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Search results

1000 results found for “MANF”

Name

Description

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  • View Data Sheet

    Name :

    NCALD Human

    Description:

    Neurocalcin Delta Recombinant Human

    Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.

    Product # :

    PRO-093

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    Description

    NCALD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-193.a.a) and having a molecular mass of 24.4kDa. NCALD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NCALD protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NCALD belongs to the neuronal calcium sensor (NCS) family. NCALD is cytosolic at inactive calcium levels; but, high intracellular calcium levels induce a conformational transformation which exposes the myristoyl group, causing protein association with membranes and partial co-localization with the perinuclear trans-golgi network. NCALD protein is a regulator of signal transduction by G protein-coupled receptor.

    • Synonyms

      Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.

    • 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 MGKQNSKLRP EVMQDLLEST DFTEHEIQEW YKGFLRDCPS GHLSMEEFKK IYGNFFPYGD ASKFAEHVFR TFDANGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISKAE MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNR DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA GQF.

    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.

    Ncald Human
  • View Data Sheet

    Name :

    EEF1E1 Human

    Description:

    Eukaryotic Translation Elongation Factor 1 Epsilon 1 Human Recombinant

    Eukaryotic translation elongation factor 1 epsilon-1, Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3, Elongation factor p18, Multisynthase complex auxiliary component p18, EEF1E1, AIMP3, P18.

    Product # :

    PRO-199

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    Description

    EEF1E1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 194 amino acids (1-174 a.a.) and having a molecular mass of 21.9kDa.EEF1E1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EEF1E1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1) shares sequence similarity with the amino-terminal ends of the Beta and Gamma subunits of EF-1. By specifically interacting with MetRS, EEF1E1 binds to a macromolecular tRNA synthtase complex which catalyzes the ligation of specific amino acids to their cognate tRNAs. Upon DNA damage, EEF1E1 translocates to the nucleus where it interacts with ATM and ATR, resulting in p53 activation.

    • Synonyms

      Eukaryotic translation elongation factor 1 epsilon-1, Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3, Elongation factor p18, Multisynthase complex auxiliary component p18, EEF1E1, AIMP3, P18.

    • 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 MAAAAELSLL EKSLGLSKGN KYSAQGERQI PVLQTNNGPS LTGLTTIAAH LVKQANKEYL LGSTAEEKAI VQQWLEYRVT QVDGHSSKND IHTLLKDLNS YLEDKVYLTG YNFTLADILL YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ HYPGIRQHLS SVVFIKNRLY TNSH.

    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.

    Eef1E1 Human
  • View Data Sheet

    Name :

    EIF5A Human

    Description:

    Eukaryotic Translation Initiation Factor 5A Human Recombinant

    EIF-5A, EIF5A1, eIF5AI, MGC99547, MGC104255, EIF5A, Eukaryotic translation initiation factor 5A-1, eIF-5A-1, eIF-5A1, Eukaryotic initiation factor 5A isoform 1, eIF-4D, Rev-binding factor.

    Product # :

    PRO-674

    Price :

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    • description
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    • More Info

    Description

    EIF5A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids and having a molecular mass of 16.8 kDa. EIF5A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF5A protein solution (1mg/ml) contains 50mM Tris-HCl, pH-7.5 and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF5A is the single protein identified to contain remarkable amino acid formed by the action of deoxyhypusine synthase and deoxyhypusine hydroxylase using spermidine as the substrate. EIF5A takes part in the first step of peptide bond formation in translation, nevertheless further experiments implicates it as a universally conserved translation elongation factor. Modulation of EIF5A is connected to proliferation and cancer. Expression of EIF-5A is upregulated in the PBMCs of HIV-1 patients. EIF5A coordinates significant cellular processes like cell viability and senescence during its effects on the stability of certain mRNAs. Heat stress-induced loss of EIF-5A in a human pancreatic cancer cell line. EIF5A stability takes part in determining the fate of the particular cell type after severe heat stress.

    • Synonyms

      EIF-5A, EIF5A1, eIF5AI, MGC99547, MGC104255, EIF5A, Eukaryotic translation initiation factor 5A-1, eIF-5A-1, eIF-5A1, Eukaryotic initiation factor 5A isoform 1, eIF-4D, Rev-binding factor.

    • 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

      MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS LLQDSGEVRE DLRLPEGDLG KEIEQKYDCG EEILITVLSA MTEEAAVAIK AMAK.

