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Search results

1000 results found for “Syntaxin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    OSM Human, 195 a.a

    Description:

    Oncostatin-M Human Recombinant (195 a.a.)

    OSM, MGC20461, Oncostatin M.

    Product # :

    CYT-735

    Price :

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    • source
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    Description

    Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids and having a molecular mass of 22kDa. The OSM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 1xPBS pH-7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of human TF-1 cells is < 0.2ng/ml, corresponding to a specific activity of > 5.0x106 units/mg.

    More Info

    • Introduction

      Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

    • Synonyms

      OSM, MGC20461, Oncostatin M.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSR.

    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.

    Oncostatin M Human 195 Aa
  • View Data Sheet

    Name :

    OXSM Human

    Description:

    3-Oxoacyl-ACP Synthase, Mitochondrial Human Recombinant

    3-Oxoacyl-ACP Synthase Mitochondrial, Type II Mitochondrial Beta-Ketoacyl Synthase, 3-Ketoacyl-Acyl Carrier Protein Synthase, FASN2D, KASI, EC 2.3.1, Beta-Ketoacyl-ACP Synthase.

    Product # :

    ENZ-751

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    Description

    OXSM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (28-459) and having a molecular mass of 48.1kDa.OXSM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OXSM solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      OXSM, a beta-ketoacyl synthetase, is essential for elongation of fatty acid chains in the mitochondria. Alternatively spliced transcript variants were found.

    • Synonyms

      3-Oxoacyl-ACP Synthase Mitochondrial, Type II Mitochondrial Beta-Ketoacyl Synthase, 3-Ketoacyl-Acyl Carrier Protein Synthase, FASN2D, KASI, EC 2.3.1, Beta-Ketoacyl-ACP Synthase.

    • 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 MGSKRKFFGT VPISRLHRRV VITGIGLVTP LGVGTHLVWD RLIGGESGIV SLVGEEYKSI PCSVAAYVPR GSDEGQFNEQ NFVSKSDIKS MSSPTIMAIG AAELAMKDSG WHPQSEADQV ATGVAIGMGM IPLEVVSETA LNFQTKGYNK VSPFFVPKIL VNMAAGQVSI RYKLKGPNHA VSTACTTGAH AVGDSFRFIA HGDADVMVAG GTDSCISPLS LAGFSRARAL STNSDPKLAC RPFHPKRDGF VMGEGAAVLV LEEYEHAVQR RARIYAEVLG YGLSGDAGHI TAPDPEGEGA LRCMAAALKD AGVQPEEISY INAHATSTPL GDAAENKAIK HLFKDHAYAL AVSSTKGATG HLLGAAGAVE AAFTTLACYY QKLPPTLNLD CSEPEFDLNY VPLKAQEWKT EKRFIGLTNS FGFGGTNATL CIAGL.

    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.

    Oxsm Human
  • View Data Sheet

    Name :

    EXOSC10 Human

    Description:

    Exosome Component 10 Human Recombinant

    Exosome component 10, Polymyositis/scleroderma autoantigen 2, Autoantigen PM/Scl 2, Polymyositis/scleroderma autoantigen 100 kDa, PM/Scl-100, P100 polymyositis-scleroderma overlap syndrome-associated autoantigen, EXOSC10, PMSCL, PMSCL2, p2, p3, p4, RRP6, Rrp6p, PM-Scl.

    Product # :

    PRO-444

    Price :

    Quantity :

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    Description

    EXOSC10 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 102 kDa. EXOSC10 is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    EXOSC10 is supplied in 20mM HEPES, pH-7.5, 100mM NaCl, 0.01mM EDTA, 0.02% SDS.

    Purity

    Greater than 93% as determined by SDS-PAGE.

    More Info

    • Introduction

      EXOSC10 is a nucleolar protein and represents one crucial component of the so-called "PM/Scl complex" or "nuclear exosome", which is an RNA-processing complex consisting of a number of exoribonucleases (not to be confused with certain multivesicular bodies which are shed by cultured cells into the culture fluid and are also called exosomes).
      Autoantibodies against EXOSC10 occur in patients suffering from polymyositis, scleroderma or polymyositis/scleroderma overlap syndromes. While antibodies to other components of the exosome complex (PM/Scl 75, several Rrp proteins) can be found in some sera, practically all patients with autoantibodies against the PM/Scl complex are positive for EXOSC10 antibodies, making this specificity an important marker. The presence of EXOSC10 autoantibodies is a comparatively "good" prognostic sign in polymyositis/scleroderma overlap syndrome unlike the poor prognosis seen when other myositis and systemic sclerosis specific autoantibodies are present.

