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Search results

1000 results found for “pcna”

Name

Description

Product #

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  • View Data Sheet

    Name :

    POP4 Human

    Description:

    Processing Of Precursor 4 Human Recombinant

    RPP29, Ribonuclease P protein subunit p29, hPOP4.

    Product # :

    PRO-1407

    Price :

    Quantity :

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    Description

    POP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a.) and having a molecular mass of 27.8kDa.POP4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POP4 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Processing of Precursor 4 (POP4) is a member of the eukaryotic/archaeal RNase P protein component 1 family. POP4 is one of the protein subunits of the small nucleolar ribonucleoprotein complexes: the endoribonuclease for mitochondrial RNA processing complex and the ribonuclease P complex. POP4 is confined to the nucleus and associates promptly with the RNA component of this complexes.POP4 is participating in processing of precursor RNAs.

    • Synonyms

      RPP29, Ribonuclease P protein subunit p29, hPOP4.

    • 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 MGSMKSVIYH ALSQKEANDS DVQPSGAQRA EAFVRAFLKR STPRMSPQAR EDQLQRKAVV LEYFTRHKRK EKKKKAKGLS ARQRRELRLF DIKPEQQRYS LFLPLHELWK QYIRDLCSGL KPDTQPQMIQ AKLLKADLHG AIISVTKSKC PSYVGITGIL LQETKHIFKI ITKEDRLKVI PKLNCVFTVE TDGFISYIYG SKFQLRSSER SAKKFKAKGT IDL.

    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.

    Pop4 Human
  • View Data Sheet

    Name :

    Tpc1808 Rat

    Description:

    Tropic 1808 Rat Recombinant

    Tropic 1808, Tpc1808.

    Product # :

    PRO-587

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
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    • More Info

    Description

    Tropic-1808 Rat Recombinant protein fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids and having a molecular mass of 29.1 kDa.The Tpc1808 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Tropic-1808 was lyophilized from 1X PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Tropic 1808 is a candidate chemotropic factor induced by nerve injury. Tpc1808 protein, similar to NGF, could promote the expression of NF-H in a time-dependent manner. Tpc1808 is the gene related to promotion of nerve growth, and both the Tpc1808 gene and the Tpc1808 recombinant protein up-regulate the expression of NF-H in PC12 cells.

    • Synonyms

      Tropic 1808, Tpc1808.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Tpc1808 although stable 10°C for 1 week, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MSYYHHHHHHMNLAQIAALNQISNLNAIRVGQVLKVSNAAGSNNTQNTTQPS
      AGVPTNTASSTTGYTVKSGDTLSAIAAANGVSLANLLSWNNLSLQAIIYPGQKL
      TIQNANNATVTTPNAPTSTPTVMPSTNGSYTVKSGDTLYGIAAKLGTNVQTLLS
      LNGLQLSSTIYVGQVLKTTGAVAGAGTATSTPTPVTPTVSKPAAANGVSTAGLS
      AAQAAWLRTAVVDAQAATAGTGVLASVTVAQAILESGWGQSALASAPYHNF
      NLYLIKVKNTWKLMTLLLS.

    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.

    Tropic 1808 Rat
  • View Data Sheet

    Name :

    LANCL1 Human

    Description:

    LanC Lantibiotic Synthetase Component C-Like 1 Human Recombinant

    GPR69A, p40, LanC-like protein 1, 40 kDa erythrocyte membrane protein, LANCL1.

    Product # :

    PRO-2004

    Price :

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    Description

    LANCL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (1-399a.a) and having a molecular mass of 47.7kDa. LANCL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LANCL1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      LanC Lantibiotic Synthetase Component C-Like 1 (LANCL1) belongs to the LanC family although formerly considered a part of the G-proteincoupled receptor superfamily. LANCL1 takes part in the biosynthesis of antimicrobial peptides. LANCL1 functions as a peptide-modifying enzyme component in eukaryotic cells. LANCL1 participates in EPS8 signaling and binds glutathione.

    • Synonyms

      GPR69A, p40, LanC-like protein 1, 40 kDa erythrocyte membrane protein, LANCL1.

