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Search results

1000 results found for “lipase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    TDO2 Human

    Description:

    Tryptophan 2,3-Dioxygenase Human Recombinant

    Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.

    Product # :

    ENZ-081

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    Description

    TDO2 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 426 amino acids (1-406 a.a.) and having a molecular mass of 50kDa. The TDO2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TDO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TDO2 is a ferrous heme enzyme that catalyzes the first and rate-limiting step in the kynurenine pathway which is the major pathway of tryptophan metabolism. TDO2 integrates oxygen into the indole moiety of tryptophan. TDO2 has broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin.

    • Synonyms

      Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.

    • 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 MSGCPFLGNN FGYTFKKLPV EGSEEDKSQT GVNRASKGGL IYGNYLHLEK VLNAQELQSE TKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VVSRMHRVSV ILKLLVQQFS ILETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQN MRVPYNRRHY RDNFKGEENE LLLKSEQEKT LLELVEAWLE RTPGLEPHGF NFWGKLEKNI TRGLEEEFIR IQAKEESEEK EEQVAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYRALQ GALMIYFYRE EPRFQVPFQL LTSLMDIDSL MTKWRYNHVC MVHRMLGSKA GTGGSSGYHY LRSTVSDRYK VFVDLFNLST YLIPRHWIPK MNPTIHKFLY TAEYCDSSYF SSDESD.

    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.

    Tdo2 Human
  • View Data Sheet

    Name :

    KLK1 Human, His

    Description:

    Kallikrein-1 Human Recombinant, His Tag

    KLK1, KLK-1, HK1, HK-1, KLKR, KLK6, Tissue Kallikrein, hKLK1, EC 3.4.21.35, Kidney/pancreas/salivary gland kallikrein, Kallikrein-1.

    Product # :

    ENZ-690

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    Description

    Kallikrein-1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 259 amino acids (25-262) and having a molecular mass of 28.7kDa.KLK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KLK1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikreins are serine protease enzymes having various physiological functions.
      Kallikreins are implicated in carcinogenesis and have potenital as novel cancer disease biomarkers. KLK1 is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK1 is functionally conserved in its ability to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen.
      Human Kallikrein-1, also called as Kallidinogenase, Kininogenase or Kininogenin, is an active protein enzyme present in saliva, pancreatic juices, and urine that catalyzes the proteolysis of bradykininogen to bradykinin.
      Kallikrein-1, which derived from human or porcine, have been used as drugs for a long time, they are mainly used in the treatment f light to medium hypertension and occlusion of cerebral and surrounding blood vessels.
      KLK1 demonstrates both trypsin- and chymotrypsin-like selectivities with Tyr/Arg preferred at site P1, Ser/Arg strongly preferred at P1', and Phe/Leu at P2.
      rs5517 in the KLK1 gene is considerably connected with hypertension in a Chinese Han population. KLK1 is expressed de novo in endothelial cells and mediates relaxation of human umbilical veins. The K allele of KLK1 promoter and TT genotype of TGF-beta1 are a genetic KLK1 -130 GN and -128 G-C, and the defenselessness factor contributing to progressive renal descent in Taiwanese primary vesicoureteric reflux children.
      Induction of KLK1 in carotid arteriosclerosis doesn’t lead to kallikrein-kinins pathway activation. Transgenic rats expressing KLK1 have impaired renal response to acute volume expansion Endothelial cells synthesize and release active form of KLK1on the surface which is important function in maintenance of circulation homeostasis.
      KLK1 participates in epidermal desquamation through cleavage of desmoglein 1 and regulation by lympho-epithelial Kazal-type-related inhibitor (LEKTI).

    • Synonyms

      KLK1, KLK-1, HK1, HK-1, KLKR, KLK6, Tissue Kallikrein, hKLK1, EC 3.4.21.35, Kidney/pancreas/salivary gland kallikrein, Kallikrein-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MIVGGWECEQ HSQPWQAALY HFSTFQCGGI LVHRQWVLTA AHCISDNYQL WLGRHNLFDD ENTAQFVHVS ESFPHPGFNM SLLENHTRQA DEDYSHDLML LRLTEPADTI TDAVKVVELP TQEPEVGSTC LASGWGSIEP ENFSFPDDLQ CVDLKILPND ECKKVHVQKV TDFMLCVGHL EGGKDTCVGD SGGPLMCDGV LQGVTSWGYV PCGTPNKPSV AVRVLSYVKW IEDTIAENS.

