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Search results

1000 results found for “Aldolase”

Name

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  • View Data Sheet

    Name :

    PHOSPHO1 Human

    Description:

    Phosphatase Orphan-1 Human Recombinant

    Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.

    Product # :

    ENZ-363

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    Description

    Human Phospho1 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 295 amino acids and having a molecular mass of 31.3 kDa. The Human Phospho1 is fused to a 14 aa His tag at N-Terminus. Human Phosphocholine Phosphatase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PHOSPHO1 is involved in mineralization process & plays a role in bone and cartilage matrix mineralization.
      PHOSPHO1 is expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix.
      Orphan-1 is collagen type -2 is specific for cartilaginous tissues. Orphan1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
      Phosphoethanolamine (2-O3POCH2CH2NH3) is a key intermediate in the formation of cephalins, it is formed in liver and brain by phosphorylation of ethanolamine.
      PHOSPHO2 and PHOSPHO1 suggest subtle differences in the charge distributions around the putative substrate entry site and in the location of potential H-bond donors.
      PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. PHOSPHO1 has been implicated in the generation of Pi for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho).

    • Synonyms

      Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.

    • Physical Appearance

      Filtered lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMSGCFP VSGLRCLSRD GRMAAQGAPR FLLTFDFDET IVDENSDDSI VRAAPGQRLP ESLRATYREG FYNEYMQRVF KYLGEQGVRP RDLSAIYEAI PLSPGMSDLL QFVAKQGACF EVILISDANT FGVESSLRAA GHHSLFRRIL SNPSGPDARG LLALRPFHTH SCARCPANMC KHKVLSDYLR ERAHDGVHFE RLFYVGDGAN DFCPMGLLAG GDVAFPRRGY PMHRLIQEAQ KAEPSSFRAS VVPWETAADV RLHLQQVLKSC.

    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.

    Phospho1 Human
  • View Data Sheet

    Name :

    FUT3 Human

    Description:

    Fucosyltransferase 3 Human Recombinant

    Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.

    Product # :

    ENZ-745

    Price :

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    Description

    FUT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (35-361 a.a) and having a molecular mass of 40.6kDa.FUT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FUT3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Fucosyltransferase 3 (FUT3) catalyzes alpha-1, 3 and alpha-1, 4 glycosidic linkages which take part in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. FUT3 takes part in blood group Lewis determination; Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme. FUT3 also operates on the corresponding 1, 4-galactosyl derivative, creating1, 3-L-fucosyl links.

    • Synonyms

      Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.

    • 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 MGSRVSRDDA TGSPRAPSGS SRQDTTPTRP TLLILLWTWP FHIPVALSRC SEMVPGTADC HITADRKVYP QADTVIVHHW DIMSNPKSRL PPSPRPQGQR WIWFNLEPPP NCQHLEALDR YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH PPLNLSAKTE LVAWAVSNWK PDSARVRYYQ SLQAHLKVDV YGRSHKPLPK GTMMETLSRY KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD LARYLQELDK DHARYLSYFR WRETLRPRSF SWALDFCKAC WKLQQESRYQ TVRSIAAWFT.

    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.

    Fut3 Human
  • View Data Sheet

    Name :

    TPSAB1 Human

    Description:

    Tryptase Alpha/Beta 1 Human Recombinant

    Tryptase Alpha/Beta 1, Tryptase Alpha II, Tryptase Beta-1, Tryptase Alpha-1, Tryptase Alpha/Beta-1, Tryptase-I, TPS1, TPS2, TPSB1, Tryptase-III, Mast Cell Alpha II Tryptase, Mast Cell Beta I Tryptase, EC 3.4.21.59.

    Product # :

    ENZ-652

    Price :

    Quantity :

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    Description

    TPSAB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 270 amino acids (31-275) and having a molecular mass of 30.1 kDa.TPSAB1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TPSAB1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tryptase alpha/beta-1 (TPSAB1) is a tryptase which is the key neutral protease present in mast cells and is discharged upon the coupled activation-degranulation response of this cell type. TPSAB1 is enzymatically active only as a heparin-stabilized tetramer, and is resistant to all known endogenous proteinase inhibitors. TPSAB1 is implicated as a mediator in the pathogenesis of asthma and other allergic and inflammatory disorders.

    • Synonyms

      Tryptase Alpha/Beta 1, Tryptase Alpha II, Tryptase Beta-1, Tryptase Alpha-1, Tryptase Alpha/Beta-1, Tryptase-I, TPS1, TPS2, TPSB1, Tryptase-III, Mast Cell Alpha II Tryptase, Mast Cell Beta I Tryptase, EC 3.4.21.59.

