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Search results

1000 results found for “cytochrome”

Name

Description

Product #

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  • View Data Sheet

    Name :

    PRDX4 Human

    Description:

    Peroxiredoxin-4 Human Recombinant

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

    Product # :

    ENZ-513

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Prdx4 Human
  • View Data Sheet

    Name :

    GLRX1 Human

    Description:

    Glutaredoxin 1 Human Recombinant

    Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin-1, Thioltransferase-1, TTase-1, GLRX, MGC117407.

    Product # :

    ENZ-391

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    Glutaredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 106 amino acids having a molecular mass of 11.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    Glutaredoxin solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

    • Synonyms

      Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin-1, Thioltransferase-1, TTase-1, GLRX, MGC117407.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ.

    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.

    Glrx1 Human
  • View Data Sheet

    Name :

    CLTA Human

    Description:

    Clathrin, Light Chain A Human Recombinant

    Clathrin light chain A, Lca, CLTA.

    Product # :

    PRO-1144

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CLTA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-218 a.a) and having a molecular mass of 26.2kDa (Molecular weight on SDS-PAGE will appear higher).CLTA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLTA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Clathrin, light chain A (CLTA) is a member of the clathrin family. Clathrin, which is a large, soluble protein, is comprised of heavy and light chains. CLTA is one of 2 clathrin light chain proteins which are supposed to function as regulatory elements. CLTA is a key cytosolic coat protein in pits and vesicles originating from the plasma membrane and the trans-Golgi network. In receptor-mediated endocytosis, receptor proteins are encapsulated by Clathrin-coated vesicles.

    • Synonyms

      Clathrin light chain A, Lca, CLTA.

    • 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 MGSHMAELDP FGAPAGAPGG PALGNGVAGA GEEDPAAAFL AQQESEIAGI ENDEAFAILD GGAPGPQPHG EPPGGPDAVD GVMNGEYYQE SNGPTDSYAA ISQVDRLQSE PESIRKWREE QMERLEALDA NSRKQEAEWK EKAIKELEEW YARQDEQLQK
      TKANNRAAEE AFVNDIDESS PGTEWERVAR LCDFNPKSSK QAKDVSRMRS VLISLKQAPL VH.

    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.

    Clta Human
  • View Data Sheet

    Name :

    Streptavidin

    Description:

    Streptavidin Recombinant

    Product # :

    PRO-791

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
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    • purity
    • More Info

    Description

    Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli. The molecular weight per tetramer is approximately 52kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized in 10mM potassium phosphate buffer pH 6.5.

    Purity

    Greater than 98.0% as determined by SDS-PAGE and HPLC.

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Streptavidin is shipped at ambient temperature, upon arrival store at -20°C.

    • Solubility

      It is recommended to reconstitute the lyophilized Streptavidin in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLT
      GRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGA
      EARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS.

    • Proteolytic Activity

      < 10-3 U/mg protein (Azocoll, 25 °C, 24 h, pH 8.0).

    • Specific Activity

      > 17U/mg (one unit binds 1 μg D-biotin).

    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.

    Streptavidin Recombinant
  • View Data Sheet

    Name :

    Cys-Protein-G

    Description:

    Cys-Protein G Recombinant

    Product # :

    PRO-1238

    Price :

    Quantity :

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    • description
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    • purity
    • More Info

    Description

    Cys-Protein G Recombinant produced in E.Coli, is a single non-glycosylated polypeptide chain containing 201 amino acids and having a cys on N-terminal. Cys-Protein G has a predicted molecular mass of approximately 21.9kDa but it migrates with an apparent molecular mass of 40kDa in SDS-PAGE. The Cys-Protein G is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized without any additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      CLPKTDTYKL ILNGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTEAVDAAT AEKVFKQYAN DNGVDGEWTY DDATKTFTVT EKPEVIDASE LTPAVTTYKL VINGKTLKGE TTTKAVDAET AEKAFKQYAN DNGVDGVWTY DDATKTFTVT E.

    • Specificity

      The recombinant Protein G is a genetically engineered protein contains 3 IgG-binding regions of protein G.

    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.

    Cys Protein G His
  • View Data Sheet

    Name :

    AIFM1 Antibody

    Description:

    Apoptosis-Inducing Factor Mitochondrion-Associated 1, Mouse Anti Human

    Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.

