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Search results

1000 results found for “methylmalonic aciduria”

Name

Description

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  • View Data Sheet

    Name :

    RARRES1 Human

    Description:

    Retinoic Acid Receptor Responder 1 Human Recombinant

    Retinoic acid receptor responder protein 1 isoform 1, TIG1, Retinoic acid receptor responder protein 1, RAR-responsive protein TIG1, RARRES1, Recombinant Human Retinoic Acid Receptor Responder 1.

    Product # :

    PRO-1514

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    • source
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    Description

    RARRES1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 275 amino acids (43-294) and having a molecular mass of 31.3 kDa. RARRES1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RARRES1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Retinoic Acid Receptor Responder 1 (RARRES1) is a part of the TIGs family. TIGs operate like tumor suppressor genes in human cancers and are greatly expressed in skin, hair follicles and endothelial cells plus in pancreas, spleen and intestine. TIGs are growth regulators which mediate the growth suppressive effects of retinoids.

    • Synonyms

      Retinoic acid receptor responder protein 1 isoform 1, TIG1, Retinoic acid receptor responder protein 1, RAR-responsive protein TIG1, RARRES1, Recombinant Human Retinoic Acid Receptor Responder 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 MGSPDDPGQP QDAGVPRRLL QQAARAALHF FNFRSGSPSA LRVLAEVQEG RAWINPKEGC KVHVVFSTER YNPESLLQEG EGRLGKCSAR VFFKNQKPRP TINVTCTRLI EKKKRQQEDY LLYKQMKQLK NPLEIVSIPD NHGHIDPSLR LIWDLAFLGS SYVMWEMTTQ VSHYYLAQLT SVRQWKTNDD TIDFDYTVLL HELSTQEIIP CRIHLVWYPG KPLKVKYHCQ ELQTPEEASG TEEGSAVVPT ELSNF.

    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.

    Rarres1 Human
  • View Data Sheet

    Name :

    CDHR5 Mouse

    Description:

    Cadherin Related Family Member 5 Mouse Recombinant

    Cadherin-related family member 5, Mu-protocadherin, Cdhr5, Mucdhl, Mupcdh, 1810074H01Rik, AI481143

    Product # :

    PRO-2647

    Price :

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    Description

    CDHR5 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 621 amino acids (29-641 a.a) and having a molecular mass of 66.3kDa.CDHR5 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CDHR5 solution (0.25mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CDHR5, also referred to ascadherin-related family member 5, is a calcium-dependent cell adhesion protein. CDHR5 is located in coated pits, and is expressed during lung and kidney developmentat at the lateral and basal surfaces of epithelia.

    • Synonyms

      Cadherin-related family member 5, Mu-protocadherin, Cdhr5, Mucdhl, Mupcdh, 1810074H01Rik, AI481143

    • 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

      QTQVCSVNQT IFRVEENTTV SEPLVNIFVP DGLHVTLGPL STPYAFRIEG KDLFLNVTPD YEENSLLQAD VECKRGDAVV VRLEVFVAVL DINDNAPKFS FEIKTFNVSE DTKVNTTVIP ETQLKATDAD INDILVYTLQ EVTPNASKFF SLEGVNYPAL KLDQTLDYFK NQNMTFMLLA RDTWEENVEP SHTATATLVL NTLPADLRTP WFLPCSFTDG YVCIHAQYSA VVPTGHKLPS PLIMSPGPIY AVDGDQAINQ SIIYSIIAGN TDGTFIINAH DGNLTMTKSI PSPMKFTLLI RADQEDMAQY SVTQAIVEAR SVTGNPLQFS QSLYYGTVVL GSEAGTAVKD KTFPSEILRI QAQYPGFPDL NSAVTYRVTN SSEFMMNKDI MLTAVPMEEA RTIRVEVEAS NTVTKDTATA VVEIQVSERE LPSTEFPTPP EAGGTTGPSS NTTMEAPLTS GTSQRPATTS SGGSVGPFPP GGTTLRPPTP ASSIPGGSPT LGTSTSPQTT TPGGDSAQTP KPGTSHPTAP TSRTSTSLMT TSSRSDSTQT PKPGTSQPMV PIPGASTSSQ PATPSGSSPQ TPKPGTSQST ATGPISGAGE QGDGQRFSTV DMALEHHHHH H

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

    Cdhr5 Mouse
  • View Data Sheet

    Name :

    MIP 1b Human

    Description:

    Macrophage Inflammatory Protein-1 Beta Human Recombinant (CCL4)

    Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.

    Product # :

    CHM-276

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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

    Description

    Macrophage Inflammatory Protein-1 beta Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7620 Dalton. The CCL4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The Activity is calculated by the ability to chemoattract Human blood monocytes using a concentration of 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.