    • Synonyms

      Exosome component 10, Polymyositis/scleroderma autoantigen 2, Autoantigen PM/Scl 2, Polymyositis/scleroderma autoantigen 100 kDa, PM/Scl-100, P100 polymyositis-scleroderma overlap syndrome-associated autoantigen, EXOSC10, PMSCL, PMSCL2, p2, p3, p4, RRP6, Rrp6p, PM-Scl.

    • 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.Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera panels).

    • coating concentration

      0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.

    • Applications

      Western-Blot with monoclonal anti-hexa-His-tag antibody & polymyositis patient sera.

    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.

    Exosc10 Human
  • View Data Sheet

    Name :

    PAX8 Human

    Description:

    Paired Box 8 Human Recombinant

    Paired Box 8, Paired Box Gene 8, PAX8.

    Product # :

    PRO-2134

    Price :

    Quantity :

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    Description

    PAX8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-287 a.a) and having a molecular mass of 33.4kDa.PAX8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PAX8 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Paired box 8, also known as PAX8 functions in thyroid follicular cell development as well as in expression of thyroid-specific genes. PAX8 complexes with TTF-1& TTF-2 in order to stimulate thyroid follicular cell differentiation and thyroid hormone biosynthesis by regulating the expression of NIS (sodium iodide symporter) , TPO (thyroid peroxidase), TG (thyroglobulin) and the TSHR (thyrotropin receptor). Defects in PAX8 are the cause of CHNG2 (congenital hypothyroidism non-goitrous type 2).

    • Synonyms

      Paired Box 8, Paired Box Gene 8, PAX8.

    • 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 MGSMPHNSIR SGHGGLNQLG GAFVNGRPLP EVVRQRIVDL AHQGVRPCDI SRQLRVSHGC VSKILGRYYE TGSIRPGVIG GSKPKVATPK VVEKIGDYKR QNPTMFAWEI RDRLLAEGVC DNDTVPSVSS INRIIRTKVQ QPFNLPMDSC VATKSLSPGH TLIPSSAVTP PESPQSDSLG STYSINGLLG IAQPGSDKRK MDDSDQDSCR LSIDSQSSSS GPRKHLRTDA FSQHHLEPLE CPFERQHYPE AYASPSHTKG EQEVNTLAMP MATPPTPPTA RPGASPTPAC

    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.

    Pax8 Human
  • View Data Sheet

    Name :

    PICK1 Human

    Description:

    Protein Interacting With PRKCA 1 Human Recombinant

    Protein Interacting With PRKCA 1, PRKCABP, Protein Kinase C-Alpha-Binding Protein, Protein Interacting With C Kinase 1, Protein Kinase C, Alpha Binding Protein, Protein Interacting With PRKCA, PRKCA-Binding Protein, PICK, PRKCA-binding protein.

    Product # :

    PKA-072

    Price :

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    Description

    PICK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 438 amino acids (1-415 a.a) and having a molecular mass of 49.0kDa. PICK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PICK1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein Interacting with PRKCA 1, also known as PICK1 includes a PDZ domain, through which it interacts with protein kinase C, alpha (PRKCA). PICK1 performs as an adaptor which binds to and arranges the subcellular localization of various membrane proteins. PICK1 interacts with multiple glutamate receptor subtypes, monoamine plasma membrane transporters, in addition to non-voltage gated sodium channels, and might target PRKCA to these membrane proteins and therefore regulates their distribution as well as function. PICK1 has also been found to perform as an anchoring protein which particularly targets PRKCA to mitochondria in a ligand-specific manner.