    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.

    Eif5A Human
  • 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
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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 :

    CHODL Human

    Description:

    Chondrolectin Human Recombinant

    Chondrolectin, Transmembrane Protein MT75, C21orf68, Chromosome 21 Open Reading Frame 68, PRED12, MT75, CHODL.

    Product # :

    PRO-1964

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    Description

    CHODL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (22-216) and having a molecular mass of 24.6 kDa.CHODL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chondrolectin (CHODL) is a type I membrane protein with a carbohydrate recognition domain characteristic of C-type lectins in its extracellular portion. In other proteins, this domain is involved in endocytosis of glycoproteins and exogenous sugar-bearing pathogens. The CHODL protein localizes mainly to the perinuclear region.

    • Synonyms

      Chondrolectin, Transmembrane Protein MT75, C21orf68, Chromosome 21 Open Reading Frame 68, PRED12, MT75, CHODL.

    • 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 MGSFCRRVVS GQKVCFADFK HPCYKMAYFH ELSSRVSFQE ARLACESEGG VLLSLENEAE QKLIESMLQN LTKPGTGISD GDFWIGLWRN GDGQTSGACP DLYQWSDGSN SQYRNWYTDE PSCGSEKCVV MYHQPTANPG LGGPYLYQWN DDRCNMKHNY ICKYEPEINP TAPVEKPYLT NQPGDTHQNV VVTEAGIIPN.

    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.

    Chodl Human
  • View Data Sheet

    Name :

    VAMP3 Human

    Description:

    Synaptobrevin-3 Human Recombinant

    VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    Product # :

    PRO-652

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    Description

    VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

    • Synonyms

      VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    • 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

      MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.

    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.

    Vamp3 Human
  • View Data Sheet

    Name :

    MAPK9 Human

    Description:

    Mitogen-Activated Protein Kinase 9 Human Recombinant

    Mitogen-activated protein kinase 9, MAP kinase 9, MAPK 9, JNK-55, Stress-activated protein kinase 1a, SAPK1a, Stress-activated protein kinase JNK2, c-Jun N-terminal kinase 2, MAPK9, JNK2, PRKM9, SAPK, p54a, JNK2A, JNK2B, JNK2BETA, p54aSAPK, JNK2ALPHA.

    Product # :

    PKA-039

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    Description

    MAPK9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-382 a.a) and having a molecular mass of 46.6kDa.MAPK9 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAPK9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitogen-activated protein kinase 9 (MAPK9) belongs to the MAP kinase family. MAP kinases function as an integration point for numerous biochemical signals, and are involved in a broad variety of cellular processes such as proliferation, differentiation, transcription regulation and development. MAPK9 targets specific transcription factors, and consequently mediates immediate-early gene expression in response to diverse cell stimuli. As an active dimer, MAPK9 can translocate to the nucleus and control transcription through its effects on c-Jun, ATF-2, and other transcription factors. MAPK9 blocks the ubiquitination of tumor suppressor p53, and so it increases the stability of p53 in nonstressed cells.

    • Synonyms

      Mitogen-activated protein kinase 9, MAP kinase 9, MAPK 9, JNK-55, Stress-activated protein kinase 1a, SAPK1a, Stress-activated protein kinase JNK2, c-Jun N-terminal kinase 2, MAPK9, JNK2, PRKM9, SAPK, p54a, JNK2A, JNK2B, JNK2BETA, p54aSAPK, JNK2ALPHA.

    • 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 MGSHMSDSKC DSQFYSVQVA DSTFTVLKRY QQLKPIGSGA QGIVCAAFDT VLGINVAVKK LSRPFQNQTH AKRAYRELVL LKCVNHKNII SLLNVFTPQK TLEEFQDVYL VMELMDANLC QVIHMELDHE RMSYLLYQML CGIKHLHSAG IIHRDLKPSN IVVKSDCTLK ILDFGLARTA CTNFMMTPYV VTRYYRAPEV ILGMGYKENV DIWSVGCIMG ELVKGCVIFQ GTDHIDQWNK VIEQLGTPSA EFMKKLQPTV RNYVENRPKY PGIKFEELFP DWIFPSESER DKIKTSQARD LLSKMLVIDP DKRISVDEAL RHPYITVWYD PAEAEAPPPQ IYDAQLEERE HAIEEWKELI YKEVMDWEER SKNGVVKDQP SAQMQQ.

    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.

