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Search results

1000 results found for “adenylate kinase”

Name

Description

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  • View Data Sheet

    Name :

    TSEN15 Human

    Description:

    tRNA Splicing Endonuclease 15 Human Recombinant

    tRNA-splicing endonuclease subunit Sen15, SEN15 homolog, HsSEN15, tRNA-intron endonuclease Sen15, TSEN15, C1orf19, SEN15.

    Product # :

    PRO-144

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    Description

    TSEN15 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 191 amino acids (1-171 a.a.) and having a molecular mass of 20.9kDa. The TSEN15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TSEN15 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      tRNA-splicing endonuclease subunit Sen15 (TSEN15) is a member of the SEN15 family. tRNA splicing is an essential process required for cell growth and division. TSEN15 is a subunit of the tRNA splicing endonuclease. TSEN15 cleaves pre-tRNA at the 5' and 3' splice sites to release the intron.

    • Synonyms

      tRNA-splicing endonuclease subunit Sen15, SEN15 homolog, HsSEN15, tRNA-intron endonuclease Sen15, TSEN15, C1orf19, SEN15.

    • 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 MEERGDSEPT PGCSGLGPDG VRGFGDGGGA PSWAPEDAWM GTHPKYLEMM ELDIGDATHV YVAFLVYLDL MESKSWHEVN CVGLPELQLI CLVGTEIEGE GLQTVVPTPI TASLSHNRIR EILKASRKLQ GDPDLPMSFT LAIVESDSTI VYYKLTDGFM LPDPQNISLR R.

    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.

    Tsen15 Human
  • View Data Sheet

    Name :

    GPT2 Human

    Description:

    Glutamic-Pyruvate Transaminase 2 Human Recombinant

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

    Product # :

    ENZ-680

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    Description

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

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Gpt2 Human
  • View Data Sheet

    Name :

    NFKBID Human

    Description:

    NF-kappa-B Inhibitor Delta Human Recombinant

    NF-kappa-B inhibitor delta, I-kappa-B-delta, IkB-delta, IkappaBdelta, IkappaBNS, T-cell activation NFKB-like protein, TA-NFKBH, NFKBID, IKBNS.

    Product # :

    PRO-1684

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    Description

    NFKBID Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313) and having a molecular mass of 35.9 kDa.NFKBID is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NFKBID belongs to the IkB family of proteins which contains four groups (IkB-alpha, IkB-beta, IkB-gamma, IkB-epsilon). NFKBID takes part in regulating inflammatory responses and cytokine, IL-2 and IL-6 expression through NFkB activity. NFKBID has 3 known alternative spliced isoforms, and is associated with RelB, NF?B p50 and NFkB p65 in nucleus. NFKBID is involeved in thymocyte selection in response to TCR induction.

    • Synonyms

      NF-kappa-B inhibitor delta, I-kappa-B-delta, IkB-delta, IkappaBdelta, IkappaBNS, T-cell activation NFKB-like protein, TA-NFKBH, NFKBID, IKBNS.

    • 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 MGSMEAGPWR VSAPPSGPPQ FPAVVPGPSL EVARAHMLAL GPQQLLAQDE EGDTLLHLFA ARGLRWAAYA AAEVLQVYRR LDIREHKGKT PLLVAAAANQ PLIVEDLLNL GAEPNAADHQ GRSVLHVAAT YGLPGVLLAV LNSGVQVDLE ARDFEGLTPL HTAILALNVA MRPSDLCPRV LSTQARDRLD CVHMLLQMGA NHTSQEIKSN KTVLHLAVQA ANPTLVQLLL ELPRGDLRTF VNMKAHGNTA LHMAAALPPG PAQEAIVRHL LAAGADPTLR NLENEQPVHL LRPGPGPEGL RQLLKRSRVA PPGLSS.

    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.

    Nfkbid Human
  • View Data Sheet

    Name :

    GOT1 Mouse

    Description:

    Glutamic-Oxaloacetic Transaminase 1 Mouse Recombinant

    Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.

    Product # :

    ENZ-872

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    Description

    GOT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (1-413a.a) and having a molecular mass of 48.6kDa.GOT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GOT1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.

