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Search results

1000 results found for “Enolase”

Name

Description

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  • View Data Sheet

    Name :

    MMP14 Human

    Description:

    Matrix Metalloproteinase-14 Recombinant Human

    Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 1.

    Product # :

    ENZ-1101

    Price :

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    Description

    Matrix Metalloproteinase-14 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 264 amino acids and having a molecular mass of 29.6kDa. MMP14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MMP14 is supplied as a 0.2 μm filtered solution conteining 20mM Tris-HCl, pH 7.4, 30 % glycerol, 300mM NaCl, 3mM CaCl2 and 10μM ZnCl2.

    Purity

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

    More Info

    • Introduction

      Matrix metalloproteinase-14 (MMP14), is a membrane-anchored zinc-binding endopeptidase which is expressed at the leading edge of different invasive carcinomas and also promotes tumor cell invasion through degradation of the extracellular matrix. MMP14 takes a vital part in extracellular matrix, ECM, remodeling by having the capability to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules for instance CD44 and integrin alpha V. MMP14 is a key enzyme in many physiological as well as pathological processes for example angiogenesis & tumor invasion.

    • Synonyms

      Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYG.

    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.

    Mmp14 Protein
  • View Data Sheet

    Name :

    PRDX2 Mouse

    Description:

    Eukaryotic Translation Initiation Factor 4E Mouse Recombinant

    PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.  

    Product # :

    ENZ-1061

    Price :

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    • More Info

    Description

    PRDX2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-198 a.a) and having a molecular mass of 24.3kDa. PRDX2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRDX2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% Glycerol 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 700 pmol/min/ug, Activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for minute. 

    More Info

    • Introduction

      PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
      If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer.

    • Synonyms

      PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.

    • 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 MGSHMASGNA QIGKSAPDFT ATAVVDGAFK EIKLSDYRGK YVVLFFYPLD FTFVCPTEII AFSDHAEDFR KLGCEVLGVS VDSQFTHLAW INTPRKEGGL GPLNIPLLAD VTKSLSQNYG VLKNDEGIAY RGLFIIDAKG VLRQITVNDL PVGRSVDEAL RLVQAFQYTD EHGEVCPAGW KPGSDTIKPN VDDSKEYFSK HN

    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.

    PRDX2 Mouse
  • View Data Sheet

    Name :

    COQ9 Human

    Description:

    Coenzyme Q9 Human Recombinant

    Ubiquinone biosynthesis protein COQ9, mitochondrial, C16orf49, COQ10D5, C16orf49, HSPC326, PSEC0129.

    Product # :

    ENZ-898

    Price :

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    • description
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    • More Info

    Description

    COQ9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (45-318 a.a) and having a molecular mass of 33.3kDa.COQ9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COQ9 protein solution (1mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquinone biosynthesis protein COQ9 (COQ9) represents a mitochondrial ubiquinone biosynthesis gene. The COQ9 protein is likely required for biosynthesis of coenzyme Q10, since mutations at this locus have been linked with autosomal-recessive neonatal-onset primary coenzyme Q10 deficiency.

    • Synonyms

      Ubiquinone biosynthesis protein COQ9, mitochondrial, C16orf49, COQ10D5, C16orf49, HSPC326, PSEC0129.

    • 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 MGSRSSDEQK QQPPNSFSQQ HSETQGAEKP DPESSHSPPR YTDQGGEEEE DYESEEQLQH RILTAALEFV PAHGWTAEAI AEGAQSLGLS SAAASMFGKD GSELILHFVT QCNTRLTRVL EEEQKLVQLG QAEKRKTDQF LRDAVETRLR MLIPYIEHWP RALSILMLPH NIPSSLSLLT SMVDDMWHYA GDQSTDFNWY TRRAMLAAIY NTTELVMMQD SSPDFEDTWR FLENRVNDAM NMGHTAKQVK STGEALVQGL MGAAVTLKNL TGLNQRR.

    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.

    Coq9 Human
  • View Data Sheet

    Name :

    EGLN3 Human

    Description:

    Egl Nine Homolog 3 Human Recombinant

    Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.

    Product # :

    PRO-1143

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    EGLN3 Human Recombinant produced in E. coli is a single polypeptide chain containing 263 amino acids (1-239) and having a molecular mass of 29.8 kDa.EGLN3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EGLN3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 300mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.