    Mapk9 Human
  • View Data Sheet

    Name :

    4 1BBL Human, His

    Description:

    4-1BB Ligand Human Recombinant, His Tag

    CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.

    Product # :

    CYT-649

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    • sds-page

    Description

    TNFSF9 Human Recombinant fused to 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (71-254 a.a.) and having a molecular mass of 23.8 kDa. The TNFSF9 37 aa His tag fusion protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Recombinant 4-1BBL solution (1mg/ml) contains 20mM Tris-HCl buffer pH-8, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE

    sds-page

    4-1BBL-His-sds-page - Product image 1

    More Info

    • Introduction

      4-1BBL is a transmembrane cytokine that is part of the tumor necrosis factor (TNF) ligand family. 4-1BBL is a bidirectional signal transducer that performs as a ligand for TNFRSF9, which is a costimulatory receptor molecule in T lymphocytes. TNFSF9 and its TNFRSF9 take part in the antigen presentation development and in the generation of cytotoxic T cells. 4-1BBR is absent from resting T lymphocytes but rapidly expressed upon antigenic stimulation. TNFSF9 reactivates anergic T lymphocytes as well as promoting T lymphocyte proliferation. 4-1BB Ligand is needed for the optimal CD8 responses in CD8 T cells. 4-1BBL is expressed in carcinoma cell lines, and is thought to be involved in T cell-tumor cell interaction. 4-1BBL is expressed by activated B cells, macrophages, dendritic cells, activated T cells, neurons and astrocytes. The interaction of 4-1BB with TNFRSF9 strongly regulates immunity and has been proposed to preferentially control T cell responses based on studies in various murin

    • Synonyms

      CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMRE GPELSPDDPA GLLDLRQGMF AQLVAQNVLL IDGPLSWYSD PGLAGVSLTGGLSYKEDTKE LVVAKAGVYY VFFQLELRRV VAGEGSGSVS LALHLQPLRS AAGAAALALT VDLPPASSEA RNSAFGFQGR LLHLSAGQRL GVHLHTEARA RHAWQLTQGA TVLGLFRVTP EIPAGLPSPR SE.

    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.

    4-1Bbl Protein
  • View Data Sheet

    Name :

    LIF Human

    Description:

    Leukemia Inhibitory Factor Human Recombinant

    CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    Product # :

    CYT-644

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    Description

    Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.

    Purity

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

    Biological Activity

    The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.

    • Background

      Leukemia Inhibitory Factor (LIF) Background

      Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.

      LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.

      Function and Applications of LIF

      LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.

      Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.

      Structure and Interactions

      LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.

    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.

    Lif Human
  • View Data Sheet

    Name :

    SNCA 1-95, Human

    Description:

    Alpha-Synuclein 1-95 Human Recombinant

    SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.

    Product # :

    PRO-2625

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    Description

    SNCA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (1-95 a.a.) and having a molecular mass of 9.3kDa.SNCA is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SNCA protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 7.5) and 0.1 M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alpha-synuclein or SNCA is a synuclein protein. SNCA mainly found in the brain, small concentration of the protein can also be located in other tissues such as heart and muscle. When looking in the brain tissue, SNCA is located in the end of the neuron, in an area called presynaptic terminal. In the presynaptic terminal SNCA has interaction with phospholipids & other proteins. Neurotransmitters are released from the synaptic vesicles in the Presynaptic terminals and act as messengers. Once released, the neurotransmitters send signals across the neurons that are crucial for the brain’s operation.

    • Synonyms

      SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFV

    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.

    Alpha Synuclein
  • View Data Sheet

    Name :

    PROCR Human, Sf9

    Description:

    Protein-c Receptor Human Recombinant, Sf9

    Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA.

    Product # :

    PRO-2438

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    Description

    PROCR Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 435 amino acids (18-210a.a.) and having a molecular mass of 49.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PROCR is expressed with a 242 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PROCR 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

      Protein-c Receptor (PROCR) is a receptor for activated protein C, a serine protease activated by and involved in the blood coagulation pathway. The PROCR protein is an N-glycosylated type I membrane protein which enhances the activation of protein C. PROCR gene mutations are linked with venous thromboembolism and myocardial infarction, as well as with late fetal loss during pregnancy. In addition, PROCR may have a role in malarial infection and has been linked with cancer.

    • Synonyms

      Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA.