    Product # :

    ANT-634

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 (AIFM1) is a mitochondrial protein which translocates to the nucleus once apoptosis has been initiated. AIFM1 causes DNA fragmentation and chromatin condensation and also triggers the release of cytochrome c and caspase-9 from mitochondria. Bcl-2 overexpression prevents the release of AIFM1 from mitochondria, but doesn’t block its apoptogenic activity.

    • Synonyms

      Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human AIFM1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human AIFM1 protein 98-609 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT22E9AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      AIFM1 antibody was purified from mouse ascitic fluids by protein-A 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.

    Aifm1 Antibody
  • View Data Sheet

    Name :

    DHRS4 Human

    Description:

    Dehydrogenase/Reductase Member 4 Human Recombinant

    Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.

    Product # :

    ENZ-207

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    Description

    DHRS4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278) and having a molecular mass of 32.1kDa.DHRS4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DHRS4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dehydrogenase/reductase SDR family member 4 (DHRS4) is a member of the short-chain dehydrogenases/reductases (SDR) family. DHRS4 reduces all trans retinal and 9-cis retinal. In addition, the DHRS4 protein can catalyze the oxidation of all trans retinol with NADP as cofactor, but with a much lower efficiency. Furthermore, DHRS4 reduces alkyl phenyl ketones and alpha dicarbonyl compounds with aromatic rings, such as pyrimidine 4 aldehyde, 3 benzoylpyridine, 4 benzoylpyridine, menadione and 4 hexanoylpyridine.

    • Synonyms

      Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.

    • 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 MGSHMHKAGL LGLCARAWNS VRMASSGMTR RDPLANKVAL VTASTDGIGF AIARRLAQDG AHVVVSSRKQ QNVDQAVATL QGEGLSVTGT VCHVGKAEDR ERLVATAVKL HGGIDILVSN AAVNPFFGSI MDVTEEVWDK TLDINVKAPA LMTKAVVPEM EKRGGGSVVI VSSIAAFSPS PGFSPYNVSK TALLGLTKTL AIELAPRNIR VNCLAPGLIK TSFSRMLWMD KEKEESMKET LRIRRLGEPE DCAGIVSFLC SEDASYITGE TVVVGGGTPS RL.

    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.

    Dhrs4 Human
  • View Data Sheet

    Name :

    LAMP2 Human

    Description:

    Lysosomal-Associated Membrane Protein 2 Human Recombinant

    Lysosomal-associated membrane protein 2, CD107b, LAMP-2, CD107 antigen-like family member B, LGP110, LAMP2.

    Product # :

    PRO-130

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    Description

    LAMP2 is a full-length cDNA coding for the human lysosomal-associated membrane protein 2 having a molecular mass of 42,488 Dalton (pH 5.88). LAMP2 protein is fused to a deca-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    LAMP2 (0.94mg/ml) is supplied in 16mM HEPES buffer pH-8.0, 130mM NaCl and 20% Glycerol.

    More Info

    • Introduction

      The protein encoded by LAMP2 belongs to a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands LAMP2 takes part in tumor cell metastasis and in addition has a role in the protection, maintenance, and adhesion of the lysosome. The effect of alternative splicing of this gene is multiple transcript variants encoding distinct proteins.

    • Synonyms

      Lysosomal-associated membrane protein 2, CD107b, LAMP-2, CD107 antigen-like family member B, LGP110, LAMP2.

    • Stability

      Store LAMP2 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.

    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.

    Lamp2 Human
  • View Data Sheet

    Name :

    CHD4 Human

    Description:

    Chromodomain Helicase DNA Binding Protein 4 Human Recombinant

    Chromodomain Helicase DNA binding protein 4, Mi-2b, Mi2-BETA, CHD-4, ATP-dependent helicase CHD4, Mi-2 autoantigen 218 kDa protein, EC 3.6.4.12, EC 3.6.1.