    • Synonyms

      Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.

    • 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 MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED

    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.

    Egln3 Human
  • View Data Sheet

    Name :

    UCHL1 (1-126) Human

    Description:

    Ubiquitin Carboxyl-Terminal Hydrolase L1 (1-126) Human Recombinant

    PGP 9.5, UCHL1, PGP9.5, PARK5.

    Product # :

    PRO-2823

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    Description

    The UCHL1 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCHL1 His-Tagged Fusion Protein, produced in E. coli, is a 19kDa protein containing 126 amino acid residues of the UCHL1 Human, 1-126 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.

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    • Synonyms

      PGP 9.5, UCHL1, PGP9.5, PARK5.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized UCHL1 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Background

      Human Ubiquitin Carboxyl-Terminal Hydrolase L1 (UCH-L1) is an important enzyme involved in the ubiquitin-proteasome system, which regulates protein degradation and turnover in cells.

      UCHL1 Function:

      UCHL1 mainly removes ubiquitin molecules from proteins, thereby recycling ubiquitin and regulating protein stability. This action is important for controlling various cellular processes and maintaining cellular homeostasis and.

      UCHL1 Structure

      UCHL1 is characterized by a catalytic domain which facilitates its hydrolase activity, allowing it to cleave ubiquitin from substrates.

      UCHL1 Role in Neurodegeneration

      UCHL1 has been implicated in neurodegenerative diseases, such as Parkinson’s and Alzheimer's disease. Its expression levels and activity can affect neuronal survival and function.

      UCH-L1 is also studied in the context of cancer. Altered levels of UCHL1 may affect on tumour progression and response to therapy.

      UCHL1 Biomarker Potential

      UCHL1 is being investigated as a potential biomarker for diseases, especially neurodegenerative disorders due to its involvement in various pathologies.

      UCHL1 Research

      Ongoing studies focus on understanding its role in various cellular contexts, its regulation, and its potential as a therapeutic target.

      In conclusion, UCHL1 is a very important component of cellular regulation, with implications in health and disease.

    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.

    Uchl1 Protein
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    Name :

    Cyclophilin F Rat

    Description:

    Cyclophilin F Rat Recombinant

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

    Product # :

    ENZ-903

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Cyclophilin F Rat
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    Name :

    ALKBH3 Human

    Description:

    ALKB Alkylation Repair Homolog 3 Human Recombinant

    Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3, Alkylated DNA repair protein alkB homolog 3, DEPC-1, Prostate cancer antigen 1, ALKBH3, ABH3, DEPC1, PCA1, FLJ43614, MGC118790, MGC118792, MGC118793.

    Product # :

    ENZ-101

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    Description

    ALKBH3 Human Recombinant fused to 39 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 325 amino acids (1-286 a.a.) and having a molecular mass of 37.9kDa. The ALKBH3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ALKBH3 solution 1mg/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.

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    • Introduction

      ALKBH3 belongs to the ALKB family of proteins and acts as a dioxygenase with a preference for RNA and single stranded DNA substrates. ALKBH3 protein repairs 1-methyladenine and 3-methylcytosine lesions in alkylated DNA and RNA and its activity is stimulated by ascorbate. ALKBH3 is expressed in a broad array of tissues and localizes to the cytoplasm and the nucleus.

    • Synonyms

      Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3, Alkylated DNA repair protein alkB homolog 3, DEPC-1, Prostate cancer antigen 1, ALKBH3, ABH3, DEPC1, PCA1, FLJ43614, MGC118790, MGC118792, MGC118793.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELDM EEKRRRARVQ GAWAAPVKSQ AIAQPATTAK SHLHQKPGQT WKNKEHHLSD REFVFKEPQQ VVRRAPEPRV IDREGVYEIS LSPTGVSRVC LYPGFVDVKE ADWILEQLCQ DVPWKQRTGI REDITYQQPR LTAWYGELPY TYSRITMEPN PHWHPVLRTL KNRIEENTGH TFNSLLCNLY RNEKDSVDWH SDDEPSLGRC PIIASLSFGA TRTFEMRKKP PPEENGDYTY VERVKIPLDH GTLLIMEGAT QADWQHRVPK EYHSREPRVN LTFRTVYPDP RGAPW.