    • 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

      ADPSQDASDG LQRLHMLQIS YFRDPYHVWY QGNASLGGHL THVLEGPDTN TTIIQLQPLQ EPESWARTQS GLQSYLLQFH GLVRLVHQER TLAFPLTIRC FLGCELPPEG SRAHVFFEVA VNGSSFVSFR PERALWQADT QVTSGVVTFT LQQLNAYNRT RYELREFLED TCVQYVQKHI SAENTKGSQT SRSYTSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    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.

    Procr Protein
  • View Data Sheet

    Name :

    ME2 Human

    Description:

    Malic Enzyme 2 Human Recombinant

    Malic enzyme 2 NAD(+)-dependent mitochondrial, NAD-ME, ODS1, Malate Dehydrogenase, NAD-dependent malic enzyme mitochondrial, pyruvic-malic carboxylase, Malic enzyme 2, EC 1.1.1.38, EC 1.1.1.

    Product # :

    ENZ-376

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    Description

    ME2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 573 amino acids and having a total molecular mass of 64.4kDa.ME2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris, 150mM NaCl, 1mM b-mercaptoethanol, 1mM EDTA, pH8.0.

    Purity

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

    More Info

    • Introduction

      ME2 catalyzes the oxidative decarboxylation of malate to pyruvate, malat + NAD(P)+? pyruvate + CO2 + NAD(P)H+, and is found both in eukaryotic and prokaryotic cells. Three different isoforms of ME are known to be in mammalian tissues: a strictly cytosolic NADP+-dependent enzyme, an NADP+-dependent mitochondriail isoform, and a mitochondrial isoenzyme that is able to use both NAD+ and NADP+ but is more effective with NAD+. The mammalian isoforms size is about 62-64 kDa. A native size of 240,000 Da proposes a tetrameric structure for the active enzyme.
      Mitochondrial NAD+-dependent ME 2 activity is seen in tissues that experience many cell divisions, like spleen, thymus, and the basal cells of the small intestinal mucosa. ME2 is also expressed all through the rapid cleavage stages of early Xenopus development. Activity for this isoform is low or nonexistent in brain, muscle, and normal and regenerating liver tissue from rat but was observed in rat adrenal cortex, pigeon and human skeletal muscle, and in heart muscle of some species. In addition, it is expressed in mitochondria of all tumor cells inspected to detain ascites tumors, hepatoma cells, and a variety of other tumors and transformed cell lines.

    • Synonyms

      Malic enzyme 2 NAD(+)-dependent mitochondrial, NAD-ME, ODS1, Malate Dehydrogenase, NAD-dependent malic enzyme mitochondrial, pyruvic-malic carboxylase, Malic enzyme 2, EC 1.1.1.38, EC 1.1.1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ME2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ME2 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 ME2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLK
      KMTSPLEKYIYIMGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGL
      FISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLYTAC
      AGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYG
      RNTLIQFEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEH
      KILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKIDSYQ
      EPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPT
      AQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILC
      NTRHISDSVFLEAAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAF
      RYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESASSPPVITEHHHHHH.

    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.

    Me2 Human
  • View Data Sheet

    Name :

    YY1 Human

    Description:

    YY1 Transcription Factor Human Recombinant

    YY1 transcription factor, YY1, DELTA, INO80S, NF-E1, UCRBP, YIN-YANG-1, Transcriptional repressor protein YY1, Delta transcription factor, Yin and yang 1, INO80 complex subunit S, YY-1.

    Product # :

    PRO-2108

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    Description

    YY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 437 amino acids (1-414) and having a molecular mass of 47.1kDa.YY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YY1 solution (0.25mg/1ml) contains PBS, 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      YY1 Transcription Factor, also known as YY1, is a part of the GLI-Kruppel class of zinc finger proteins. YY1 has a positive and negative effect on a various cellular and viral genes by binding to sites overlapping the transcription start site. YY1 leads histone deacetylases and histone acetyltransferases to a promoter in order to activate or repress the promoter.

