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Search results

1000 results found for “PCNA”

Name

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  • View Data Sheet

    Name :

    SPARC Mouse

    Description:

    Secreted Protein Acidic & Rich in Cysteine Mouse Recombinant

    Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine

    Product # :

    PRO-2658

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    Description

    SPARC Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (18-302a.a) and having a molecular mass of 33.3kDa.SPARC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Secreted Protein Acidic & Rich in Cysteine (SPARC) protein is coded by the SPARC gene in humans. SPARC is a glycoprotein located in bones that binds to calcium. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, mainly in areas of tissue morphogenesis and remodelling. Asides from calcium, SPARC can also bind to collagen.

    • Synonyms

      Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine

    • 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

      APQQTEVAEE IVEEETVVEE TGVPVGANPV QVEMGEFEDG AEETVEEVVA DNPCQNHHCK HGKVCELDES NTPMCVCQDP TSCPAPIGEF EKVCSNDNKT FDSSCHFFAT KCTLEGTKKG HKLHLDYIGP CKYIAPCLDS ELTEFPLRMR DWLKNVLVTL YERDEGNNLL TEKQKLRVKK IHENEKRLEA GDHPVELLAR DFEKNYNMYI FPVHWQFGQL DQHPIDGYLS HTELAPLRAP LIPMEHCTTR FFETCDLDND KYIALEEWAG CFGIKEQDIN KDLVIHHHHH 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.

    Sparc Mouse
  • View Data Sheet

    Name :

    NT-proBNP Human

    Description:

    NT-Pro-B-type Natriuretic Protein Human Recombinant

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    Product # :

    CYT-1118

    Price :

    Quantity :

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    • sds-page

    Description

    NT-Pro-B-type Natriuretic Protein Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 76 amino acid and having a molecular mass of approximately 8.5kDa. NT-proBNP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0 and 150mM NaCl.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    sds-page

    NT-ProBNP sds-page - Product image 1

    More Info

    • Introduction

      Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis,vasorelaxation,diuresis and inhibition of renin and aldosterone secretion. BNP plays a key role in cardiovascular homeostasis. BNP also helps restore the body's salt and water balance andimproves heart function.

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HPLGSPGSAS DLETSGLQEQ RNHLQGKLSE LQVEQTSLEP LQESPRPTGV WKSREVATEG IRGHRKMVLY TLRAPR.

    • Background

      What is the molecular weight / Mw of NT-proBNP?
      NT-proBNP has a total Mw of 8.5kDa.

      What is the source or expression system of NT-proBNP?
      Escherichia Coli.

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

      What is the Biological Activity of NT-proBNP?
      The biological functionality of NT-proBNP will be determined in the future.

      What is the amino acid sequence of NT-proBNP?
      HPLGSPGSAS DLETSGLQEQ RNHLQGKLSE LQVEQTSLEP LQESPRPTGV WKSREVATEG IRGHRKMVLY TLRAPR.

      What applications can NT-proBNP be used in?
      NT-proBNP can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for NT-proBNP?
      The endotoxin level is minimal, NT-proBNP 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.

    Nt Probnp Human
  • View Data Sheet

    Name :

    NUCB2 Mouse

    Description:

    Nucleobindin-2 Mouse Recombinant

    Nefa, Calnuc, AI607786, Nucleobindin-2, DNA-binding protein NEFA, Nucb2.

    Product # :

    PRO-605

    Price :

    Quantity :

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    • description
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    Description

    NUCB2 Mouse Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain (amino acids 25-420) containing 417 amino acids and having a molecular mass of 49kDa.NUCB2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleobindin-2 (NUCB2) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 is localized in neuronal perikarya and dendrites of mouse brain.

    • Synonyms

      Nefa, Calnuc, AI607786, Nucleobindin-2, DNA-binding protein NEFA, Nucb2.

    • 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 MVPIDVDKTK VHNTEPVENA RIEPPDTGLY YDEYLKQVIE VLETDPHFRE KLQKADIEEI RSGRLSQELD LVSHKVRTRL DELKRQEVGR LRMLIKAKLD ALQDTGMNHH LLLKQFEHLN HQNPNTFESR DLDMLIKAAT ADLEQYDRTR HEEFKKYEMMKEHERREYLK TLSEEKRKEE ESKFEEMKRK HEDHPKVNHP GSKDQLKEVW EETDGLDPND FDPKTFFKLH DVNNDGFLDE QELEALFTRE LEKVYNPQNA EDDMIEMEEE RLRMREHVMS EIDNNKDRLV TLEEFLRATE KKEFLEPDSW ETLDQQQLFT EDELKEYESI IAIQENELKKRAEELQKQKE DLQRQHDHLE AQKQEYHQAV QHLEQKKLQQ GIAPSGPAGE LKFEPHT.