    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.

    Klk1 Human His
  • View Data Sheet

    Name :

    PGD Human

    Description:

    Phosphogluconate Dehydrogenase Human Recombinant

    EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.

    Product # :

    ENZ-501

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    Description

    PGD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 503 amino acids (1-483 a.a.) and having a molecular mass of 55.3 kDa. The PGD is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PGD solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      6PGD is the second dehydrogenase in the pentose phosphate shunt. Pentose is neccesary for nucleic acid biosynthesis. The pentose phosphate cycle is a major source of NADPH 6PGD deficiency is usually asymptomatic, and the inheritance of this disorder is autosomal dominant. PGD deficiency raises the erythrocyte pyruvate kinase levels of activity and decreases glutathione synthetase, resulting in hemolysis.

    • Synonyms

      EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA.

    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.

    Pgd Human
  • View Data Sheet

    Name :

    UROD Human

    Description:

    Uroporphyrinogen Decarboxylase Human Recombinant

    UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.

    Product # :

    ENZ-536

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    Description

    UROD Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 43 kDa. The UROD is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UROD Human solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl, 1mM EDTA & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UROD is the fifth enzyme in the human heme biosynthetic pathway and is in charge for the transfer of uroporphyrinogen to coproporphyrinogen through the deletion of four carboxymethyl side chains. UROD Mutations and deficiency result in 3 autosomal disorders in humans: familial porphyria cutanea tarda (f-PCT), sporadic porphyria cutanea tarda (s-PCT) and hepatoerythropoietic porphyria (HEP).

    • Synonyms

      UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.

    • 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 MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT LQVNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH SRLLRQN.

    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.

    Urod Human
  • View Data Sheet

    Name :

    CKMT3 Human

    Description:

    Creatine Kinase Muscle Type-3 Human Recombinant

    Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.

    Product # :

    CKI-272

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    Description

    CKMT3 Human Recombinant produced in Pichia Pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to MM Isoenzyme in ELISA.The CKMT3 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    Each mg of protein contains 20mM Tris pH-8, 1mM EDTA and 1mM DTT.

    Purity

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

    Biological Activity

    The biological activity measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 500 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 2,000ng/ml.

    More Info

    • Introduction

      The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

    • Synonyms

      Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles.

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

    Ckmmitiii Human
  • View Data Sheet

    Name :

    Placental Lactogen Caprine

    Description:

    Placental Lactogen Caprine Recombinant

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

    Product # :

    CYT-510

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized caprine recombinant placental lactogen although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of caprine recombinant placental lactogen at > 0.1 mg/ml and up to 4 mg/ml and filter sterilization caprine recombinant placental lactogen can be stored at 4C for several weeks.

    • Solubility

      It is recommended to reconstitute the lyophilized caprine recombinant placental lactogen in sterile water or 0.4% NaHCO3 adjusted tp pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.

    • Amino Acid Sequence

      The sequence of the first four N-terminal amino acids was determined and was found to be Ala-Glu-Asn-Tyr.

    • Protein content

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

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

    Placental Lactogen Caprine
  • View Data Sheet

    Name :

    AKR7A3 Human, His

    Description:

    Aldo-Keto Reductase Family 7 Member A3 Human Recombinant, His Tag

    AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    Product # :

    ENZ-484

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    Description

    AKR7A3 Human Recombinant fused to a 39 amino acids His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 370 amino acids (1-331 a.a.) and having a molecular mass of 41.6 kDa. The AKR7A3 is fused to a 39 amino acid His tag at n-terminal and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR7A3 solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately < 0.1 units/mg.
    Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.

    More Info

    • Introduction

      AKR7A3, takes part in the detoxification of aldehydes and ketones. AKR7A3 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A3 participates in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

    • Synonyms

      AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEM SRQLSRARPA TVLGAMEMGR RMDAPTSAAV TRAFLERGHT EIDTAFVYSE GQSETILGGL GLRLGGSDCR VKIDTKAIPL FGNSLKPDSL RFQLETSLKR LQCPRVDLFY LHMPDHSTPV EETLRACHQL HQEGKFVELG LSNYAAWEVA EICTLCKSNG WILPTVYQGM YNAITRQVET ELFPCLRHFG LRFYAFNPLA GGLLTGKYKY EDKDGKQPVG RFFGNTWAEM YRNRYWKEHH FEGIALVEKA LQAAYGASAP SMTSATLRWM YHHSQLQGAH GDAVILGMSS LEQLEQNLAA AEEGPLEPAV VDAFNQAWHL VAHECPNYFR.