    • Synonyms

      YY1 transcription factor, YY1, DELTA, INO80S, NF-E1, UCRBP, YIN-YANG-1, Transcriptional repressor protein YY1, Delta transcription factor, Yin and yang 1, INO80 complex subunit S, YY-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 MGSMASGDTL YIATDGSEMP AEIVELHEIE VETIPVETIE TTVVGEEEEE DDDDEDGGGG DHGGGGGHGH AGHHHHHHHH HHHPPMIALQ PLVTDDPTQV HHHQEVILVQ TREEVVGGDD SDGLRAEDGF EDQILIPVPA PAGGDDDYIE QTLVTVAAAG KSGGGGSSSS GGGRVKKGGG KKSGKKSYLS GGAGAAGGGG ADPGNKKWEQ KQVQIKTLEG EFSVTMWSSD EKKDIDHETV VEEQIIGENS PPDYSEYMTG KKLPPGGIPG IDLSDPKQLA EFARMKPRKI KEDDAPRTIA CPHKGCTKMF RDNSAMRKHL HTHGPRVHVC AECGKAFVES SKLKRHQLVH TGEKPFQCTF EGCGKRFSLD FNLRTHVRIH TGDRPYVCPF DGCNKKFAQS TNLKSHILTH AKAKNNQ.

    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.

    Yy1 Human
  • View Data Sheet

    Name :

    GEMIN6 Human

    Description:

    Gem-Associated Protein 6 Human Recombinant

    Gem-associated protein 6, Gemin-6, SIP2, GEMIN6.

    Product # :

    PRO-1394

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    Description

    GEMIN6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167a.a) and having a molecular mass of 21.9kDa. GEMIN6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GEMIN6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gem-Associated Protein 6 (GEMIN6) is a member of a large macromolecular complex, localized to both the cytoplasm and the nucleus, which takes part in the cytoplasmic assembly of small nuclear ribonucleoproteins (snRNPs). SMN, GEMIN2, GEMIN3, GEMIN4, and GEMIN5 are additional members of this complex.

    • Synonyms

      Gem-associated protein 6, Gemin-6, SIP2, GEMIN6.

    • 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 MGSMSEWMKK GPLEWQDYIY KEVRVTASEK NEYKGWVLTT DPVSANIVLV NFLEDGSMSV TGIMGHAVQT VETMNEGDHR VREKLMHLFT SGDCKAYSPE DLEERKNSLK KWLEKNHIPI TEQGDAPRTL CVAGVLTIDP PYGPENCSSS NEIILSRVQD LIEGHLTASQ.

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    Gemin6 Human
  • View Data Sheet

    Name :

    CD84 Human, Sf9

    Description:

    CD84 Human Recombinant, Sf9

    CD84 Molecule, Signaling Lymphocytic Activation Molecule 5, Leukocyte Differentiation Antigen CD84, CD84 Antigen (Leukocyte Antigen), Cell Surface Antigen MAX.3, Hly9-Beta, SLAMF5, Leucocyte Differentiation Antigen CD84, Leukocyte Antigen CD84, SLAM Family Member 5, CD84 Antigen, HCD84, MCD84, LY9B, SLAM family member 5, Cell surface antigen MAX.3, Hly9-beta, Leukocyte differentiation antigen CD84, Signaling lymphocytic activation molecule 5.

    Product # :

    PRO-2409

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    Description

    CD84 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 213 amino acids (22-225 a.a.) and having a molecular mass of 23.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CD84 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD84 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD84 belongs to the signaling lymphocyte activation molecule (SLAM) family which forms a subset of the greater CD2 cell-surface receptor Ig superfamily. CD84, a membrane glycoprotein, is a homophilic adhesion molecule found in various immune cells types and takes part in regulating receptor-mediated signaling in those cells.

    • Synonyms

      CD84 Molecule, Signaling Lymphocytic Activation Molecule 5, Leukocyte Differentiation Antigen CD84, CD84 Antigen (Leukocyte Antigen), Cell Surface Antigen MAX.3, Hly9-Beta, SLAMF5, Leucocyte Differentiation Antigen CD84, Leukocyte Antigen CD84, SLAM Family Member 5, CD84 Antigen, HCD84, MCD84, LY9B, SLAM family member 5, Cell surface antigen MAX.3, Hly9-beta, Leukocyte differentiation antigen CD84, Signaling lymphocytic activation molecule 5.

    • 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

      ADPKDSEIFT VNGILGESVT FPVNIQEPRQ VKIIAWTSKT SVAYVTPGDS ETAPVVTVTH RNYYERIHAL GPNYNLVISD LRMEDAGDYK ADINTQADPY TTTKRYNLQI YRRLGKPKIT QSLMASVNST CNVTLTCSVE KEEKNVTYNW SPLGEEGNVL QIFQTPEDQE LTYTCTAQNP
      VSNNSDSISA RQLCADIAMG FRTHHTGHHH HHH.