    • 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 MGSMAQRAFP NPYADYNKSL AEGYFDAAGR LTPEFSQRLT NKIRELLQQM ERGLKSADPR DGTGYTGWAG IAVLYLHLYD VFGDPAYLQL AHGYVKQSLN CLTKRSITFL CGDAGPLAVA AVLYHKMNNE KQAEDCITRL IHLNKIDPHA PNEMLYGRIG YIYALLFVNK NFGVEKIPQS HIQQICETIL TSGENLARKR NFTAKSPLMY EWYQEYYVGA AHGLAGIYYY LMQPSLQVSQ GKLHSLVKPS VDYVCQLKFP SGNYPPCIGD NRDLLVHWCH GAPGVIYMLI QAYKVFREEK YLCDAYQCAD VIWQYGLLKK GYGLCHGSAG NAYAFLTLYN LTQDMKYLYR ACKFAEWCLE YGEHGCRTPD TPFSLFEGMA GTIYFLADLL VPTKARFPAF EL.

    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.

    Lancl1 Human
  • View Data Sheet

    Name :

    LCN1 Human

    Description:

    Lipocalin-1 Human Recombinant

    Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.

    Product # :

    ENZ-825

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    LCN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (19-176 a.a) and having a molecular mass of 20.1kDa. LCN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lipocalin-1 (LCN1) belongs to the lipocalin family of small secretory proteins. Lipocalins are extracellular transport proteins, which bind to various hydrophobic ligands. LCN1 protein is the principal lipid binding protein in tears and is overproduced in response to numerous stimuli including infection and stress. LCN1 is a marker for chromosome aneuploidy as well as an autoantigen in Sjogren's syndrome.

    • Synonyms

      Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.

    • 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 MGSHMHHLLA SDEEIQDVSG TWYLKAMTVD REFPEMNLES VTPMTLTTLE GGNLEAKVTM LISGRCQEVK AVLEKTDEPG KYTADGGKHV AYIIRSHVKD HYIFYCEGEL HGKPVRGVKL VGRDPKNNLE ALEDFEKAAG ARGLSTESIL IPRQSETCSP GSD.

    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.

    Lcn1 Human
  • View Data Sheet

    Name :

    LCN2 Mouse

    Description:

    Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Mouse Recombinant

    Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.

    Product # :

    ENZ-875

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • formulation
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    • More Info

    Description

    LCN2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (21-200 a.a) and having a molecular mass of 23.3kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCN2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
      They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

    • Synonyms

      Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.

    • 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 MGSQDSTQNL IPAPSLLTVP LQPDFRSDQF RGRWYVVGLA GNAVQKKTEG SFTMYSTIYE LQENNSYNVT SILVRDQDQG CRYWIRTFVP SSRAGQFTLG NMHRYPQVQS YNVQVATTDY NQFAMVFFRK TSENKQYFKI TLYGRTKELS PELKERFTRF AKSLGLKDDN IIFSVPTDQC IDN.

    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.

    Lcn2 Mouse
  • View Data Sheet

    Name :

    CDC123 Human

    Description:

    Cell Division Cycle 123 Human Recombinant

    C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    Product # :

    PRO-1463

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    Description

    CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.

    • Synonyms

      C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    • 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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD

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    Cdc123 Human
  • View Data Sheet

    Name :

    TREX2 Human

    Description:

    Three Prime Repair Exonuclease 2 Human Recombinant

    Three Prime Repair Exonuclease 2, 3'-5' exonuclease TREX2 long form.

    Product # :

    ENZ-095

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    Description

    TREX2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (1-236a.a.) and having a molecular mass of 28.0 kDa. TREX2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TREX2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 5mM DTT and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TREX2 holds a 3-prime-to-5-prime exonuclease activity and eliminates mismatched, modified, fragmented, and normal nucleotides to produce the appropriate 3-prime termini for following steps in the DNA metabolic pathways. TREX2 has a role in DNA replication, repair, and recombination.

    • Synonyms

      Three Prime Repair Exonuclease 2, 3'-5' exonuclease TREX2 long form.

    • 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 MSEAPRAETF VFLDLEATGL PSVEPEIAEL SLFAVHRSSL ENPEHDESGA LVLPRVLDKL TLCMCPERPF TAKASEITGL SSEGLARCRK AGFDGAVVRT LQAFLSRQAG PICLVAHNGF DYDFPLLCAE LRRLGARLPR DTVCLDTLPA LRGLDRAHSH GTRARGRQGY SLGSLFHRYF RAEPSAAHSA EGDVHTLLLI FLHRAAELLA WADEQARGWA HIEPMYLPPD DPSLEA

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    Trex2 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 :

    CEACAM21 Human

    Description:

    Carcinoembryonic Antigen-Related Cell Adhesion Molecule 21 Human Recombinant

    Carcinoembryonic Antigen-Related Cell Adhesion Molecule 21, CEACAM3, R29124_1.