    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.

    Akr7A3 Human
  • View Data Sheet

    Name :

    NNMT Human, Active

    Description:

    Nicotinamide N-Methyltransferase Human Recombinant, Active

    Nicotinamide N-methyltransferase, EC 2.1.1.1, NNMT.

    Product # :

    ENZ-1060

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    Description

    NNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-264 a.a) and having a molecular mass of 37.7kDa.NNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NNMT protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37C.

    More Info

    • Introduction

      NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.

    • Synonyms

      Nicotinamide N-methyltransferase, EC 2.1.1.1, NNMT.

    • 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 MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC LDGVKGDLLI DIGSGPTIYQ LLSACESFKE IVVTDYSDQN LQELEKWLKK EPEAFDWSPV VTYVCDLEGN RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG AVPLPPADCV LSTLCLDAAC PDLPTYCRAL RNLGSLLKPG GFLVIMDALK SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ SYSSTMANNE GLFSLVARKL SRPL.

    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.

    Nnmt Human Active
  • View Data Sheet

    Name :

    UPRT Human

    Description:

    Uracil Phosphoribosyltransferase Human Recombinant

    Uracil phosphoribosyltransferase homolog, Uracil phosphoribosyltransferase (FUR1) homolog (S.cerevisiae), FUR1, Uracil Phosphoribosyltransferase, RP11-311P8.3, UPP, UPRT, UPRTase, UMP pyrophosphorylase, uprt.

    Product # :

    ENZ-742

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    Description

    UPRT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 332 amino acids (1-309 a.a) and having a molecular mass of 36.2kDa.UPRT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UPRT protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UPRT is a uracil phosphoribosyltransferase, that catalyzes the alteration of uracil and 5-phosphoribosyl-1-R-diphosphate to uridine monophosphate (UMP). This reaction is a significant part of nucleotide metabolism, specifically the pyrimidine salvage pathway. UPRT is restricted to the nucleus and cytoplasm and is a possible target for rational design of drugs to cure cancer and parasitic infections.

    • Synonyms

      Uracil phosphoribosyltransferase homolog, Uracil phosphoribosyltransferase (FUR1) homolog (S.cerevisiae), FUR1, Uracil Phosphoribosyltransferase, RP11-311P8.3, UPP, UPRT, UPRTase, UMP pyrophosphorylase, uprt.

    • 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 MGSMATELQC PDSMPCHNQQ VNSASTPSPE QLRPGDLILD HAGGNRASRA KVILLTGYAH SSLPAELDSG ACGGSSLNSE GNSGSGDSSS YDAPAGNSFL EDCELSRQIG AQLKLLPMND QIRELQTIIR DKTASRGDFM FSADRLIRLV VEEGLNQLPY KECMVTTPTG YKYEGVKFEK GNCGVSIMRS GEAMEQGLRD CCRSIRIGKI LIQSDEETQR AKVYYAKFPP DIYRRKVLLM YPILSTGNTV IEAVKVLIEH GVQPSVIILL SLFSTPHGAK SIIQEFPEIT ILTTEVHPVA PTHFGQKYFG TD.

    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.

    Uprt Human
  • View Data Sheet

    Name :

    KLK13 Human

    Description:

    Kallikrein-13 Human Recombinant

    Kallikrein-13, KLK-L4, KLKL4, Kallikrein-like protein 4.

    Product # :

    ENZ-846

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    Description

    KLK13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (17-277 a.a) and having a molecular mass of 31.3kDa.KLK13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLK13 protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikreins are a subgroup of serine proteases having various physiological functions. Many kallikreins are implicated in carcinogenesis and some have potential of becoming novel cancer and other disease biomarkers. Kallikrein-13 (KLK13) is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK13 gene expression is regulated by steroid hormones and may be useful as a marker for breast cancer.

    • Synonyms

      Kallikrein-13, KLK-L4, KLKL4, Kallikrein-like protein 4.