    • Synonyms

      Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase 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 MGSMAPPSVF AQVPQAPPVL VFKLTADFRD DPDPRKVNLG VGAYRTDESQ PWVLPVVRKV EQKIANDNSL NHEYLPILGL AEFRSCASRL VLGDNSPAIR ENRVGGVQSL GGTGALRIGA DFLGRWYNGT DNKNTPIYVS SPTWENHNAV FSAAGFKDIR PYCYWDAEKR GLDLQGFLND LENAPEFSIF VLHACAHNPT GTDPTPEQWK QIAAVMQRRF LFPFFDSAYQ GFASGDLEKD AWAIRYFVSE GFELFCAQSF SKNFGLYNER VGNLTVVGKE SDSVLRVLSQ MEKIVRITWS NPPAQGARIV AATLSDPELF KEWKGNVKTM ADRILTMRSE LRARLEALKT PGTWSHITEQ IGMFSFTGLN PKQVEYLVNE KHIYLLPSGR INMCGLTTKN LDYVATSIHE AVTKIQ.

    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.

    Got1 Mouse
  • View Data Sheet

    Name :

    RAC1 Human, His

    Description:

    Ras-Related C3 Botulinum Toxin substrate 1 Human Recombinant, His Tag

    P21-RAC1, RAC-1, RAC1, RAS-like protein TC25, MIG5, Cell-migration-inducing gene 5 protein,Ras-related C3 botulinum toxin substrate 1, rho family small GTP binding protein Rac1, TC-25, MGC111543.

    Product # :

    PRO-731

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    Description

    Ras-Related C3 Botulinum Toxin substrate 1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 23.6 kDa. RAC1 contains a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RAC1 His Tag protein solution contains 20mM Tris-HCl pH7.5, 1mM EDTA, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RAC1 is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. RAC-1 regulates the actin cytoskeleton but also other cellular processes. RAC1 have been shown to be involved in the regulation of cell-cell adhesion.

    • Synonyms

      P21-RAC1, RAC-1, RAC1, RAS-like protein TC25, MIG5, Cell-migration-inducing gene 5 protein,Ras-related C3 botulinum toxin substrate 1, rho family small GTP binding protein Rac1, TC-25, MGC111543.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG QEDYDRLRPLSYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSALTQRGLKTVFD EAIRAVLCPP PVKKRKRKCL LL.

    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.

    Rac1 Human His
  • View Data Sheet

    Name :

    MDH E. coli

    Description:

    Malate Dehydrogenase Recombinant

    Malate dehydrogenase cytoplasmic, EC 1.1.1.37, Cytosolic malate dehydrogenase, MDHA, MOR2, MDH-s, MGC:1375, MDH1.

    Product # :

    ENZ-598

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    Description

    MDH Recombinant produced in E. coli is a single polypeptide chain containing 336 amino acids (1-312) and having a molecular mass of 34.9kDa.MDH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Malate dehydrogenase (EC1.1.1.37) is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of pyruvate using NADPH.
      Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondrial membrane. Once in the cytosol, the malate is oxidized back to oxaloacetate by cytosolic malate dehydrogenase. Finally, phosphoenol-pyruvate carboxy kinase (PEPCK) converts oxaloacetate to phosphoenol pyruvate.

    • Synonyms

      Malate dehydrogenase cytoplasmic, EC 1.1.1.37, Cytosolic malate dehydrogenase, MDHA, MOR2, MDH-s, MGC:1375, MDH1.

    • 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 MGSHMKVAVL GAAGGIGQAL ALLLKTQLPS GSELSLYDIA PVTPGVAVDL SHIPTAVKIK GFSGEDATPA LEGADVVLIS AGVARKPGMD RSDLFNVNAG IVKNLVQQVA KTCPKACIGI ITNPVNTTVA IAAEVLKKAG VYDKNKLFGV TTLDIIRSNT FVAELKGKQP GEVEVPVIGG HSGVTILPLL SQVPGVSFTE QEVADLTKRI QNAGTEVVEA KAGGGSATLS MGQAAARFGL SLVRALQGEQ GVVECAYVEG DGQYARFFSQ PLLLGKNGVE ERKSIGTLSA FEQNALEGML DTLKKDIALG EEFVNK

    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.