    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.

    Nucb2 Mouse
  • View Data Sheet

    Name :

    CXCL5 Rat

    Description:

    Epithelial Neutrophil-Activating Protein 78 Rat Recombinant (CXCL5)

    C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

    Product # :

    CHM-267

    Price :

    Quantity :

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    • description
    • source
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    • More Info

    Description

    Epithelial Neutrophil-Activating Protein 78 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids and having a molecular mass of 10.0kDa.The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) 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 neutrophils using a concentration range of 10.0-100.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.

    • Synonyms

      C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ENA-78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.

    • Background

      What is the molecular weight/Mw of CXCL5 RAT Protein?
      CXCL5 RAT Protein has a total Mw of 10.0kDa.

      What is the source or expression system of CXCL5 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 RAT Protein?
      CXCL5 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 RAT Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

      What is the amino acid sequence of CXCL5 RAT Protein?
      APFSAMVATE LRCVCLTLAP RINPKMIANL EVIPAGPHCP KVEVIAKLKN QKDNVCLDPQ APLIKKVIQK ILGSENKKTK RNALALVRSA STQ.

      What applications can CXCL5 RAT Protein be used in?
      CXCL5 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 RAT Protein?
      The endotoxin level is minimal, CXCL5 RAT 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.

    Ena 78 Rat
  • View Data Sheet

    Name :

    FAM84A Human

    Description:

    Family with Sequence Similarity 84, Member A Human Recombinant

    Family with Sequence Similarity 84 Member A, Neurological/Sensory 1, Neurologic Sensory Protein 1, NSE1, PP11517, Protein FAM84A.

    Product # :

    PRO-1610

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    Description

    FAM84A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 34.9kDa.FAM84A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FAM84A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      FAM84A is a member of the FAM84 family of proteins and is primarily expressed in testis. FAM84A is restricted to a subcellular membrane region in which there is no interaction between adjoining cells and takes part in cell morphology. Additionally, FAM84A expression increases cell motility which can result in invasion and metastasis of cancer cells. FAM84A is up-regulated in pancreatic cancer, colorectal cancer lung cancer, bladder cancer tissues and cholangiocarcinoma.

    • Synonyms

      Family with Sequence Similarity 84 Member A, Neurological/Sensory 1, Neurologic Sensory Protein 1, NSE1, PP11517, Protein FAM84A.

    • 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 MGSMGNQLDR ITHLNYSELP TGDPSGIEKD ELRVGVAYFF SDDEEDLDER GQPDKFGVKA PPGCTPCPES PSRHHHHLLH QLVLNETQFS AFRGQECIFS KVSGGPQGAD LSVYAVTALP ALCEPGDLLE LLWLQPAPEP PAPAPHWAVY VGGGQIIHLH QGEIRQDSLY EAGAANVGRV VNSWYRYRPL VAELVVQNAC GHLGLKSEEI CWTNSESFAA WCRFGKREFK AGGEVPAGTQ PPQQQYYLKV HLGENKVHTA RFHSLEDLIR EKRRIDASGR LRVLQELADL VDDKE.

    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.

    Fam84A Human
  • View Data Sheet

    Name :

    PDLIM1 Human

    Description:

    PDZ And LIM Domain 1 Human Recombinant

    PDZ And LIM Domain Protein 1, Carboxyl Terminal LIM Domain Protein 1, Epididymis Secretory Protein Li 112m, C-Terminal LIM Domain Protein 1, LIM Domain Protein CLP-36, hCLIM1, HEL-S-112, CLP-36, Elfin.

    Product # :

    PRO-1848

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    Description

    PDLIM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-329) and having a molecular mass of 38.7 kDa. PDLIM1 is fused to a 25 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The PDLIM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl, 1mM DTT, 2mM EDTA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      PDLIM1, a cytoplasmic protein linked to the cytoskeleton, belongs to the enigma protein family. PDLIM1 holds two protein interacting domains - PDZ domain at the amino terminal end and one to three LIM domains at the carboxyl terminal. PDLIM1 enables bringing other LIM interacting proteins to the cytoskeleton. Pseudogenes related to PDLIM1 are situated on chromosomes 3, 14 and 17.