    Citations

    More Info

    • Introduction

      Macrophage Inflammatory Proteins belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now also named CCL3 and CCL4. Both factors are produced by macrophages after they are stimulated with bacterial endotoxins. MIP-1a and MIP-1b activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. MIP-1a and MIP-1b induce synthesis and release of other pro-inflammatory cytokines such as interleukin-1 (IL-1), IL-6 and TNF-alpha from fibroblasts and macrophages. CCL3 and CCL4 genes are both located on human chromosome 17.

    • Synonyms

      Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL4 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 Macrophage Inflammatory Protein-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Met-Gly-Ser.

    • Background

      What is the molecular weight/Mw of MIP 1B HUMAN Protein?
      MIP 1B HUMAN Protein has a total Mw of 7.62kDa.

      What is the source or expression system of MIP 1B HUMAN Protein?
      Escherichia Coli.

      What is the Purity of MIP 1B HUMAN Protein?
      MIP 1B HUMAN Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1B HUMAN Protein?
      The Activity is calculated by the ability to chemoattract Human blood monocytes using a concentration of 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.

      What is the amino acid sequence of MIP 1B HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Met-Gly-Ser.

      What applications can MIP 1B HUMAN Protein be used in?
      MIP 1B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for MIP 1B HUMAN Protein?
      The endotoxin level is minimal, MIP 1B HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant MIP 1B HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of MIP 1B HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.




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

    Mip 1B Human
  • View Data Sheet

    Name :

    CYB5R2 Human

    Description:

    Cytochrome B5 Reductase 2 Human Recombinant

    CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.

    Product # :

    ENZ-799

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    Quantity :

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    • description
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    Description

    CYB5R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a.) and having a molecular mass of 33.8kDa. CYB5R2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    CYB5R2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cytochrome b5 reductase 2 (CYB5R2) is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. CYB5R2 is responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).

    • Synonyms

      CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMNSRRRE PITLQDPEAK YPLPLIEKEK ISHNTRRFRF GLPSPDHVLG LPVGNYVQLL AKIDNELVVR AYTPVSSDDD RGFVDLIIKI YFKNVHPQYP EGGKMTQYLE NMKIGETIFF RGPRGRLFYH GPGNLGIRPD QTSEPKKTLA DHLGMIAGGT GITPMLQLIR HITKDPSDRT RMSLIFANQT EEDILVRKEL EEIARTHPDQ FNLWYTLDRP PIGWKYSSGF VTADMIKEHL PPPAKSTLIL VCGPPPLIQT AAHPNLEKLG YTQDMIFTY.

    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.

    Cyb5R2 Human
  • View Data Sheet

    Name :

    HPGD Mouse

    Description:

    Hydroxyprostaglandin Dehydrogenase 15-(NAD) Mouse Recombinant

    15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC:1.1.1.141), 15-PGDH, Hpgd, Pgdh1, Prostaglandin dehydrogenase 1.

    Product # :

    ENZ-1027

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    Description

    HPGD Mouse Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (1-269) and having a molecular mass of 31.6kDa. HPGD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The HPGD solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HPGD is the essential enzyme of prostaglandin degradation. 15-PGDH protein strongly decreases the biologic activity of these molecules by catalyzing the oxidation of the 15-hydroxyl group of prostaglandins to a keto group. GDH1 is involved in numerous physiologic and cellular processes, for instance inflammation.

    • Synonyms

      15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC:1.1.1.141), 15-PGDH, Hpgd, Pgdh1, Prostaglandin dehydrogenase 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 MGSMHVNGKV ALVTGAAQGI GKAFAEALLL HGAKVALVDW NLEAGVKCKA ALDEQFEPQK TLFVQCDVAD QKQLRDTFRK VVDHFGRLDI LVNNAGVNNE KNWEQTLQIN LVSVISGTYL GLDYMSKQNG GEGGIIINMS SLAGLMPVAQ QPVYCASKHG IIGFTRSAAM AANLMKSGVR LNVICPGFVD TPILESIEKE ENMGQYIEYK DQIKAMMKFY GVLHPSTIAN GLINLIEDDA LNGAIMKITA SKGIHFQDYD ISPLLVKAPL TS.

    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.

    Hpgd Mouse
  • View Data Sheet

    Name :

    NDUFS4 Human

    Description:

    Histidine NADH Dehydrogenase Fe-S Protein 4 Human Recombinant

    AQDQ, NDUFS4, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 mitochondrial, NADH-ubiquinone oxidoreductase 18 kDa subunit, Complex I-18 kDa, CI-18 kDa, Complex I-AQDQ, CI-AQDQ.