    Mdh
  • View Data Sheet

    Name :

    DOK4 Human

    Description:

    Docking Protein 4 Human Recombinant

    docking protein 4, Downstream of tyrosine kinase 4, IRS-5, IRS5.

    Product # :

    PRO-1895

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    Description

    DOK4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-326 a.a) and having a molecular mass of 39.4kDa.DOK4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DOK4 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Docking Protein 4(DOK4) is a member of the DOK family. DOK proteins are enzymatically inert adaptor or scaffolding proteins. The DOK proteins present a docking platform for the compilation of multimolecular signaling complexes. DOK4 serves in RET-mediated neurite outgrowth and has a positive role in activation of the MAP kinase pathway. DOK4 is a putative link with downstream effectors of RET in neuronal differentiation. DOK4 is involved in the regulation of the immune response induced by T-cells.

    • Synonyms

      docking protein 4, Downstream of tyrosine kinase 4, IRS-5, IRS5.

    • 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 MGSMATNFSD IVKQGYVKMK SRKLGIYRRC WLVFRKSSSK GPQRLEKYPD EKSVCLRGCP KVTEISNVKC VTRLPKETKR QAVAIIFTDD SARTFTCDSE LEAEEWYKTL SVECLGSRLN DISLGEPDLL APGVQCEQTD RFNVFLLPCP NLDVYGECKL QITHENIYLW DIHNPRVKLV SWPLCSLRRY GRDATRFTFE AGRMCDAGEG LYTFQTQEGE QIYQRVHSAT LAIAEQHKRV LLEMEKNVRL LNKGTEHYSY PCTPTTMLPR SAYWHHITGS QNIAEASSYA GEGYGAAQAS SETDLLNRFI LLKPKPSQGD SSEAKTPSQ.

    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.

    Dok4 Human
  • View Data Sheet

    Name :

    GHK-Cu

    Description:

    GHK-Cu

    Copper Tripeptide-1

    Product # :

    HOR-063

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    Description

    GHK-Cu is a synthetic single, non-glycosylated polypeptide chain containing 3 amino acids, having a molecular mass of 401.91 Dalton and a Molecular formula of C14H22N6O4Cu.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Gly-His-Lys.

    • Background

      GHK-Cu is located in human plasma and has an ability to modify gene expression to a healthier state, influencing more than 4,000 human genes. GHK-Cu can change pathological gene expression to a healthy mode, mainly in chronic conditions as metastatic cancer, COPD and Ulcerative Colitis. GHK-Cu was discovered to be effective in systemic repair and neuroprotection.

      What is the molecular weight/Mw of GHK-CU Protein?
      GHK-CU Protein has a total Mw of 0.40kDa.

      What is the Purity of GHK-CU Protein?
      GHK-CU Protein is >97% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of GHK-CU Protein?
      Gly-His-Lys.

      What applications can GHK-CU Protein be used in?
      GHK-CU Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GHK-CU Protein?
      The endotoxin level is minimal, GHK-CU Protein was purified using conventional chromatography techniques.

      Who supplies GHK-CU that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of GHK-CU?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    GHK-Cu
  • View Data Sheet

    Name :

    FUT5 Human

    Description:

    Fucosyltransferase 5 Human Recombinant

    FUT-5

    Product # :

    ENZ-1199

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    Description

    The FUT5 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FUT5 His-Tagged Fusion Protein produced in E. coli, is a 30kDa protein containing 172 amino acid residues of the FUT5 Human, 203-374 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      FUT-5

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized FUT5 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      Fucosyltransferase 5 also known as FUT5 is a glycosyltransferase which takes part in the biosynthesis of glycolipids and glycoproteins. FUT5 mainly catalyzes the transfer of fucose (a monosaccharide) to the type 2 chain of oligosaccharides (Galβ1-4GlcNAc). FUT5 takes an important part in various biological processes which include regulation of inflammation, cell-cell interactions and immune response modulation. FUT5 is expressed mainly in tissues such as the pancreas, liver and various immune cells.