    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.

    Alkbh3 Human
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    Name :

    GSTP2 Mouse

    Description:

    Glutathione S-Transferase pi 2 Mouse Recombinant

    Glutathione S-transferase P 2, Gst P2, GST YF-YF, GST class-pi, GST-piA.

    Product # :

    ENZ-943

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    Description

    GSTP2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 210 amino acids (1-210 a.a.) and having a molecular mass of 23.5kDa. The GSTP2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTP2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in the protection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2 induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer of the dentate gyrus, which at the end leads to structural and functional damage.

    • Synonyms

      Glutathione S-transferase P 2, Gst P2, GST YF-YF, GST class-pi, GST-piA.

    • 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

      MPPYTIVYFP SPGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY GQLPKFEDGD LTLYQSNAIL RHLGRSLGLY GKNQREAAQV DMVNDGVEDL RGKYGTMIYR NYENGKNDYV KALPGHLKPF ETLLSQNQGG KAFIVGDQIS FADYNLLDLL LIHQVLAPGC LDNFPLLSAY VARLSARPKI KAFLSSPEHV NRPINGNGKQ.

    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.

    Mouse Gstp2
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    Name :

    Prolactin Ovine

    Description:

    Prolactin Ovine Recombinant

    Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    Product # :

    CYT-240

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    Description

    Prolactin Ovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 23 kDa. The Prolactin n 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

    Is fully biologically active as evidenced by inducing proliferation of Nb2 cells.

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    • Introduction

      Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

    • Synonyms

      Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prl 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 Prolactin in sterile 18MΩ-cm H2O or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Thr-Pro-Val-Cys-Pro.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.93 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC DNAman computer analysis program of protein sequences.

    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.

    Prolactin Ovine
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    Name :

    RALA Mouse

    Description:

    V-ral Simian Leukemia Viral Oncogene Homolog A Mouse Recombinant

    Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA. 

    Product # :

    PRO-2497

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    Description

    RALA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a) and having a molecular mass of 25.7kDa. RALA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RALA protein solution (0.5mg/ml) 20mM Tris-Hcl buffer (pH8.5) containing 30% glycerol, 0.1M NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

    • Synonyms

      Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA.

    • 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 MGSHMAANKP KGQNSLALHK VIMVGSGGVG KSALTLQFMY DEFVEDYEPT KADSYRKKVV LDGEEVQIDI LDTAGQEDYA AIRDNYFRSG EGFLCVFSIT EMESFAATAD FREQILRVKE DENVPFLLVG NKSDLEDKRQ VSVEEAKNRA DQWNVNYVET SAKTRANVDK VFFDLMREIR ARKMEDSKEK NGKKKRKSLA KRIRERC

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    Rala Mouse
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    Name :

    Y.Enterocolitica (O:9) YopD

    Description:

    Yersinia Enterocolitica (O:9) YopD Recombinant

    Product # :

    PRO-2276

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    Description

    Recombinant Yersinia Enterocolitica (O:9) YopD produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 34,603 Dalton. Y.Enterocolitica (O:9) YopD is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Y.Enterocolitica (O:9) YopD is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgG- and IgM- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.

    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.

    Yenterocolitica O 9 Yopd
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    Name :

    Cyclophilin F Rat Bioactive

    Description:

    Cyclophilin-F Rat Recombinant Bioactive

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

    Product # :

    ENZ-1019

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    Description

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

    Source

    Escherichia Coli.

    Formulation

    Cyclophilin F protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,300 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmol of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.

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    • Introduction

      PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

    • Synonyms

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

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

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

    Cyclophilin F Rat Bioactive
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    Name :

    TXNRD1 Human

    Description:

    Thioredoxin Reductase 1 Human Recombinant

    Thioredoxin reductase 1 cytoplasmic, TR, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.

    Product # :

    ENZ-518

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    Description

    TXNRD1 Human Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 508 amino acids (161-647 a.a.) and having a molecular mass of 55.7 kDa. TXNRD1 protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    TXNRD1 Human solution (0.5mg/ml) containing 1x PBS pH-7.4 & 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 15 units/mg, and was measured in a coupled assay with 5,5'-Dithiobis(2-nitrobenzoic acid)(DTNB)and NADPH. The amount of TNB generated by NADPH was measured in absorbance at 412 nm.