    Product # :

    ENZ-421

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    Description

    NDUFS4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (43-175 a.a.) and having a molecular mass of 15.5 kDa.The NDUFS4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFS4 solution contains 20mM Tris pH-8 & 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NDUFS4 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), the primary multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I is involved in cellular ATP production, the main source of energy for numerous vital processes in living cells. NDUFS4 removes electrons from NADH and passes them by a series of diverse protein-coupled redox centers to the electron acceptor ubiquinone. NDUFS4 presents a hotspot of mutations in the genetic apparatus of oxidative phosphorylation and the correct assembly of the subunit it encodes is essential for completion of the assembly of complex I.

    • Synonyms

      AQDQ, NDUFS4, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 mitochondrial, NADH-ubiquinone oxidoreductase 18 kDa subunit, Complex I-18 kDa, CI-18 kDa, Complex I-AQDQ, CI-AQDQ.

    • 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

      MAQDQTQDTQ LITVDEKLDI TTLTGVPEEH IKTRKVRIFV PARNNMQSGV NNTKKWKMEF DTRERWENPL MGWASTADPL SNMVLTFSTK EDAVSFAEKN GWSYDIEERK VPKPKSKSYG ANFSWNKRTR VSTK.

    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.

    Ndufs4 Human
  • View Data Sheet

    Name :

    STAMBP Human

    Description:

    STAM Binding Protein Human Recombinant

    STAM-binding protein, Associated molecule with the SH3 domain of STAM, Endosome-associated ubiquitin isopeptidase, AMSH, EC 3.1.2.15, EC 3.4.19, MICCAP.

    Product # :

    PRO-017

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    Description

    STAMBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424) and having a molecular mass of 50kDa. STAMBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE..

    Citations

    More Info

    • Introduction

      STAM Binding Protein (STAMBP) is a zinc metalloprotease which specifically cleaves Lys-63-linked polyubiquitin chains, however it doesn’t cleave Lys-48-linked polyubiquitin chains. STAMBP has a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. In addition, STAMBP potentiates BMP signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. STAMBP also has a major role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is essential for efficient EGFR degradation but not for its internalization. STAMBP is also involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.

    • Synonyms

      STAM-binding protein, Associated molecule with the SH3 domain of STAM, Endosome-associated ubiquitin isopeptidase, AMSH, EC 3.1.2.15, EC 3.4.19, MICCAP.

    • 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 MGSMSDHGDV SLPPEDRVRA LSQLGSAVEV NEDIPPRRYF RSGVEIIRMA SIYSEEGNIE HAFILYNKYI TLFIEKLPKH RDYKSAVIPE KKDTVKKLKE IAFPKAEELK AELLKRYTKE YTEYNEEKKK EAEELARNMA IQQELEKEKQ RVAQQKQQQL EQEQFHAFEE MIRNQELEKE RLKIVQEFGK VDPGLGGPLV PDLEKPSLDV FPTLTVSSIQ PSDCHTTVRP AKPPVVDRSL KPGALSNSES IPTIDGLRHV VVPGRLCPQF LQLASANTAR GVETCGILCG KLMRNEFTIT HVLIPKQSAG SDYCNTENEE ELFLIQDQQG LITLGWIHTH PTQTAFLSSV DLHTHCSYQM MLPESVAIVC SPKFQETGFF KLTDHGLEEI SSCRQKGFHP HSKDPPLFCS CSHVTVVDRA VTITDLR.

    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.

    Stambp Human
  • View Data Sheet

    Name :

    STRADA Human

    Description:

    STE20-Related Kinase Adaptor Alpha Human Recombinant

    LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.

    Product # :

    PRO-1992

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    Description

    STRADA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314a.a) and having a molecular mass of 37kDa. STRADA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      STE20-Related Kinase Adaptor Alpha (STRADA) is a part of the STE- 20 like kinase family which stimulates MAPK pathways by activating MAPKKK. STRADA is an upstream activator of LKB1 and also leads the sub-cellular localization of LKB1 by fixing it in the cytoplasm. The interaction between STRADA-LKB1 leads to phosphorylation of STRADA and enhanced autophosphorylation of LKB1.

    • Synonyms

      LYK5, NY-BR-96, PMSE, Stlk, STRAD, STE20-related kinase adapter protein alpha, STRAD alpha, STE20-related adapter protein, Serologically defined breast cancer antigen NY-BR-96, STRADA.

    • 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 MGSMSFLVSK PERIRTNDAS SESIASFSKQ EVMSSFLPEG GCYELLTVIG KGFEDLMTVN LARYKPTGEY VTVRRINLEA CSNEMVTFLQ GELHVSKLFN HPNIVPYRAT FIADNELWVV TSFMAYGSAK DLICTHFMDG MNELAIAYIL QGVLKALDYI HHMGYVHRSV KASHILISVD GKVYLSGLRS NLSMISHGQR QRVVHDFPKY SVKVLPWLSP EVLQQNLQGY DAKSDIYSVG ITACELANGH VPFKDMPATQ MLLEKLNGTV PCLLDTSTIP AEELTMSPSR SVANSGLSDS LTTSTPRPSN GPVPAPS.

