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Search results

1000 results found for “Aldolase”

Name

Description

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  • View Data Sheet

    Name :

    MMP12 Human (1-33)

    Description:

    Matrix Metalloproteinase 12 (1-33 a.a.) Human Recombinant

    Product # :

    ENZ-1201

    Price :

    Quantity :

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    Description

    The MMP12 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The MMP12 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 33 amino acid residues of the MMP12 Human, 1-33 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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized MMP12 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.

    • Amino Acid Sequence

      MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFG.

    • Background

      Matrix Metalloproteinase 12 also known as MMP12 is 1 of the main enzymes in the MMP family which is primarily produced by macrophages and neutrophils. MMP12 is implicated in the breakdown of elastin and in the development of chronic inflammatory diseases, such as emphysema, COPD and atherosclerosis. MMP12 is upregulated and contributes to tissue remodeling in inflammatory responses which is essential for wound healing and immune defense. MMP12 catalyzes the cleavage of collagen, elastin and other ECM components. Its activity is regulated in normal tissues to avoid pathological degradation.

    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.

    Mmp12 Enzyme
  • View Data Sheet

    Name :

    IDE Human, Active

    Description:

    Insulin-Degrading Enzyme Human Recombinant

    Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1. 

    Product # :

    ENZ-1192

    Price :

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    Description

    IDE Human, Active Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (42-1019 a.a) containing a total of 984 amino acids, having a molecular mass of 114 kDa. IDE is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IDE solution (0.5mg/ml) contains 10% Glycerol, 100mM NaCl, 0.05% Brij35 and 20mM Tris-HCl buffer (pH 7.5).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is greater than 3,000 pmol/min/ug in which 1 unit will convert 1.0 pmole of Mca-RPPGFSAFK(Dnp)-OH to MCA-Pro-Leu-OH per minute at pH 7.5 at 25°C.

    Citations

    More Info

    • Synonyms

      Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.

    • Physical Appearance

      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

      MNNPAIKRIG NHITKSPEDK REYRGLELAN GIKVLLISDP TTDKSSAALD VHIGSLSDPP NIAGLSHFCE HMLFLGTKKY PKENEYSQFL SEHAGSSNAF TSGEHTNYYF DVSHEHLEGA LDRFAQFFLC PLFDESCKDR EVNAVDSEHE KNVMNDAWRL FQLEKATGNP KHPFSKFGTG NKYTLETRPN QEGIDVRQEL LKFHSAYYSS NLMAVCVLGR ESLDDLTNLV VKLFSEVENK NVPLPEFPEH PFQEEHLKQL YKIVPIKDIR NLYVTFPIPD LQKYYKSNPG HYLGHLIGHE GPGSLLSELK SKGWVNTLVG GQKEGARGFM FFIINVDLTE EGLLHVEDII LHMFQYIQKL RAEGPQEWVF QECKDLNAVA FRFKDKERPR GYTSKIAGIL HYYPLEEVLT AEYLLEEFRP DLIEMVLDKL RPENVRVAIV SKSFEGKTDR TEEWYGTQYK QEAIPDEVIK KWQNADLNGK FKLPTKNEFI PTNFEILPLE KEATPYPALI KDTAMSKLWF KQDDKFFLPK ACLNFEFFSP FAYVDPLHCN MAYLYLELLK DSLNEYAYAA ELAGLSYDLQ NTIYGMYLSV KGYNDKQPIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIPQLLS RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS
      QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGY IVFSGPRRAN GIQGLRFIIQ SEKPPHYLES RVEAFLITME KSIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI ISQQYNFDRD NTEVAYLKTL TKEDIIKFYK EMLAVDAPRR HKVSVHVLAR EMDSCPVVGE FPCQNDINLS QAPALPQPEV IQNMTEFKRG LPLFPLVKPH INFMAAKLHH HHHH.

    • Background

      Insulin-degrading enzyme (IDE) is a crucial protease that plays a significant role in maintaining glucose homeostasis by degrading insulin and other bioactive peptides. Dysregulation of IDE has been implicated in various metabolic disorders, particularly type 2 diabetes mellitus. IDE is also associated with the clearance of amyloid-beta peptides in the brain, making it relevant to Alzheimer's disease pathology. Studying the recombinant form of IDE is fundamental to understanding its functional mechanisms and exploring potential avenues for therapeutic interventions.

      The primary goal of this research is to express and purify recombinant IDE using diverse expression systems. Recombinant DNA techniques will be employed to construct expression vectors containing the IDE gene, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant IDE will be purified using affinity chromatography or other appropriate methods, facilitating subsequent biochemical and biophysical characterization.