    • 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 MGSHMIVGGQ EAPRSKWPWQ VSLRVHGPYW MHFCGGSLIH PQWVLTAAHC VGPDVKDLAA LRVQLREQHL YYQDQLLPVS RIIVHPQFYT AQIGADIALL ELEEPVNVSS HVHTVTLPPA SETFPPGMPC WVTGWGDVDN DERLPPPFPL KQVKVPIMEN HICDAKYHLG AYTGDDVRIV RDDMLCAGNT RRDSCQGDSG GPLVCKVNGT WLQAGVVSWG EGCAQPNRPG IYTRVTYYLD WIHHYVPKKP.

    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.

    Tpsab1 Human
  • View Data Sheet

    Name :

    UGP2 Human

    Description:

    UDP-Glucose Pyrophosphorylase 2 Human Recombinant

    UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.

    Product # :

    ENZ-832

    Price :

    Quantity :

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    Description

    UGP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (1-508 a.a) and having a molecular mass of 59.3kDa.UGP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UGP2 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UDP-Glucose Pyrophosphorylase 2, also known as UGP2 is an essential intermediary in mammalian carbohydrate inter conversions. UGP2 transfers a glucose moiety from glucose-1-phosphate to MgUTP and forms UDP-glucose and MgPPi. UDP-glucose is a direct precursor of glycogen in the liver and muscle tissue, moreover in lactating mammary gland it is converted to UDP-galactose which is next converted to lactose.

    • Synonyms

      UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.

    • 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 MGSMSRFVQD LSKAMSQDGA SQFQEVIRQE LELSVKKELE KILTTASSHE FEHTKKDLDG FRKLFHRFLQ EKGPSVDWGK IQRPPEDSIQ PYEKIKARGL PDNISSVLNK LVVVKLNGGL GTSMGCKGPK SLIGVRNENT FLDLTVQQIE HLNKTYNTDV PLVLMNSFNT DEDTKKILQK YNHCRVKIYT FNQSRYPRIN KESLLPVAKD VSYSGENTEA WYPPGHGDIY ASFYNSGLLD TFIGEGKEYI FVSNIDNLGA TVDLYILNHL MNPPNGKRCE FVMEVTNKTR ADVKGGTLTQ YEGKLRLVEI AQVPKAHVDE FKSVSKFKIF NTNNLWISLA AVKRLQEQNA IDMEIIVNAK TLDGGLNVIQ LETAVGAAIK SFENSLGINV PRSRFLPVKT TSDLLLVMSN LYSLNAGSLT MSEKREFPTV PLVKLGSSFT KVQDYLRRFE SIPDMLELDH LTVSGDVTFG KNVSLKGTVI IIANHGDRID IPPGAVLENK IVSGNLRILD 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.

    Ugp2 Human
  • View Data Sheet

    Name :

    GLU-C S.aureus

    Description:

    Glutamyl endopeptidase Staphylococcal Recombinant

    Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.

    Product # :

    ENZ-955

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    Description

    Recombinant Staphylococcal GLU-C produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 267 amino acids and having a molecular mass of 28.9kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glutamyl endopeptidase (GLU-C) is an enzyme which cleaves peptide bonds on the carboxyl-terminal side of glutamic acid and, less frequently, aspartic acid (for example: Glu-|-Xaa, Asp-|-Xaa). GLU-C is a pathogenic factor involved in the adherence and colonization of human tissue. GLU-C preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. GLU-C is required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. GLU-C is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. Furthermore, GLU-C protects bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. GLU-C may also be involved in the stability of secreted lipases.

    • Synonyms

      Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

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

    • Amino Acid Sequence

      MLPNNDRHQI TDTTNGHYAP VTYIQVEAPT GTFIASGVVV GKDTLLTNKH VVDATHGDPH ALKAFPSAIN QDNYPNGGFT AEQITKYSGE GDLAIVKFSP NEQNKHIGEV VKPATMSNNA ETQVNQNITV TGYPGDKPVA TMWESKGKIT YLKGEAMQYD LSTTGGNSGS PVFNEKNEVI GIHWGGVPNE FNGAVFINEN VRNFLKQNIE DIHFANDDQP NNPDNPDNPN NPDNPNNPDE PNNPDNPNNP DNPDNGDNNN SDNPDAA.

    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.

    Glu C Saureus
  • View Data Sheet

    Name :

    ACOT8 Human

    Description:

    Acyl-CoA Thioesterase 8 Human Recombinant

    Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.

    Product # :

    ENZ-712

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    Description

    ACOT8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-319) and having a molecular mass of 38.3kDa. ACOT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACOT8 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Acyl-CoA Thioesterase 8 (ACOT8) is a group of enzymes which catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), granting the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. ACOT8 mediate Nef-induced down-regulation of CD4. ACOT8 contends with BAAT (Bile acid CoA: amino acid N-acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). ACOT8 prefers medium-length fatty acyl-CoAs.