    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.

    Strada Human
  • View Data Sheet

    Name :

    OTUB2 Human

    Description:

    Ubiquitin Aldehyde Binding 2 Human Recombinant

    Ubiquitin thioesterase OTUB2, Deubiquitinating enzyme OTUB2, OTU domain-containing ubiquitin aldehyde-binding protein 2, Otubain-2, Ubiquitin-specific-processing protease OTUB2, OTUB2, C14orf137, OTB2, OTU2.

    Product # :

    PRO-214

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    Description

    OTUB2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 254 amino acids (1-234 a.a.) and having a molecular mass of 29.4kDa.OTUB2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OTUB2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ubiquitin thioesterase OTUB2 (OTUB2) is a member of the peptidase C65 family. OTUB2 functions as a hydrolase which can remove conjugated ubiquitin from proteins in vitro and may thus play a key regulatory role at the level of protein turnover by preventing degradation.

    • Synonyms

      Ubiquitin thioesterase OTUB2, Deubiquitinating enzyme OTUB2, OTU domain-containing ubiquitin aldehyde-binding protein 2, Otubain-2, Ubiquitin-specific-processing protease OTUB2, OTUB2, C14orf137, OTB2, OTU2.

    • 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 MSETSFNLIS EKCDILSILR DHPENRIYRR KIEELSKRFT AIRKTKGDGN CFYRALGYSY LESLLGKSRE IFKFKERVLQ TPNDLLAAGF EEHKFRNFFN AFYSVVELVE KDGSVSSLLK VFNDQSASDH IVQFLRLLTS AFIRNRADFF RHFIDEEMDI KDFCTHEVEP MATECDHIQI TALSQALSIA LQVEYVDEMD TALNHHVFPE AATPSVYLLY KTSHYNILYA ADKH.

    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.

    Otub2 Human
  • View Data Sheet

    Name :

    CBX3 Human

    Description:

    Chromobox Homolog 3 Human Recombinant

    Chromobox homolog 3 (Drosophila HP1 gamma), Heterochromatin protein 1 homolog gamma, Modifier 2 protein, HP1 gamma homolog, HECH, HP1Hs-gamma.

    Product # :

    PRO-1057

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    Description

    CBX3 Human Recombinant produced in E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.4kDa.CBX3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CBX3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CBX3 takes part in transcriptional silencing in heterochromatin-like complexes. CBX3 identifies and binds histone H3 tails methylated at 'Lys-9', thereby create an epigenetic repression. Additionally, CBX3 takes part in the formation of functional kinetochore by interacting with MIS12 complex proteins.

    • Synonyms

      Chromobox homolog 3 (Drosophila HP1 gamma), Heterochromatin protein 1 homolog gamma, Modifier 2 protein, HP1 gamma homolog, HECH, HP1Hs-gamma.

    • 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 MGSHMASNKT TLQKMGKKQN GKSKKVEEAE PEEFVVEKVL DRRVVNGKVE YFLKWKGFTD ADNTWEPEEN LDCPELIEAF LNSQKAGKEK DGTKRKSLSD SESDDSKSKK KRDAADKPRG FARGLDPERI IGATDSSGEL MFLMKWKDSD EADLVLAKEA NMKCPQIVIA FYEERLTWHS CPEDEAQ.

    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.

    Cbx3 Human
  • View Data Sheet

    Name :

    CCDC25 Human

    Description:

    Coiled-Coil Domain Containing 25 Human Recombinant

    Coiled-coil domain-containing protein 25, CCDC25.

    Product # :

    PRO-1655

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    Description

    CCDC25 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-208 a.a) and having a molecular mass of 26.9kDa.CCDC25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CCDC25 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Coiled-Coil Domain Containing 25 (CCDC25) is a 208 amino acid protein belonging to the CCDC25 family.

    • Synonyms

      Coiled-coil domain-containing protein 25, CCDC25.

    • 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 MGSMVFYFTS SSVNSSAYTI YMGKDKYENE DLIKHGWPED IWFHVDKLSS AHVYLRLHKG ENIEDIPKEV LMDCAHLVKA NSIQGCKMNN VNVVYTPWSN LKKTADMDVG QIGFHRQKDV KIVTVEKKVN EILNRLEKTK VERFPDLAAE KECRDREERN EKKAQIQEMK KREKEEMKKK REMDELRSYS SLMKVENMSS NQDGNDSDEF M.

    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.

    Ccdc25 Human
  • View Data Sheet

    Name :

    CCL16 Human

    Description:

    LEC/NCC-4 Human Recombinant

    C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.

    Product # :

    CHM-237

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    Description

    CCL16 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids and having a molecular mass of 11.2 kDa. The CCL16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL16 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.