      The second objective is to investigate the substrate specificity and catalytic activity of the purified IDE. In vitro enzymatic assays will be conducted to analyse the ability of the recombinant IDE to degrade insulin and other potential substrates. The effects of various factors, such as pH, temperature, and potential modulators, on IDE activity will be evaluated. Additionally, the interactions between IDE and its substrates will be explored using binding assays.

      The third objective is to elucidate the three-dimensional structure of the IDE recombinant using techniques like X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Structural insights into the active site and binding pockets of IDE will provide valuable information for understanding its substrate recognition and catalytic mechanisms. This knowledge could be instrumental in designing targeted therapeutic compounds.

      By characterizing the IDE recombinant, this research aims to contribute to our understanding of its role in insulin metabolism, glucose regulation, and potential therapeutic applications. The findings from this study may have implications for the development of novel treatments for diabetes and other related disorders.

    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.

    Ide Human Active
  • View Data Sheet

    Name :

    ELANE Mouse

    Description:

    Elastase-2 Mouse Recombinant

    Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.

    Product # :

    ENZ-1105

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    Description

    ELANE Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (27-265a.a.) fused to a 6 aa His Tag at C-terminus containing 245 amino acids and having a molecular mass of 26.8kDa.ELANE shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ELANE protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 30% Glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Elastase-2 (ELANE) is a serine protease that belongs to the chymotrypsin family. ELANE breaks down elastin, an elastic fiber together with collagen and controls the mechanical properties of connective tissue. The neutrophil form breaks down the Outer membrane protein A (OmpA) of E. coli and other Gram-negative bacteria. ELANEis inhibited by the acute-phase protein alpha 1-antitrypsin (A1AT), which binds almost irreversibly to the active site of elastase and trypsin.A1AT is usually secreted by the liver cells into the serum. A1AD leads to uninhibited destruction of elastic fiber by elastase.

    • Synonyms

      Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.

    • 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

      SEIVGGRPAR PHAWPFMASL QRRGGHFCGA TLIARNFVMS AAHCVNGLNF RSVQVVLGAH
      DLRRQERTRQ TFSVQRIFEN GFDPSQLLND IVIIQLNGSA TINANVQVAQ LPAQGQGVGD
      RTPCLAMGWG RLGTNRPSPS VLQELNVTVV TNMCRRRVNV CTLVPRRQAG ICFGDSGGPL
      VCNNLVQGID SFIRGGCGSG LYPDAFAPVA EFADWINSII RSHNDHLLTH PKDREGRTNH 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.

    Elastase 2 Mouse
  • View Data Sheet

    Name :

    IL12 Human

    Description:

    Interleukin-12 Human Recombinant

    NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    Product # :

    CYT-101

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
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    Description

    Interleukin-12 Human Recombinant produced in HEK cells is a glycosylated heterodimer, having a total molecular weight of 57kDa.The IL12 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    IL12 was lyophilized from a 0.2µm filtered solution containing 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent release of IFN-gamma from the human NK92 cell line in presence of 20ng/mL rIL-2.
    The EC50 is 0.5ng/ml.

    Citations

    More Info

    • Introduction

      IL-12 is a heterodimeric cytokine that stimulates the production of IFNgamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. IL-12 is an initiator of cell-mediated immunity.

    • Synonyms

      NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL12 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 IL12 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    • Amino Acid Sequence

      IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond between cysteines in red in sequences below.
      >IL-12 A
      RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLP
      LELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQ
      IFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS.
      >IL-12B
      IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAG
      QYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTD
      LTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAV
      HKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGK
      SKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS.

    • Background

      What is the molecular weight/Mw of IL12 HUMAN Protein?
      IL12 HUMAN Protein has a total Mw of 57kDa.

      What is the source or expression system of IL12 HUMAN Protein?
      HEK.

      What is the Purity of IL12 HUMAN Protein?
      IL12 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12 HUMAN Protein?
      The specific activity was determined by the dose-dependent release of IFN-gamma from the human NK92 cell line in presence of 20ng/mL rIL-2.
      The EC50 is 0.5ng/ml.
      What is the amino acid sequence of IL12 HUMAN Protein?
      IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond between cysteines in red in sequences below.
      >IL-12 A
      RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLP
      LELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQ
      IFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS.
      >IL-12B
      IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAG
      QYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTD
      LTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAV
      HKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGK
      SKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS.

      What applications can IL12 HUMAN Protein be used in?
      IL12 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12 HUMAN Protein?
      The endotoxin level is minimal, IL12 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12 HUMAN 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 IL12 HUMAN?
      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.