    • Synonyms

      PDZ And LIM Domain Protein 1, Carboxyl Terminal LIM Domain Protein 1, Epididymis Secretory Protein Li 112m, C-Terminal LIM Domain Protein 1, LIM Domain Protein CLP-36, hCLIM1, HEL-S-112, CLP-36, Elfin.

    • 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 MGSEFMTTQQ IDLQGPGPWG FRLVGGKDFE QPLAISRVTP GSKAALANLC IGDVITAIDG ENTSNMTHLE AQNRIKGCTD NLTLTVARSE HKVWSPLVTE EGKRHPYKMN LASEPQEVLH IGSAHNRSAM PFTASPASST TARVITNQYN NPAGLYSSEN ISNFNNALES KTAASGVEAN SRPLDHAQPP SSLVIDKESE VYKMLQEKQE LNEPPKQSTS FLVLQEILES EEKGDPNKPS GFRSVKAPVT KVAASIGNAQ KLPMCDKCGT GIVGVFVKLR DRHRHPECYV CTDCGTNLKQ KGHFFVEDQI YCEKHARERV TPPEGYEVVT VFPK

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    Pdlim1 Human
  • View Data Sheet

    Name :

    PEX19 Human

    Description:

    Peroxisomal Biogenesis Factor 19 Human Recombinant

    Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.

    Product # :

    PRO-925

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    Description

    PEX19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 34.6 kDa.The PEX19 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PEX19 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEX19 is vital for peroxisome biogenesis in Saccharomyces cerevisiae. PEX19 is limited to the outer surface of peroxisomes in liver cells and is has a part in the early stage of peroxisome membrane assembly, prior to the import of matrix protein.

    • Synonyms

      Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.

    • 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 MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQC

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    Pex19 Human
  • View Data Sheet

    Name :

    PEX26 Human

    Description:

    Peroxisomal Biogenesis Factor 26 Human Recombinant

    PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.

    Product # :

    PRO-1544

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    Description

    PEX26 Human Recombinant produced in E. coli is a single polypeptide chain containing 269 amino acids (1-246) and having a molecular mass of 29.3kDa. PEX26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PEX26 solution (0.5mg/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.

    More Info

    • Introduction

      Peroxisomal Biogenesis Factor 26 (PEX26) which is a part of the peroxin-26 gene family is probably required for protein import into peroxisomes. PEX26 attaches PEX1 and PEX6 to peroxisome membranes to form heteromeric AAA ATPase complexes needed for the import of proteins into peroxisomes. Deficiencies in this gene are the cause of peroxisome biogenesis disorder complementation group 8. PBD is a group of peroxisomal disorders evolving from a failure of protein import into the peroxisomal membrane or matrix.

    • Synonyms

      PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.

    • 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 MGSMKSDSST SAAPLRGLGG PLRSSEPVRA VPARAPAVDL LEEAADLLVV HLDFRAALET CERAWQSLAN HAVAEEPAGT SLEVKCSLCV VGIQALAEMD RWQEVLSWVL QYYQVPEKLP PKVLELCILL YSKMQEPGAV LDVVGAWLQD PANQNLPEYG ALAEFHVQRV LLPLGCLSEA EELVVGSAAF GEERRLDVLQ AIHTARQQQK QEHSGSEEAQ KPNLEGSVSH KFLSLPMLVR QLWDSAVSH.

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    Pex26 Human
  • View Data Sheet

    Name :

    PFDN5 Human

    Description:

    Prefoldin Subunit 5 Human Recombinant

    Prefoldin subunit 5, C-Myc-binding protein Mm-1, Myc modulator 1, PFDN5, MM1, PFD5, MM-1.

    Product # :

    PRO-901

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    Description

    PFDN5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154 a.a.) and having a molecular mass of 19.5kDa.PFDN5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PFDN5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PFDN5 is a member of the prefoldin alpha subunit family. Prefoldin (PFDN) being a ubiquitously expressed heterohexameric co-chaperone, is required for proper folding of nascent proteins, in particular, tubulin and actin. PFDN5 is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold properly. The PFDN5 protein may also limit the transcriptional activity of the proto-oncogene c-Myc.