    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 total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    Citations

    More Info

    • Introduction

      Human CCL16, also called HCC-4, liver-expressed chemokine (LEC), and lymphocyte and monocyte chemoattractant (LMC), is a novel CC chemokine recognized by bioinformatics. NCC-4 cDNA encodes a 120 amino acids along with a 23 amino acids signal peptide that is cleaved to generate 97 amino acid protein. HCC4 is vaguely related to other CC chemokines, showing less than 30% sequence identity. Among CC chemokines, CCL-16 has the largest similarity to HCC-1. 2 potential polyadenylation signals are present on the human HCC-4 gene, and as a result, 2 transcripts containing roughly 1,500 base pairs and 500 base pairs have been detected. HCC-4 is expressed weakly by some lymphocytes, including NK cells, T cells, and some T cell clones. The expression of HCC-4 in monocytes is greatly upregulated in the presence of IL-10.
      CCL16 shows chemotactic activity for lymphocytes and monocytes rather than to neutrophils. NCC-4 has potent myelosuppressive activity, suppresses proliferation of myeloid progenitor cells. CCL16 demonstrates chemotactic activity for monocytes and thp-1 monocytes, rather than for resting lymphocytes and neutrophils. HCC-4 induces a calcium flux in thp-1 cells that desensitized prior to the expression of rantes.

    • Synonyms

      C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL16 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 CCL16in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

    • Background

      What is the molecular weight/Mw of CCL16 HUMAN Protein?
      CCL16 HUMAN Protein has a total Mw of 11.2kDa.

      What is the source or expression system of CCL16 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL16 HUMAN Protein?
      CCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL16 HUMAN Protein?
      Determined by its ability to chemoattract total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL16 HUMAN Protein?
      QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

      What applications can CCL16 HUMAN Protein be used in?
      CCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL16 HUMAN Protein?
      The endotoxin level is minimal, CCL16 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL16 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL16 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Ccl16 Human
  • View Data Sheet

    Name :

    PKM2 Human

    Description:

    Tumor Type M2 Pyruvate Kinase Human Recombinant

    Pyruvate kinase isozymes M1/M2, EC 2.7.1.40, Pyruvate kinase muscle isozyme, Pyruvate kinase 2/3, Cytosolic thyroid hormone-binding protein, CTHBP, THBP1, M2PK, PKM2, PK3, PK2, PKM, TCB, OIP3, MGC3932, Tumor Type M2 Pyruvate Kinase.

    Product # :

    PKA-339

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    Description

    PKM2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 551 amino acids (1-531 a.a.) and having a molecular mass of 60.1kDa. The PKM2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PKM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The Specific activity is > 25,000 pmol/min/ug. 1 unit will form 1pmol of phospho(enol)pyruvate to pyruvate per minute at pH 7.5 at 37°C.

    Citations

    More Info

    • Introduction

      Pyruvate kinase is a key enzyme in the glycolytic pathway. The M2 isoenzyme of pyruvate kinase is specifically expressed at high levels in tumor cells, and can be measured in plasma of patients with advanced breast cancer. The marker is useful for measuring disease activity, sensitivity to chemotherapy and recurrence.

    • Synonyms

      Pyruvate kinase isozymes M1/M2, EC 2.7.1.40, Pyruvate kinase muscle isozyme, Pyruvate kinase 2/3, Cytosolic thyroid hormone-binding protein, CTHBP, THBP1, M2PK, PKM2, PK3, PK2, PKM, TCB, OIP3, MGC3932, Tumor Type M2 Pyruvate Kinase.

    • 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 MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE ATAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P.

    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.

    Pkm2 Human
  • View Data Sheet

    Name :

    TPK1 Human

    Description:

    Thiamin Pyrophosphokinase 1 Human Recombinant

    Thiamin pyrophosphokinase 1, hTPK1, Placental protein 20, PP20, Thiamine pyrophosphokinase 1, TPK1, THMD5.

    Product # :

    PKA-023

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    Description

    TPK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-243 a.a.) and having a molecular mass of 29.8kDa.TPK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPK1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thiamin pyrophosphokinase 1 (TPK1) is a homodimer which catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. TPK1 is found in the heart, kidney, testis, small intestine and peripheral blood leukocytes, and at very low levels in a variety of tissues. TPK1 gene defects cause the thiamine metabolism dysfunction syndrome type 5, episodic encephalopathy type (THMD5), which is an autosomal recessive metabolic disorder due to an inborn error of thiamine metabolism.

    • Synonyms

      Thiamin pyrophosphokinase 1, hTPK1, Placental protein 20, PP20, Thiamine pyrophosphokinase 1, TPK1, THMD5.