    Il 12 Human Hek
  • View Data Sheet

    Name :

    IDH1

    Description:

    Isocitrate Dehydrogenase-1 Yeast Recombinant

    Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

    Product # :

    ENZ-289

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    Description

    Recombinant Saccharomyces Cerevisiae ICDH (NADP) derived from yeast host cells by using over-expression system, is full length same as designated ICD1 from Saccharomyces Cerevisiae. The N-terminal amino acid Phenylalanine residue next to Met is substituted with Alanine for overexpression. The ICDH is purified by proprietary chromatographic techniques.

    Source

    Yeast cells.

    Formulation

    One ml of solution contains 0.075 mol/l KPO4, 50% Glycerol, pH 7.1.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 115 U/mg.

    Citations

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    • Introduction

      Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.

    • Synonyms

      Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

    • 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.

    • Unit Definition

      One unit is defined as 1 µmol of NAD+ production per minute under the assay conditions (25°C, pH 7.5).

    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.

    Isocitrate Dehydrogenase
  • View Data Sheet

    Name :

    PRDX1 Antibody

    Description:

    Peroxiredoxin-1, Mouse Anti Human

    Peroxiredoxin-1, EC 1.11.1.15, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Proliferation-associated gene protein, Natural killer cell-enhancing factor A, NKEF-A, PRDX1, TDPX2, PRDX-1, PAG, PAGA, PRX1, PAGB, PRXI, MSP23, NKEFA.

    Product # :

    ANT-394

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    Citations

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    • Introduction

      PRDX1 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX1 is an important protector of red blood cells against reactive oxygen species and in tumor prevention. PRDX1 is antioxidant protective in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX1 has a proliferative effect and is involved in cancer development or progression. Peroxiredoxin-1 is plays a role in redox regulation of the cell. Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. Peroxiredoxin is involved in eliminating peroxides generated during metabolism. Peroxiredoxin participates in the signaling cascades of growth factors and TNF-alpha by regulating the intracellular concentrations of h(2)o(2).

    • Synonyms

      Peroxiredoxin-1, EC 1.11.1.15, Thioredoxin peroxidase 2, Thioredoxin-dependent peroxide reductase 2, Proliferation-associated gene protein, Natural killer cell-enhancing factor A, NKEF-A, PRDX1, TDPX2, PRDX-1, PAG, PAGA, PRX1, PAGB, PRXI, MSP23, NKEFA.

    • Immunogen

      Anti-human PRDX1 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PRDX1 amino acids 1-199 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT1D8AT.

    • Applications

      PRDX1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1000 ~ 2000. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      PRDX1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Prdx1 Antibody
  • View Data Sheet

    Name :

    Adiponectin Mouse, HEK

    Description:

    Adiponectin Mouse Recombinant, HEK

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-435

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    Description

    The Acrp30 Mouse Recombinant is fused with FLAG tag having a total Mw of 26kDa.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M PBS buffer,0.075M NaCl, pH7.4.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml.  An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.

    Citations

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    • Introduction

      Adiponectin is an important negative regulator in hematopoiesis and immune systems. It may be involved in ending inflammatory responses through its inhibitory functions. Inhibits endothelial nf-kappa-b signaling through a camp-dependent pathway. Inhibits tnf-alpha- induced expression of endothelial adhesion molecules. Involved in the control of fat metabolism and insulin sensitivity.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Stability

      Store lyophilized APM-1 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 reconstitute the lyophilized Acrp30 Mouse in sterile 18M-cm H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293.

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of ADIPONECTIN Protein?
      Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml. An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.

      What is the amino acid sequence of ADIPONECTIN Protein?
      EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.

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

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

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

    Adiponectin Mouse Hek
  • View Data Sheet

    Name :

    Adiponectin Porcine, HEK

    Description:

    Adiponectin Porcine Recombinant, HEK derived

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-696

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    Description

    The Acrp30 Porcine Recombinant contains a total of 238 amino acids having a molecular Mass of 26kDa. The Porcine Adiponectin is fused to a 13 amino acid long N-terminal FLAG tag.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    Sterile filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 90% as determined by SDS PAGE.

    Citations

    More Info

    • Introduction

      Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Stability

      For long term, store lyophilized AdipoQ 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.The lyophilized protein remains stable for 24 months when stored at -20°C.

    • Solubility

      Add deionized water and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.

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

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

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

    Adiponectin Porcine Hek
  • View Data Sheet

    Name :

    ADA Human

    Description:

    Adenosine Deaminase Human Recombinant

    Adenosine deaminase, Adenosine aminohydrolase, ADA1, EC 3.5.4.4.