    • Synonyms

      Prefoldin subunit 5, C-Myc-binding protein Mm-1, Myc modulator 1, PFDN5, MM1, PFD5, MM-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA.

    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.

    Pfdn5 Human
  • View Data Sheet

    Name :

    CCL28 Mouse

    Description:

    Mucosae-Associated Epithelial Chemokine Mouse Recombinant (CCL28)

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-369

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    Description

    CCL28 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.6 kDa. The CCL28 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer pH-7.4 and 150mM 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 mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.

    • Background

      What is the molecular weight/Mw of CCL28 MOUSE Protein?
      CCL28 MOUSE Protein has a total Mw of 12.6kDa.

      What is the source or expression system of CCL28 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL28 MOUSE Protein?
      CCL28 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 MOUSE Protein?
      Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CCL28 MOUSE Protein?
      SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.

      What applications can CCL28 MOUSE Protein be used in?
      CCL28 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 MOUSE Protein?
      The endotoxin level is minimal, CCL28 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.

    Ccl28 Mouse
  • 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.

    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 :

    PLA2G2D Human

    Description:

    Secreted Phospholipase A2-IID Human Recombinant

    Group IID secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIID, GIID sPLA2, PLA2IID, sPLA(2)-IID, Secretory-type PLA, stroma-associated homolog, SPLASH, sPLA2S, PLA2G2D.

    Product # :

    ENZ-326

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    Description

    Secreted Phospholipase A2-IID Human Recombinant was produced with N-terminal His-Tag. PLA2G2D His-Tagged Fusion protein is 16.4 kDa containing 125 amino acid residues of the human secreted phospholipase A2-IID and 16 additional amino acid residues – His-Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
      The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
      This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso- PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
      In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large: small ratio of surfactant aggregates in rats.

    • Synonyms

      Group IID secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIID, GIID sPLA2, PLA2IID, sPLA(2)-IID, Secretory-type PLA, stroma-associated homolog, SPLASH, sPLA2S, PLA2G2D.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add 0.2 ml of 0.1M Acetate buffer pH-4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10 μg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MRGSHHHHHHGMASHMGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGR GQPKDATDWCCQTHDCCYDHLKTQGCGIYKYYRYNFSQGNIHCSDKGSWC EQQLCACDKEVAFCLKRNLDTYQKRLRFYWRPHCRGQTPGC.

    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.

    Pla2G2D Human
  • View Data Sheet

    Name :

    PLA2G2E Human

    Description:

    Secreted Phospholipase A2-IIE Human Recombinant

    Group IIE secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIIE, GIIE sPLA2, sPLA(2)-IIE, sPLA2-IIE, PLA2G2E.

    Product # :

    ENZ-327

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    Description

    Secreted Phospholipase A2-IIE Human Recombinant manufactured with N-terminal His-Tag. PLA2G2E His-Tagged Fusion Protein is 15.8 kDa protein containing 123 amino acid residues of the human secreted phospholipase A2-IIE and 16 additional amino acid residues – His-Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
      The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso-PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
      In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.

    • Synonyms

      Group IIE secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GIIE, GIIE sPLA2, sPLA(2)-IIE, sPLA2-IIE, PLA2G2E.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add 0.2 ml of 0.1M Acetate buffer pH-4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10 μg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMNLVQ FGVMIEKMTG KSALQYNDYG CYCGIGGSHW PVDQTDWCCH AHDCCYGRLE KLGCEPKLEK YLFSVSERGI FCAGRTTCQR LTCECDKRAA LCFRRNLGTY NRKYAHYPNK LCTGPTPPC

    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.

    Pla2G2E Human
  • View Data Sheet

    Name :

    PNRC2 Human

    Description:

    Proline-Rich Nuclear Receptor Coactivator 2 Human Recombinant

    Proline-rich nuclear receptor coactivator 2, PNRC2.

    Product # :

    PRO-1534

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    Description

    PNRC2 Human Recombinant produced in E. coli is a single polypeptide chain containing 162 amino acids (1-139) and having a molecular mass of 18kDa. PNRC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PNRC2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Proline-Rich Nuclear Receptor Coactivator 2 (PNRC2) takes part in controlling the energy balance between energy storage and energy expenditure. PNRC2 is involved in nonsense-mediated mRNA decay (NMD) by operating as a bridge between the mRNA decapping complex and the NMD machinery. PNRC2 is needed for UPF1/RENT1 localization to the P-body and also plays a role as a nuclear receptor coactivator.