    • Synonyms

      Acyl-coenzyme A thioesterase 8, hACTE-III, HNAACTE, the, PTE-1, PTE-2, PTE1, PTE2, Acyl-CoA thioesterase 8, Choloyl-coenzyme A thioesterase, HIV-Nef-associated acyl-CoA thioesterase, PTE-2, Peroxisomal acyl-coenzyme A thioester hydrolase 1, Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II, ACTEIII, hACTEIII, the, ACOT8.

    • 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 MGSMSSPQAP EDGQGCGDRG DPPGDLRSVL VTTVLNLEPL DEDLFRGRHY WVPAKRLFGG QIVGQALVAA AKSVSEDVHV HSLHCYFVRA GDPKLPVLYQ VERTRTGSSF SVRSVKAVQH GKPIFICQAS FQQAQPSPMQ HQFSMPTVPP PEELLDCETL IDQYLRDPNL QKRYPLALNR IAAQEVPIEI KPVNPSPLSQ LQRMEPKQMF WVRARGYIGE GDMKMHCCVA AYISDYAFLG TALLPHQWQH KVHFMVSLDH SMWFHAPFRA DHWMLYECES PWAGGSRGLV HGRLWRQDGV LAVTCAQEGV IRVKPQVSES KL.

    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.

    Acot8 Human
  • View Data Sheet

    Name :

    CTSZ Human

    Description:

    Cathepsin-Z Human Recombinant

    Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.

    Product # :

    ENZ-748

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    Description

    CTSZ Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (62-303) and having a molecular mass of 29.5kDa.CTSZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTSZ 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.

    Citations

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.

    • 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 MGSLPKSWDW RNVDGVNYAS ITRNQHIPQY CGSCWAHAST SAMADRINIK RKGAWPSTLL SVQNVIDCGN AGSCEGGNDL SVWDYAHQHG IPDETCNNYQ AKDQECDKFN QCGTCNEFKE CHAIRNYTLW RVGDYGSLSG REKMMAEIYA NGPISCGIMA TERLANYTGG IYAEYQDTTY INHVVSVAGW GISDGTEYWI VRNSWGEPWG ERGWLRIVTS TYKDGKGARY NLAIEEHCTF GDPIV.

    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.

    Ctsz Human
  • View Data Sheet

    Name :

    HRP

    Description:

    Horseradish Peroxidase

    Horseradish Peroxidase, HRP, EC 1.11.1.7.

    Product # :

    ENZ-321

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    Description

    HRP consists of the basic isoenzyme having a molecular weight of 44 kDa.The Horseradish Peroxidase is purified by affinity chromatography, which results in an enzyme of high specific activity and purity.

    Source

    Root extracts of horseradish.

    Purity

    (A403/A275) = RZ: 3.0.

    Biological Activity

    276 U/mg (25°C, guaiacol as the hydrogen donor, pH-7 and H2O2 as substrates).

    Citations

    More Info

    • Introduction

      The enzyme horseradish peroxidase, found in horseradish, is used extensively in molecular biologyand in antibody amplification and detection, among other things. For example, "In recent years the technique of marking neurons with the enzyme horseradish peroxidase (HRP) has become a major tool. In its brief history, this method has probably been used by more neurobiologists than have used the Golgi stainsince its discovery in 1870." Horseradish peroxidase is also highly used in techniques such as Western blottingand ELISAs.
      HRP is widely used as an enzymatic label in immunoassays. Usually, the enzyme is coupled to antibodies, lectins or haptens. Coupling to antibodies etc. may be performed through the carbohydrate side chains of the HRP.

    • Synonyms

      Horseradish Peroxidase, HRP, EC 1.11.1.7.

    • Physical Appearance

      Sterile Filtered red-brown lyophilized powder.

    • Stability

      Lyophilized HRP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HRP should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized HRP in sterile 18MΩ-cm H2O not less than 100 µg/ml.

    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.

    Horseradish Peroxidase
  • View Data Sheet

    Name :

    NANS Human

    Description:

    N-acetylneuraminic acid synthase Human Recombinant

    Sialic acid synthase, N-acetylneuraminate synthase, N-acetylneuraminate-9-phosphate synthase, N-acetylneuraminic acid phosphate synthase, N-acetylneuraminic acid synthase, NANS, SAS.

    Product # :

    ENZ-024

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    Description

    NANS 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 379 amino acids (1-359 a.a.) and having a molecular mass of 42.4kDa. The NANS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NANS solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NANS is a 359 amino acid protein that contains one AFP (antifreeze proteins)-like domain and functions in the biosynthesis of sialic acids. The ubiquitously expressed NANS enzymatically catalyzes the H2O-dependent formation of N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), both of which are sialic acids. NANS uses N-acetylmannosamine 6-phosphate as a substrate for Neu5Ac synthesis and mannose 6-phosphate as a substrate for KDN synthesis.

    • Synonyms

      Sialic acid synthase, N-acetylneuraminate synthase, N-acetylneuraminate-9-phosphate synthase, N-acetylneuraminic acid phosphate synthase, N-acetylneuraminic acid synthase, NANS, SAS.