    Product # :

    PRO-1637

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    Description

    CEACAM21 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (35-240) and having a molecular mass of 25.0kDa.CEACAM21 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CEACAM21 solution 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

      Carcinoembryonic Antigen-Related Cell Adhesion Molecule 21 (CEACAM21) belongs to the family of carcinoembryonic antigen-related cell adhesion molecules (CEACAMs), which are used by a number of bacterial pathogens to bind and invade host cells. The transmembrane protein guides phagocytosis of several bacterial species which is dependent on the small GTPase Rac. CEACAM21 is assumed to have a central role in controlling human-specific pathogens by the innate immune system.

    • Synonyms

      Carcinoembryonic Antigen-Related Cell Adhesion Molecule 21, CEACAM3, R29124_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 MGSWLFIASA PFEVAEGENV HLSVVYLPEN LYSYGWYKGK TVEPNQLIAA YVIDTHVRTP GPAYSGRETI SPSGDLHFQN VTLEDTGYYN LQVTYRNSQI EQASHHLRVY ESVAQPSIQA SSTTVTEKGS VVLTCHTNNT GTSFQWIFNN QRLQVTKRMK LSWFNHVLTI DPIRQEDAGE YQCEVSNPVS SNRSDPLKLT VKSDDNTLG.

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    Ceacam21 Human
  • View Data Sheet

    Name :

    PRMT1 Mouse

    Description:

    Protein Arginine Methyltransferase 1 Mouse Recombinant

    ANM1, HCP1, HRMT1L2, IR1B4, Interferon receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, Prmt1, AW214366, 6720434D09Rik.

    Product # :

    ENZ-365

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    Description

    PRMT1 Mouse Recombinant 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 (1mg/ml) contains 40mM Tris-HCl pH 8.0, 100mM NaCl, 4mM MgCl2, 2mM DTT and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is defined as the amount of enzyme that transfer 1.0nmole of methyl group per minute at 37C and was found to be > 30nmol/min/mg.

    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.
      PRMT1is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

    • Synonyms

      ANM1, HCP1, HRMT1L2, IR1B4, Interferon receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, Prmt1, AW214366, 6720434D09Rik.

    • 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 SCGQAESSEK PNAEDMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF HNRHLFKDKV VLDVGSGTGILCMFAAKAGA RKVIGIECSS ISDYAVKIVK ANKLDHVVTI IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVLHAR DKWLAPDGLI FPDRATLYVT AIEDRQYKDY KIHWWENVYG
      FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK VEDLTFTSPF CLQVKRNDYVHALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED YLTVKTGEEI FGTIGMRPNA KNNRDLDFTI DLDFKGQLCE LSCSTDYRMR.

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    Prmt1 Mouse
  • View Data Sheet

    Name :

    GNG12 Human

    Description:

    Guanine Nucleotide Binding Protein Gamma 12 Human Recombinant

    Guanine Nucleotide Binding Protein (G Protein), Gamma 12, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12.

    Product # :

    PRO-2184

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    Description

    GNG12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 92 amino acids (1-69 a.a) and having a molecular mass of 10.1kDa. GNG12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GNG12 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Guanine Nucleotide Binding Protein Gamma 12, also known as GNG12 belongs to the Guanine nucleotide-binding proteins (G proteins) which are involved as a modulator or transducer in a variety of transmembrane signaling systems. In addition, the beta as well as gamma chains are essential for the GTPase activity, for replacement of GDP by GTP, and also for G protein-effector interaction.

    • Synonyms

      Guanine Nucleotide Binding Protein (G Protein), Gamma 12, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSSKTAS TNNIAQARRT VQQLRLEASI ERIKVSKASA DLMSYCEEHA RSDPLLIGIP TSENPFKDKK TC.

    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.

    Gng12 Human
  • View Data Sheet

    Name :

    PRPSAP2 Human

    Description:

    Phosphoribosyl Pyrophosphate Synthetase-Associated Protein 2 Human Recombinant

    PAP41, Phosphoribosyl pyrophosphate synthase-associated protein 2, PRPP synthase-associated protein 2, 41 kDa phosphoribosypyrophosphate synthetase-associated protein, PRPSAP2.

    Product # :

    PRO-1801

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    Description

    PRPSAP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 392 amino acids (1-369) and having a molecular mass of 43.3kDa. PRPSAP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRPSAP2 solution (0.25mg/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

      Phosphoribosyl Pyrophosphate Synthetase-Associated Protein 2 (PRPSAP2) is a protein which relates with the enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes the formation of phosphoribosylpyrophosphate which is a substrate for synthesis of purine, pyrimidine, histidine, tryptophan and NAD. PRS is a complex with 2 catalytic subunits and 2 associated subunits. PRPSAP2 encodes a non-catalytic associated subunit of PRS.