    • Synonyms

      Proline-rich nuclear receptor coactivator 2, PNRC2.

    • 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 MGSMGGGERY NIPAPQSRNV SKNQQQLNRQ KTKEQNSQMK IVHKKKERGH GYNSSAAAWQ AMQNGGKNKN FPNNQSWNSS LSGPRLLFKS QANQNYAGAK FSEPPSPSVL PKPPSHWVPV SFNPSDKEIM TFQLKTLLKV QV.

    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.

    Pnrc2 Human
  • View Data Sheet

    Name :

    TNNT2 Human, His

    Description:

    Cardiac Muscle Troponin T Human Recombinant, His Tag

    CMH2, RCM3, TnTC, cTnT, CMPD2, MGC3889, TNNT2, Troponin T- cardiac muscle, Cardiac muscle troponin T, troponin T type 2 (cardiac).

    Product # :

    PRO-703

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    Description

    TNNT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 305 amino acids (1-285 a.a.) and having a molecular mass of 36.4 kDa. The TNNT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TNNT2 solution contains 20mM Tris pH-8.0, 50% glycerol, 0.1mM PMSF, 0.5M NaCl, 1mM DTT and 100mM imidazole.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNNT2 is the tropomyosin-binding subunit of the troponin complex, which is situated on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration. Mutations in TNNT2 gene are related with familial hypertrophic cardiomyopathy as well as with dilated cardiomyopathy. TNNT2 mutation takes part in hypertrophic cardiomyopathy.

    • Synonyms

      CMH2, RCM3, TnTC, cTnT, CMPD2, MGC3889, TNNT2, Troponin T- cardiac muscle, Cardiac muscle troponin T, troponin T type 2 (cardiac).

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSDIEEVVEE YEEEEQEEAA VEEQEEAAEE DAEAEAETEE TRAEEDEEEE EAKEAEDGPM EESKPKPRSF MPNLVPPKIP DGERVDFDDI HRKRMEKDLN ELQALIEAHF ENRKKEEEEL VSLKDRIERR RAERAEQQRI RNEREKERQN RLAEERARRE EEENRRKAED EARKKKALSN MMHFGGYIQK TERKSGKRQT EREKKKKILA ERRKVLAIDH LNEDQLREKA KELWQSIYNL EAEKFDLQEK FKQQKYEINV LRNRINDNQK VSKTRGKAKV TGRWK.

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    Tnnt2 Human
  • View Data Sheet

    Name :

    PPA E.Coli

    Description:

    Inorganic Pyrophosphatase E.Coli Recombinant

    Inorganic pyrophosphatase, Pyrophosphate phospho-hydrolase, PPase, ppa, b4226, JW4185.

    Product # :

    ENZ-149

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    Description

    PPA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (1-176 a.a.) and having a molecular mass of 21.9kDa.PPA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPA 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.

    More Info

    • Introduction

      Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

    • Synonyms

      Inorganic pyrophosphatase, Pyrophosphate phospho-hydrolase, PPase, ppa, b4226, JW4185.

    • 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 MSLLNVPAGK DLPEDIYVVI EIPANADPIK YEIDKESGAL FVDRFMSTAM FYPCNYGYIN HTLSLDGDPV DVLVPTPYPL QPGSVIRCRP VGVLKMTDEA GEDAKLVAVP HSKLSKEYDH IKDVNDLPEL LKAQIAHFFE HYKDLEKGKW VKVEGWENAE AAKAEIVASF ERAKNK.

    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.

    Ppa Ecoli
  • View Data Sheet

    Name :

    PQBP1 Human

    Description:

    Polyglutamine Binding Protein 1 Human Recombinant

    Golyglutamine binding protein 1, Polyglutamine tract-binding protein 1, 38kDa nuclear protein containing a WW domain, mental retardation X-linked 55, Sutherland-Haan X-linked mental retardation syndrome, Npw38, MRXS3, MRX55, MRXS8, RENS1, SHS.