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    Cd84 Human Sf9
  • View Data Sheet

    Name :

    GSTM1 Human, Sf9

    Description:

    Glutathione S-Transferase M1 Human Recombinant, Sf9

    GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.

    Product # :

    ENZ-1092

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    Description

    GSTM1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (1-218a.a.) fused to a 9 aa His Tag at C-terminus containing 227 amino acids and having a molecular mass of 26.8kDa. GSTM1 shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    GSTM1 protein solution (0.5mg/ml) contains 40% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

    • Synonyms

      GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.

    • 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

      ADPMPMILGY WDIRGLAHAI RLLLEYTDSS YEEKKYTMGD APDYDRSQWL NEKFKLGLDF PNLPYLIDGA HKITQSNAIL CYIARKHNLC GETEEEKIRV DILENQTMDN HMQLGMICYN PEFEKLKPKY LEELPEKLKL YSEFLGKRPW FAGNKITFVD FLVYDVLDLH RIFEPKCLDA FPNLKDFISR FEGLEKISAY MKSSRFLPRP VFSKMAVWGN KHHHHHH.

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    Gstm1 Protein
  • View Data Sheet

    Name :

    REG4 Human, Sf9

    Description:

    Regenerating Islet-Derived 4 Human Recombinant, Sf9

    Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.

    Product # :

    PRO-2595

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    Description

    REG4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (23-158 a.a.) and fused to a 9 aa His Tag at C-terminus containing a total of 145 amino acids and having a molecular mass of 17kDa.REG4 shows multiple bands between 13.5-18kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    REG4 protein solution (0.25mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.

    • Synonyms

      Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.

    • 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

      ADPDIIMRPS CAPGWFYHKS NCYGYFRKLR NWSDAELECQ SYGNGAHLAS ILSLKEASTI
      AEYISGYQRS QPIWIGLHDP QKRQQWQWID GAMYLYRSWS GKSMGGNKHC AEMSSNNNFL TWSSNECNKR QHFLCKYRPH HHHHH

    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.

    Reg4 Protein
  • View Data Sheet

    Name :

    CHMP5 Human

    Description:

    Charged Multivesicular Body Protein 5 Human Recombinant

    Charged Multivesicular Body Protein 5, SNF7 Domain-Containing Protein 2, Chromosome 9 Open Reading Frame 83, Chromatin-Modifying Protein 5, Apoptosis-Related Protein PNAS-2, Vacuolar Protein Sorting-Associated Protein 60, Chromatin Modifying Protein 5, HSPC177, PNAS-2, HVps60, SNF7DC2, CGI-34, C9orf83.

    Product # :

    PRO-1232

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    Description

    CHMP5 Human Recombinant produced in E. coli is a single polypeptide chain containing 243 amino acids (1-219) and having a molecular mass of 27.0 kDa.CHMP5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CHMP5 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

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    • Introduction

      Charged Multivesicular Body Protein 5 (CHMP5) is a member of the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins comprise the ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and development of endocytic multivesicular bodies (MVBs). Certain CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP the CHMP1A, is essential for both MVB formation and regulation of cell cycle progression.

    • Synonyms

      Charged Multivesicular Body Protein 5, SNF7 Domain-Containing Protein 2, Chromosome 9 Open Reading Frame 83, Chromatin-Modifying Protein 5, Apoptosis-Related Protein PNAS-2, Vacuolar Protein Sorting-Associated Protein 60, Chromatin Modifying Protein 5, HSPC177, PNAS-2, HVps60, SNF7DC2, CGI-34, C9orf83.

    • 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 MGSH MNRLFG KAKPKAPPPS LTDCIGTVDS RAESIDKKIS RLDAELVKYK DQIKKMREGP AKNMVKQKAL RVLKQKRMYE QQRDNLAQQS FNMEQANYTI QSLKDTKTTV DAMKLGVKEM KKAYKQVKID QIEDLQDQLE DMMEDANEIQ EALSRSYGTP ELDEDDLEAE LDALGDELLA DEDSSYLDEA ASAPAIPEGV PTDTKNKDGV LVDEFGLPQI PAS

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    Chmp5 Human
  • View Data Sheet

    Name :

    FCGR3A Human, Sf9

    Description:

    CD16a Human Recombinant, Sf9

    Low affinity immunoglobulin gamma Fc region receptor III-A, CD16a antigen, Fc-gamma, RIII-alpha, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcR-10, IgG Fc receptor III-2, CD16a, FCGR3A, FCG3, FCGR3, IGFR3, CD16, FCGRIII.