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    • Introduction

      TXNRD1 belongs to the selenium-containing pyridine nucleotide-disulphide oxidoreductase family, which has a conserved catalytic site of Cys-Val-Asn-Val-Gly-Cys. TXNRD1 decreases thioredoxins as well as other substrates, and participates in selenium metabolism and protection against oxidative stress. Inhibition of TXNRD1 activity serves as a potential treatment for cancer, AIDS and other autoimmune diseases as well as bacterial infections and parasitic diseases.

    • Synonyms

      Thioredoxin reductase 1 cytoplasmic, TR, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.

    • 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 MYDYDLIIIG GGSGGLAAAK EAAQYGKKVM VLDFVTPTPL GTRWGLGGTC VNVGCIPKKL MHQAALLGQALQDSRNYGWK VEETVKHDWD RMIEAVQNHI GSLNWGYRVA LREKKVVYEN AYGQFIGPHR IKATNNKGKE KIYSAERFLI ATGERPRYLGIPGDKEYCIS SDDLFSLPYC PGKTLVVGAS YVALECAGFL AGIGLDVTVM VRSILLRGFD QDMANKIGEH MEEHGIKFIR QFVPIKVEQIEAGTPGRLRV VAQSTNSEEI IEGEYNTVML AIGRDACTRK IGLETVGVKI NEKTGKIPVT DEEQTNVPYI YAIGDILEDK VELTPVAIQAGRLLAQRLYA GSTVKCDYEN VPTTVFTPLE YGACGLSEEK AVEKFGEENI EVYHSYFWPL EWTIPSRDNN KCYAKIICNT KDNERVVGFH VLGPNAGEVT QGFAAALKCG LTKKQLDSTI GIHPVCAEVF TTLSVTKRSG ASILQAGC.

    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.

    Txnrd1 Human
  • View Data Sheet

    Name :

    GST, His

    Description:

    Glutathione S-Transferase Recombinant, His Tag

    Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    Product # :

    ENZ-451

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    Description

    Recombinant Schistosoma japonicum GST full length protein contains a total of 244 amino acids (1-218 a.a.) expressed in E.coli, having a molecular mass of 28.3kDa. The GST protein is fused to a 20 amino acids His-Tag at N-terminus. The GST protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GST is supplied in PBS pH 7.4 & 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    >10 units/mg, & is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH-6.5 at 25C.

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    • Introduction

      Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
      The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions.

    • Synonyms

      Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    • 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 MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMAIIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALDVVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.

    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.

    Glutathione S Transferase His
  • View Data Sheet

    Name :

    AK2 Human

    Description:

    Adenylate Kinase 2 Human Recombinant

    ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.

    Product # :

    PKA-260

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    Description

    AK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 259 amino acids and having a molecular mass of 28.6 kDa. AK2 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AK2 solution containing 20mM Tris pH-7.5, 5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 1.5 units/ml. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 25C.

    More Info

    • Introduction

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

    • Synonyms

      ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      AK2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAPSVPAAEP EYPKGIRAVL LGPPGAGKGTQAPRLAENFC VCHLATGDML RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG FPRTVRQAEM LDDLMEKRKE KLDSVIEFSIPDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI.

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

    Ak2 Human
  • View Data Sheet

    Name :

    ACE2 (18-740) Human, Fc

    Description:

    Angiotensin Converting Enzyme 2 (18-740 a.a.), Fc Human Recombinant

    Product # :

    ENZ-1126

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    Description

    The HEK293 derived ACE2 Human recombinant protein contains the amino acids 18-740 fused to Fc tag at C-terminal. ACE2 Protein binds to SARS Coronavirus-2 [ CoV-2019 ] Spike receptor binding domain.

    Source

    HEK293 Cells

    Formulation

    ACE2 Human protein solution is supplied in 50mM Tris-HCl, pH7.5, and 150mM NaCl and glycerol.

    Purity

    ACE-2 Protein is >95% pure as determined SDS-PAGE.

    Biological Activity

    ACE2 activity was measured by its binding ability in a functional ELISA.

    The immobilized Recombinant Human ACE2 protein binds to SARS CoV2 Spike protein Receptor Binding Domain at 2ug per ml.