    • 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 MGSHMEHAFT PLEPLLSTGN LKYCLVILNQ PLDNYFRHLW NKALLRACAD GGANRLYDIT EGERESFLPE FINGDFDSIR PEVREYYATK GCELISTPDQ DHTDFTKCLK MLQKKIEEKD LKVDVIVTLG GLAGRFDQIM ASVNTLFQAT HITPFPIIII
      QEESLIYLLQ PGKHRLHVDT GMEGDWCGLI PVGQPCMQVT TTGLKWNLTN DVLAFGTLVS TSNTYDGSGV VTVETDHPLL WTMAIKS.

    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.

    Tpk1 Human
  • View Data Sheet

    Name :

    ldhA E. coli

    Description:

    Fermentative D-lactate Dehydrogenase, NAD-Dependent E.Coli Recombinant

    D-lactate dehydrogenase, D-LDH, Fermentative lactate dehydrogenase, ldhA, hslI, htpH, b1380, JW1375.

    Product # :

    ENZ-632

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    Description

    ldhA E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1kDa.ldhA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ldhA solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      D-lactate dehydrogenase (ldha) is a member of the D-isomer specific 2-hydroxyacid dehydrogenase family. In enzymology, an ldha (cytochrome) is an enzyme which catalyzes the chemical reaction. Therefore, the 2 substrates of the ldha enzyme are (D)-lactate and ferricytochrome c, whereas its 2 products are pyruvate and ferrocytochrome c.

    • Synonyms

      D-lactate dehydrogenase, D-LDH, Fermentative lactate dehydrogenase, ldhA, hslI, htpH, b1380, JW1375.

    • 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 MGSHMKLAVY STKQYDKKYL QQVNESFGFE LEFFDFLLTE KTAKTANGCE AVCIFVNDDG SRPVLEELKK HGVKYIALRC AGFNNVDLDA AKELGLKVVR VPAYDPEAVA EHAIGMMMTL NRRIHRAYQR TRDANFSLEG LTGFTMYGKT AGVIGTGKIG VAMLRILKGF GMRLLAFDPY PSAAALELGV EYVDLPTLFS ESDVISLHCP LTPENYHLLN EAAFEQMKNG VMIVNTSRGA LIDSQAAIEA LKNQKIGSLG MDVYENERDL FFEDKSNDVI QDDVFRRLSA CHNVLFTGHQ AFLTAEALTS ISQTTLQNLS NLEKGETCPN ELV.

    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.

    Ldha E Coli
  • View Data Sheet

    Name :

    GSTM4 Human

    Description:

    Glutathione S-Transferase MU 4 Human Recombinant

    Glutathione S-transferase Mu 4, EC=2.5.1.18, GST class-mu 4, GST-Mu2, GSTM4-4, GSTM4, GTM4, GSTM4-4, MGC9247, MGC131945.

    Product # :

    ENZ-492

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    Description

    GSTM4 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 27.7 kDa. The GSTM4 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTM4 Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.05M NaCl & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GSTM4 is part of the glutathione s-transferase (GST) family of proteins. There are eight families of GST proteins, namely alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have a variety of functions throughout the cell. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione.

    • Synonyms

      Glutathione S-transferase Mu 4, EC=2.5.1.18, GST class-mu 4, GST-Mu2, GSTM4-4, GSTM4, GTM4, GSTM4-4, MGC9247, MGC131945.

    • 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 MSMTLGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL ENQAMDVSNQ LARVCYSPDF EKLKPEYLEE LPTMMQHFSQ FLGKRPWFVG DKITFVDFLA YDVLDLHRIF EPNCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPKPLYT RVAVWGNK.

    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.

    Gstm4 Human
  • View Data Sheet

    Name :

    COMMD6 Human

    Description:

    COMM Domain Containing 6 Human Recombinant

    COMM domain-containing protein 6, COMM Domain Containing 6, COMMD6, MSTP076, COMM domain-containing protein 6 isoform b, Acrg.

    Product # :

    PRO-2052

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    Description

    COMMD6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 108 amino acids (1-85) and having a molecular mass of 12kDa.COMMD6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The COMMD6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      COMM Domain Containing (COMMD6) which is a part of the NF-kappa-B -inhibiting proteins, contains one COMM domain. COMMD6 down-regulates the activation of NF-kappa-B and inhibits TNF-induced NFKB1 activation.

    • Synonyms

      COMM domain-containing protein 6, COMM Domain Containing 6, COMMD6, MSTP076, COMM domain-containing protein 6 isoform b, Acrg.

    • 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 MGSMEASSEP PLDAKSDVTN QLVDFQWKLG MAVSSDTCRS LKYPYVAVML KVADHSGQVK TKCFEMTIPQ FQNFYRQFKE IAAVIETV.

    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.