    Product # :

    PRO-2360

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    Description

    FCGR3A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 200 amino acids (18-208 a.a.) and having a molecular mass of 22.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).FCGR3A is fused with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    FCGR3A protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Low affinity immunoglobulin gamma Fc region receptor III-A (FCGR3A) is a receptor for the Fc portion of immunoglobulin G, and is involved in the elimination of antigen-antibody complexes from the circulation, as well as other antibody-dependent responses. FCGR3A needs to associate with the gamma subunit of Fc epsilon. The FCGR3A receptor is expressed on natural killer (NK) cells as an integral membrane glycoprotein anchored through a transmembrane peptide, while FCGR3B is expressed on polymorphonuclear neutrophils (PMN) where the receptor is anchored through a phosphatidylinositol (PI) linkage. In addition, FCGR3A is expressed on macrophages, subpopulation of T-cells, immature thymocytes and placental trophoblasts. FCGR3A mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis. FCGR3A gene mutations are linked with susceptibility to recurrent viral infections, susceptibility to systemic lupus erythematosus, and alloimmune neonatal neutropenia.

    • Synonyms

      Low affinity immunoglobulin gamma Fc region receptor III-A, CD16a antigen, Fc-gamma, RIII-alpha, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcR-10, IgG Fc receptor III-2, CD16a, FCGR3A, FCG3, FCGR3, IGFR3, CD16, FCGRIII.

    • 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

      ADPMRTEDLP KAVVFLEPQW YRVLEKDSVT LKCQGAYSPE DNSTQWFHNE SLISSQASSY FIDAATVDDS GEYRCQTNLS TLSDPVQLEV HIGWLLLQAP RWVFKEEDPI HLRCHSWKNT ALHKVTYLQN GKGRKYFHHN SDFYIPKATL KDSGSYFCRG LFGSKNVSSE TVNITITQGL AVSTISSFFP PGYQHHHHHH.

    • Background

      CD16A, also known as Fc gamma receptor IIIA (FcγRIIIA), is a key receptor involved in immune responses and antibody-dependent cell-mediated cytotoxicity (ADCC). This research paper aims to explore the structure, function, and therapeutic implications of CD16A, shedding light on its diverse roles in immune regulation and targeted therapies.

      CD16A is a transmembrane protein expressed primarily on natural killer (NK) cells, macrophages, and a subset of activated neutrophils. It interacts with the Fc portion of immunoglobulin G (IgG) antibodies, thereby mediating ADCC. Upon binding to IgG-coated target cells, CD16A triggers intracellular signaling cascades that initiate immune effector functions, leading to target cell destruction.

      The structure of CD16A consists of an extracellular domain responsible for IgG binding, a transmembrane domain, and an intracellular domain involved in signal transduction. Genetic polymorphisms in CD16A have been identified, leading to variations in its affinity for IgG subclasses and influencing immune responses and disease susceptibility.

      The function of CD16A extends beyond its role in ADCC. It also participates in immune cell activation, cytokine production, and regulation of immune responses. CD16A engagement on NK cells can trigger cytotoxicity and cytokine release, contributing to antiviral and antitumor immune responses. Moreover, CD16A-mediated cross-talk between immune cells modulates immune surveillance and inflammation.

      Therapeutically, CD16A has emerged as a potential target for immunotherapy. Monoclonal antibodies designed to enhance CD16A-mediated ADCC have shown promising results in the treatment of cancer. By engaging CD16A on immune effector cells, these antibodies facilitate targeted cell killing and tumor eradication. Additionally, CD16A-based immunotherapies have been explored in infectious diseases and autoimmune disorders.

      The availability of CD16A human recombinant proteins has facilitated extensive research and drug development efforts. Recombinant CD16A proteins serve as valuable tools for studying CD16A interactions, optimizing immunotherapeutic strategies, and evaluating the efficacy of novel therapeutic agents.

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    Fcgr3A Human Sf9
  • View Data Sheet

    Name :

    PMM1 Human

    Description:

    Phosphomannomutase 1 Human Recombinant

    Phosphomannomutase 1, PMM 1, PMMH-22, PMM1, PMMH22, Sec53.

