLP
      VMVWIHGGGL MVGAASTYDG LALAAHENVV VVTIQYRLGI WGFFSTGDEH SRGNWGHLDQ
      VAALRWVQDN IASFGGNPGS VTIFGESAGG ESVSVLVLSP LAKNLFHRAI SESGVALTSV
      LVKKGDVKPL AEQIAITAGC KTTTSAVMVH CLRQKTEEEL LETTLKMKFL SLDLQGDPRE
      SQPLLGTVID GMLLLKTPEE LQAERNFHTV PYMVGINKQE FGWLIPMQLM SYPLSEGQLD
      QKTAMSLLWK SYPLVCIAKE LIPEATEKYL GGTDDTVKKK DLFLDLIADV MFGVPSVIVA
      RNHRDAGAPT YMYEFQYRPS FSSDMKPKTV IGDHGDELFS VFGAPFLKEG ASEEEIRLSK
      MVMKFWANFA RNGNPNGEGL PHWPEYNQKE GYLQIGANTQ AAQKLKDKEV AFWTNLFAKK AVEKPPQTEH IELHHHHHH.

    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.

    Ces1 Human
  • View Data Sheet

    Name :

    PRSS3 Human, HEK

    Description:

    Protease Serine 3 Human Recombinant, HEK

    Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.

    Product # :

    ENZ-1194

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    Description

    PRSS3 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 238 amino acids (16-247 a.a.) and having a molecular mass of 26kDa. PRSS3 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    PRSS3 protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 10,000pmol/min/ug, and is defined as the amount of enzyme that cleaves 1pmol of McaRPKPVE-Nval-WRK(Dnp)-NH2 per minute at pH 8.0 at 37℃.

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    • Synonyms

      Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.

    • 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

      VPFDDDDKIV GGYTCEENSL PYQVSLNSGS HFCGGSLISE QWVVSAAHCY KTRIQVRLGE HNIKVLEGNE QFINAAKIIR HPKYNRDTLD NDIMLIKLSS PAVINARVST ISLPTAPPAA GTECLISGWG NTLSFGADYP DELKCLDAPV LTQAECKASY PGKITNSMFC VGFLEGGKDS CQRDSGGPVV CNGQLQGVVS WGHGCAWKNR PGVYTKVYNY VDWIKDTIAA NSHHHHHH.

    • Background

      PRSS3 is a member of the serine protease family, characterized by its specific enzymatic activity mediated by the serine residue in the catalytic triad. PRSS3's structure consists of a catalytic domain, a substrate-binding site, and disulfide bridges that help maintain its stability. Understanding the molecular characteristics of PRSS3 is crucial for elucidating its functions.

      Physiological Functions: PRSS3 is primarily expressed in the pancreas, where it plays a vital role in the digestion of dietary proteins. It contributes to the breakdown of proteins into smaller peptides, facilitating their absorption in the small intestine. PRSS3 is part of a complex enzymatic network that ensures proper digestion and nutrient absorption.

      Pathological Implications: Research has shown that abnormal PRSS3 activity or expression can be associated with various diseases. For example, alterations in PRSS3 have been linked to pancreatic diseases, including pancreatitis and pancreatic cancer. Investigating PRSS3's role in disease pathogenesis can provide valuable insights into the development and progression of these conditions.

      Biomedical Research: PRSS3 human recombinant proteins are valuable tools in biomedical research. Researchers use these recombinant proteins to study PRSS3's enzymatic properties, interactions with other molecules, and potential therapeutic applications. They can perform controlled experiments to gain a deeper understanding of PRSS3's functions.

      Therapeutic Potential: PRSS3's involvement in diseases like pancreatitis and pancreatic cancer has raised interest in its therapeutic potential. Researchers explore the development of inhibitors or modulators targeting PRSS3 as potential treatments for these diseases. Additionally, PRSS3's role in protein digestion has implications for digestive disorders and enzyme replacement therapies.

      Diagnostic Markers: PRSS3 levels or activity may serve as diagnostic markers for certain diseases. Changes in PRSS3 expression in pancreatic tissue or serum may be indicative of pancreatic disorders. Research in this area aims to establish PRSS3 as a diagnostic tool for early disease detection.