    Product # :

    PRO-112

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    Description

    CHD4 is a full-length cDNA coding for the human Mi-2 beta isoform having a molecular mass of 221,298 Dalton (pH 5.8). CHD4 protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    CHD4 is supplied in 20mM HEPES buffer pH-8.0 and 500mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CHD4 is a member of a family of alleged chromodomain helicase-DNA-binding proteins. Biochemically, CHD4 is a component of the nucleosome transformation and deacetylase (NuRD) complex that takes part in transcription regulation. Autoantibodies targeting the CHD4 are a serologic feature of idiopathic inflammatory myopathies (IIM). In IIM Mi-2 antibodies are characterized by diagnostic sensitivity and specificity of approximately 4-18% and 98-100%, respectively. Moreover, anti-CHD4 antibodies are related to dermatomyositis (frequency up to 31%) and have a great positive predictive value for this type of disease subset. Anti-CHD4 are the only defined myositis-specific autoantibodies clearly focused to a nuclear target. An additional slightly outstanding feature of Mi-2 antibodies relates to their frequency in children, which is similar to that in adults.

    • Synonyms

      Chromodomain Helicase DNA binding protein 4, Mi-2b, Mi2-BETA, CHD-4, ATP-dependent helicase CHD4, Mi-2 autoantigen 218 kDa protein, EC 3.6.4.12, EC 3.6.1.

    • 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-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.

    • coating concentration

      0.3-0.7 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with myositis sera ormonoclonal anti-hexa-His-tag antibody.

    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.

    Chd4 Human
  • View Data Sheet

    Name :

    PYCRL Human

    Description:

    Pyrroline-5-Carboxylate Reductase Like Human Recombinant

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

    Product # :

    ENZ-678

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Pycrl Human
  • View Data Sheet

    Name :

    CXCL16 Mouse

    Description:

    CXCL16 Mouse Recombinant

    C-X-C motif chemokine 16, Small-inducible cytokine B16, Transmembrane chemokine CXCL16, Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein, SR-PSOX, Cxcl16, Srpsox, Zmynd15, AV290116, BB024863, 0910001K24Rik.

    Product # :

    CHM-363

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    • source
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    Description

    CXCL16 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 9.9kDa. The CXCL16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract murine lymphocytes using a concentration range of 100-1000ng/ml corresponding to a Specific Activity of 1,000-10,000IU/mg.

    More Info

    • Introduction

      Mouse CXCL16 is a nonELR motif including CXC chemokine with a transmembrane domain. Mouse CXCL16 cDNA encodes a 246 a.a. precursor protein with a putative 26 a.a. residue signal peptide, an 88 a.a. residue chemokine domain, an 87 a.a. residue mucinlike spacer region, a 22 a.a. residue transmembrane domain, and a 23 a.a. residue cytoplasmic tail.
      CXCL16 induces a strong chemotactic response and calcium mobilization. Furthermore, CXCL16 acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis.
      Mouse CXCL16 is generated by dendritic cells in lymphoid organ T cell zones as well as by cells in the splenic red pulp both as membranebound and soluble forms. CXCR6/Bonzo (STRL33 and TYMSTR) is the receptor for CXCL16. CXCL16 is expressed in the spleen, lymph nodes, and Peyer patches. It is also expressed in non-lymphoid tissues such as lung, kidney, small intestine, and thymus, with weak expression in heart and liver and no expression in brain and purified B- and T-cells.
      CXCL16 deficiency is linked to breast cancer progression. In addition, CXCL16 is involved in immunological liver injury by regulating T lymphocyte infiltration in liver tissue. Furtheremore, CXCL16 has a distinctive role in the maintenance of cardiac allograft tolerance mediated by natural killer T cells. Moreover, CXCL16 has a significant role in not only the production of IFN-gamma by NKT cells, but also promotion of Th1-inclined immune responses mediated by NKT cells.

    • Synonyms

      C-X-C motif chemokine 16, Small-inducible cytokine B16, Transmembrane chemokine CXCL16, Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein, SR-PSOX, Cxcl16, Srpsox, Zmynd15, AV290116, BB024863, 0910001K24Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL16 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 CXCL16 Mouse in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NQGSVAGSCS CDRTISSGTQ IPQGTLDHIR KYLKAFHRCP FFIRFQLQSK SVCGGSQDQW VRELVDCFER KECGTGHGKS FHHQKHLP.

    • Background

      What is the molecular weight/Mw of CXCL16 MOUSE Protein?
      CXCL16 MOUSE Protein has a total Mw of 9.9kDa.