    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.

    Fut5 Human
  • View Data Sheet

    Name :

    RNASE1 Human

    Description:

    Ribonuclease 1 Human Recombinant

    RNASE1, ribonuclease A family member 1, pancreatic, RAC1, RIB1, RNS1, ribonuclease pancreatic, HP-RNase, RIB-1, RNase UpI-1, RNase 1, Ribonuclease A, RNase A, Ribonuclease 1.

    Product # :

    ENZ-1168

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    Description

    RNASE1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (29-156 a.a) containing a total of 134 amino acids, having a molecular mass of 15.3kDa. RNASE1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The RNASE1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >  3 X 10^6 unit/mg. Defined by the amount of enzyme that  hydrolyzes 1nmole of RNA per minute at 25˚C.

    Citations

    More Info

    • Introduction

      Ribonuclease 1R (NASE1) is a small protein which is a part of pancreatic ribonuclease enzyme family. NASE1 has 4 disulfide bonds in its native state and cleaves speciallyafter pyrimidine nucleotides.Cleavage takes place in 2 steps: first, the 3’,5’-phosphodiester bond is cleaved to craete a 2’,3’-cyclic phosphodiester intermediate; than, the cyclic phosphodiester is hydrolyzed to a 3’-monophosphate. NASE1is activated the most with single stranded RNA.NASE1inhibited by alkylation of His12 and His119 and activated by potassium and sodium salts.NASE1hydrolyzes RNA from protein samples.

    • Synonyms

      RNASE1, ribonuclease A family member 1, pancreatic, RAC1, RIB1, RNS1, ribonuclease pancreatic, HP-RNase, RIB-1, RNase UpI-1, RNase 1, Ribonuclease A, RNase A, Ribonuclease 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

      KESRAKKFQR QHMDSDSSPS SSSTYCNQMM RRRNMTQGRC KPVNTFVHEP LVDVQNVCFQ EKVTCKNGQG NCYKSNSSMH ITDCRLTNGS RYPNCAYRTS PKERHIIVAC EGSPYVPVHF DASVEDSTHH HHHH

    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.

    Rnase1 Human
  • View Data Sheet

    Name :

    GDA Mouse

    Description:

    Guanine Deaminase Mouse Recombinant

    Guanine deaminase, Guanase, Guanine aminase, Guanine aminohydrolase, GAH.

    Product # :

    ENZ-1058

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    Description

    GDA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 477 amino acids (1-454 a.a) and having a molecular mass of 53.4kDa.GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDA protein solution (0.5mg/ml) containing 20mM Tris-HCl(pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol .

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 4,000 pmol/min/ug, and is defined as
    the amount of enzyme that convert guanine to xanthine per minute at pH 8.0 at 37°C.

    Citations

    More Info

    • Introduction

      GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

    • Synonyms

      Guanine deaminase, Guanase, Guanine aminase, Guanine aminohydrolase, GAH.

    • 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 MGSMCAARTP PLALVFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE SSQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHAPQ YAFAGSNVDL PLLEWLNKYT FPTEQRFRST DVAEEVYTRV VRRTLKNGTT TACYFGTIHT DSSLILAEIT DKFGQRAFVG KVCMDLNDTV PEYKETTEES VKETERFVSE MLQKNYPRVK PIVTPRFTLS CTETLMSELG NIAKTHDLYI QSHISENREE IEAVKSLYPS YKNYTDVYDK NNLLTNKTVM AHGCYLSEEE LNIFSERGAS IAHCPNSNLS LSSGLLNVLE VLKHKVKIGL GTDVAGGYSY SMLDAIRRAV MVSNVLLINK VNEKNLTLKE VFRLATLGGS QALGLDSEIG NFEVGKEFDA LLINPRASDS PIDLFYGDFV GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.

    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.

    Gda Mouse
  • View Data Sheet

    Name :

    ADFP Human

    Description:

    Adipose Differentiation-Related Protein Human Recombinant

    Adipophilin, Adipose differentiation-related protein, ADRP, ADFP, MGC10598.