    • 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 MGSGGVSQES SKVLNTNGTS GFLPGGYTCF PHSQPWQAAL LVQGRLLCGG VLVHPKWVLT AAHCLKEGLK VYLGKHALGR VEAGEQVREV VHSIPHPEYR RSPTHLNHDH DIMLLELQSP VQLTGYIQTL PLSHNNRLTP GTTCRVSGWG TTTSPQVNYP KTLQCANIQL RSDEECRQVY PGKITDNMLC AGTKEGGKDS CEGDSGGPLV CNRTLYGIVS WGDFPCGQPD RPGVYTRVSR YVLWIRETIR KYETQQQKWL KGPQ.

    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.

    Klk13 Human
  • View Data Sheet

    Name :

    UBE2A Human

    Description:

    Ubiquitin Conjugating Enzyme E2A Human Recombinant

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

    Product # :

    ENZ-514

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSTPARRRLM RDFKRLQEDP PAGVSGAPSE NNIMVWNAVI FGPEGTPFED GTFKLTIEFT EEYPNKPPTV RFVSKMFHPN VYADGSICLD ILQNRWSPTY DVSSILTSIQ SLLDEPNPNS PANSQAAQLY QENKREYEKR VSAIVEQSWR DC.

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

    Ube2A Human
  • View Data Sheet

    Name :

    CHI3L2 Human, Sf9

    Description:

    Chitinase 3-Like 2 Human Recombinant, Sf9

    Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, Chitinase-3-like protein 2.

    Product # :

    ENZ-932

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    Description

    CHI3L2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 372 amino acids (27-390a.a.) and having a molecular mass of 41.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CHI3L2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CHI3L2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chitinase 3-Like 2 (CHI3L2) is similar to bacterial chitinases but lacks chitinase activity. CHI3L2 protein is secreted and is involved in cartilage biogenesis. CHI3L2 is a lectin, which binds chitooligosaccharides and other glycans with high affinity, but not heparin.

    • Synonyms

      Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, Chitinase-3-like protein 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

      YKLVCYFTNW SQDRQEPGKF TPENIDPFLC SHLIYSFASI ENNKVIIKDK SEVMLYQTIN SLKTKNPKLK ILLSIGGYLF GSKGFHPMVD SSTSRLEFIN SIILFLRNHN FDGLDVSWIY PDQKENTHFT VLIHELAEAF QKDFTKSTKE RLLLTAGVSA GRQMIDNSYQ VEKLAKDLDF INLLSFDFHG SWEKPLITGH NSPLSKGWQD RGPSSYYNVE YAVGYWIHKG MPSEKVVMGI PTYGHSFTLA SAETTVGAPA SGPGAAGPIT ESSGFLAYYE ICQFLKGAKI TRLQDQQVPY AVKGNQWVGY DDVKSMETKV QFLKNLNLGG AMIWSIDMDD FTGKSCNQGP YPLVQAVKRS LGSLLEHHHH HH.

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    Chi3L2 Human Sf9
  • View Data Sheet

    Name :

    GAD1 Human

    Description:

    Glutamate Decarboxylase 1 Human Recombinant

    Glutamate Decarboxylase 1 (Brain, 67kDa), GAD, Glutamate Decarboxylase 67 KDa Isoform, 67 KDa Glutamic Acid Decarboxylase, GAD-67, EC 4.1.1.15, CPSQ1, SCP, Glutamate Decarboxylase 1 (Brain, 67kD), Glutamate Decarboxylase 1, GAD67, EC 4.1.1, GAD1.

    Product # :

    ENZ-789

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    Description

    GAD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (1-224) and having a molecular mass of 27.7kDa.GAD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GAD1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamate Decarboxylase 1 (GAD1) is one of several forms of glutamic acid decarboxylase. GAD1 is responsible for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. A pathogenic role for the GAD1 enzyme has been identified in the human pancreas since it has been detected as an autoantigen and an autoreactive T cell target type II diabetes. The GAD1 protein may also have a role in the stiff man syndrome. GAD1 enzyme deficiency leads to pyridoxine dependency with seizures. GAD1 also catalyzes the production of GABA.

    • Synonyms

      Glutamate Decarboxylase 1 (Brain, 67kDa), GAD, Glutamate Decarboxylase 67 KDa Isoform, 67 KDa Glutamic Acid Decarboxylase, GAD-67, EC 4.1.1.15, CPSQ1, SCP, Glutamate Decarboxylase 1 (Brain, 67kD), Glutamate Decarboxylase 1, GAD67, EC 4.1.1, GAD1.