    • Synonyms

      PAP41, Phosphoribosyl pyrophosphate synthase-associated protein 2, PRPP synthase-associated protein 2, 41 kDa phosphoribosypyrophosphate synthetase-associated protein, PRPSAP2.

    • 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 MGSMFCVTPP ELETKMNITK GGLVLFSANS NSSCMELSKK IAERLGVEMG KVQVYQEPNR ETRVQIQESV RGKDVFIIQT VSKDVNTTIM ELLIMVYACK TSCAKSIIGV IPYFPYSKQC KMRKRGSIVS KLLASMMCKA GLTHLITMDL HQKEIQGFFN IPVDNLRASP FLLQYIQEEI PDYRNAVIVA KSPASAKRAQ SFAERLRLGI AVIHGEAQDA ESDLVDGRHS PPMVRSVAAI HPSLEIPMLI PKEKPPITVV GDVGGRIAII VDDIIDDVDS FLAAAETLKE RGAYKIFVMA THGLLSSDAP RRIEESAIDE VVVTNTIPHE VQKLQCPKIK TVDISMILSE AIRRIHNGES MSYLFRNIGL DD.

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    Prpsap2 Human
  • View Data Sheet

    Name :

    CHP Human

    Description:

    Calcium Binding Protein P22 Human Recombinant

    CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.

    Product # :

    PRO-847

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    Description

    CHP Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-195 a.a.) and having a molecular mass of 24.7 kDa. The CHP is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHP Human solution containing 20mM Tris-HCl pH-7.5 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calcium-binding protein P22 is a phosphoprotein that binds to the sodium-hydrogen exchangers (NHEs). CHP is an essential cofactor which maintains the physiological activity of NHE family members. CHP has protein sequence resemblance to calcineurin B and it is also identified to be an endogenous inhibitor of calcineurin activity.CHP is necessary for constitutive membrane traffic. CHP Inhibits GTPase-stimulated Na(+)/H(+) exchange. CHP inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1.

    • Synonyms

      CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.

    • 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 MMGSRASTLL RDEELEEIKK ETGFSHSQIT RLYSRFTSLD KGENGTLSRE DFQRIPELAI NPLGDRIINA FFPEGEDQVN FRGFMRTLAH FRPIEDNEKS KDVNGPEPLN SRSNKLHFAF RLYDLDKDEK ISRDELLQVL RMMVGVNISD EQLGSIADRT IQEADQDGDS AISFTEFVKV LEKVDVEQKM SIRFLH.

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    Chp Human
  • View Data Sheet

    Name :

    CKS1B Human

    Description:

    CDC28 Protein Kinase Regulatory Subunit 1B Human Recombinant

    CDC28 Protein Kinase Regulatory Subunit 1B, CDC28 Protein Kinase 1B, Cyclin-Dependent Kinases Regulatory Subunit 1, NB4 Apoptosis/Differentiation Related Protein, CDC2-Associated Protein CKS1, Cell Division Control Protein CKS1, CDC28 Protein Kinase 1, PNAS-143, PNAS-16, PNAS-18, CKS-1, ckshs1.

    Product # :

    PRO-1834

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    Description

    CKS1B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (1-79) and having a molecular mass of 12.0 kDa. CKS1B is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The CKS1B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CKS1B protein which binds to the catalytic subunit of cyclin dependent kinases is vital for their biological function. The CKS1B mRNA is expressed in HeLa cells during the course of cell cycle in several forms which suggests that the encoded protein has a particular function. Two transcript variants were identified for this gene however it seems that only one of them encodes a protein.

    • Synonyms

      CDC28 Protein Kinase Regulatory Subunit 1B, CDC28 Protein Kinase 1B, Cyclin-Dependent Kinases Regulatory Subunit 1, NB4 Apoptosis/Differentiation Related Protein, CDC2-Associated Protein CKS1, Cell Division Control Protein CKS1, CDC28 Protein Kinase 1, PNAS-143, PNAS-16, PNAS-18, CKS-1, ckshs1.