    • 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 MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC AKFQKSELEF KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR YAEEVGIFFT ASGMDEMAVE FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC FLQCTSAYPL QPEDVNLRVI SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT LDKTWKGSDH SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV DNHGKKIKS.

    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.

    Nans Human
  • View Data Sheet

    Name :

    DMGO

    Description:

    Dimethylglycine Oxidase Recombinant

    DMGO, Dimethylglycine Oxidase.

    Product # :

    ENZ-318

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    Description

    Dimethylglycine oxidase Recombinant originated from Arthrobacter globifomis fused to His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 850 amino acids and having a molecular mass of 92.1 kDa. The DMGO is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Recombinant Dimethylglycine Oxidase solution contains 20mM Tris-HCl pH7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Dimethylglycine oxidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative demethylation of dimethylglycine to yield sarcosine, formaldehyde, and hydrogen peroxide. The N-terminal region binds FAD covalently so it is yellowish.

    • Synonyms

      DMGO, Dimethylglycine Oxidase.

    • Physical Appearance

      Sterile filtered liquid formulation 1 mg/ml.

    • 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 MASTPRIVII GAGIVGTNLA DELVTRGWNN ITVLDQGPLN MPGGSTSHAP GLVFQTNPSK TMASFAKYTVEKLLSLTEDG VSCFNQVGGL EVATTETRLA DLKRKLGYAA AWGIEGRLLS PAECQELYPL LDGENILGGL HVPSDGLASA ARAVQLLIKRTESAGVTYRG STTVTGIEQS GGRVTGVQTA DGVIPADIVV SCAGFWGAKI GAMIGMAVPL LPLAHQYVKT TPVPAQQGRN DQPNGARLPILRHQDQDLYY REHGDRYGIG SYAHRPMPVD VDTLGAYAPE TVSEHHMPSR LDFTLEDFLP AWEATKQLLP ALADSEIEDG FNGIFSFTPDGGPLLGESKE LDGFYVAEAV WVTHSAGVAK AMAELLTTGR SETDLGECDI TRFEDVQLTP EYVSETSQQN FVEIYDVLHP LQPRLSPRNLRVSPFHARHK ELGAFFLEAG GWERPYWFEA NAALLKEMPA EWLPPARDAW SGMFSSPIAA AEAWKTRTAV AMYDMTPLKR LEVSGPGALKLLQELTTADL AKKPGAVTYT LLLDHAGGVR SDITVARLSE DTFQLGANGN IDTAYFERAA RHQTQSGSAT DWVQVRDTTG GTCCIGLWGPLARDLVSKVS DDDFTNDGLK YFRAKNVVIG GIPVTAMRLS YVGELGWELY TSADNGQRLW DALWQAGQPF GVIAAGRAAF SSLRLEKGYRSWGTDMTTEH DPFEAGLGFA VKMAKESFIG KGALEGRTEE ASARRLRCLT IDDGRSIVLG KEPVFYKEQA VGYVTSAAYG YTVAKPIAYSYLPGTVSVGD SVDIEYFGRR ITATVTEDPL YDPKMTRLRG.

    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.

    Dimethylglycine Oxidase
  • View Data Sheet

    Name :

    APRT Human

    Description:

    Adenine Phosphoribosyltransferase Human Recombinant

    EC 2.4.2.73, MGC125857, AMP diphosphorylase, Adenine phosphoribosyltransferase, APRT, AMP, MGC125856, MGC129961, DKFZp686D13177.

    Product # :

    ENZ-487

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    Description

    APRT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (1-180 a.a.) and having a molecular mass of 19.6 kDa. The APRT is purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      APRT is part of the purine/pyrimidine phosphoribosyltransferase family. APRT enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). APRT produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in APRT causes 2,8-dihydroxyadenine urolithiasis. APRT catalyzes a salvage reaction resulting in the formation of AMP.

    • Synonyms

      EC 2.4.2.73, MGC125857, AMP diphosphorylase, Adenine phosphoribosyltransferase, APRT, AMP, MGC125856, MGC129961, DKFZp686D13177.

    • 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

      MADSELQLVE QRIRSFPDFP TPGVVFRDIS PVLKDPASFR AAIGLLARHL KATHGGRIDY IAGLDSRGFL FGPSLAQELG LGCVLIRKRG KLPGPTLWAS YSLEYGKAEL EIQKDALEPG QRVVVVDDLL ATGGTMNAAC ELLGRLQAEV LECVSLVELT SLKGREKLAP VPFFSLLQYE.

    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.

    Aprt Human
  • View Data Sheet

    Name :

    ARF1 Human

    Description:

    ADP-Ribosylation Factor 1 Human Recombinant

    ARF-1, ADP-ribosylation factor 1.