    Commd6 Human
  • View Data Sheet

    Name :

    CCL2 Human

    Description:

    Monocyte Chemotactic Protein-1 Human Recombinant (CCL2)

    Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

    Product # :

    CHM-271

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    Description

    Monocyte Chemotactic Protein-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 76 amino acids and having a molecular mass of 8.6kDa. The MCP-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCL2 was lyophilized from a concentrated (1mg/ml) sterile solution without any additives.

    Purity

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

    Biological Activity

    The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/ml.

    Citations

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.

    • Synonyms

      Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCP-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL2 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 Monocyte Chemotactic Protein-1in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.

    • Background

      What is the molecular weight/Mw of CCL2 HUMAN Protein?
      CCL2 HUMAN Protein has a total Mw of 8.6kDa.

      What is the source or expression system of CCL2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL2 HUMAN Protein?
      CCL2 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL2 HUMAN Protein?
      The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/ml.

      What is the amino acid sequence of CCL2 HUMAN Protein?
      QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.

      What applications can CCL2 HUMAN Protein be used in?
      CCL2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL2 HUMAN Protein?
      The endotoxin level is minimal, CCL2 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL2 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL2 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Mcp 1 Human
  • View Data Sheet

    Name :

    CCL12 Mouse

    Description:

    Monocyte Chemotactic Protein-5 Mouse Recombinant (CCL12)

    C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.

    Product # :

    CHM-266

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    Description

    MCP-5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 82 amino acids and having a molecular mass of 9.3kDa. The MCP5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    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 human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.

    Citations

    More Info

    • Introduction

      MCP-5 (CCL12) is a cloned mouse CC chemokine most closely related to human MCP1 (66% amino acid sequence identity in the mature protein). MCP5 is expressed constitutively in the thymus and the lymph nodes. Under inflammatory conditions, moreover CCL12 expression is induced in activated macrophages and mast cells. The mouse MCP1 gene is mapped to the CC chemokine cluster on chromosome 11. Recombinant CCL12 is a potent chemoattractant for monocytes and lymphocytes but not neutrophils. At high concentrations, MCP-5 also chemoattracts eosinophils. CCL12 is a functional ligand for CCR2.

    • Synonyms

      C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP5 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 MCP5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.

    • Background

      What is the molecular weight/Mw of CCL12 MOUSE Protein?
      CCL12 MOUSE Protein has a total Mw of 9.3kDa.

      What is the source or expression system of CCL12 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL12 MOUSE Protein?
      CCL12 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL12 MOUSE Protein?
      Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.

      What is the amino acid sequence of CCL12 MOUSE Protein?
      GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.

      What applications can CCL12 MOUSE Protein be used in?
      CCL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL12 MOUSE Protein?
      The endotoxin level is minimal, CCL12 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL12 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL12 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Mcp 5 Mouse
  • View Data Sheet

    Name :

    CPOX Human

    Description:

    Coproporphyrinogen Oxidase Human Recombinant

    CPO, CPX, HCP, Coproporphyrinogen-III oxidase, mitochondrial, COX, Coprogen oxidase, Coproporphyrinogenase, CPOX.

    Product # :

    ENZ-701

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    Description

    CPOX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (111-454) and having a molecular mass of 41.6kDa. CPOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Coproporphyrinogen Oxidase (CPOX) which is localized to the internal membrane space of erythrocytes takes part in the 6th phase of heme biosynthesis. CPOX catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III. Mutations in human CPOX gene forecast the clinical result of the disease, with either hepatic hereditary coproporphyria or hematological manifestations of erythropoietic harderoporphyria.

    • Synonyms

      CPO, CPX, HCP, Coproporphyrinogen-III oxidase, mitochondrial, COX, Coprogen oxidase, Coproporphyrinogenase, CPOX.

    • 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 MGSTSLGRPE EEEDELAHRC SSFMAPPVTD LGELRRRPGD MKTKMELLIL ETQAQVCQAL AQVDGGANFS VDRWERKEGG GGISCVLQDG CVFEKAGVSI SVVHGNLSEE AAKQMRSRGK VLKTKDGKLP FCAMGVSSVI HPKNPHAPTI HFNYRYFEVE EADGNKQWWF GGGCDLTPTY LNQEDAVHFH RTLKEACDQH GPDLYPKFKK WCDDYFFIAH RGERRGIGGI FFDDLDSPSK EEVFRFVQSC ARAVVPSYIP LVKKHCDDSF TPQEKLWQQL RRGRYVEFNL LYDRGTKFGL FTPGSRIESI LMSLPLTARW EYMHSPSENS KEAEILEVLR HPRDWVR.

    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.

    Cpox Human
  • View Data Sheet

    Name :

    HTF Human

    Description:

    Holo Transferrin Human

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    Product # :

    PRO-315

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    Description

    Human Holo Transferrin is a glycoprotein of approximately 77 kDa.