    More Info

    • Introduction

      ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      ACE-2 Human Recombinant Protein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Purification Method

      Purified by Protein-G chromatographic technique.

    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.

    Ace2 Protein
  • View Data Sheet

    Name :

    PPP3CA Human

    Description:

    Protein Phosphatase 3, Catalytic subunit, Alpha Isozyme Human Recombinant

    Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform, CAM-PRP catalytic subunit, Calmodulin-dependent calcineurin A subunit alpha isoform, PPP3CA, CALNA, CAN, CALN, CCN1, CNA1, PPP2B, CALNA1.

    Product # :

    ENZ-051

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    Description

    PPP3CA Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 534 amino acids (1-511 a.a.) and having a molecular mass of 60kDa. The PPP3CA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPP3CA solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PPP3CA (aka Calcineurin A) is a major soluble calmodulin binding protein in the brain and a Ca2+/calmodulin dependent serine/threonine protein phosphatase, with a relatively limited substrate specificity. PPP3CA activates the T cells of the immune system and can be blocked by drugs. PPP3CA activates NFATc (a transcription factor) by dephosphorylating it. The activated NFATc is subsequently translocated into the nucleus, where it upregulates the expression of interleukin 2.

    • Synonyms

      Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform, CAM-PRP catalytic subunit, Calmodulin-dependent calcineurin A subunit alpha isoform, PPP3CA, CALNA, CAN, CALN, CCN1, CNA1, PPP2B, CALNA1.

    • 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 TGSMSEPKAI DPKLSTTDRV VKAVPFPPSH RLTAKEVFDN DGKPRVDILK AHLMKEGRLE ESVALRIITE GASILRQEKN LLDIDAPVTV CGDIHGQFFD LMKLFEVGGS PANTRYLFLG DYVDRGYFSI ECVLYLWALK ILYPKTLFLL RGNHECRHLT EYFTFKQECK IKYSERVYDA CMDAFDCLPL AALMNQQFLC VHGGLSPEIN TLDDIRKLDR FKEPPAYGPM CDILWSDPLE DFGNEKTQEH FTHNTVRGCS YFYSYPAVCE FLQHNNLLSI LRAHEAQDAG YRMYRKSQTT GFPSLITIFS APNYLDVYNN KAAVLKYENN VMNIRQFNCS PHPYWLPNFM DVFTWSLPFV GEKVTEMLVN VLNICSDDEL GSEEDGFDGA TAAARKEVIR NKIRAIGKMA RVFSVLREES ESVLTLKGLT PTGMLPSGVL SGGKQTLQSA IKGFSPQHKI TSFEEAKGLD RINERMPPRR DAMPSDANLN SINKALTSET NGTDSNGSNS SNIQ.

    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.

    Ppp3Ca Human
  • View Data Sheet

    Name :

    CKMB1 Human

    Description:

    Creatine Kinase MB Isoenzyme Type-1 Human Recombinant

    Creatine Kinase MB 1, CKMB1

    Product # :

    CKI-269

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    Description

    CKMB1 Human Recombinant produced in E.Coli is a non covalently linked heterodimer that consists of 381 a.a. and having a total Mw of ~85.6kDa. The CKMB1 is purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    CKMB1 was lyophilized a concentrated solution containing 20mM Tris, 150mM NaCl, pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    CKMB1 activity was measured kinetically by the CK-NAC assay at 37°C which was found to be between 500-600 units/mg. 1U converts 1µmole of creatine phosphate to creatine/min at 37˚C

    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 MB Isoenzyme Type-1, CK MB1

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized CKMB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CKMB1 in sterile 18MΩ-cm H2O at 0.1 mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CKM1
      MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ

      CKB
      MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K

    • Background

      What is the molecular weight / Mw of CKMB1 Protein?
      CKMB1 Protein is a non covalently heterodimer having a total Mw of 85.6

      What is the source or expression system of CKMB1 Protein?
      Escherichia Coli.

      What is the Purity of CKMB1 Protein?
      CKMB1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CKMB1 Protein?
      The activity was determined kinetically by the CK-NAC assay at 37°C which ranges between 500-600 U/mg.

      What is the amino acid sequence of CKMB1 Protein?
      CKM1
      MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ
      CKB
      MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K

      What applications can CKMB1 Protein be used in?
      CKMB1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CKMB1 Protein?
      The endotoxin level is minimal, CKMB1 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.