      What is the source or expression system of CXCL16 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL16 MOUSE Protein?
      CXCL16 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL16 MOUSE Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 100-1000ng/ml corresponding to a Specific Activity of 1,000-10,000IU/mg.

      What is the amino acid sequence of CXCL16 MOUSE Protein?
      NQGSVAGSCS CDRTISSGTQ IPQGTLDHIR KYLKAFHRCP FFIRFQLQSK SVCGGSQDQW VRELVDCFER KECGTGHGKS FHHQKHLP.

      What applications can CXCL16 MOUSE Protein be used in?
      CXCL16 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL16 MOUSE Protein?
      The endotoxin level is minimal, CXCL16 MOUSE 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.

    Cxcl16 Mouse
  • View Data Sheet

    Name :

    NANA E.Coli

    Description:

    N-Acetylneuraminate Lyase E.Coli Recombinant

    N-acetylneuraminate lyase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, NALase, Sialate lyase, Sialic acid aldolase, Sialic acid lyase, nanA, npl, b3225, JW3194.

    Product # :

    ENZ-128

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    Description

    NANA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a.) and having a molecular mass of 34.7kDa.NANA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NANA protein solution (1mg/ml) 20mM Tris-HCl buffer (pH8.0) and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-acetylneuraminate lyase (NanA) is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NanA catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. NanA is inhibited by reduction with NaBH4 in the presence of the substrate, which indicates that it belongs to the Schiff-base-forming Class I aldolases. NanA is strongly inhibited by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide, it is also inhibited competitively by the reaction product, pyruvate, and its structurally related compounds, dihydroxyacetone and DL-glyceraldehyde.

    • Synonyms

      N-acetylneuraminate lyase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, NALase, Sialate lyase, Sialic acid aldolase, Sialic acid lyase, nanA, npl, b3225, JW3194.

    • 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 MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE AFVQSLSERE QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF DAVSAVTPFY YPFSFEEHCD HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD QINTLVTLPG
      VGALKQTSGD LYQMEQIRRE HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG.

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    Nana Ecoli
  • View Data Sheet

    Name :

    SlyD E.Coli

    Description:

    FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant

    FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.

    Product # :

    ENZ-338

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    Description

    SlyD Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids and having a molecular mass of 21 kDa.

    Source

    Escherichia Coli.

    Formulation

    SlyD protein solution contains 20mM Tris pH-7.5.

    Purity

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

    Biological Activity

    Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      SlyD accessiton#: NP_755987 is a putative folding helper protein from the Escherichia coli cytosol, which has N-terminal prolyl isomerase domain of the FKBP type and a most likely unstructured C-terminal tail. SlyD is an important factor in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, and exhibits several activities including that of a peptidyl-prolyl isomerase.

    • Synonyms

      FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH.

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    Slyd
  • View Data Sheet

    Name :

    FUR E.Coli

    Description:

    Ferric Uptake Regulator E.Coli Recombinant

    ECs0714, Ferric uptake regulation protein, Ferric uptake regulator, Z0831, FUR, ECK0671, JW0669, b0683.

    Product # :

    PRO-622

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    Description

    Ferric Uptake Regulator Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids and having a molecular mass of 16.7kDa.

    Source

    Escherichia Coli.

    Formulation

    The Ferric Uptake Regulator protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 2mM CaCl2 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ferric Uptake Regulator protein NCBI Accession No.: NP_415209 is a DNA-binding protein which controls iron-responsive genes. Ferric Uptake Regulator has a molecular mass of 17-kDa and plays a role in global transcriptional repressor that in the existence of iron regulates functions as diverse as iron acquisition, oxidative stress, and virulence. In Escherichia coli, members of the Ferric Uptake Regulator family regulate the expression of at least 100 genes that function in processes as diverse as the biosynthesis and transport of siderophores, the expression of virulence factors, the alleviation of oxidative and NO-induced stress, and the inhibition of ferritin production through the expression of RyhB.

    • Synonyms

      ECs0714, Ferric uptake regulation protein, Ferric uptake regulator, Z0831, FUR, ECK0671, JW0669, b0683.