    • Synonyms

      Protein Interacting With PRKCA 1, PRKCABP, Protein Kinase C-Alpha-Binding Protein, Protein Interacting With C Kinase 1, Protein Kinase C, Alpha Binding Protein, Protein Interacting With PRKCA, PRKCA-Binding Protein, PICK, PRKCA-binding 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 MGSMFADLDY DIEEDKLGIP TVPGKVTLQK DAQNLIGISI GGGAQYCPCL YIVQVFDNTP AALDGTVAAG DEITGVNGRS IKGKTKVEVA KMIQEVKGEV TIHYNKLQAD PKQGMSLDIV LKKVKHRLVE NMSSGTADAL GLSRAILCND GLVKRLEELE RTAELYKGMT EHTKNLLRAF YELSQTHRAF GDVFSVIGVR EPQPAASEAF VKFADAHRSI EKFGIRLLKT IKPMLTDLNT YLNKAIPDTR LTIKKYLDVK FEYLSYCLKV KEMDDEEYSC IALGEPLYRV STGNYEYRLI LRCRQEARAR FSQMRKDVLE KMELLDQKHV QDIVFQLQRL VSTMSKYYND CYAVLRDADV FPIEVDLAHT TLAYGLNQEE FTDGEEEEEE EDTAAGEPSR DTRGAAGPLD KGGSWCDS.

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    Pick1 Human
  • View Data Sheet

    Name :

    CD207 Human, sf9

    Description:

    CD207 Human Recombinant, sf9

    C-type lectin domain family 4 member K, Langerin, CD207, CD207 Molecule, CD207 Molecule, Langerin, CD207 Antigen, Langerin, CLEC4K, Langerhans Cell Specific C-Type Lectin, Langerin.

    Product # :

    PRO-2317

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    Description

    CD207 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 273 amino acids (65-328 a.a.) and having a molecular mass of 30.9kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). CD207 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD207 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD207 (C-type lectin domain family 4 member K) is expressed in Langerhans cells which are immature dendritic cells of the epidermis and mucosa. Moreover, CD207 is expressed in several other dendritic cell types including dermal CD103+ DCs and splenic CD8+ DCs. Langerin is localized in the Birbeck granules, the organelles present in the cytoplasm of Langerhans cells and comprised of superimposed and zippered membranes. CD207 is a C-type lectin with mannose binding specificity, and it has been suggested that mannose binding by the CD207 protein leads to internalization of antigen into Birbeck granules thus providing access to a nonclassical antigen-processing pathway.

    • Synonyms

      C-type lectin domain family 4 member K, Langerin, CD207, CD207 Molecule, CD207 Molecule, Langerin, CD207 Antigen, Langerin, CLEC4K, Langerhans Cell Specific C-Type Lectin, Langerin.

    • 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

      ADPPRFMGTI SDVKTNVQLL KGRVDNISTL DSEIKKNSDG MEAAGVQIQM VNESLGYVRS QFLKLKTSVE KANAQIQILT RSWEEVSTLN AQIPELKSDL EKASALNTKI RALQGSLENM SKLLKRQNDI LQVVSQGWKY FKGNFYYFSL IPKTWYSAEQ FCVSRNSHLT SVTSESEQEF LYKTAGGLIY WIGLTKAGME GDWSWVDDTP FNKVQSARFW IPGEPNNAGN NEHCGNIKAP SLQAWNDAPC DKTFLFICKR PYVPSEPHHH HHH.

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    Cd207 Human Sf9
  • View Data Sheet

    Name :

    TPSAB1 Human

    Description:

    Tryptase Alpha/Beta 1 Human Recombinant

    Tryptase Alpha/Beta 1, Tryptase Alpha II, Tryptase Beta-1, Tryptase Alpha-1, Tryptase Alpha/Beta-1, Tryptase-I, TPS1, TPS2, TPSB1, Tryptase-III, Mast Cell Alpha II Tryptase, Mast Cell Beta I Tryptase, EC 3.4.21.59.

    Product # :

    ENZ-652

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    Description

    TPSAB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 270 amino acids (31-275) and having a molecular mass of 30.1 kDa.TPSAB1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TPSAB1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tryptase alpha/beta-1 (TPSAB1) is a tryptase which is the key neutral protease present in mast cells and is discharged upon the coupled activation-degranulation response of this cell type. TPSAB1 is enzymatically active only as a heparin-stabilized tetramer, and is resistant to all known endogenous proteinase inhibitors. TPSAB1 is implicated as a mediator in the pathogenesis of asthma and other allergic and inflammatory disorders.

    • Synonyms

      Tryptase Alpha/Beta 1, Tryptase Alpha II, Tryptase Beta-1, Tryptase Alpha-1, Tryptase Alpha/Beta-1, Tryptase-I, TPS1, TPS2, TPSB1, Tryptase-III, Mast Cell Alpha II Tryptase, Mast Cell Beta I Tryptase, EC 3.4.21.59.