    Source

    Human serum.

    Formulation

    The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
    May contain traces of buffer salts.

    Purity

    Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

    Citations

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.

    • Iron Content

      The Iron content was estimated by ICP and was found to be 1232 ppm.

    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.

    Holo Transferrin Human
  • View Data Sheet

    Name :

    ALDOC Human, His

    Description:

    Aldolase C Fructose-Bisphosphate Human Recombinant, His Tag

    Fructose-bisphosphate aldolase C, Brain-type aldolase, ALDOC, ALDC.

    Product # :

    ENZ-085

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    Description

    ALDOC Human Recombinant fused to a 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 384 amino acids (1-364 a.a) and having a molecular mass of 41.6 kDa. The ALDOC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ALDOC 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.

    Citations

    More Info

    • Introduction

      Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.

    • Synonyms

      Fructose-bisphosphate aldolase C, Brain-type aldolase, ALDOC, ALDC.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA NHAY.

    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.

    Aldoc Human
  • View Data Sheet

    Name :

    TACO1 Human

    Description:

    Translational Activator of Mitochondrially Encoded Cytochrome C Oxidase Human Recombinant

    Translational Activator Of Mitochondrially Encoded Cytochrome C Oxidase, CCDC44, Coiled-Coil Domain-Containing Protein 44, Coiled-Coil Domain Containing 44, Clone HQ0477 PRO0477p, Translational Activator Of Cytochrome C Oxidase 1, Translational Activator Of Mitochondrially-Encoded Cytochrome C Oxidase I.

    Product # :

    PRO-1746

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    Description

    TACO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (61-297 a.a) and having a molecular mass of 28.8kDa.TACO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TACO1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Translational activator of mitochondrially encoded cytochrome c oxidase I (TACO1) belongs to the TACO1 family. TACO1 is a mitochondrial protein which functions as a translational activator of mitochondrially-encoded cytochrome c oxidase 1. Mutations in this gene are associated with Leigh syndrome.

    • Synonyms

      Translational Activator Of Mitochondrially Encoded Cytochrome C Oxidase, CCDC44, Coiled-Coil Domain-Containing Protein 44, Coiled-Coil Domain Containing 44, Clone HQ0477 PRO0477p, Translational Activator Of Cytochrome C Oxidase 1, Translational Activator Of Mitochondrially-Encoded Cytochrome C Oxidase I.

    • 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 MGSNKWSKVR HIKGPKDVER SRIFSKLCLN IRLAVKEGGP NPEHNSNLAN ILEVCRSKHM PKSTIETALK MEKSKDTYLL YEGRGPGGSS LLIEALSNSS HKCQADIRHI LNKNGGVMAV GARHSFDKKG VIVVEVEDRE KKAVNLERAL EMAIEAGAEDVKETEDEEER NVFKFICDAS SLHQVRKKLD SLGLCSVSCA LEFIPNSKVQ LAEPDLEQAA HLIQALSNHE DVIHVYDNIE

    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.

    Taco1 Human
  • View Data Sheet

    Name :

    F7 Human

    Description:

    Coagulation Factor VIIa Human Recombinant

    Coagulation factor VII, EC 3.4.21.21, Serum prothrombin conversion accelerator, SPCA, Proconvertin, Eptacog alfa, F7.

    Product # :

    PRO-331

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    Description

    Factor VIIa Human Recombinant produced in BHK is a glycosylated polypeptide two-chain dimer consisting of 406 amino acids with a molecular weight of 50kD.The Factor-VIIa is purified by proprietary chromatographic techniques.

    Source

    BHK cells (Baby Hamster Kidney Cells).

    Formulation

    The protein 1 mg/ml was lyophilized after from a sterile solution containing 10mg sucrose pH-6.

    Purity

    Greater than 98.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The potency per mg was tested and found to be 50,000Units/mg.

    Citations

    More Info

    • Introduction

      Coagulation factor VII is a vitamin K-dependent factor which is essential for hemostasis. It circulates in the blood as a zymogen which is later converted to an active form by factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of factor VII, a heavy chain with a catalytic domain and a light chain with 2 EGF-like domains are generated, and the two chains are held together by a disulfide bond. The presence of factor III and calcium ions further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Alternative splicing of factor VII results in 2 transcripts. Defects in coagulation factor VII can cause coagulopathy. Coagulation factor VII initiates the extrinsic pathway of blood coagulation. Minor proteolysis converts factor VII to factor VIIa by factors Xa, XIIa, IXa, or thrombin. Factor VIIa also converts factor IX to factor IXa in the presence of tissue factor and calcium.

    • Synonyms

      Coagulation factor VII, EC 3.4.21.21, Serum prothrombin conversion accelerator, SPCA, Proconvertin, Eptacog alfa, F7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    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.

    Factor Viia Human
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