    • 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 MGSMSHKQIY YSDKYDDEEF EYRHVMLPKD IAKLVPKTHL MSESEWRNLG VQQSQGWVHY MIHEPEPHIL LFRRPLPKKP KK

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    Cks1B Human
  • View Data Sheet

    Name :

    PTPN6 Human

    Description:

    Protein Tyrosine Phosphatase Non Receptor Type-6 Human Recombinant

    Tyrosine-protein phosphatase non-receptor type 6, EC 3.1.3.48, Protein-tyrosine phosphatase 1C, PTP-1C, Hematopoietic cell protein-tyrosine phosphatase, SH-PTP1, Protein-tyrosine phosphatase SHP-1, PTPN6, HCP, HCPH, SHP1, HPTP1C, SHP-1L.

    Product # :

    PKA-221

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    Description

    PTPN6 Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain containing 300 amino acids and having a molecular mass of 34.3 kDa. The protein coding region of the catalytic domain of PTPN6 (amino acids 243-541). The catalytic domain of PTPN6 was overexpressed as insoluble protein aggregates (inclusion bodies). The recombinant PTPN6 protein was purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. Additional amino acid(Met) is attached at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 25mM Tris-HCl, pH 7.5, 2mM b-mercaptoethanol, 1mM EDTA, 1mMDTT and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PTPN6 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.

    • Synonyms

      Tyrosine-protein phosphatase non-receptor type 6, EC 3.1.3.48, Protein-tyrosine phosphatase 1C, PTP-1C, Hematopoietic cell protein-tyrosine phosphatase, SH-PTP1, Protein-tyrosine phosphatase SHP-1, PTPN6, HCP, HCPH, SHP1, HPTP1C, SHP-1L.

    • 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

      MGFWEEFES LQKQEVKNLH QRLEGQRPEN KGKNRYKNIL PFDHSRVILQ GRDSNIPGSD YINANYIKNQ LLGPDENAKT YIASQGCLEA TVNDFWQMAW QENSRVIVMT TREVEKGRNK CVPYWPEVGM QRAYGPYSVT NCGEHDTTEY KLRTLQVSPL DNGDLIREIW HYQYLSWPDH GVPSEPGGVL SFLDQINQRQ ESLPHAGPII VHCSAGIGRT GTIIVIDMLM ENISTKGLDCDIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEVLQSQK GQESEYGNITY.

    • Unit Definition

      One unit will hydrolyze 1 nanomole of p-nitrophenylphosphatate per minute at pH 7.5 at 37°C using 10mM of substrate.

    • Specific Activity

      >5,000 U/mg of PTPN6.

    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.

    Ptpn6 Human
  • View Data Sheet

    Name :

    CNPY3 Human

    Description:

    Canopy 3 Homolog Human Recombinant

    CAG4A, ERDA5, PRAT4A, TNRC5, Protein canopy homolog 3, CTG repeat protein 4a, Expanded repeat-domain protein CAG/CTG 5, Protein associated with TLR4, Trinucleotide repeat-containing gene 5 protein,CNPY3.

    Product # :

    PRO-1386

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    Description

    CNPY3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (31-278 a.a.) and having a molecular mass of 29.9kDa. CNPY3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CNPY3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Canopy 3 homolog (CNPY3) is a 271 a.aToll-like receptor specific co-chaperone for HSP90B1. CNPY3 is necessitated for proper TLR folding, excluding that of TLR3, and so controls TLR exit from the endoplasmic reticulum. Therefore, CNPY3i s required for both innate and adaptive immune responses.

    • Synonyms

      CAG4A, ERDA5, PRAT4A, TNRC5, Protein canopy homolog 3, CTG repeat protein 4a, Expanded repeat-domain protein CAG/CTG 5, Protein associated with TLR4, Trinucleotide repeat-containing gene 5 protein,CNPY3.

    • 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 MGSGPSQAGA EENDWVRLPS KCEVCKYVAV ELKSAFEETG KTKEVIGTGY GILDQKASGV KYTKSDLRLI EVTETICKRL LDYSLHKERT GSNRFAKGMS ETFETLHNLV HKGVKVVMDI PYELWNETSA EVADLKKQCD VLVEEFEEVI EDWYRNHQEE DLTEFLCANH VLKGKDTSCL AEQWSGKKGD TAALGGKKSK KKSSRAKAAG GRSSSSKQRK ELGGLEGDPS PEEDEGIQKA SPLTHSPPDE L.

    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.

    Cnpy3 Human
  • View Data Sheet

    Name :

    MAP1LC3A Human

    Description:

    Microtubule-Associated Protein 1 Light Chain 3 Alpha Human Recombinant

    ATG8E, LC3, LC3A, MAP1ALC3, MAP1BLC3, MLP3A.