    • 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 MGSMASSTPS SSATSSNAGA DPNTTNLRPT TYDTWCGVAH GCTRKLGLKI CGFLQRTNSL EEKSRLVSAF KERQSSKNLL SCENSDRDAR FRRTETDFSN LFARDLLPAK NGEEQTVQFL LEVVDILLNY VRKTFDRSTK VLDFHHPHQL LEGMEGFNLE LSDHPESLEQ ILVDCRDTLK YGVRTGHPRF FNQLSTGLDI IGLAGEWLTS TANTNMPSDM RECWLLR.

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    Gad1 Human
  • View Data Sheet

    Name :

    UBE2T Human

    Description:

    Ubiquitin-Conjugating Enzyme E2T Human Recombinant

    EC 6.3.2.19, HSPC150, PIG50, Ubiquitin-conjugating enzyme E2 T, Ubiquitin-protein ligase T, Ubiquitin carrier protein T, Cell proliferation-inducing gene 50 protein, UBE2T.

    Product # :

    ENZ-506

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    Description

    UBE2T Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids (1-197 a.a.) and having a molecular mass of 23.6 kDa. The UBE2T is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2T solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2T is part of the E2 ubiquitin-conjugating enzyme family that participates in the protein degradation pathway. UBE2T catalyzes the ATP-dependent attachment of ubiquitin to target proteins, thus tagging them for subsequent destruction by the proteasome. UBE2T is an important factor of the Faconi anemia pathway of DNA damage repair and, upon self-inactivation, may negatively regulate the Faconi pathway.

    • Synonyms

      EC 6.3.2.19, HSPC150, PIG50, Ubiquitin-conjugating enzyme E2 T, Ubiquitin-protein ligase T, Ubiquitin carrier protein T, Cell proliferation-inducing gene 50 protein, UBE2T.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MQRASRLKRE LHMLATEPPP GITCWQDKDQ MDDLRAQILG GANTPYEKGV FKLEVIIPER YPFEPPQIRF LTPIYHPNID SAGRICLDVL KLPPKGAWRP SLNIATVLTS IQLLMSEPNP DDPLMADISS EFKYNKPAFL KNARQWTEKH ARQKQKADEE EMLDNLPEAG DSRVHNSTQK RKASQLVGIE KKFHPDVLEH HHHHH.

    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.

    Ube2T Human
  • View Data Sheet

    Name :

    GSTM2 Human

    Description:

    Glutathione S-Transferase MU 2 Human Recombinant

    Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    Product # :

    ENZ-003

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    Description

    GSTM2 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 238 amino acids (1-218 a.a.) and having a molecular mass of 27.9kDa. The GSTM2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol,
    0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is < 25 units/mg, and is defined as the amount of enzyme that conjugate 1.0 µmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.

    More Info

    • Introduction

      Glutathione S-transferase Mu 2 (GSTM2) belongs to the glutathione s-transferase (GST) family of proteins. GSTM2 is a glutathione S-transferase that belongs to the mu class. There are 8 families of GST proteins, specifically: alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have various functions throughout the cell. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are structured in a gene cluster on chromosome 1p13.3 and are proven to be highly polymorphic. These genetic variants can change an individual''s susceptibility to carcinogens and toxins as well as have an effect on the toxicity and efficacy of several drugs.

    • Synonyms

      Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    • 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 MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK.

    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.

    Gstm2 Human
  • View Data Sheet

    Name :

    STK17A Human

    Description:

    Serine/Threonine Kinase 17A Human Recombinant

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

    Product # :

    PKA-314

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Stk17A Human
  • View Data Sheet

    Name :

    UGDH Mouse

    Description:

    UDP-Glucose Dehydrogenase Mouse Recombinant

    GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.

    Product # :

    ENZ-1070

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    Description

    UGDH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-493a.a.) and having a molecular mass of 57.2kDa. UGDH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UGDH protein solution (0.5mg/ml) containing 20mM MES buffer (pH5.0), 20% glycerol 150mM NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500 pmol/min/ug, and is defined as the amount of enzyme that converts 1.0 pmole of UDP-glucose to UDP-glucuronate per minute at pH 8.7 at 37°C.

    More Info

    • Introduction

      UGDH is part of the UDP-glucose/GDP-mannose dehydrogenase family and is a widely expressed enzyme localized in the liver. UGDH transfers UDP-glucose to UDP-glucuronate and thus takes part in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated products are ordinary molecules of the extracellular matrix and participate in signal transduction, cell migration, and cancer growth and metastasis.

    • Synonyms

      GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.