    Product # :

    PRO-405

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    Description

    ADFP Human Recombinant produced in E.Coli is a signle, non-glycosylated, Polypeptide chain containing 444 amino acids and having a molecular mass of 49 kDa. The protein contains an extra 8 amino acid His tag at N-terminus. The ADFP amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q99541 amino acids 4–437.The ADFP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human ADFP was lyophilized from 0.5mg/ml solution containing 20mM Tris pH-7.5, and 20mM NaCl.

    Purity

    Greater than 95% as determined by SDS PAGE.

    Citations

    More Info

    • Introduction

      ADFP is related with the globule surface membrane material. ADFP is a major constituent of the globule surface. Rise in mRNA levels is one of the initial indications of adipocyte differentiation. Mycobacterium leprae regulates ADFP expression to facilitate the accumulation of lipids within infected macrophages for intracellular survival. ADFP is expressed in lipid droplets of vitamin A-storing hepatic stellate cells and additionally in lipid droplets of steatotic hepatocytes. ADFP expression has a role in clear cell renal carcinoma differentiation. ADFP is a component of the lipid droplets in THP-1 cells.

    • Synonyms

      Adipophilin, Adipose differentiation-related protein, ADRP, ADFP, MGC10598.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS VAVDPQPSVV TRVVNLPLVS STYDLMSSAY LSTKDQYPYL KSVCEMAENG VKTITSVAMT SALPIIQKLE PQIAVANTYA CKGLDRIEER LPILNQPSTQ IVANAKGAVT GAKDAVTTTV TGAKDSVAST ITGVMDKTKG AVTGSVEKTK SVVSGSINTV LGSRMMQLVS SGVENALTKS ELLVEQYLPL TEEELEKEAK KVEGFDLVQK PSYYVRLGSL STKLHSRAYQ QALSRVKEAK QKSQQTISQL HSTVHLIEFA RKNVYSANQK IQDAQDKLYL SWVEWKRSIG YDDTDESHCA EHIESRTLAI ARNLTQQLQT TCHTLLSNIQ GVPQNIQDQA KHMGVMAGDI YSVFRNAASF KEVSDSLLTS SKGQLQKMKE SLDDVMDYLV NNTPLNWLVG PFYPQLTESQ NAQDQGAEMD KSSQETQRSEHKTH.

    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.

    Adfp Human
  • View Data Sheet

    Name :

    Activin-A Rat

    Description:

    Activin-A Rat Recombinant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-147

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    Description

    Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml

    Citations

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

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

      Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 26.2 kDa.

      What is the source or expression system of Activin A Protein?
      Ecoli

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

      What is the Biological Activity of Activin A Protein?
      Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.

      What is the endotoxin level for Activin A Protein?
      The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of ACTIVIN A Protein?
      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

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

    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.

    Inhba Rat
  • View Data Sheet

    Name :

    SARS Human

    Description:

    Seryl-tRNA Synthetase Human Recombinant

    Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    Product # :

    ENZ-229

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    Description

    SARS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 537 amino acids (1-514) and having a molecular mass of 61.2kDa.SARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SARS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Seryl-tRNA synthetase, cytoplasmic (SARS) is a member of the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases’ role is to catalyze the aminoacylation of tRNAs by their corresponding amino acids, as a result linking amino acids with tRNA-contained nucleotide triplets. The SARS enzyme catalyzes the attachment of serine to tRNA (Ser). SARS enzyme is probably able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be then converted into selenocysteinyl-tRNA (Sec).