    Product # :

    ENZ-147

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    Description

    ADA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 383 amino acids (1-363) and having a molecular mass of 42.9 kDa.The ADA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ADA protein 0.5mg/ml is supplied in 20mM Tris-HCL, pH-8, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately >25 units/mg. Enzymatic activity was confirmed by measuring the amount of enzyme that deaminates 1.0 umol of adenosine to inosine per minute at pH 7.5 at 25C.

    Citations

    More Info

    • Introduction

      ADA catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. ADA has a vital part in purine metabolism and in adenosine homeostasis. ADA performs as a positive regulator of T-cell coactivation, by binding DPP4 which regulates lymphocyte-epithelial cell adhesion.

    • Synonyms

      Adenosine deaminase, Adenosine aminohydrolase, ADA1, EC 3.5.4.4.

    • Physical Appearance

      ADA is supplied as a 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 MAQTPAFDKP KVELHVHLDG SIKPETILYY GRRRGIALPA NTAEGLLNVI GMDKPLTLPD FLAKFDYYMP AIAGCREAIK RIAYEFVEMK AKEGVVYVEV RYSPHLLANS KVEPIPWNQA EGDLTPDEVV ALVGQGLQEG ERDFGVKARS ILCCMRHQPN WSPKVVELCK KYQQQTVVAI DLAGDETIPG SSLLPGHVQA YQEAVKSGIH RTVHAGEVGS AEVVKEAVDI LKTERLGHGY HTLEDQALYN RLRQENMHFE ICPWSSYLTG AWKPDTEHAV IRLKNDQANY SLNTDDPLIF KSTLDTDYQM TKRDMGFTEE EFKRLNINAA KSSFLPEDEK RELLDLLYKA YGMPPSASAG QNL

    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.

    Ada Human
  • View Data Sheet

    Name :

    ST6GALNAC5 Human

    Description:

    ST6GALNAC5 Human Recombinant

    Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5, GD1 alpha synthase, GalNAc alpha-2,6-sialyltransferase V, ST6GalNAc V, ST6GalNAcV, Sialyltransferase 7E, SIAT7-E, SIAT7E

    Product # :

    ENZ-1153

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    Description

    ST6GALNAC5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 316 amino acids (30-336a.a.) and having a molecular mass of 36.4kDa.ST6GALNAC5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ST6GALNAC5 protein solution (0.25mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 or ST6GALNAC5, is part of the glycosyltransferase 29 group of proteins. ST6GALNAC5 is a sialyltransferase that takes part in the synthesis of ganglioside GD1a. This protein is part of the protein glycosylation transduction, meaning, modification of proteins. ST6GALNAC5 is expressed strictly in the brain tissue, and is a crucial component in breast cancer cells metastasis to the brain tissue. It is thought to enable cancer cells to go through the blood-brain barrier.

    • Synonyms

      Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5, GD1 alpha synthase, GalNAc alpha-2,6-sialyltransferase V, ST6GalNAc V, ST6GalNAcV, Sialyltransferase 7E, SIAT7-E, SIAT7E

    • 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

      ADLGGQKERP PQQQQQQQQQ QQQASATGSS QPAAESSTQQ RPGVPAGPRP LDGYLGVADH KPLKMHCRDC ALVTSSGHLL HSRQGSQIDQ TECVIRMNDA PTRGYGRDVG NRTSLRVIAH SSIQRILRNR HDLLNVSQGT VFIFWGPSSY MRRDGKGQVY NNLHLLSQVL PRLKAFMITR HKMLQFDELF KQETGKDRKI SNTWLSTGWF TMTIALELCD RINVYGMVPP DFCRDPNHPS VPYHYYEPFG PDECTMYLSH ERGRKGSHHR FITEKRVFKN WARTFNIHFF QPDWKPESLA INHPENKPVF HHHHHH

    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.

    St6Galnac5 Human
  • View Data Sheet

    Name :

    TPO Human

    Description:

    Thyroid Peroxidase Human Recombinant

    Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    Product # :

    ENZ-285

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    Description

    Thyroid Peroxidase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing 834 amino acids and having a molecular mass of 92,872 Dalton (excluding glycosylation), 101 kDa total mass.The TPO is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TPO is supplied in 16mM HEPES pH-7.6, 160mM NaCl, 0.08mM Kl and 20% glycerol.

    Purity

    Greater than 95% as determined by Densitometric Analysis

    Citations

    More Info

    • Introduction

      Thyroid Peroxidase (TPO) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. Its identity with the formerly so-called `microsomal antigen` has been shown several years ago. As an integral membrane glycoprotein it is restricted to the apical plasma membrane of the follicular epithelial cells and comprises two identical subunits of approx. 100 kDa molecular weight. The hemoprotein TPO plays a key role in the thyroid hormone biosynthesis by catalysing both the iodination of tyrosyl residues and the coupling of iodotyrosyl residues in thyroglobulin (TG) to form precursors of the thyroid hormones T4 and T3.