    • 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 MGSMVEIKKI CCIGAGYVGG PTCSVIAHMC PEIRVTVVDV NEARINAWNS PTLPIYEPGL KEVVESCRGK NLFFSTNIDD AIREADLVFI SVNTPTKTYG MGKGRAADLK YIEACARRIV QNSNGYKIVT EKSTVPVRAA ESIRRIFDAN TKPNLNLQVL SNPEFLAEGT AIKDLKNPDR VLIGGDETPE GQKAVRALCA VYEHWVPKEK ILTTNTWSSE LSKLAANAFL AQRISSINSI SALCEATGAD VEEVATAIGM DQRIGNKFLK ASVGFGGSCF QKDVLNLVYL CEALNLPEVA RYWQQVIDMN DYQRRRFASR IIDSLFNTVT DKKIAILGFA FKKDTGDTRE SSSIYISKYL MDEGAHLHIY DPKVPREQIV VDLSHPGVSA DDQVSRLVTI SKDPYEACDG AHALVICTEW DMFKELDYER IHKKMLKPAF IFDGRRVLDG LHSELQTIGF QIETIGKKVS SKRIPYTPGE IPKFSLQDPP NKKPKV.

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    Ugdh Mouse
  • View Data Sheet

    Name :

    Thrombin

    Description:

    Human Thrombin

    Product # :

    PRO-339

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    Description

    Thrombin was purified from human plasma.

    Source

    Human Plasma.

    Formulation

    Lyophilized protein containing mannitol, sodium chloride, calcium chloride.

    Biological Activity

    The specific activity was found to be 116 US Units/mg protein.

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    • Introduction

      Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.

    • Physical Appearance

      lyophilized powder.

    • Stability

      Lyophilized Human Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution human thrombin 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 human thrombin in sterile a 0.9% NaCl solution at 500U/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.

    Thrombin Human
  • View Data Sheet

    Name :

    HDDC3 Human

    Description:

    HD domain containing 3 Human Recombinant

    Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1, HD domain-containing protein 3, Metazoan SpoT homolog 1, MESH1, Penta-phosphate guanosine-3'-pyrophosphohydrolase, (ppGpp)ase, HDDC3.

    Product # :

    ENZ-184

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    Description

    HDDC3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (1-140) and having a molecular mass of 17.9kDa.HDDC3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HDDC3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Guanosine-3',5'-bis(diphosphate)-pyrophosphohydrolase MESH1 (HDDC3) contains an active site for ppGpp hydrolysis and a conserved His-Asp-box motif for Mn(2+) binding. In accordance with its structure, HDDC3 effectively catalyzes the hydrolysis of guanosine 3',5'-diphosphate (ppGpp) both in vitro and in vivo. In addition, HDDC3 suppresses SpoT-deficient lethality and RelA-induced delayed cell growth in bacteria.

    • Synonyms

      Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1, HD domain-containing protein 3, Metazoan SpoT homolog 1, MESH1, Penta-phosphate guanosine-3'-pyrophosphohydrolase, (ppGpp)ase, HDDC3.

    • 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 MGSEAAQLLE AADFAARKHR QQRRKDPEGT PYINHPIGVA RILTHEAGIT DIVVLQAALL HDTVEDTDTT LDEVELHFGA QVRRLVEEVT DDKTLPKLER KRLQVEQAPH SSPGAKLVKL ADKLYNLRDL NRCTPEVKIQ.

    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.

    Hddc3 Human
  • View Data Sheet

    Name :

    UBE2L3 Human

    Description:

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant

    Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    Product # :

    ENZ-342

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    Description

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids & having a molecular mass of 17.9 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 50mM HEPES (pH-7.5) 150mM NaCl, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Human Ubquitin-conjugating enzyme 7 (UbcH7) is a ubiquitin-conjugating enzyme (E2) mediating c-fos degradation, transcription factor NF-B maturation, and human papilloma virus-mediated p53 and Myc protein degradation, in vitro. The ubiquitin-conjugating enzymes (E2s) are essential components of the post-translational protein ubiquitination pathway, mediating the transfer of activated ubiquitin to substrate proteins. The human UBE2L1-UBE2L4 gene could potentially encode different isoforms of the UbcH7. UBE2L3 gene, located at chromosome 22q11.2, is the only identical family member with introns and encodes a polypeptide sequence identical to that of UbcH7.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    • 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

      MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK RPVD.

    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.