    Product # :

    PRO-867

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    Description

    ARF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8 kDa. The ARF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARF1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARF1 is a small guanine nucleotide-binding protein that increases the enzymatic activities of cholera toxin. ARF1 is necessary and ubiquitous in eukaryotes. ARF1 takes part in vesicular transport and functioning via phospholipase D activation. ARF1 is involved in membrane traffic and organelle integrity which are closely tied to their reversible association with membranes and distinct interactions with membrane phospholipids.

    • Synonyms

      ARF-1, ADP-ribosylation factor 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 MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ 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.

    Arf1 Human
  • View Data Sheet

    Name :

    NDUFV2 Human

    Description:

    NADH Dehydrogenase Flavoprotein 2 Human Recombinant

    CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    Product # :

    ENZ-743

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    Description

    NDUFV2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (33-249 a.a) and having a molecular mass of 26.1kDa.NDUFV2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NDUFV2 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.

    Citations

    More Info

    • Introduction

      NADH Dehydrogenase Flavoprotein 2 (NDUFV2) is a 24 kDa Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysisthe. NDUFV2 is aslo involved in electron transfer. Mutations in NDUFV2 are implicated in Parkinson's disease, bipolar disorder, schizophrenia, and have been discovered in one case of early onset hypertrophic cardiomyopathy and encephalopathy.

    • Synonyms

      CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    • 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 MGSGAGGALF VHRDTPENNP DTPFDFTPEN YKRIEAIVKN YPEGHKAAAV LPVLDLAQRQ NGWLPISAMN KVAEVLQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK VGETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTAK DIEEIIDELK AGKIPKPGPR SGRFSCEPAG GLTSLTEPPK GPGFGVQAGL.

    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.

    Ndufv2 Human
  • View Data Sheet

    Name :

    ARL2 Human

    Description:

    ADP-Ribosylation Factor-Like 2 Human Recombinant

    ADP-ribosylation factor-like protein 2, ARL2, ARFL2.

    Product # :

    PRO-074

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    Description

    ARL2 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 204 amino acids (1-184 a.a.) and having a molecular mass of 23kDa. The ARL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARL2 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF, 1mM DTT and 40% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARL2 is a member of the ADP-ribosylation factor (ARF) family. ARL2 functions as a component of a secretory pathway which is involved in the Ca2-dependent release of acetylcholine. ARL2 has a role in the folding of tubule proteins, thus playing a significant role in microtubule dynamics and cell cycle progression. Unlike other members of the ARF family, ARL2 doesn’t act as an activator of the catalytic subunit of cholera toxin.

    • Synonyms

      ADP-ribosylation factor-like protein 2, ARL2, ARFL2.

    • 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 MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL LIFANKQDLP GALSSNAIRE ALELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI FTAD.

    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.

    Arl2 Human
  • View Data Sheet

    Name :

    NEU1 Human

    Description:

    Sialidase 1 Human Recombinant

    Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

    Product # :

    ENZ-645

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    Description

    NEU1 Human Recombinant produced in E. coli is a single polypeptide chain containing 393 amino acids (48-415) and having a molecular mass of 42.9 kDa.NEU1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NEU1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Sialidase 1 (NEU1) is a lysosomal enzyme which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, the NEU1 enzyme is part of a heterotrimeric complex in cooperation with beta-galactosidase and cathepsin A. NEU1 gene mutations may lead to sialidosis, a lysosomal storage disease that can be the type 1 (cherry red -myoclonus syndrome or normosomatic type), which is late-onset, or the type 2 (the dysmorphic type), which takes place at an earlier age with increased acuteness.

    • Synonyms

      Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

    • 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 MGSHMENDFG LVQPLVTMEQ LLWVSGRQIG SVDTFRIPLI TATPRGTLLA FAEARKMSSS DEGAKFIALR RSMDQGSTWS PTAFIVNDGD VPDGLNLGAV VSDVETGVVF LFYSLCAHKA GCQVASTMLV WSKDDGVSWS TPRNLSLDIG TEVFAPGPGS GIQKQREPRK GRLIVCGHGT LERDGVFCLL SDDHGASWRY GSGVSGIPYG QPKQENDFNP DECQPYELPD GSVVINARNQ NNYHCHCRIV LRSYDACDTL RPRDVTFDPE LVDPVVAAGA VVTSSGIVFF SNPAHPEFRV NLTLRWSFSN GTSWRKETVQ LWPGPSGYSS LATLEGSMDG EEQAPQLYVL YEKGRNHYTE SISVAKISVY GTL

    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.

    Neu1 Human
  • View Data Sheet

    Name :

    BACE1 Human

    Description:

    Beta-Secretase 1 Human Recombinant

    Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE,  ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.

    Product # :

    ENZ-1119

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    Description

    BACE1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 442 amino acids (22-457 a.a.) and having a molecular mass of 49.2kDa. BACE1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    BACE1 protein solution containing Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.