    Product # :

    PRO-495

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    Description

    MAP1LC3A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-120 a.a.) and having a molecular mass of 15.1 kDa. The MAP1LC3A is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAP1LC3A solution (1mg/ml) contains 20mM Tris-HCl pH-8.0, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAP1LC3A takes part in formation of autophagosomal vacuoles and is one of the light chain subunits that functions together with both MAP1A and/or MAP1B. MAP1LC3A has an important part in neuronal development and in maintaining the balance between neuronal plasticity and rigidity. MAP1LC3A is expressed as two alternatively spliced isoforms that are expressed in testis, brain, heart, liver and skeletal muscle, but are absent in thymus and peripheral blood leukocytes.

    • Synonyms

      ATG8E, LC3, LC3A, MAP1ALC3, MAP1BLC3, MLP3A.

    • 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

      MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG LEHHHHHH.

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

    Map1Lc3A Human
  • View Data Sheet

    Name :

    COPS7A Human

    Description:

    COP9 Signalosome Subunit 7A Human Recombinant

    COP9 Signalosome Subunit 7A, COPS7A, Dermal Papilla-Derived Protein 10, CSN7A, SGN7a, JAB1-Containing Signalosome Subunit 7a, COP9 Complex Subunit 7a, COP9 Constitutive Photomorphogenic Homolog Subunit 7A, COP9 Signalosome Complex Subunit 7a, DERP10, Signalosome Subunit 7a.

    Product # :

    PRO-1947

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    Description

    COPS7A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275) and having a molecular mass of 32.7 kDa.COPS7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The COPS7A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COP9 Signalosome Subunit 7A (COPS7A) is a component of the COP9 signalosome complex (CSN), a complex involved in a variety of cellular and developmental processes. The CSN complex is a vital regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, thus leading to decrease in the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. This complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, probably through its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN stimulates and protects degradation by the Ubl system, respectively.

    • Synonyms

      COP9 Signalosome Subunit 7A, COPS7A, Dermal Papilla-Derived Protein 10, CSN7A, SGN7a, JAB1-Containing Signalosome Subunit 7a, COP9 Complex Subunit 7a, COP9 Constitutive Photomorphogenic Homolog Subunit 7A, COP9 Signalosome Complex Subunit 7a, DERP10, Signalosome Subunit 7a.

    • 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 MGSMSAEVKV TGQNQEQFLL LAKSAKGAAL ATLIHQVLEA PGVYVFGELL DMPNVRELAE SDFASTFRLL TVFAYGTYAD YLAEARNLPP LTEAQKNKLR HLSVVTLAAK VKCIPYAVLL EALALRNVRQ LEDLVIEAVY ADVLRGSLDQ RNQRLEVDYS IGRDIQRQDL SAIARTLQEW CVGCEVVLSG IEEQVSRANQ HKEQQLGLKQ QIESEVANLK KTIKVTTAAA AAATSQDPEQ HLTELREPAP GTNQRQPSKK ASKGKGLRGS AKIWSKSN.

    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.

    Cops7A Human
  • View Data Sheet

    Name :

    VTA1 Human

    Description:

    Vps20-Associated 1 Homolog Human Recombinant

    Vacuolar protein sorting-associated protein VTA1 homolog, DRG-1, LYST-interacting protein 5, LIP5, SKD1-binding protein 1, SBP1, VTA1, C6orf55, DRG1My012, HSPC228.

    Product # :

    PRO-1044

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    Description

    VTA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-307 a.a.) and having a molecular mass of 36.5kDa.VTA1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    VTA1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vps20-associated 1 homolog (VTA1) is a member of the VTA1 family. The VTA1 protein is involved in the endosomal multivesicular bodies (MVB) pathway. Furthermore, VTA1 is interacts with CHMP1B, CHMP2A, CHMP5, VPS4B, KIAA0174 (IST1) and possibly CHMP3. VTA1 is believed to be a cofactor of VPS4A/B, which catalyzes membrane-associated ESCRT-III assemblies. In addition, VTA1 is involved in the sorting and down-regulation of EGFR and also in HIV-1 budding.

    • Synonyms

      Vacuolar protein sorting-associated protein VTA1 homolog, DRG-1, LYST-interacting protein 5, LIP5, SKD1-binding protein 1, SBP1, VTA1, C6orf55, DRG1My012, HSPC228.