    Product # :

    PRO-1101

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    Description

    PQBP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 289 amino acids (1-265) and having a molecular mass of 33.0kDa.PQBP1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PQBP1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PQBP1 is a transcription repressor which is connected to polyglutamine tract-containing transcription regulators and connective genes for neurodegenerative disorders. PQBP1 is restricts to the nucleus and can be found in neurons all over the brain, with high levels in hippocampus, olfactory bulb and cerebellar cortex. PQBP1 holds a WWP/WW domain that binds proline-rich motifs and a C2 domain which is able to stimulate Ca2+-dependent phospholipid signaling.

    • Synonyms

      Golyglutamine binding protein 1, Polyglutamine tract-binding protein 1, 38kDa nuclear protein containing a WW domain, mental retardation X-linked 55, Sutherland-Haan X-linked mental retardation syndrome, Npw38, MRXS3, MRX55, MRXS8, RENS1, SHS.

    • 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 MGSHMPLPVA LQTRLAKRGI LKHLEPEPEE EIIAEDYDDD PVDYEATRLE GLPPSWYKVF DPSCGLPYYW NADTDLVSWL SPHDPNSVVT KSAKKLRSSN ADAEEKLDRS HDKSDRGHDK SDRSHEKLDR GHDKSDRGHD KSDRDRERGY DKVDRERERD RERDRDRGYD KADREEGKER RHHRREELAP YPKSKKAVSR KDEELDPMDP SSYSDAPRGT WSTGLPKRNE AKTGADTTAA GPLFQQRPYP SPGAVLRANA EASRTKQQD

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    Pqbp1 Human
  • View Data Sheet

    Name :

    CDC37 Human

    Description:

    Cell Division Cycle 37 Human Recombinant

    P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.

    Product # :

    PRO-464

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    Description

    CDC37 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids and having a molecular mass of 44.4 kDa.

    Source

    Escherichia Coli.

    Formulation

    The CDC37 protein solution contains 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDC37 is an essential protein in Saccharomyces cerevisiae and is a molecular chaperone with precise function in cell signal transduction. CDC37 forms a complex/associates with Hsp90 molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. CDC37 also forms complex with a number of protein kinases such as CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. CDC34 is involved in directing Hsp90 to its target kinases. CDC37 up-regulation is a common early event in some localized human cancers. CDC37 is necessary for maintaining prostate tumor cell growth and represents a novel target in the exploration for multitargeted therapies. CDC37 plays a role in regulating Hsp90 ATPase activity. CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells. Tnf-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. CDC37 and heat shock protein 90 bind specifically to the kinase domain of LKB1.

    • Synonyms

      P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.

    • 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

      MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDVSV.

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    Cdc37 Human
  • 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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    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 :

    CDNF Mouse

    Description:

    Cerebral Dopamine Neurotrophic Factor Mouse Recombinant

    Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.

    Product # :

    CYT-729

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    Description

    CDNF Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.5kDa.The CDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.

    More Info

    • Introduction

      CDNF is a member of the ARMET family and acts as a trophic factor for dopamine neurons. CDNF inhibits the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the dopaminergic function and inhibits the degeneration of dopaminergic neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.

    • Synonyms

      Cerebral dopamine neurotrophic factor, ARMET-like protein 1, Conserved dopamine neurotrophic factor, Cdnf, Armetl1, 9330140G23.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.

    • Background

      What is the molecular weight/Mw of CDNF Protein?
      CDNF Protein has a total Mw of 18.5kDa.

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

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

      What is the Biological Activity of CDNF Protein?
      CDNF Mouse is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-30 µg/mL on a nitrocellulose-coated microplate.

      What is the amino acid sequence of CDNF Protein?
      QGLEAGVGPR ADCEVCKEFL DRFYNSLLSR GIDFSADTIE KELLNFCSDA KGKENRLCYY LGATTDAATK ILGEVTRPMS VHIPAVKICE KLKKMDSQIC ELKYGKKLDL ASVDLWKMRV AELKQILQRW GEECRACAEK SDYVNLIREL APKYVEIYPQ TEL.

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

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

    Cdnf Mouse
  • View Data Sheet

    Name :

    PRMT1 Human

    Description:

    Protein Arginine Methyltransferase 1 Human Recombinant

    ANM1, HCP1, HRMT1L2, IR1B4, INF receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, PRMT1, HMT2.