    • 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 MGSHMIVGGQ EAPRSKWPWQ VSLRVHGPYW MHFCGGSLIH PQWVLTAAHC VGPDVKDLAA LRVQLREQHL YYQDQLLPVS RIIVHPQFYT AQIGADIALL ELEEPVNVSS HVHTVTLPPA SETFPPGMPC WVTGWGDVDN DERLPPPFPL KQVKVPIMEN HICDAKYHLG AYTGDDVRIV RDDMLCAGNT RRDSCQGDSG GPLVCKVNGT WLQAGVVSWG EGCAQPNRPG IYTRVTYYLD WIHHYVPKKP.

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    Tpsab1 Human
  • View Data Sheet

    Name :

    Procalcitonin Mouse

    Description:

    Procalcitonin Mouse Recombinant

    Calcitonin, Calca, Calc.

    Product # :

    HOR-014

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    Description

    Procalcitonin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val26-Ser136) containing 121 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 13.6kDa.

    Source

    Escherichia Coli.

    Formulation

    Procalcitonin was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 94.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Calcitonin, Calca, Calc.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASVPLRSILESS PGMATLSEEE VRLLAALVQD YMQMKARELE QEEEQEAEGS SLDSPRSKRC GNLSTCMLGT YTQDLNKFHT FPQTSIGVEA PGKKRDVAKD LETNHQSHFG N.

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    Procalcitonin Mouse
  • View Data Sheet

    Name :

    GPX3 Human

    Description:

    Glutathione Peroxidase 3 Human Recombinant

    Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.

    Product # :

    ENZ-579

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    Description

    GPX3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (21-226) and having a molecular mass of 25.7kDa.GPX3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GPX3 solution contains 20mM Tris-HCl buffer (pH7.5), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutathione peroxidase 3 (GPX3) is a member of the glutathione peroxidase family, which acts in the detoxification of hydrogen peroxide. GPX3 shields cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. The GPX3 protein is one of only a few proteins known in higher vertebrates to contain selenocysteine, which occurs at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA.

    • Synonyms

      Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.

    • 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 MQSRGQEKSK MDCHGGISGT IYEYGALTID GEEYIPFKQY AGKYVLFVNV ASYCGLTGQY IELNALQEEL APFGLVILGF PCNQFGKQEP GENSEILPTL KYVRPGGGFV PNFQLFEKGD VNGEKEQKFY TFLKNSCPPT SELLGTSDRL FWEPMKVHDI RWNFEKFLVG PDGIPIMRWH HRTTVSNVKM DILSYMRRQA ALGVKRK.

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    Gpx3 Human
  • View Data Sheet

    Name :

    TSHR Human

    Description:

    Thyroid Stimulating Hormone Receptor Human Recombinant

    Product # :

    HOR-051

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    Description

    Recombinant Human Thyroid Stimulating Hormone Receptor produced in E. coli forms a dimer migrating at 46kDa on SDS-PAGE. TSHR Human contains multiple Leucine rich repeats with a histidine tag at N-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    TSHR solution (0.9mg/ml) contains PBS & 25mM K2CO3.

    Purity

    Protein is >85%.

    More Info

    • 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.

    • Applications

      Serological assay for TSH receptor autoantibody.

    • Background

      The thyroid-stimulating hormone receptor (TSHR) is a critical component of the hypothalamic-pituitary-thyroid axis, playing an essential role in regulating thyroid function. TSHR, located on the surface of thyroid follicular cells, mediates the effects of thyroid-stimulating hormone (TSH) by stimulating the production and release of thyroid hormones. Research into human TSHR has revealed its significance not only in normal thyroid physiology but also in the pathogenesis of various thyroid disorders, including Graves' disease and thyroid cancer. This paper aims to provide an overview of research publications and information on human TSHR, highlighting its structure, function, and clinical implications.

      What is the molecular weight/Mw of TSHR Protein?
      TSHR Protein has a total Mw of 46kDa.

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

      What is the Purity of TSHR Protein?
      TSHR Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of TSHR Protein?
      The biological functionality of TSHR Protein will be determined in the future.

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

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


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    Tshr Human
  • View Data Sheet

    Name :

    CSNK2A1 Antibody

    Description:

    Casein Kinase 2 alpha, Mouse Anti Human

    Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.