    Ckmbi Human
  • View Data Sheet

    Name :

    Welqut Protease

    Description:

    Welqut Protease Staphylococcus aureus Recombinant

    Product # :

    ENZ-1113

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    Description

    Welqut Protease Recombinant is a single, non-glycosylated polypeptide chain containing 204 amino acids and having a molecular mass of 22kDa. The Welqut Protease is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Welqut Protease contains 10 mM Na2HPO4, 50% glycerol, 1.8 mM KH2PO4, pH 7.3, 140 mM NaCl and 2.7 mM KCl.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WELQut Protease is an extremely specific and recombinant serine protease from Staphylococcus aureus. The WELQut Protease identifies and accurately cleaves recombinant proteins that has a recognition sequence added to them, with the amino acid sequence Trp, Glu, Leu, Gln, X (any amino acid). WELQut Protease cut externally from the recognition sequence, therefor doesn’t leave extra amino acids bound to the target protein. The protease isn’t temperature sensitive (works in 4-30°C) or pH sensitive (pH 6.5-9.0), also, there is no need in any particular buffers.

    • 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.

    • Unit Definition

      Each unit is defined as the amount of enzyme required to cleave ≥99% of 100μg of a control protein in 16 h at 20°C. Enzyme activity is assayed in 100μl 100 mM Tris-HCl (pH 8.0).

    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.

    Welqut Protease
  • View Data Sheet

    Name :

    PLA2G7 Human

    Description:

    Secreted Phospholipase A2-VII Human Recombinant

    Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.

    Product # :

    ENZ-436

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    Description

    PLA2G7 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 420 amino acids fragment (22-441) having a total molecular mass of 52.29kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The PLA2G7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PLA2G7 protein is supplied in 20mM Tris-HCl pH-8.0, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
      PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
      PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
      PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population.

    • Synonyms

      Platelet-activating factor acetylhydrolase, PAF acetylhydrolase, PAF 2-acylhydrolase, LDL-associated phospholipase A2, LDL-PLA(2), 2-acetyl-1-alkylglycerophosphocholine esterase, 1-alkyl-2-acetylglycerophosphocholine esterase, PLA2G7, PAFAH, LP-PLA2, LDL-PLA2.

    • 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. Please avoid 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.

    Pla2G7 Human
  • View Data Sheet

    Name :

    ADAT2 Human

    Description:

    Adenosine Deaminase, tRNA-specific 2 Human Recombinant

    DEADC1, TAD2.

    Product # :

    ENZ-561

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    Description

    Recombinant Human ADAT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (1-191 a.a) and having a molecular mass of 23.2 kDa. ADAT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ADAT2 (0.5mg/ml) protein contains 20mM Tris-HCl buffer pH-8, 2mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Adenosine Deaminase (ADA), also recognized as ADAT2 is an enzyme that takes part in purine metabolism. ADAT2 is necessary for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. ADAT2 is involved in the deamination of adenosine-34 to inosine in numerous tRNAs. ADAT2 is part of the cytidine and deoxycytidylate deaminase protein family, ADAT2 employs zinc as a cofactor. ADAT2 is a 191 amino acid enzyme that exists as two isoforms formed by alternative splicing events.

    • Synonyms

      DEADC1, TAD2.

    • 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 MEAKAAPKPA ASGACSVSAE ETEKWMEEAM HMAKEALENT EVPVGCLMVY NNEVVGKGRN EVNQTKNATR HAEMVAIDQV LDWCRQSGKS PSEVFEHTVL YVTVEPCIMC AAALRLMKIP LVVYGCQNER FGGCGSVLNI ASADLPNTGR PFQCIPGYRA EEAVEMLKTF YKQENPNAPK SKVRKKECQK S.

    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.

    Adat2 Human
  • View Data Sheet

    Name :

    UMOD Human

    Description:

    Uromodulin Human

    Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    Product # :

    ENZ-381

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    Description

    Uromodulin Human Native protein produced from Human Urine, is a glycosylated polypeptide chain having a total Mw of 80 kDa on SDS-PAGE.

    Source

    Human Urine.

    Formulation

    The UMOD protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing deionized water.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

    • Synonyms

      Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at 2-8°C. DO NOT FREEZE!