    • Synonyms

      Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    • Stability

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

    • coating concentration

      0.15-0.375 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.

    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.

    Thyroid Peroxidase Human
  • View Data Sheet

    Name :

    LGMN Human

    Description:

    Legumain Human Recombinant

    Legumain, PRSC1, Protease, Cysteine, 1 (Legumain), Asparaginyl Endopeptidase, Protease, Cysteine 1, EC 3.4.22.34, Cysteine Protease 1, LGMN1, AEP.

    Product # :

    ENZ-923

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    Description

    LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (18-433 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 422 amino acids and having a molecular mass of 48.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).LGMN is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LGMN protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    lgmn human sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Legumain, also known as LGMN, is a cysteine endopeptidase which demonstrates strict specificity for hydrolysis of asparaginyl bonds. Furthermore, LGMN can also cleave aspartyl bonds slowly, in particular under acidic conditions. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.

    • Synonyms

      Legumain, PRSC1, Protease, Cysteine, 1 (Legumain), Asparaginyl Endopeptidase, Protease, Cysteine 1, EC 3.4.22.34, Cysteine Protease 1, LGMN1, AEP.

    • 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

      VPIDDPEDGG KHWVVIVAGS NGWYNYRHQA DACHAYQIIH RNGIPDEQIV VMMYDDIAYS EDNPTPGIVI NRPNGTDVYQ GVPKDYTGED VTPQNFLAVL RGDAEAVKGI GSGKVLKSGP QDHVFIYFTD HGSTGILVFP NEDLHVKDLN ETIHYMYKHK MYRKMVFYIE ACESGSMMNH LPDNINVYAT TAANPRESSY ACYYDEKRST YLGDWYSVNW MEDSDVEDLT KETLHKQYHL VKSHTNTSHV MQYGNKTIST MKVMQFQGMK RKASSPVPLP PVTHLDLTPS PDVPLTIMKR KLMNTNDLEE SRQLTEEIQR HLDARHLIEK SVRKIVSLLA ASEAEVEQLL SERAPLTGHS CYPEALLHFR THCFNWHSPT YEYALRHLYV LVNLCEKPYP LHRIKLSMDH VCLGHYHHHH HH.

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

    Lgmn Human
  • View Data Sheet

    Name :

    GOT1 Human, Active

    Description:

    Glutamic-Oxaloacetic Transaminase 1 Human Recombinant, Active

    EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    Product # :

    ENZ-1001

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    Description

    GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GOT1 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8.0, 2mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 50 units/mg, and is defined as the amount of enzyme that converts 1umole of a-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C.

    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

      EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    • 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 MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ.

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    Got1 Human Active
  • View Data Sheet

    Name :

    GroES Human, His

    Description:

    GroES (HSP10) Human Recombinant, His Tag

    CPN10, GROES, HSP10, HSPE1, Chaperonin-10, 10 kDa heat shock protein mitochondrial, 10 kDa chaperonin, Early-pregnancy factor, EPF.

    Product # :

    HSP-040

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    Description

    GroES His Protein is 12.0 kDa protein containing 111 amino acid residues of the GroES Human and the 10 aa N-Terminal His-tag.

    Source

    E. coli

    Formulation

    GroES His Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 0.05M phosphate buffer, 0.075 M NaCl, pH 7.4.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HSP10 is part of the molecular chaperons, that are crucial for thir efficient folding of proteins in normal as well as stress conditions. GroES function is to bind to HSP60 in the presence of ATP, thus causing a change in the HSP60 conformation & enclosing the protein substrate within the complex. ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein. GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques.

    • Synonyms

      CPN10, GROES, HSP10, HSPE1, Chaperonin-10, 10 kDa heat shock protein mitochondrial, 10 kDa chaperonin, Early-pregnancy factor, EPF.

    • Stability

      Store lyophilized GroES His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted GroES His 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.

    • Amino Acid Sequence

      MKHHHHHHAS AGQAFRKFLP LFDRVLVERS AAETVTKGGI MLPEKSQGKV LQATVVAVGS GSKGKGGEIQ PVSVKVGDKV LLPEYGGTKV VLDDKDYFLF RDGDILGKYV D.

    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.

    Groes His Human
  • View Data Sheet

    Name :

    HAUS1 Human

    Description:

    HAUS Augmin-Like Complex, Subunit 1 Human Recombinant

    HAUS augmin-like complex subunit 1, Coiled-coil domain-containing protein 5, Enhancer of invasion-cluster, HEI-C, HAUS1, CCDC5, HEIC, HsT1461.