      Future Directions: Continued research on PRSS3 human recombinant and its roles in health and disease is essential. This includes investigating its regulation, substrate specificity, and potential interactions with other proteins. Such studies may uncover novel therapeutic targets and diagnostic strategies.

    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.

    Prss3 Enzyme
  • View Data Sheet

    Name :

    METAP1D Human

    Description:

    Methionyl Aminopeptidase 1D Human Recombinant

    MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.

    Product # :

    ENZ-759

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    Description

    METAP1D Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (20-335a.a) and having a molecular mass of 37.4kDa. METAP1D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The METAP1D solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Methionyl Aminopeptidase 1D (METAP1D) is a part of the peptidase M24A family. METAP1D which is overexpressed in colon cancer cell lines participates in tumorigenesis. METAP1D eliminates methionine from the N-terminus of nascent proteins.

    • Synonyms

      MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.

    • 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 MGSSSPLNHI YLHKQSSSQQ RRNFFFRRQR DISHSIVLPA AVSSAHPVPK HIKKPDYVTT GIVPDWGDSI EVKNEDQIQG LHQACQLARH VLLLAGKSLK VDMTTEEIDA LVHREIISHN AYPSPLGYGG FPKSVCTSVN NVLCHGIPDS RPLQDGDIIN IDVTVYYNGY HGDTSETFLV GNVDECGKKL VEVARRCRDE AIAACRAGAP FSVIGNTISH ITHQNGFQVC PHFVGHGIGS YFHGHPEIWH HANDSDLPME EGMAFTIEPI ITEGSPEFKV LEDAWTVVSL DNQRSAQFEH TVLITSRGAQ ILTKLPHEA.

    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.

    Metap1D Human
  • View Data Sheet

    Name :

    ACP6 Human

    Description:

    Acid Phosphatase-6 Human Recombinant

    Acid Phosphatase 6, Lysophosphatidic, Acid Phosphatase-Like Protein 1, PACPL1, ACPL1, LPAP, Lysophosphatidic Acid Phosphatase Type 6, Lysophosphatidic Acid Phosphatase 6, Acid Phosphatase Like 1, EC 3.1.3.2, Lysophosphatidic acid phosphatase type 6.

    Product # :

    ENZ-865

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    Description

    ACP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (33-428a.a) and having a molecular mass of 47.7kDa. ACP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACP6 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1000 units/mg, and is defined as the amount of enzyme which hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at PH 5.0 at 37C.

    More Info

    • Introduction

      Acid Phosphatase-6, also known as ACP6 is Hydrolyzes lysophosphatidic acid (LPA) which contains a medium length fatty acid chain to the corresponding monoacylglycerol. ACP6 shows highest activity with lysophosphatidic acid which contains myristate (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower activity with C18:0 as well as C6:0 lysophosphatidic acid.

    • Synonyms

      Acid Phosphatase 6, Lysophosphatidic, Acid Phosphatase-Like Protein 1, PACPL1, ACPL1, LPAP, Lysophosphatidic Acid Phosphatase Type 6, Lysophosphatidic Acid Phosphatase 6, Acid Phosphatase Like 1, EC 3.1.3.2, Lysophosphatidic acid phosphatase type 6.

    • 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 MGSELQEADG QCPVDRSLLK LKMVQVVFRH GARSPLKPLP LEEQVEWNPQ LLEVPPQTQF DYTVTNLAGG PKPYSPYDSQ YHETTLKGGM FAGQLTKVGM QQMFALGERL RKNYVEDIPF LSPTFNPQEV FIRSTNIFRN LESTRCLLAG LFQCQKEGPI IIHTDEADSE VLYPNYQSCW SLRQRTRGRR QTASLQPGIS EDLKKVKDRM GIDSSDKVDF FILLDNVAAE QAHNLPSCPM LKRFARMIEQ RAVDTSLYIL PKEDRESLQM AVGPFLHILE SNLLKAMDSA TAPDKIRKLY LYAAHDVTFI PLLMTLGIFD HKWPPFAVDL TMELYQHLES KEWFVQLYYH GKEQVPRGCP DGLCPLDMFL NAMSVYTLSP EKYHALCSQT QVMEVGNEE.