    • Synonyms

      Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    • 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 MGSMVLDLDL FRVDKGGDPA LIRETQEKRF KDPGLVDQLV KADSEWRRCR FRADNLNKLK NLCSKTIGEK MKKKEPVGDD ESVPENVLSF DDLTADALAN LKVSQIKKVR LLIDEAILKC DAERIKLEAE RFENLREIGN LLHPSVPISN DEDVDNKVER IWGDCTVRKK YSHVDLVVMV DGFEGEKGAV VAGSRGYFLK GVLVFLEQAL IQYALRTLGS RGYIPIYTPF FMRKEVMQEV AQLSQFDEEL YKVIGKGSEK SDDNSYDEKY LIATSEQPIA ALHRDEWLRP EDLPIKYAGL STCFRQEVGS HGRDTRGIFR VHQFEKIEQF VYSSPHDNKS WEMFEEMITT AEEFYQSLGI PYHIVNIVSG SLNHAASKKL DLEAWFPGSG AFRELVSCSN CTDYQARRLR IRYGQTKKMM DKVEFVHMLN ATMCATTRTI CAILENYQTE KGITVPEKLK EFMPPGLQEL IPFVKPAPIE QEPSKKQKKQ HEGSKKKAAA RDVTLENRLQ NMEVTDA.

    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.

    Sars Human
  • View Data Sheet

    Name :

    ALDH3A1 Human

    Description:

    Aldehyde Dehydrogenase 3 Family Member A1 Human Recombinant

    Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.

    Product # :

    ENZ-479

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    Description

    ALDH3A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 473 amino acids (1-453 a.a.) and having a molecular mass of 52.5 kDa. ALDH3A1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ALDH3A1 solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity was found to be < 1 units/ml. Activity was obtained by measuring the increase of NADP in absorbance at 340 nm resulting from the reduction of NAD. 1 unit will oxidize 1umole of acetaldehyde to acetic acid per minute at pH 8 at 25°C in the presence of beta-NAD, potassium and thiols.

    Citations

    More Info

    • Introduction

      ALDH3A1 is involved in the detoxification of alcohol-derived acetaldehyde. ALDH3A1 participates in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. ALDH3A1 oxidizes aromatic aldehyde substrates and toxic aldehydes. ALDH3A1 forms a cytoplasmic homodimer that oxidizes aromatic and medium-chain saturated and unsaturated aldehyde substrates. ALDH3A1 promotes resistance to UV and 4-hydroxy-2-nonenal-induced oxidative damage in the cornea.

    • Synonyms

      Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA DLHKNEWNAY YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI HSEPLGVVLV IGTWNYPFNL TIQPMVGAIA AGNAVVLKPS ELSENMASLL ATIIPQYLDK DLYPVINGGV PETTELLKER FDHILYTGST GVGKIIMTAA AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS GQTCVAPDYI LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVLPIVCVRSLEE AIQFINQREK PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL PFGGVGNSGM GSYHGKKSFE TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM TQH.

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    Aldh3A1 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 :

    CANT1 Human

    Description:

    Calcium Activated Nucleotidase 1 Human Recombinant

    Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.

    Product # :

    PRO-1010

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    Description

    CANT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (63-401 a.a.) and having a molecular mass of 40.5kDa. CANT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CANT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Calcium-activated nucleotidase 1 (CANT1) is a member of the apyrase family. The CANT1 protein is calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is as follows: UDP > GDP > UTP > GTP. Moreover, CANT1 has a very low activity towards ADP and an even lower activity towards ATP. As well as it doesn’t hydrolyze AMP and GMP. CANT1’s specific function is yet unknown, nevertheless its substrates are involved in several key signaling functions, including Ca2+ release, through activation of pyrimidinergic signaling. Mutations in the CANT1 gene are linked with Desbuquois dysplasia with hand anomalies.

    • Synonyms

      Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.

    • 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 MGSHMRPAPG RPPTHNAHNW RLGQAPANWY NDTYPLSPPQ RTPAGIRYRI AVIADLDTES RAQEENTWFS YLKKGYLTLS DSGDKVAVEW DKDHGVLESH LAEKGRGMEL SDLIVFNGKL YSVDDRTGVV YQIEGSKAVP WVILSDGDGT VEKGFKAEWL AVKDERLYVG GLGKEWTTTT GDVVNENPEW VKVVGYKGSV DHENWVSNYN ALRAAAGIQP PGYLIHESAC WSDTLQRWFF LPRRASQERY SEKDDERKGA NLLLSASPDF GDIAVSHVGA VVPTHGFSSF KFIPNTDDQI IVALKSEEDS GRVASYIMAF TLDGRFLLPE TKIGSVKYEG IEFI.