    • 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

      MTDNNTALKK AGLKVTLPRL KILEVLQEPD NHHVSAEDLY KRLIDMGEEI GLATVYRVLN QFDDAGIVTR HNFEGGKSVF ELTQQHHHDH LICLDCGKVI EFSDDSIEAR QREIAAKHGI RLTNHSLYLY GHCAEGDCRE DEHAHEGK.

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    Ferric Uptake Regulator
  • View Data Sheet

    Name :

    TRIAP1 Human

    Description:

    TP53 Regulated Inhibitor Of Apoptosis 1 Human Recombinant

    TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.

    Product # :

    PRO-1771

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    • More Info

    Description

    TRIAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 99 amino acids (1-76 a.a) and having a molecular mass of 11.2kDa.TRIAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TRIAP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TRIAP1 has a p53-binding site in its second exon. TRIAP1 expression is reduced by small interfering RNA enhanced apoptosis, while overexpression of TRIAP1 protects cells from apoptosis triggered by DNA damage. TRIAP1 is highly induced when cells have low levels of genotoxic stresses, but not when DNA damage is severe. TRIAP1 is able to control apoptotic pathways by interacting with Hsp70 which inhibits activity of apoptosis protease activating factor-1.

    • Synonyms

      TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMNSVGEA CTDMKREYDQ CFNRWFAEKF LKGDSSGDPC TDLFKRYQQC VQKAIKEKEI PIEGLEFMGH GKEKPENSS

    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.

    Triap1 Human
  • View Data Sheet

    Name :

    CINP Human

    Description:

    Cyclin-Dependent Kinase 2 Interacting Protein Human Recombinant

    Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    Product # :

    PKA-269

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    Description

    CINP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.4 kDa.The CINP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CINP protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.

    • Synonyms

      Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.

    • Physical Appearance

      CINP 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 MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLLN KDKIELDSSS PASKENEEKV CLEYNEELEK LCEELQATLD GLTKIQVKME KLSSTTKGIC ELENYHYGEE SKRPPLFHTW PTTHFYEVSH KLLEMYRKEL LLKRTVAKEL AHTGDPDLTL SYLSMWLHQP YVESDSRLHL ESMLLETGHR AL

    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.

    Cinp Human
  • View Data Sheet

    Name :

    CNOT7 Mouse

    Description:

    CCR4-NOT Transcription Complex, Subunit 7 Mouse Recombinant

    CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.

    Product # :

    PRO-908

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    Description

    CNOT7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-248 a.a) and having a molecular mass of 31.1kDa.CNOT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNOT7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCR4-Not transcription complex, subunit 7 (CNOT7) is a ubiquitous transcription factor. CNOT7 is a component of the CCR4 complex which functions as a general transcription regulation complex. Furthermore, CNOT7 binds to an anti-proliferative protein, BTG1 (B-cell translocation protein 1), which negatively regulates cell proliferation.

    • Synonyms

      CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.

    • 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 MGSMPAATVD HSQRICEVWA CNLDEEMKKI RQVIRKYNYV AMDTEFPGVV ARPIGEFRSN ADYQYQLLRC NVDLLKIIQL GLTFMNEQGE YPPGTSTWQF NFKFNLTEDM YAQDSIELLT TSGIQFKKHE EEGIETQYFA ELLMTSGVVL CEGVKWLSFH SGYDFGYLIK ILTNSNLPEE ELDFFEILRL FFPVIYDVKY LMKSCKNLKM FFEDHIDDAK YCGHLYGLGS GSSYVQNGTG NAYEEEASKQ 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.

    Cnot7 Mouse
  • View Data Sheet

    Name :

    CCL22 Human, His

    Description:

    Macrophage-Derived Chemokine Human Recombinant (CCL22), His Tag

    C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

    Product # :

    CHM-367

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    • SDS-PAGE

    Description

    MDC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 90 amino acids (25-93 a.a.) and having a molecular mass of 10.3 kDa. The MDC is fused to 21 amino acid His-Tag at N-terminus purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MDC protein contains phosphate-buffered Saline (PBS) pH7.4 and 10% glycerol.

    Purity

    Greater than 95% as determined by Analysis by SDS-PAGE.