    Citations

    More Info

    • Introduction

      Beta-secretase 1 or BACE1 or beta-site amyloid precursor protein cleaving enzyme 1, is a protein that is encoded by the BACE1 gene in humans. Expression of BACE1 is seen primarily in neurons as it is crucial for the creation of myelin sheats in the peripheric nervous system. Beta-secretase 1 is a proteas that is located in the cell membrane (transmembrane). The enzyme consists of 2 active sites (aspartate residues) in the extracellular domain that can act as a dimer.

    • Synonyms

      Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.

    • 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

      TQHGIRLPLR SGLGGAPLGL RLPRETDEEP EEPGRRGSFV EMVDNLRGKS GQGYYVEMTV GSPPQTLNIL VDTGSSNFAV GAAPHPFLHR YYQRQLSSTY RDLRKGVYVP YTQGKWEGEL GTDLVSIPHG PNVTVRANIA AITESDKFFI NGSNWEGILG LAYAEIARPD DSLEPFFDSL VKQTHVPNLF SLQLCGAGFP LNQSEVLASV GGSMIIGGID HSLYTGSLWY TPIRREWYYE VIIVRVEING QDLKMDCKEY NYDKSIVDSG TTNLRLPKKV FEAAVKSIKA ASSTEKFPDG FWLGEQLVCW QAGTTPWNIF PVISLYLMGE VTNQSFRITI LPQQYLRPVE DVATSQDDCY KFAISQSSTG TVMGAVIMEG FYVVFDRARK RIGFAVSACH VHDEFRTAAV EGPFVTLDME DCGYNIPQTD ESTLMTHHHH HH.

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

    Bace1 Human
  • View Data Sheet

    Name :

    NUDT14 Human

    Description:

    Nudix Type Motif 14 Human Recombinant

    UGPP, UGPPase, Uridine diphosphate glucose pyrophosphatase, UDPG pyrophosphatase, Nucleoside diphosphate-linked moiety X motif 14, Nudix motif 14, NUDT14.

    Product # :

    ENZ-691

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    Description

    NUDT14 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222) and having a molecular mass of 26.5kDa. NUDT14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT14 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Uridine diphosphate glucose pyrophosphatase (NUDT14), is a part of the nudix hydrolase family. NUDT14 is a cytoplasmic protein which contains one nudix hydrolase domain and acts as the sugar donor in numerous glycosylation reactions, including those involved in the production of glycogen. NUDT14 hydrolyzes ADP-ribose into ribose 5-phosphate and AMP, and UDP-glucose to glucose 1-phosphate and UMP. NUDT14 is a homodimer which binds magnesium as a cofactor and is encoded by a gene located on human chromosome 14.

    • Synonyms

      UGPP, UGPPase, Uridine diphosphate glucose pyrophosphatase, UDPG pyrophosphatase, Nucleoside diphosphate-linked moiety X motif 14, Nudix motif 14, NUDT14.

    • 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 MGSMERIEGA SVGRCAASPY LRPLTLHYRQ NGAQKSWDFM KTHDSVTVLL FNSSRRSLVL VKQFRPAVYA GEVERRFPGS LAAVDQDGPR ELQPALPGSA GVTVELCAGL VDQPGLSLEE VACKEAWEEC GYHLAPSDLR RVATYWSGVG LTGSRQTMFY TEVTDAQRSG PGGGLVEEGE LIEVVHLPLE GAQAFADDPD IPKTLGVIFG VSWFLSQVAP NLDLQ.

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    Nudt14 Human
  • View Data Sheet

    Name :

    PRDX4 Human

    Description:

    Peroxiredoxin-4 Human Recombinant

    EC 1.11.1.15, AOE37-2, Peroxiredoxin-IV, Prx-IV, Thioredoxin peroxidase AO372, Thioredoxin-dependent peroxide reductase A0372, Antioxidant enzyme AOE372.

    Product # :

    ENZ-513

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    Description

    PRDX4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 255 amino acids (38-271 a.a.) and having a molecular mass of 28.8kDa. PRDX4 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PRDX4 Human solution containing 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately 230-310 pmole/min/µg.
    Enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX4 and peroxide for 20 min at room temperature. Specific activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25 C for 1 minute.

    Citations

    More Info

    • Introduction

      PRDX4 is an antioxidant enzyme that is part of the peroxiredoxin family. PRDX4 is localized to the cytoplasm. PRDX4 reduces hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. PRDX4 has a regulatory part in the activation of the transcription factor NF-kappaB. PRDX4 participates in redox regulation of the cell. PRDX4 regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

    • Synonyms

      EC 1.11.1.15, AOE37-2, Peroxiredoxin-IV, Prx-IV, Thioredoxin peroxidase AO372, Thioredoxin-dependent peroxide reductase A0372, Antioxidant enzyme AOE372.