    Product # :

    ENZ-364

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    Description

    PRMT1 Human Recombinant (a.a. 1-353) fused with His-MBP tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 750 amino acids and having a molecular mass of 84 kDa.The PRMT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRMT1 solution contains 40mM Tris-HCl pH 8.0, 100mM NaCl, 4mM MgCl2, 2mM DTT & 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
      The PRMT1 protein functions as a histone methyltransferase specific for H4.
      PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
      PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
      CAF1 is a new regulator of PRMT1-dependent arginine methylation.
      PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
      PRMT1 plays a post-translationally part in regulating the transcriptional activity.
      PRMT1 is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

    • Synonyms

      ANM1, HCP1, HRMT1L2, IR1B4, INF receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, PRMT1, HMT2.

    • 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

      MHHHHHHMKI EEGKLVIWIN GDKGYNGLAE VGKKFEKDTG IKVTVEHPDK LEEKFPQVAA TGDGPDIIFW AHDRFGGYAQ SGLLAEITPD KAFQDKLYPF TWDAVRYNGK LIAYPIAVEA LSLIYNKDLL PNPPKTWEEI PALDKELKAK GKSALMFNLQ EPYFTWPLIA ADGGYAFKYE NGKYDIKDVG VDNAGAKAGL TFLVDLIKNK HMNADTDYSI AEAAFNKGET AMTINGPWAW SNIDTSKVNY GVTVLPTFKG QPSKPFVGVL SAGINAASPN KELAKEFLEN YLLTDEGLEA VNKDKPLGAV ALKSYEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTNSSSNN NNNNNNNNLG IEGRGSHMAA AEAANCIMEV SCGQAESSEKPNAEDMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF HNRHLFKDKV VLDVGSGTGI LCMFAAKAGA RKVIGIECSS ISDYAVKIVK ANKLDHVVTI IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVLYAR DKWLAPDGLI FPDRATLYVT AIEDRQYKDY KIHWWENVYG FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK VEDLTFTSPF CLQVKRNDYV HALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED YLTVKTGEEI FGTIGMRPNA KNNRDLDFTI DLDFKGQLCE LSCSTDYRMR.

    • Unit Definition

      One unit will transfer 1pmol of methyl group to synthetic peptide of histone H4 for 10 minutes at 37°C.

    • Specific Activity

      10,000 Units/ml.

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

    Prmt1 Human
  • View Data Sheet

    Name :

    GLUL Human

    Description:

    Glutamine Synthetase Human Recombinant

    GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    Product # :

    ENZ-544

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    Description

    GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLUL Human solution containing 20mM Tris-HCl pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

    • Synonyms

      GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    • 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 MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.

    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.

    Glul Human
  • View Data Sheet

    Name :

    TXNRD1 Human

    Description:

    Thioredoxin Reductase 1 Human Recombinant

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

    Product # :

    ENZ-518

    Price :

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    • description
    • source
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    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Txnrd1 Human
  • View Data Sheet

    Name :

    LIN28 Human, TAT

    Description:

    LIN28-TAT Human Recombinant

    CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    Product # :

    PRO-2495

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    Description

    Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (including 13- residue C-terminal TAT peptide) and having a molecular mass of 24.4kDa. The LIN28 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIN28 protein solution was formulated in PBS with 50mM arginine

    Purity

    Greater than 90% as determined by SDS-PAGE (coomassie staining).

    More Info

    • Introduction

      LIN28 is a marker of undifferentiated human embryonic stem cells and it increases the productivity of the formation of induced pluripotent stem cells from human fibroblasts. LIN28 acts as a 'translational enhancer and therefore leading specific mRNAs to polysomes and causes an increased protein synthesis. LIN28 binds let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells.

    • Synonyms

      CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    • 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

      GPSVSNQQFA GGCAKAAEEA PEEAPEDAAR AADEPQLLHG AGICKWFNVR MGFGFLSMTA RAGVALDPPV DVFVHQSKLH MEGFRSLKEG EAVEFTFKKS AKGLESIRVT GPGGVFCIGS ERRPKGKSMQ KRRSKGDRCY NCGGLDHHAK ECKLPPQPKK CHFCQSISHM VASCPLKAQQ GPSAQGKPTY FREEEEEIHS PTLLPEAQNG GYGRKKRRQR RR.

    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.

    Human Lin28
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