    • 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 MGSHMAALAP LPPLPAQFKS IQHHLRTAQE HDKRDPVVAY YCRLYAMQTG MKIDSKTPEC RKFLSKLMDQ LEALKKQLGD NEAITQEIVG CAHLENYALK MFLYADNEDR AGRFHKNMIK SFYTASLLID VITVFGELTD ENVKHRKYAR WKATYIHNCL KNGETPQAGP VGIEEDNDIE ENEDAGAASL PTQPTQPSSS STYDPSNMPS GNYTGIQIPP GAHAPANTPA EVPHSTGVAS NTIQPTPQTI PAIDPALFNT ISQGDVRLTP EDFARAQKYC KYAGSALQYE DVSTAVQNLQ KALKLLTTGR E.

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    Vta1 Human
  • View Data Sheet

    Name :

    RGN Human

    Description:

    Regucalcin Human Recombinant

    Regucalcin, RC, Gluconolactonase, GNL, Senescence marker protein 30, SMP-30, RGN, SMP30.

    Product # :

    PRO-915

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    Description

    RGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 319 amino acids (1-299 a.a.) and having a molecular mass of 35.4kDa.RGN is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RGN protein solution (0.5mg/ml) containing 20mM Tris-HCl, pH8.0, 2M Urea and 20% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Regucalcin (RGN) is a member of the SMP-30/CGR1 family. Regucalcin is a Ca (2+)-binding protein which does not contain EF-hand motif of Ca (2+)-binding domain. RGN has a critical role in the keep of intracellular Ca2+ homeostasis due to activating of Ca2+ pump enzymes in the plasma membrane (basolateral membrane), microsomes (endoplasmic reticulum) and mitochondria of many cells. Moreover, RGN plays a multifunctional role in the regulation of cell functions in the liver, kidney cortex, heart and brain and a suppressor protein for cell signaling systems in many cell types.

    • Synonyms

      Regucalcin, RC, Gluconolactonase, GNL, Senescence marker protein 30, SMP-30, RGN, SMP30.

    • 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 MSSIKIECVL PENCRCGESP VWEEVSNSLL FVDIPAKKVC RWDSFTKQVQ RVTMDAPVSS VALRQSGGYV ATIGTKFCAL NWKEQSAVVL ATVDNDKKNN RFNDGKVDPA GRYFAGTMAE ETAPAVLERH QGALYSLFPD HHVKKYFDQV DISNGLDWSL
      DHKIFYYIDS LSYSVDAFDY DLQTGQISNR RSVYKLEKEE QIPDGMCIDA EGKLWVACYN GGRVIRLDPV TGKRLQTVKL PVDKTTSCCF GGKNYSEMYV TCARDGMDPE GLLRQPEAGG IFKITGLGVK GIAPYSYAG.

    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.

    Rgn Human
  • View Data Sheet

    Name :

    RP9 Human

    Description:

    Retinitis Pigmentosa 9 Human Recombinant

    Retinitis pigmentosa 9 protein, Pim-1-associated protein, PAP-1, RP9.

    Product # :

    PRO-1314

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    Description

    RP9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (1-155 a.a.) and having a molecular mass of 20.7kDa.RP9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RP9 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Retinitis pigmentosa 9 (RP9) is assumed to be a target protein for the PIM1 kinase. The RP9 protein may have some roles in B-cell proliferation in association with PIM1. RP9 can be bound and phosphorylated by the protooncogene PIM1 product, a serine/threonine protein kinase. RP9 localizes in nuclear speckles containing the splicing factors, and has a part in pre-mRNA splicing. RP9 gene mutations result in autosomal dominant retinitis pigmentosa-9.

    • Synonyms

      Retinitis pigmentosa 9 protein, Pim-1-associated protein, PAP-1, RP9.

    • 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 MGSMSSRPGR EDVGAAGARR PREPPEQELQ RRREQKRRRH DAQQLQQLKH LESFYEKPPP GLIKEDETKP EDCIPDVPGN EHAREFLAHA PTKGLWMPLG KEVKVMQCWR CKRYGHRTGD KECPFFIKGN QKLEQFRVAH EDPMYDIIRD NKRHEKDV.

    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.

    Rp9 Human
  • View Data Sheet

    Name :

    RPN2 Human

    Description:

    Ribophorin II Human Recombinant

    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2, Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit, RIBIIR, Ribophorin II, RPN-II, Ribophorin-2, RPN2, SWP1, RPNII.