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    Acp6 Human
  • View Data Sheet

    Name :

    BLVRB Human

    Description:

    Biliverdin Reductase B Human Recombinant

    FLR, BVRB, SDR43U1, MGC117413, BLVRB, Flavin reductase, FR, NADPH-dependent diaphorase, NADPH-flavin reductase, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, Green heme-binding protein, GHBP.

    Product # :

    ENZ-387

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    Description

    BLVRB Human Recombinant amino produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids having a molecular mass of 22.1 kDa.The BLVRB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 20mM Tris-HCl buffer pH 8.5, 10% glycerol, and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.

    • Synonyms

      FLR, BVRB, SDR43U1, MGC117413, BLVRB, Flavin reductase, FR, NADPH-dependent diaphorase, NADPH-flavin reductase, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, Green heme-binding protein, GHBP.

    • 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

      MAVKKIAIFG ATGQTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPRPAHV VVGDVLQAAD VDKTVAGQDA VIVLLGTRND LSPTTVMSEG ARNIVAAMKA HGVDKVVACT SAFLLWDPTK VPPRLQAVTD DHIRMHKVLR ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD LGHFMLRCLT TDEYDGHSTY PSHQYQ.

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    Blvrb Human
  • View Data Sheet

    Name :

    HPGDS Human

    Description:

    Hematopoietic Prostaglandin D Synthase Human Recombinant

    Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.

    Product # :

    ENZ-616

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    Description

    HPGDS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-199 a.a.) and having a molecular mass of 25.9kDa.HPGDS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HPGDS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the sigma class glutathione-S-transferase family. The HPGDS enzyme catalyzes the conversion of PGH2 to PGD2 and has a role in the production of prostanoids in the immune system and mast cells. The presence of the HPGDS enzyme can be utilized to identify the differentiation stage of human megakaryocytes. Furthermore, HPGDS is a prostaglandin involved in smooth muscle contraction/relaxation and an effective inhibitor of platelet aggregation, and the conjugation of glutathione with a extensive range of aryl halides and organic isothiocyanates. In addition, HPGDS displays low glutathione-peroxidase activity towards cumene hydroperoxide. HPGDS is expressed in a number of megakaryocytic cell lines but not in platelets. HPGDS is highly expressed in the adipose tissue, macrophages and placenta; however it is expressed at lower levels in the lung, heart, lymph nodes, appendix, bone marrow and fetal liver.

    • Synonyms

      Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.

    • 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 MGSHMPNYKL TYFNMRGRAE IIRYIFAYLD IQYEDHRIEQ ADWPEIKSTL PFGKIPILEV DGLTLHQSLA IARYLTKNTD LAGNTEMEQC HVDAIVDTLD DFMSCFPWAE KKQDVKEQMF NELLTYNAPH LMQDLDTYLG GREWLIGNSV TWADFYWEIC
      STTLLVFKPD LLDNHPRLVT LRKKVQAIPA VANWIKRRPQ TKL.

    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.

    Hpgds Human
  • View Data Sheet

    Name :

    STK17A Human

    Description:

    Serine/Threonine Kinase 17A Human Recombinant

    DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.

    Product # :

    PKA-314

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    STK17A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (64-321 a.a) and having a molecular mass of 31.9kDa.STK17A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STK17A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STK17A belongs to the DAP kinase-associated apoptosis-inducing protein kinase family and encodes an autophosphorylated nuclear protein with a protein kinase domain. STK17A acts as a positive regulator of apoptosis. STK17A is greatly expressed in the placenta with lower levels in the heart, lung, skeletal muscle, kidney and pancreas.

    • Synonyms

      DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.

    • 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 MGSGRELGRG KFAVVRKCIK KDSGKEFAAK FMRKRRKGQD CRMEIIHEIA VLELAQDNPW VINLHEVYET ASEMILVLEY AAGGEIFDQC VADREEAFKE KDVQRLMRQI LEGVHFLHTR DVVHLDLKPQ NILLTSESPL GDIKIVDFGL SRILKNSEEL REIMGTPEYV APEILSYDPI SMATDMWSIG VLTYVMLTGI SPFLGNDKQE TFLNISQMNL SYSEEEFDVL SESAVDFIRT LLVKKPEDRA TAEECLKHPW L.

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

    Stk17A Human
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