    SDS-PAGE

    CCL22 HUMAN, HIS-SDS-PAGE - Product image 1

    More Info

    • Introduction

      MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
      CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
      Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.

    • Synonyms

      C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGPYGANMED SVCCRDYVRY RLPLRVVKHF YWTSDSCPRP GVVLLTFRDK EICADPRVPW VKMILNKLSQ.

    • Background

      What is the molecular weight/Mw of CCL22 HUMAN, HIS Protein?
      CCL22 HUMAN, HIS Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CCL22 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL22 HUMAN, HIS Protein?
      CCL22 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL22 HUMAN, HIS Protein?
      The biological functionality of CCL22 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL22 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGPYGANMED SVCCRDYVRY RLPLRVVKHF YWTSDSCPRP GVVLLTFRDK EICADPRVPW VKMILNKLSQ

      What applications can CCL22 HUMAN, HIS Protein be used in?
      CCL22 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL22 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL22 HUMAN, HIS Protein was purified using conventional chromatography techniques.

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    Mdc Human His
  • View Data Sheet

    Name :

    Myoglobin

    Description:

    Myoglobin Human

    Myoglobin, MB, PVALB, MGC13548.

    Product # :

    PRO-565

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    Description

    Human Myoglobin produced in Human Cardiac Tissues having a molecular mass of 17.5kDa. Myoglobin is released from recently injured myocardial cells within a few hours of Infarction. Peak levels are reached more quickly than CK-MB or Troponin complex.

    Source

    Human Cardiac Tissues.

    Formulation

    The protein solution is in 0.05M phosphate buffer pH 7.5 containing 0.15M NaCl and 0.09% NaN3. Filtered through a 0.2µM membrane.

    Purity

    Greater than 96.0%.

    More Info

    • Introduction

      Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. It is a haemoprotein that contributs to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobin’s molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is uninfluenced by the oxygen pressure in the surrounding tissue. Myoglobin is frequently referred to as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. Myoglobin is responsible for the pigments that make meat red. The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. Myoglobin is found in Type I muscle, Type II A and Type II B, but it is mostly deemed that myoglobin is not found in smooth muscle. Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. Even though the released myoglobin is filtered by the kidneys, it is toxic to the renal tubular epithelium and thus may cause acute renal failure.

    • Synonyms

      Myoglobin, MB, PVALB, MGC13548.

    • Physical Appearance

      Sterile Filtered red solution.

    • Stability

      Human Myoglobin should be stored at 2-8°C.

    • Human Virus Test

      Starting material donor tested and certified negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.

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    Myoglobin Human
  • View Data Sheet

    Name :

    CRTAM Human

    Description:

    Cytotoxic and Regulatory T Cell Molecule Human Recombinant

    Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.

    Product # :

    PRO-2247

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    Description

    CRTAM produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 278 amino acids (18-287 a.a.) and having a molecular mass of 31.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CRTAM is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytotoxic and Regulatory T Cell Molecule, also known as CRTAM belongs to the immunoglobulin superfamily which complies with the structural characteristics of the JAM family and is phylogenetically more closely related to nectin-like proteins. CRTAM is implicated in epithelial cell adhesion. Furthermore, CRTAM interacts with CADM1 as well as promotes natural killer (NK) cell cytotoxicity.

    • Synonyms

      Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.

    • 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

      SLTNHTETIT VEEGQTLTLK CVTSLRKNSS LQWLTPSGFT IFLNEYPALK NSKYQLLHHS ANQLSITVPN VTLQDEGVYK CLHYSDSVST KEVKVIVLAT PFKPILEASV IRKQNGEEHV VLMCSTMRSK PPPQITWLLG NSMEVSGGTL HEFETDGKKC NTTSTLIIHT YGKNSTVDCI IRHRGLQGRK LVAPFRFEDL VTDEETASDA LERNSLSSQD PQQPTSTVSV TEDSSTSEID KEEKEQTTQD PDLTTEANPQ YLGLARKKSG LEHHHHHH.

    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.

    Crtam Human
  • View Data Sheet

    Name :

    C9ORF103 Human

    Description:

    Chromosome 9 Open Reading Frame 103 Human Recombinant

    Chromosome 9 open reading frame 103, bA522I20.2, Gluconate kinase, glucokinase-like protein, probable gluconokinase, GNTK, EC 2.7.1.12.