    • 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 MWETEERPRT REEECHFYAG GQVYPGEASR VSVADHSLHL SKAKISKPAP YWEGTAVIDG EFKELKLTDY RGKYLVFFFY PLDFTFVCPT EIIAFGDRLE EFRSINTEVV ACSVDSQFTH LAWINTPRRQ GGLGPIRIPL LSDLTHQISK DYGVYLEDSG HTLRGLFIID DKGILRQITL NDLPVGRSVD ETLRLVQAFQ YTDKHGEVCP AGWKPGSETI IPDPAGKLKY FDKLN.

    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.

    Prdx4 Human
  • View Data Sheet

    Name :

    MDP1 Human

    Description:

    Magnesium-Dependent Phosphatase 1 Human Recombinant

    Magnesium-dependent phosphatase 1, MGC5987, MDP-1, FN6Pase, fructosamine-6-phosphatase, SFTB3, SFTPB, MDP1.

    Product # :

    ENZ-044

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    Description

    MDP1 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 200 amino acids (1-176 a.a.) and having a molecular mass of 22.6kDa. The MDP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MDP1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Magnesium-dependent phosphatase 1 (MDP1) is a memeber of the HAD-like hydrolase superfamily. MDP1 is a magnesium-dependent phosphatase which may act as a tyrosine phosphatase. MDP1 is inhibited by vanadate and zinc, and slightly by calcium.

    • Synonyms

      Magnesium-dependent phosphatase 1, MGC5987, MDP-1, FN6Pase, fructosamine-6-phosphatase, SFTB3, SFTPB, MDP1.

    • 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 MGSHMARLPK LAVFDLDYTL WPFWVDTHVD PPFHKSSDGT VRDRRGQDVR LYPEVPEVLK RLQSLGVPGA AASRTSEIEG ANQLLELFDL FRYFVHREIY PGSKITHFER LQQKTGIPFS QMIFFDDERR NIVDVSKLGV TCIHIQNGMN LQTLSQGLET FAKAQTGPLR SSLEESPFEA.

    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.

    Mdp1 Human
  • View Data Sheet

    Name :

    NRAS Human

    Description:

    Neuroblastoma RAS Viral Oncogene Homolog Human Recombinant

    GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.

    Product # :

    PRO-794

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    Description

    NRAS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-186 a.a.) and having a molecular mass of 20.8kDa. The NRAS is purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The NRAS protein solution contains 20mM Tris-HCl pH-7.5, 100mM NaCl, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NRAS binds GDP/GTP and has intrinsic GTPase activity. NRAS is a membrane protein that shuttles between the Golgi apparatus and the plasma membrane. This transport is regulated through palmitoylation and depalmitoylation by the ZDHHC9-GOLGA7 complex. NRAS is activated to a GTP-bound form by a GTPase activating protein and inactivated to a GDP-bound form by a guanine nucleotide-exchange factor. Defects in this NRAS gene result in juvenile myelomonocytic leukemia.

    • Synonyms

      GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.

    • 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

      MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSSDDGTQG CMGLPC.

    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.

    Nras Human
  • View Data Sheet

    Name :

    FARS2 Human

    Description:

    Phenylalanyl-tRNA Synthetase 2 Human Recombinant

    Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.

    Product # :

    ENZ-111

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    Description

    FARS2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (37-451 a.a.) and having a molecular mass of 50.6kDa.FARS2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FARS2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 1mM EDTA and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Phenylalanyl-tRNA synthetase 2 mitochondrial (FARS2) is a member of the class II aminoacyl- tRNA synthetase family. FARS2 is a mitochondrial matrix protein. FARS2 when acting as a monomer, catalyzes the ATP-dependent conversion of L-phenylalanine and tRNA (Phe) to L-phenlalanyltRNA (Phe), an event which is vital for proper translation and protein expression.

    • Synonyms

      Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.

    • 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 MPAAECATQR APGSVVELLG KSYPQDDHSN LTRKVLTRVG RNLHNQQHHP LWLIKERVKE HFYKQYVGRF GTPLFSVYDN LSPVVTTWQN FDSLLIPADH PSRKKGDNYY LNRTHMLRAH TSAHQWDLLH AGLDAFLVVG DVYRRDQIDS QHYPIFHQLE AVRLFSKHEL FAGIKDGESL QLFEQSSRSA HKQETHTMEA VKLVEFDLKQ TLTRLMAHLF GDELEIRWVD CYFPFTHPSF EMEINFHGEW LEVLGCGVME QQLVNSAGAQ DRIGWAFGLG LERLAMILYD IPDIRLFWCE DERFLKQFCV SNINQKVKFQ PLSKYPAVIN DISFWLPSEN YAENDFYDLV RTIGGDLVEK VDLIDKFVHP KTHKTSHCYR ITYRHMERTL SQREVRHIHQ ALQEAAVQLL GVEGRF.

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    Fars2 Human
  • View Data Sheet

    Name :

    FBP1 Human, Active

    Description:

    Fructose-1,6-Bisphosphatase 1, BioActive Human Recombinant

    Fructose-1,6-bisphosphatase 1, FBPase 1,  D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.