    Product # :

    PRO-1077

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    Description

    HAUS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278 a.a) and having a molecular mass of 34.4kDa.HAUS1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HAUS1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HAUS augmin-like complex subunit 1 (HAUS1) is 1 of 8 subunits of the 390kDa human augmin complex/ HAUS complex. The augmin complex is a microtubule-binding complex required in microtubule generation within the mitotic spindle and is imperative to mitotic spindle compilation. HAUS1 contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. HAUS1 is broadly expressed, especially in the pancreas, kidney, skeletal muscle, liver and heart. However it is weakly expressed in the lung, brain and placenta. HAUS1-depleted cells hold functional cell cycle checkpoints, but the depletion reduces the G2/M cell cycle compartment and stimulates apoptosis. The HAUS1 protein level remains constant through the cell cycle.

    • Synonyms

      HAUS augmin-like complex subunit 1, Coiled-coil domain-containing protein 5, Enhancer of invasion-cluster, HEI-C, HAUS1, CCDC5, HEIC, HsT1461.

    • 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 MGSHMEPQEE RETQVAAWLK KIFGDHPIPQ YEVNPRTTEI LHHLSERNRV RDRDVYLVIE DLKQKASEYE SEAKYLQDLL MESVNFSPAN LSSTGSRYLN ALVDSAVALE TKDTSLASFI PAVNDLTSDL FRTKSKSEEI KIELEKLEKN LTATLVLEKC
      LQEDVKKAEL HLSTERAKVD NRRQNMDFLK AKSEEFRFGI KAAEEQLSAR GMDASLSHQS LVALSEKLAR LKQQTIPLKK KLESYLDLMP NPSLAQVKIE EAKRELDSIE AELTRRVDMM EL.

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    Haus1 Human
  • View Data Sheet

    Name :

    ACKA E.Coli

    Description:

    Acetate Kinase E.Coli Recombinant

    Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.

    Product # :

    PKA-063

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    Description

    Recombinant ACKA produced in E.coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400) and having a molecular mass of 45.7 kDa.The ACKA is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      E.Coli Acetate Kinase, also knowns as ACKA, catalyzes the formation of acetyl phosphate from acetate and ATP and also catalyzes the reverse reaction. ACKA takes part in synthesis of various ATP formed catabolically during anaerobic growth of the organism.

    • Synonyms

      Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.

    • 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 MGSMSSKLVL VLNCGSSSLK FAIIDAVNGE EYLSGLAECF HLPEARIKWK MDGNKQEAAL GAGAAHSEAL NFIVNTILAQ KPELSAQLTA IGHRIVHGGE KYTSSVVIDE SVIQGIKDAA SFAPLHNPAH LIGIEEALKS FPQLKDKNVA VFDTAFHQTM PEESYLYALP YNLYKEHGIR RYGAHGTSHF YVTQEAAKML NKPVEELNII TCHLGNGGSV SAIRNGKCVD TSMGLTPLEG LVMGTRSGDI DPAIIFHLHD TLGMSVDAIN KLLTKESGLL GLTEVTSDCR YVEDNYATKE DAKRAMDVYC HRLAKYIGAY TALMDGRLDA VVFTGGIGEN AAMVRELSLG KLGVLGFEVD HERNLAARFG KSGFINKEGT RPAVVIPTNE ELVIAQDASR LTA.

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    Acka Ecoli
  • View Data Sheet

    Name :

    HPRT1 Human

    Description:

    Hypoxanthine-Guanine Phosphoribosyltransferase Human Recombinant

    Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.

    Product # :

    ENZ-524

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    Description

    HPRT1 Recombinant Human 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 26.7 kDa. The HPRT1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HPRT1 Human solution containing 20mM Tris HCl pH-8, & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.

    • Synonyms

      Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.

    • 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 MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV RQYNPKMVKV ASLLVKRTPR SVGYKPDFVG FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA.

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    Hprt1 Human
  • View Data Sheet

    Name :

    DTD2 Human

    Description:

    D-Tyrosyl-tRNA Deacylase 2 Human Recombinant

    D-Tyrosyl-TRNA Deacylase 2 (Putative), Chromosome 14 Open Reading Frame 126, Probable D-Tyrosyl-TRNA(Tyr) Deacylase 2, EC 3.1.-.-,C14orf126

    Product # :

    ENZ-763

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    Description

    DTD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (1-168) and having a molecular mass of 21.0 kDa. DTD2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The DTD2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DTD2 is e member of the DTD family. DTD2 protein hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr) as a defense mechanism against a harmful effect of D-tyrosine.