    Product # :

    PRO-1025

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    Description

    C9ORF103 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (1-187) and having a molecular mass of 23.1kDa.C9ORF103 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The C9ORF103 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      C9orf103 is a member of the gluconokinase gntK/gntV family. C9orf103 takes part in carbohydrate acid metabolism and D-gluconate degradation.

    • Synonyms

      Chromosome 9 open reading frame 103, bA522I20.2, Gluconate kinase, glucokinase-like protein, probable gluconokinase, GNTK, EC 2.7.1.12.

    • 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 MGSHMAAPGA LLVMGVSGSG KSTVGALLAS ELGWKFYDAD DYHPEENRRK MGKGIPLNDQ DRIPWLCNLH DILLRDVASG QRVVLACSAL KKTYRDILTQ GKDGVALKCE ESGKEAKQAE MQLLVVHLSG SFEVISGRLL KREGHFMPPE LLQSQFETL PPAAPENFIQ ISVDKNVSEI IATIMETLKM K

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    C9Orf103 Human
  • View Data Sheet

    Name :

    TFB2M Human

    Description:

    Transcription Factor B2, Mitochondrial Human Recombinant

    Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.

    Product # :

    PRO-1259

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    Description

    TFB2M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (20-396 a.a) and having a molecular mass of 45.8kDa.TFB2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TFB2M protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription Factor B2, Mitochondrial (TFB2M) is an S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. In addition, TFB2M is essential for basal transcription of mitochondrial DNA, most likely via its interaction with POLRMT and TFAM. TFB2M promotes transcription independently of the methyltransferase activity. TFB2M like TFB1M, activates transcription of mitochondrial DNA more effectively, whilst having less methyltransferase activity.

    • Synonyms

      Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.

    • 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 MGSMAGRFCI LGSEAATRKH LPARNHCGLS DSSPQLWPEP DFRNPPRKAS KASLDFKRYV TDRRLAETLA QIYLGKPSRP PHLLLECNPG PGILTQALLE AGAKVVALES DKTFIPHLES LGKNLDGKLR VIHCDFFKLD PRSGGVIKPP AMSSRGLFKN LGIEAVPWTA DIPLKVVGMF PSRGEKRALW KLAYDLYSCT SIYKFGRIEV NMFIGEKEFQ KLMADPGNPD LYHVLSVIWQ LACEIKVLHM EPWSSFDIYT RKGPLENPKR RELLDQLQQK LYLIQMIPRQ NLFTKNLTPM NYNIFFHLLK HCFGRRSATV IDHLRSLTPL DARDILMQIG KQEDEKVVNM HPQDFKTLFE TIERSKDCAY KWLYDETLED R.

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    Tfb2M Human
  • View Data Sheet

    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.

    More Info

    • 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.

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    Cyclophilin F Rat
  • View Data Sheet

    Name :

    MTHFD2 Human

    Description:

    MTHFD2 Human Recombinant

    Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.

    Product # :

    ENZ-853

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    Description

    MTHFD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (30-350) and having a molecular mass of 37.2kDa.MTHFD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MTHFD2 solution (1mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MTHFD2 plays a role as a homodimer which requires magnesium and inorganic phosphate. MTHFD2 has a pseudogene on chromosome 7 and owns 3 different enzymatic activities. Each of the activities catalyzes 1 of 3 sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses.

    • Synonyms

      Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.

    • 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 MGSLAAVRNE AVVISGRKLA QQIKQEVRQE VEEWVASGNK RPHLSVILVG ENPASHSYVL NKTRAAAVVG INSETIMKPA SISEEELLNL INKLNNDDNV DGLLVQLPLP EHIDERRICN AVSPDKDVDG FHVINVGRMC LDQYSMLPAT PWGVWEIIKR TGIPTLGKNV VVAGRSKNVG MPIAMLLHTD GAHERPGGDA TVTISHRYTP KEQLKKHTIL ADIVISAAGI PNLITADMIK EGAAVIDVGI NRVHDPVTAK PKLVGDVDFE GVRQKAGYIT PVPGGVGPMT VAMLMKNTII AAKKVLRLEE REVLKSKELG VATN.

    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.

    Mthfd2 Human
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