    Product # :

    ENZ-349

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    Description

    RPN2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 539 amino acids (23-540) and having a molecular mass of 59.2kDa.RPN2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPN2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribophorin 2 (RPN2) is a dolichyl-diphosphooligosaccharide protein glycosyltransferase subunit 2. The Ribophorin 2 protein is part of an N-oligosaccharyl transferase complex which links high mannose oligosaccharides to asparagine residues found in the Asn-X-Ser/Thr consensus motif of nascent polypeptide chains. RPN2 is analogous in sequence to the yeast oligosaccharyl transferase subunit SWP1.

    • Synonyms

      Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2, Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit, RIBIIR, Ribophorin II, RPN-II, Ribophorin-2, RPN2, SWP1, RPNII.

    • 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 MLTPTHYLTK HDVERLKASL DRPFTNLESA FYSIVGLSSL GAQVPDAKKA CTYIRSNLDP SNVDSLFYAA QASQALSGCE ISISNETKDL LLAAVSEDSS VTQIYHAVAA LSGFGLPLAS QEALSALTAR LSKEETVLAT VQALQTASHL SQQADLRSIV
      EEIEDLVARL DELGGVYLQF EEGLETTALF VAATYKLMDH VGTEPSIKED QVIQLMNAIF SKKNFESLSE AFSVASAAAV LSHNRYHVPV VVVPEGSASD THEQAILRLQ VTNVLSQPLT QATVKLEHAK SVASRATVLQ KTSFTPVGDV FELNFMNVKF SSGYYDFLVE VEGDNRYIAN
      TVELRVKIST EVGITNVDLS TVDKDQSIAP KTTRVTYPAK AKGTFIADSH QNFALFFQLV DVNTGAELTP HQTFVRLHNQ KTGQEVVFVA EPDNKNVYKF ELDTSERKIE FDSASGTYTL YLIIGDATLK NPILWNVADV VIKFPEEEAP STVLSQNLFT PKQEIQHLFR EPEKRPPTV.

    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.

    Rpn2 Human
  • View Data Sheet

    Name :

    Protein A

    Description:

    Staphylococcal Protein A Recombinant

    Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    Product # :

    PRO-356

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    Description

    Recombinant Staphylococcal Protein A produced in E.Coli is a non-glycosylated, Polypeptide chain having a molecular mass of 46.7 kDa.Recombinant Staphylococcal Protein A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains no additives.

    Purity

    Greater than 95.0% as determined by RP-HPLC.

    Biological Activity

    Greater than 95.0% binding activity to human IgG.

    More Info

    • Introduction

      Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).

    • Synonyms

      Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

      SPA should be stored at -20°C.

    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.

    Protein A
  • View Data Sheet

    Name :

    CEA Human, His

    Description:

    Carcinoembryonic Antigen Human Recombinant, His Tag

    Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.

    Product # :

    PRO-2407

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    Description

    CEA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 659 amino acids (35-685a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-150kDa). CEA is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CEA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
      There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
      The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
      CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
      The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
      Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed.

    • Synonyms

      Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.

    • 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

      KLTIESTPFN VAEGKEVLLL VHNLPQHLFG YSWYKGERVD GNRQIIGYVI GTQQATPGPA YSGREIIYPN ASLLIQNIIQ NDTGFYTLHV IKSDLVNEEA TGQFRVYPEL PKPSISSNNS KPVEDKDAVA FTCEPETQDA TYLWWVNNQS LPVSPRLQLS NGNRTLTLFN VTRNDTASYK CETQNPVSAR RSDSVILNVL YGPDAPTISP LNTSYRSGEN LNLSCHAASN PPAQYSWFVN GTFQQSTQEL FIPNITVNNS GSYTCQAHNS DTGLNRTTVT TITVYAEPPK PFITSNNSNP VEDEDAVALT CEPEIQNTTY LWWVNNQSLP VSPRLQLSND NRTLTLLSVT RNDVGPYECG IQNKLSVDHS DPVILNVLYG PDDPTISPSY TYYRPGVNLS LSCHAASNPP AQYSWLIDGN IQQHTQELFI SNITEKNSGL YTCQANNSAS GHSRTTVKTI TVSAELPKPS ISSNNSKPVE DKDAVAFTCE PEAQNTTYLW WVNGQSLPVS PRLQLSNGNR TLTLFNVTRN DARAYVCGIQ NSVSANRSDP VTLDVLYGPD TPIISPPDSS YLSGANLNLS CHSASNPSPQ YSWRINGIPQ QHTQVLFIAK ITPNNNGTYA CFVSNLATGR NNSIVKSITV SASGTSPGLS ALEHHHHHH.

    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.

    Ceacam5 Human
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