    • Synonyms

      D-Tyrosyl-TRNA Deacylase 2 (Putative), Chromosome 14 Open Reading Frame 126, Probable D-Tyrosyl-TRNA(Tyr) Deacylase 2, EC 3.1.-.-,C14orf126

    • 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 MGSMAEGSRI PQARALLQQC LHARLQIRPA DGDVAAQWVE VQRGLVIYVC FFKGADKELL PKMVNTLLNV KLSETENGKH VSILDLPGNI LIIPQATLGG RLKGRNMQYH SNSGKEEGFE LYSQFVTLCE KEVAANSKCA EARVVVEHGT YGNRQVLKLD TNGPFTHLIE F

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    Dtd2 Human
  • View Data Sheet

    Name :

    DUSP18 Human

    Description:

    Dual Specificity Phosphatase 18 Human Recombinant

    Dual specificity protein phosphatase 18, Low molecular weight dual specificity phosphatase 20, LMW-DSP20, DUSP18, LMWDSP20, VHP, DUSP26.

    Product # :

    ENZ-582

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    Description

    DUSP18 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-188) and having a molecular mass of 23.6kDa.DUSP18 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DUSP18 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol, 0.1mM PMSF and 1mM EDTA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Dual specificity phosphatase 18 (DUSP18) belongs to the dual-specificity phosphatase (DSP) family, which catalyzes dephosphorylation of phosphotyrosine and phosphothreonine residues. DUSP18 has a preferential enzymatic activity for phosphorylated tyrosine residues over threonine residues, in addition DUSP18 dephosphorylates p-nitrophenyl phosphate (pNPP) in vitro. Furthermore, DUSP18 is inhibited by iodoarectic acid and is activated by manganese ions. DUSP18 is extensively expressed with the highest levels in the liver, brain, ovary and testis.

    • Synonyms

      Dual specificity protein phosphatase 18, Low molecular weight dual specificity phosphatase 20, LMW-DSP20, DUSP18, LMWDSP20, VHP, DUSP26.

    • 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 MGSHMTAPSC AFPVQFRQPS VSGLSQITKS LYISNGVAAN NKLMLSSNQI TMVINVSVEV VNTLYEDIQY MQVPVADSPN SRLCDFFDPI ADHIHSVEMK QGRTLLHCAA GVSRSAALCL AYLMKYHAMS LLDAHTWTKS CRPIIRPNSG FWEQLIHYEF
      QLFGKNTVHM VSSPVGMIPD IYEKEVRLMI PL.

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    Dusp18 Human
  • View Data Sheet

    Name :

    SNCA Delta-NAC Human

    Description:

    Alpha Synuclein Delta-NAC Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-161

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    Description

    A-Synuclein Delta-NAC Human Recombinant which is a deletion mutant of the a-synuclein that lacks the NAC region (amino acid 61-95), produced in E.Coli is a single, non-glycosylated polypeptide chain of 111 amino acids having a molecular mass of 11.9kDa (molecular size on SDS-PAGE will appear higher), with 6 amino acids added as a linker. The Recombinant Human a-Synuclein Delta-NAC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA Delta-NAC protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK GTEIWMKKDQ LGKNEEGAPQ EGILEDMPVD PDNEAYEMPS EEGYQDYEPE A.

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    Snca Delta Nac Human
  • View Data Sheet

    Name :

    SRM Human

    Description:

    Spermidine Synthase Human Recombinant

    Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.

    Product # :

    ENZ-027

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    Description

    SRM 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 322 amino acids (1-302 a.a.) and having a molecular mass of 36kDa. The SRM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SRM solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SRM is an enzyme which catalyzes the transfer of the propylamine group from S-adenosylmethioninamine to putrescine in the biosynthesis of spermidine. The polyamines putrescine, spermine and spermidine are ubiquitous polycationic mediators of cell growth and differentiation. The SRM protein is one of four enzymes in the polyamine-biosynthetic pathway and completes the final step of spermidine biosynthesis.

    • Synonyms

      Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.

    • 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 MEPGPDGPAA SGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV VQCEIDEDVI QVSKKFLPGM AIGYSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP AESLFKESYY QLMKTALKED GVLCCQGECQ WLHLDLIKEM RQFCQSLFPV VAYAYCTIPT YPSGQIGFML CSKNPSTNFQ EPVQPLTQQQ VAQMQLKYYN SDVHRAAFVL PEFARKALND VS.

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    Srm Human
  • View Data Sheet

    Name :

    CA1 Human

    Description:

    Carbonic Anhydrase-1 Human Recombinant

    CA-1, CA1, CAI, CA-I, Carbonate dehydratase I, Carbonic anhydrase I, Carbonic anhydrase 1, Car1.