    • Solubility

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

    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.

    Umod
  • View Data Sheet

    Name :

    CoV-2 3CL

    Description:

    Coronavirus 2019 3CL Protease Recombinant

    Product # :

    SARS-058

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    Description

    Recombinant Coronavirus 2019 3CL Protease having a Mw of approximately 33.8 kDa was purified from E. coli. The CoV-2 3CL contains 306 amino acids and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    CoV-2 3CL solution contains 5 % Trehalose, 0.02 % Tween-20 and PBS, pH 7.4.

    Purity

    Protein is >98% pure as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    CoV-2 3CL is a cysteine protease that cleaves proteins with sequences including LQ(S/A/G).  The cleavage takes c-terminal to the glutamine residue. 

    More Info

    • Introduction

      The SARS CoV-2 3CL protease (C30 Endopeptidase) derived from human SARS-CoV-2 is a C30-type cysteine protease situated in the NS3 segment. SARS CoV-2 3CL protease biological functionality is needed to process viral polyproteins to functional complete units. SARS CoV-2 3CL protease (main protease) is the core protease protein in CoV and corresponds to non-structural protein 5. SARS CoV-2 3CL cleaves the CoV polyprotein at 11 locations. SARS CoV-2 3CL protease has a cysteine-histidine catalytic dyad at its active site and cleaves a Gln–(Ser/Ala/Gly) peptide bond. SARS CoV-2 3CL protease at position P1 cleaves the bond between the glutamine and serine/alanine/glycine. SARS CoV-2 3CL protease is necessary in the processing of the CoV replicase polyprotein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; 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. CoV-2 3CL is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      SGFRKMAFPS GKVEGCMVQV TCGTTTLNGL WLDDVVYCPR HVICTSEDML NPNYEDLLIR KSNHNFLVQA GNVQLRVIGH SMQNCVLKLK VDTANPKTPK YKFVRIQPGQ TFSVLACYNG SPSGVYQCAM RPNFTIKGSF LNGSCGSVGF NIDYDCVSFC YMHHMELPTG VHAGTDLEGN FYGPFVDRQT AQAAGTDTTI TVNVLAWLYA AVINGDRWFL NRFTTTLNDF NLVAMKYNYE PLTQDHVDIL GPLSAQTGIA VLDMCASLKE LLQNGMNGRT ILGSALLEDE FTPFDVVRQC SGVTFQ

    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.

    product_image.jpg
  • View Data Sheet

    Name :

    GAPDH Mouse

    Description:

    GAPDH Mouse Recombinant

    Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, Gapdh, Gapd, Glyceraldehyde-3-phosphate dehydrogenase isoform 2, G3PD, GAPD, HEL-S-162eP.

    Product # :

    ENZ-860

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    GAPDH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 356 amino acids (1-333a.a.) and having a molecular mass of 38.2kDa.GAPDH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GAPDH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GAPDH is a catalytic enzyme normally known to play a role in glycolysis. GAPDH exists as a tetramer composed of 36-kDa subunits and has a range of intracellular functions. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Besides functioning as a glycolytic enzyme in cytoplasm, GAPDH has function in intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and DNA repair. GAPDH catalyzes a vital energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains.

    • Synonyms

      Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, Gapdh, Gapd, Glyceraldehyde-3-phosphate dehydrogenase isoform 2, G3PD, GAPD, HEL-S-162eP.

    • 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 MGSMVKVGVN GFGRIGRLVT RAAICSGKVE IVAINDPFID LNYMVYMFQY DSTHGKFNGT VKAENGKLVI NGKPITIFQE RDPTNIKWGE AGAEYVVEST GVFTTMEKAG AHLKGGAKRV IISAPSADAP MFVMGVNHEK YDNSLKIVSN ASCTTNCLAP LAKVIHDNFG IVEGLMTTVH AITATQKTVD GPSGKLWRDG RGAAQNIIPA STGAAKAVGK VIPELNGKLT GMAFRVPTPN VSVVDLTCRL EKPAKYDDIK KVVKQASEGP LKGILGYTED QVVSCDFNSN SHSSTFDAGA GIALNDNFVK LISWYDNEYG YSNRVVDLMA YMASKE.

    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.

    Gapdh Mouse
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