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    Cant1 Human
  • View Data Sheet

    Name :

    KMT5A Human

    Description:

    Lysine Methyltransferase 5A Human Recombinant

    KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.

    Product # :

    ENZ-1080

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    Description

    KMT5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 165 amino acids (195-352 a.a.) and having a molecular mass of 18.9kDa (Migrates at 18-28 kDa on SDS-PAGE under reducing conditions).KMT5A is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KMT5A protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 5mM DTT, 0.2M NaCl, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lysine Methyltransferase 5A (KMT5A) is an enzyme which catalyzes both histones and non-histone proteins. KMT5A contributes to the maintenance of proper higher-order structure of DNA during mitosis. KMT5A takes part in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. KMT5A plays a role as a barrier to prevent cellular senescence through chromatinmediated regulation of senescence-associated metabolic remodeling. KMT5A mediates monomethylation of p53/TP53 at 'Lys-382', which leads to repress p53/TP53-target genes. The loss of KMT5A simultaneously stimulate nucleolar function and retinoblastoma protein-mediated mitochondrial metabolism.

    • Synonyms

      KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.

    • 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

      MKAELQSEER KRIDELIESG KEEGMKIDLI DGKGRGVIAT KQFSRGDFVV EYHGDLIEIT DAKKREALYA QDPSTGCYMY YFQYLSKTYC VDATRETNRL GRLINHSKCG NCQTKLHDID GVPHLILIAS RDIAAGEELL YDYGDRSKAS IEAHPWLKHH HHHHH.

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    Kmt5A Human
  • View Data Sheet

    Name :

    LDHB Human

    Description:

    Lactate Dehydrogenase B Human Recombinant

    Lactate Dehydrogenase B, Renal Carcinoma Antigen NY-REN-46, LDH Heart Subunit, EC 1.1.1.27, LDH-B, LDH-H, Epididymis Secretory Protein Li 281, Testicular Secretory Protein Li 25, Lactate Dehydrogenase H Chain, HEL-S-281, EC 1.1.1 , LDHBD, TRG-5.

    Product # :

    ENZ-967

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    Description

    LDHB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-334) and having a molecular mass of 36.6kDa.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >300 units/mg, in which 1 unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per min at pH 7.5 at 37°.

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Lactate Dehydrogenase B, Renal Carcinoma Antigen NY-REN-46, LDH Heart Subunit, EC 1.1.1.27, LDH-B, LDH-H, Epididymis Secretory Protein Li 281, Testicular Secretory Protein Li 25, Lactate Dehydrogenase H Chain, HEL-S-281, EC 1.1.1 , LDHBD, TRG-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

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

    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.

    Human Ldhb
  • 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.

    Citations

    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.

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    Glyatl2 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

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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 :

    MAK16 Human

    Description:

    MAK16 Human Recombinant

    Protein MAK16 homolog, NNP78, Protein RBM13, RBM13, MAK16L, RBM13.

    Product # :

    PRO-2086

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    Description

    MAK16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a) and having a molecular mass of 37.8kDa (Molecular size on SDS-PAGE will appear higher).MAK16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAK16 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MAK16 is a member of the MAK16 family.

    • Synonyms

      Protein MAK16 homolog, NNP78, Protein RBM13, RBM13, MAK16L, RBM13.

    • 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 MGSMQSDDVI WDTLGNKQFC SFKIRTKTQS FCRNEYSLTG LCNRSSCPLA NSQYATIKEE KGQCYLYMKV IERAAFPRRL WERVRLSKNY EKALEQIDEN LIYWPRFIRH KCKQRFTKIT QYLIRIRKLT LKRQRKLVPL SKKVERREKR REEKALIAAQ LDNAIEKELL ERLKQDTYGD IYNFPIHAFD KALEQQEAES DSSDTEEKDD DDDDEEDVGK REFVEDGEVD ESDISDFEDM DKLDASSDED QDGKSSSEEE EEKALSAKHK GKMPLRGPLQ RKRAYVEIEY EQETEPVAKA KTT.

    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.