    Product # :

    ENZ-462

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    Description

    Recombinant Human Carbonic anhydrase 1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261 a.a) and having a molecular mass of 31 kDa. Carbonic anhydrase 1 is fused to a 20 amino acids His-Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Carbonic anhydrase 1 is a zinc metalloenzyme that catalyses reversible hydration of CO2 (CO2 + H2O ? HCO3- + H+). Carbonic anhydrase 1 is essential to many biological processes such as cellular respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, salvia, and gastric acid. Carbonic anhydrase 1 is abundant in erythrocytes and an early marker for erythroid differentiation.

    • Synonyms

      CA-1, CA1, CAI, CA-I, Carbonate dehydratase I, Carbonic anhydrase I, Carbonic anhydrase 1, Car1.

    • 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 MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F.

    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.

    Carbonic Anhydrase 1 Human
  • View Data Sheet

    Name :

    CAPSL Human

    Description:

    Calcyphosine-Like Human Recombinant

    Calcyphosine-like protein, CAPSL, MGC26610.

    Product # :

    PRO-185

    Price :

    Quantity :

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    Shipped with Ice Packs

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    More Info

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

    Description

    CAPSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-208) and having a molecular mass of 26.3 kDa.The CAPSL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CAPSL protein at 1mg/ml in 20mM Tris-HCL, pH-8, 0.2M NaCl, 5mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CAPSL is a calcium-binding protein holding two conserved calcium-binding motifs (EF-hands) which are found in a superfamily of calcium sensors and calcium signal modulators. In addition, the CAPSL gene is in the same linkage disequilibrium (LD) block as the IL7R gene and there is well known association between the CAPSL-IL7R locus and type 1 diabetes.

    • Synonyms

      Calcyphosine-like protein, CAPSL, MGC26610.

    • Physical Appearance

      CAPSL is supplied as a 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 MAGTARHDRE MAIQAKKKLT TATDPIERLR LQCLARGSAG IKGLGRVFRI MDDDNNRTLD FKEFMKGLND YAVVMEKEEV EELFQRFDKD GNGTIDFNEF LLTLRPPMSR ARKEVIMQAF RKLDKTGDGV ITIEDLREVY NAKHHPKYQN GEWSEEQVFR KFLDNFDSPY DKDGLVTPEE FMNYYAGVSA SIDTDVYFII MMRTAWKL

    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.

    Capsl Human
  • View Data Sheet

    Name :

    PGPEP1 Human

    Description:

    Pyroglutamyl-Peptidase I Human Recombinant

    Pyroglutamyl-peptidase 1, EC 3.4.19.3, 5-oxoprolyl-peptidase, Pyroglutamyl aminopeptidase I, PAP-I, Pyroglutamyl-peptidase I, PGP-I, Pyrrolidone-carboxylate peptidase, PGPEP1, PGPI, PGP, Pcp.

    Product # :

    ENZ-672

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
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    • More Info
    • Citations

    Description

    PGPEP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-209) and having a molecular mass of 25.5kDa.PGPEP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PGPEP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Pyroglutamyl-Peptidase I (PGPEP1) is an omega peptidase which detaches pyroglutamyl residues from the amino termini of peptides and proteins. PGPEP1 is a cytosolic cysteine peptidase which is expressed in most cell types. PGPEP1 enzyme has need of s a thiol-reducing agent for activity. PGPEP1 is possibly involved in the inactivation of biologically active peptides which have an amino terminal pyroglutamyl group, for instance peptides as neurotensin, luteinizing hormone releasing hormone, and thyrotropinreleasing hormone.

    • Synonyms

      Pyroglutamyl-peptidase 1, EC 3.4.19.3, 5-oxoprolyl-peptidase, Pyroglutamyl aminopeptidase I, PAP-I, Pyroglutamyl-peptidase I, PGP-I, Pyrrolidone-carboxylate peptidase, PGPEP1, PGPI, PGP, Pcp.

    • 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 MGSMEQPRKA VVVTGFGPFG EHTVNASWIA VQELEKLGLG DSVDLHVYEI PVEYQTVQRL IPALWEKHSP QLVVHVGVSG MATTVTLEKC GHNKGYKGLD NCRFCPGSQC CVEDGPESID SIIDMDAVCK RVTTLGLDVS VTISQDAGRY LCDFTYYTSL YQSHGRSAFV HVPPLGKPYN ADQLGRALRA IIEEMLDLLE QSEGKINYCH KH.

    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.

    Pgpep1 Human
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