    Product # :

    ENZ-1145

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    Description

    FBP1 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-338) and having a molecular mass of 39.0 kDa.FBP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FBP1 protein solution (1mg/ml) contains 1mM DTT, 10% glycerol and 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 7,000pmol/min/ug, and is determined by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. 1 unit oxidizes 1.0pmole of fructose 1,6 diphosphate to fructose 6- phosphate and inorganic phosphate per minute at pH 9.5 at 37˚C.

    Citations

    More Info

    • Introduction

      FBP1 or Fructose-1, 6-bisphosphatase 1 is an enzyme, catalyzing the formation of fructose 6-phosphate & inorganic phosphate from fructose 1, 6-bisphosphate. FBP1 is part of the gluconeogenesis regulatory enzymes. Mutations in the enzyme gene can result in metabolic acidosis & hypoglycemia.

    • Synonyms

      Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.

    • 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 MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ

    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.

    Fbp1 Enzyme
  • View Data Sheet

    Name :

    PYCRL Human

    Description:

    Pyrroline-5-Carboxylate Reductase Like Human Recombinant

    Pyrroline-5-carboxylate reductase 3, P5C reductase 3, P5CR 3, Pyrroline-5-carboxylate reductase-like protein, PYCRL.

    Product # :

    ENZ-678

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    Quantity :

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    • description
    • source
    • formulation
    • purity
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    • Citations

    Description

    PYCRL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (1-274) and having a molecular mass of 31kDa.PYCRL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PYCRL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Pyrroline-5-Carboxylate Reductase Like (PYCRL) is a member of the pyrroline-5-carboxylate reductase family and acts as a homodecamer. PYCRL plays a key role in proline bio-synthesis. Proline serves as a non-enzymatic antioxidant to reduce damage caused by reactive oxygen species (ROS) in microorganisms, animals and plants. In the final stage of proline biosynthesis, PYCRL catalyzes the reduction of aldehyde dehydrogenase 4A1 (ALDH4A1) to proline with NAD(P)H as the cofactor.

    • Synonyms

      Pyrroline-5-carboxylate reductase 3, P5C reductase 3, P5CR 3, Pyrroline-5-carboxylate reductase-like protein, PYCRL.

    • 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 MGSMAAAEPS PRRVGFVGAG RMAGAIAQGL IRAGKVEAQH ILASAPTDRN LCHFQALGCR TTHSNQEVLQ SCLLVIFATK PHVLPAVLAE VAPVVTTEHI LVSVAAGVSL STLEELLPPN TRVLRVLPNL PCVVQEGAIV MARGRHVGSS ETNLLQHLLE ACGRCEEVPE AYVDIHTGLS GSGVAFVCAF SEALAEGAVK MGMPSSLAHR IAAQTLLGTA KMLLHEGQHP AQLRSDVCTP GGTTIYGLHA LEQGGLRAAT MSAVEAATCR AKELSRK.

    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.

    Pycrl Human
  • View Data Sheet

    Name :

    AK2 Mouse

    Description:

    Adenylate Kinase 2 Mouse Recombinant

    Adenylate kinase 2 mitochondrial isoform a, Ak-2, D4Ertd220e, mitochondrial, ATP-AMP transphosphorylase 2, ATP:AMP phosphotransferas, Adenylate monophosphate kinase.

    Product # :

    PKA-107

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    • source
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    Description

    AK2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-239 a.a) and having a molecular mass of 29kDa.AK2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AK2 protein solution (0.5mg/ml) containing 20mM Tris-Hcl buffer (pH8.5), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 40 units/mg. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 37C.

    Citations

    More Info

    • Introduction

      Adenylate kinases play a role in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. There are 3 types of adenylate kinase isozymes, AK1, AK2, and AK3 in vertebrates. Expression of these isozymes are tissue-specific and developmentally regulated. AK2 is localized in the mitochondrial intermembrane space and is involved in apoptosis. AK2 is mutated in individuals with reticular dysgenesis.

    • Synonyms

      Adenylate kinase 2 mitochondrial isoform a, Ak-2, D4Ertd220e, mitochondrial, ATP-AMP transphosphorylase 2, ATP:AMP phosphotransferas, Adenylate monophosphate kinase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      AK2 Mouse 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 MGSHMAPNVL ASEPEIPKGI RAVLLGPPGA GKGTQAPKLA ENFCVCHLAT GDMLRAMVAS GSEL TMDAGKLVSD EMVVELIEKN LETPSCKNGF LLDGFPRTVR QAEMLDDLME KRKEKLDSVI EFSIQDSLLI RRITGRLIHP KSGRS
      NPPKEPMKDD ITGEPLIRRS DDNEKALKTR LEAYHTQTTP LVEYYRKRGI HCAIDASQTP DIVFASILAA FSKATCKDLV MFI

    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.

    Ak2 Mouse
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