    Mak16 Human
  • View Data Sheet

    Name :

    RAB18 Human

    Description:

    RAB18, Member RAS Oncogene Family Human Recombinant

    RAB18 member RAS oncogene family, RAB18LI1, WARBM3, RAB18 small GTPase, ras-related protein Rab-18.

    Product # :

    PRO-976

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    RAB18 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-206) and having a molecular mass of 24.5 kDa.RAB18 is fused to a 15 amino acid His-Tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RAB18 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5) and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RAB18 belongs to a family of Ras-related small GTPase which is lipid-anchored to the cytoplasmic side of the cell membrane. RAB18 takes part in apical recycling, endocytosis and protein transport between early endosomes and the plasma membrane.

    • Synonyms

      RAB18 member RAS oncogene family, RAB18LI1, WARBM3, RAB18 small GTPase, ras-related protein Rab-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

      MASMTGGQQM GRGSHMDEDV LTTLKILIIG ESGVGKSSLL LRFTDDTFDP ELAATIGVDF KVKTISVDGN KAKLAIWDTA GQERFRTLTP SYYRGAQGVI LVYDVTRRDT FVKLDNWLNE LETYCTRNDI VNMLVGNKID KENREVDRNE GLKFARKHSM LFIEASAKTC DGVQCAFEEL VEKIIQTPGL WESENQNKGV KLSHREEGQG GGACGGYCSV 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.

    Rab18 Human
  • View Data Sheet

    Name :

    RNGTT Human

    Description:

    RNA Guanylyltransferase And 5'-Phosphatase Human Recombinant

    RNA Guanylyltransferase And 5'-Phosphatase, CAP1A, RNA Guanylyltransferase And 5-Phosphatase, HCAP1, HCE1, HCE, MRNA-Capping Enzyme, HCAP 3, mRNA-capping enzyme.

    Product # :

    ENZ-823

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    RNGTT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 620 amino acids (1-597a.a) and having a molecular mass of 70.9kDa. RNGTT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNGTT protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 40% glycerol, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RNA Guanylyltransferase And 5'-Phosphatase also known as RNGTT is a bifunctional mRNA-capping enzyme which exhibits RNA 5'-triphosphatase activity in the N-terminal section and mRNA guanylyltransferase activity in the C-terminal section. In addition, RNGTT catalyzes the first two steps of cap formation, through removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and also by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.

    • Synonyms

      RNA Guanylyltransferase And 5'-Phosphatase, CAP1A, RNA Guanylyltransferase And 5-Phosphatase, HCAP1, HCE1, HCE, MRNA-Capping Enzyme, HCAP 3, mRNA-capping enzyme.

    • 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 MGSMAHNKIP PRWLNCPRRG QPVAGRFLPL KTMLGPRYDS QVAEENRFHP SMLSNYLKSL KVKMGLLVDL TNTSRFYDRN DIEKEGIKYI KLQCKGHGEC PTTENTETFI RLCERFNERN PPELIGVHCT HGFNRTGFLI CAFLVEKMDW SIEAAVATFA QARPPGIYKG DYLKELFRRY GDIEEAPPPP LLPDWCFEDD EDEDEDEDGK KESEPGSSAS FGKRRKERLK LGAIFLEGVT VKGVTQVTTQ PKLGEVQQKC HQFCGWEGSG FPGAQPVSMD KQNIKLLDLK PYKVSWKADG TRYMMLIDGT NEVFMIDRDN SVFHVSNLEF PFRKDLRMHL SNTLLDGEMI IDRVNGQAVP RYLIYDIIKF NSQPVGDCDF NVRLQCIERE IISPRHEKMK TGLIDKTQEP FSVRNKPFFD ICTSRKLLEG NFAKEVSHEM DGLIFQPTGK YKPGRCDDIL KWKPPSLNSV DFRLKITRMG GEGLLPQNVG LLYVGGYERP FAQIKVTKEL KQYDNKIIEC KFENNSWVFM RQRTDKSFPN AYNTAMAVCN SISNPVTKEM LFEFIDRCTA ASQGQKRKHH LDPDTELMPP PPPKRPRPLT.

    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.

    Rngtt Human
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