    Product # :

    ANT-372

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      The Casein kinase 2 (EC 2.7.11.1) is a serine/threonine-selective protein kinase that is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm and other cellular processes. Casein kinase 2 activity has been reported to be activated following Wnt signaling pathway activation. A Pertussis toxin-sensitive G protein and Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2. Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm.

    • Synonyms

      Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.

    • Immunogen

      Anti-human CSNK2A1 mAb is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CSNK2A1 amino acids 1-391 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P3G1AT.

    • Applications

      CSNK2A1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      CSNK2A1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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    Csnk2A1 Antibody
  • View Data Sheet

    Name :

    DSIP

    Description:

    Delta Sleep Inducing Peptide

    Product # :

    HOR-030

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    Description

    DSIP Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH

    • Background

      Delta Sleep-Inducing Peptide (DSIP), also known as Sleep-Promoting Peptide, is a neuropeptide that has been the subject of extensive research due to its potential role in sleep regulation, stress response, and neuroprotection. This nonapeptide, first isolated from the cerebral venous blood of rabbits during sleep, has been shown to induce slow-wave sleep, modulate pain perception, and exhibit potential antioxidant and immunomodulatory properties.

      DSIP's primary function is its interaction with the sleep regulatory system. By modulating the release of certain neurotransmitters, DSIP can influence sleep patterns, particularly promoting slow-wave sleep, the most restorative stage of sleep. Studies by Kovalzon et al. (2011) have demonstrated that DSIP can enhance sleep quality in rats, suggesting potential applications in sleep disorders and the promotion of healthy sleep patterns.

      In addition to its sleep-inducing effects, DSIP has been shown to possess neuroprotective properties. Research by Zolotarev et al. (2014) found that DSIP could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.

      Given its sleep-inducing and neuroprotective effects, DSIP has been proposed as a potential therapeutic agent for a variety of conditions, including sleep disorders, chronic pain, and neurodegenerative diseases. For instance, a study by Spong et al. (2016) found that DSIP could improve sleep quality in patients with chronic insomnia, indicating its potential as a therapeutic agent in the treatment of sleep disorders.

      While research on DSIP is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of DSIP in humans. However, the existing body of research suggests that DSIP could be a promising tool in the treatment of sleep disorders, chronic pain, and neurodegenerative diseases.

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    Dsip
  • View Data Sheet

    Name :

    Humanin

    Description:

    Humanin

    Product # :

    HOR-042

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    Description

    Humanin Synthetic is a single, non-glycosylated polypeptide chain containing 24 amino acids, having a molecular mass of 2687 Dalton and a Molecular formula of C119H204N34O32S2 .

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH.

    • Background

      Humanin, a small peptide derived from the mitochondrial genome, has emerged as a remarkable molecule with diverse cellular protective functions. This research paper aims to provide a comprehensive analysis of Humanin, exploring its biochemical properties, mechanisms of action, and potential therapeutic applications in various disease contexts.

      Humanin, initially discovered for its role in neuroprotection, has since garnered interest for its broad spectrum of cytoprotective effects. Derived from the mitochondrial 16S ribosomal RNA, this small peptide plays a critical role in safeguarding cells from various stressors (Harvey, 2008). This paper delves into the complexities of Humanin, uncovering its multifaceted nature and potential clinical applications.

      Humanin is a 24-amino acid peptide with a unique secondary structure that contributes to its cellular protective functions. It localizes to both the cytoplasm and mitochondria, where it interacts with various proteins involved in apoptotic and oxidative stress pathways (Hoang et al., 2019). Additionally, Humanin can undergo post-translational modifications, further diversifying its actions.

      Humanin exerts its protective effects through multiple mechanisms. It interacts with the pro-apoptotic protein Bax, inhibiting its translocation to the mitochondria and preventing the release of cytochrome c (Hashimoto et al., 2001). Humanin also modulates the activities of caspases, key mediators of cell death pathways, thereby promoting cell survival in stressful conditions (Nakagawa et al., 2002).

      Beyond its initial recognition as a neuroprotective agent, Humanin has demonstrated cytoprotective effects in various cell types, including cardiomyocytes, neurons, and endothelial cells (Chai et al., 2019). It attenuates oxidative stress, reduces mitochondrial dysfunction, and promotes cell viability, thereby safeguarding cells from a multitude of insults.