    Product # :

    ENZ-023

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    Description

    PMM1 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 282 amino acids (1-262 a.a.) and having a molecular mass of 31.9kDa. The PMM1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PMM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 100mM NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphomannomutase 1 (PMM1) is an enzyme involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. PMM1 catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for the synthesis of dolichol-phosphate-mannose, which is crucial for N-linked glycosylation and accordingly the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol (GPI) anchored proteins. Additionally, PMM1 may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.

    • Synonyms

      Phosphomannomutase 1, PMM 1, PMMH-22, PMM1, PMMH22, Sec53.

    • 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 MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV VGGSDYCKIA EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR LPKKRGTFIE FRNGMLNISP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR FSRGGMISFD VFPEGWDKRY CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV VSPQDTVQRC REIFFPETAH EA.

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    Pmm1 Human
  • View Data Sheet

    Name :

    GATM Human

    Description:

    Glycine Amidinotransferase Human Recombinant

    Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.

    Product # :

    ENZ-583

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    Description

    GATM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (38-423) and having a molecular mass of 46.9kDa (Molecular size on SDS-PAGE will appear higher).GATM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycine amidinotransferase mitochondrial (GATM) is a mitochondrial enzyme which is a member of the amidinotransferase family. The GATM enzyme is involved in creatine biosynthesis, where it catalyzes the transfer of a guanido group from L-arginine to glycine, resulting in guanidinoacetic acid, the immediate precursor of creatine, which has an imperative role in energy metabolism in muscle tissues. GATM is significant in embryonic and central nervous system development. GATM gene mutations cause arginine:glycine amidinotransferase deficiency, an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders.

    • Synonyms

      Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.

    • 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 MGSMSTQAAT ASSRNSCAAD DKATEPLPKD CPVSSYNEWD PLEEVIVGRA ENACVPPFTI EVKANTYEKY WPFYQKQGGH YFPKDHLKKA VAEIEEMCNI LKTEGVTVRR PDPIDWSLKY KTPDFESTGL YSAMPRDILI VVGNEIIEAP MAWRSRFFEY
      RAYRSIIKDY FHRGAKWTTA PKPTMADELY NQDYPIHSVE DRHKLAAQGK FVTTEFEPCF DAADFIRAGR DIFAQRSQVT NYLGIEWMRR HLAPDYRVHI ISFKDPNPMH IDATFNIIGP GIVLSNPDRP CHQIDLFKKA GWTIITPPTP IIPDDHPLWM SSKWLSMNVL MLDEKRVMVD
      ANEVPIQKMF EKLGITTIKV NIRNANSLGG GFHCWTCDVR RRGTLQSYLD.

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    Gatm Human
  • View Data Sheet

    Name :

    MAPT Human

    Description:

    Microtubule-Associated Protein Tau Human Recombinant

    TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.

    Product # :

    PRO-295

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    Description

    MAPT Recombinant Human (Isoform-4) produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (1-352 a.a.) and having a molecular mass of 38.9 kDa (Real molecular weight on SDS-PAGE will be shift up). The MAPT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAPT solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPT is a neuronal microtubule associated protein localized mostly on axons.
      MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain.

    • Synonyms

      TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.

    • 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 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL.

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    Mapt Human
  • View Data Sheet

    Name :

    AHCY Human, Sf9

    Description:

    Adenosylhomocysteinase Human Recombinant, Sf9

    EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

    Product # :

    ENZ-1034

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    • description
    • source
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    Description

    AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    AHCY protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.

    • Synonyms

      EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

    • 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

      ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH 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.

    Ahcy Human Sf9
  • View Data Sheet

    Name :

    CDKN1A Human

    Description:

    Cyclin-Dependent Kinase Inhibitor 1A Human Recombinant

    Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

    Product # :

    PKA-043

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    Quantity :

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    Description

    CDKN1A Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (1-164) and having a molecular mass of 20.2 kDa.CDKN1A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDKN1A solution contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDKN1A holds a key part in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. When collaborating with CDK2 complexes, CDKN1A aids to prevent kinase activity and inhibits progression through G1/S. Nevertheless, CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D. CDKN1A is a vital intermediary by which p53/TP53 facilitates its part as an inhibitor of cellular proliferation as a reaction to DNA impairment.

    • Synonyms

      Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

    • 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 MSEPAGDVRQ NPCGSKACRR LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLE GDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLV PRSGEQAEGS PGGPGDSQGR KRRQTSMTDF YHSKRRLIFS KRKP.

    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.

    Cdkn1A Human
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