    Ube2L3 Human
  • View Data Sheet

    Name :

    PTRHD1 Human

    Description:

    Peptidyl-TRNA Hydrolase Domain Containing 1 Human Recombinant

    C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.

    Product # :

    ENZ-826

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    Description

    PTRHD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (1-140 a.a) and having a molecular mass of 18.2kDa.PTRHD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTRHD1 protein solution (1mg/ml) containing Phosphate buffer saline (pH 7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Putative peptidyl-tRNA hydrolase PTRHD1 (PTRHD1) is a 140 amino acid protein, which is encoded by a gene located on human chromosome 2p23.3. Chromosome 2 is the second largest human chromosome; it consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. Several genetic diseases are linked to genes on chromosome 2.

    • Synonyms

      C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.

    • 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 MGSMHRGVGP AFRVVRKMAA SGAEPQVLVQ YLVLRKDLSQ APFSWPAGAL VAQACHAATA ALHTHRDHPH TAAYLQELGR MRKVVLEAPD ETTLKELAET LQQKNIDHML WLEQPENIAT CIALRPYPKE EVGQYLKKFR LFK.

    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.

    Ptrhd1 Human
  • View Data Sheet

    Name :

    PI16 Human

    Description:

    Peptidase Inhibitor 16 Human Recombinant

    Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

    Product # :

    ENZ-113

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    Description

    The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.

    • Synonyms

      Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized PI16 Human recombinant 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 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

      LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.

    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.

    Pi16 Human
  • View Data Sheet

    Name :

    SSU72 Human

    Description:

    SSU72 RNA Polymerase II CTD Phosphatase Human Recombinant

    SSU72 RNA polymerase II CTD phosphatase homolog (S. cerevisiae), HSPC182, CTD phosphatase SSU72, Ssu72 RNA polymerase II CTD phosphatase homolog (yeast), PNAS-120, RNA polymerase II subunit A C-terminal domain phosphatase SSU72, EC 3.1.3.16.

    Product # :

    ENZ-243

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    Description

    SSU72 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (1-194) and having a molecular mass of 25.0kDa.SSU72 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SSU72 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SSU72 is an extremely conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. SSU72 interacts with TFIIB, Rb and DNAM-1 and operates to catalyze the dephosphorylation of target proteins, and taking part in RNA processing and termination via dephosphorylation of Pol II. SSU72 is found in multiple alternatively spliced isoforms.

    • Synonyms

      SSU72 RNA polymerase II CTD phosphatase homolog (S. cerevisiae), HSPC182, CTD phosphatase SSU72, Ssu72 RNA polymerase II CTD phosphatase homolog (yeast), PNAS-120, RNA polymerase II subunit A C-terminal domain phosphatase SSU72, EC 3.1.3.16.

    • 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 MGSMPSSPLR VAVVCSSNQN RSMEAHNILS KRGFSVRSFG TGTHVKLPGP APDKPNVYDF KTTYDQMYND LLRKDKELYT QNGILHMLDR NKRIKPRPER FQNCKDLFDL ILTCEERVYD QVVEDLNSRE QETCQPVHVV NVDIQDNHEE ATLGAFLICE LCQCIQHTED MENEIDELLQ EFEEKSGRTF LHTVCFY

    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.

    Ssu72 Human
  • View Data Sheet

    Name :

    PTRH2 Human

    Description:

    Peptidyl-tRNA Hydrolase 2 Human Recombinant

    Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.

    Product # :

    ENZ-045

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    • More Info

    Description

    PTRH2 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 137 amino acids (64-179 a.a.) and having a molecular mass of 14.9kDa. The PTRH2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTRH2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidyl-tRNA hydrolase 2 (PTRH2) is a mitochondrial protein. PTRH2 is released during apoptosis from the mitochondria to the cytoplasm. When in the cytoplasm, PTRH2 regulates the function of 2 transcriptional regulators, TLE5 and TLE1, thus promoting caspase-independent cell death. Natural substrates for PTRH2 may be petidyl-tRNAs which drop off the ribosome during protein synthesis.

    • Synonyms

      Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.

    • 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 MEYKMILVVR NDLKMGKGKV AAQCSHAAVS AYKQIQRRNP EMLKQWEYCG QPKVVVKAPD EETLIALLAH AKMLGLTVSL IQDAGRTQIA PGSQTVLGIG PGPADLIDKV TGHLKLY.

    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.

    Ptrh2 Human
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