      The multifaceted protective functions of Humanin offer promising therapeutic potential in various disease contexts. Research has shown its efficacy in mitigating neurodegenerative disorders, cardiovascular diseases, and age-related pathologies (Muzumdar et al., 2009). Furthermore, Humanin's ability to attenuate inflammation and promote tissue repair opens new avenues for therapeutic interventions.

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    Humanin
  • View Data Sheet

    Name :

    Adiponectin Mouse, His

    Description:

    Adiponectin Mouse Recombinant, His Tag

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-537

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    • sds-page

    Description

    The Adiponectin Mouse is created as a recombinant protein with a 21 a.a N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 27.2kDa protein containing 251 amino acid residues of the Acrp30 Mouse, 18-247 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Acrp30 Mouse is a sterile filtered liquid formulation containing (1mg/ml) 20mM Tris-HCl pH-8, 1mM DTT and 10% Glycerol.

    Purity

    Acrp30 Mouse purity is greater than 90% as determined by SDS-PAGE.

    sds-page

    Adiponectin-sds-page - Product image 1

    More Info

    • Introduction

      Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • 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 MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 27.2kDa.

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

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of ADIPONECTIN Protein?
      The biological functionality of ADIPONECTIN Protein will be determined in the future.

      What is the amino acid sequence of ADIPONECTIN Protein?
      MGSSHHHHHH SSGLVPRGSH MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.

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

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

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

    Acrp30 Mouse His
  • View Data Sheet

    Name :

    CSTF1 Human

    Description:

    Cleavage Stimulation Factor 1 Human Recombinant

    Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

    Product # :

    PRO-1170

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    Description

    CSTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-431 a.a) and having a molecular mass of 49.4kDa.CSTF1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSTF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.

    • Synonyms

      Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

    • 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

      MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DVEHHHHHH.

    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.

    Cstf1 Human
  • View Data Sheet

    Name :

    CTACK Human

    Description:

    CTACK Human Recombinant (CCL27)

    ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.

    Product # :

    CHM-373

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    • SDS-PAGE

    Description

    CTACK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids (25-112 a.a.) and having a molecular mass of 10.3kDa. CTACK protein is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CTACK Human solution containing 10mM sodium citrate pH-3.5 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    SDS-PAGE

    CTACK Human-SDS-PAGE - Product image 1

    More Info

    • Introduction

      CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.

    • Synonyms

      ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.

    • 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

      MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.

    • Background

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

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

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

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

      What is the amino acid sequence of CTACK HUMAN Protein?
      MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.

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

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

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

    Ctack Human
  • View Data Sheet

    Name :

    ACSF2 Human

    Description:

    Acyl-CoA Synthetase Family Member 2 Human Recombinant

    Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.

    Product # :

    ENZ-919

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    Description

    ACSF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (42-615 a.a) and having a molecular mass of 66.1kDa. ACSF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    ACSF2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline pH 7.4 and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acyl-CoA synthetase family member 2, also known as ACSF2 is a member of the ATP-dependent AMP-binding enzyme family. Acyl-CoA synthetases are a family of enzymes which catalyze the thioesterification of fatty acids with coenzymeA to form activated intermediates, which play a basic part in lipid metabolism as well as homeostasis of lipid-related processes. ACSF2 is required for the complex of lipid synthesis, energy production via beta-oxidation, protein acylation and fatty-acid dependent transcriptional regulation. Moreover, ACSF2 is required for fatty acid import into cells by the process of vectorial acylation.

    • Synonyms

      Acyl-CoA Synthetase Family Member 2, PPARG Binding, Long Chain Fatty Acid Acyl Co-A Ligase Like, Acyl-CoA Synthetase Family Member 2, Mitochondrial, EC 6.2.1.26, EC 6.2.1.-, FLJ20920, EC 6.2.1, AVYV493, ACSMW, Acyl-CoA synthetase family member 2, mitochondrial.

    • 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 MGSLSSREVD RMVSTPIGGL SYVQGCTKKH LNSKTVGQCL ETTAQRVPER EALVVLHEDV RLTFAQLKEE VDKAASGLLS IGLCKGDRLG MWGPNSYAWV LMQLATAQAG IILVSVNPAY QAMELEYVLK KVGCKALVFP KQFKTQQYYN VLKQICPEVE NAQPGALKSQ RLPDLTTVIS VDAPLPGTLL LDEVVAAGST RQHLDQLQYN QQFLSCHDPI NIQFTSGTTG SPKGATLSHY NIVNNSNILG ERLKLHEKTP EQLRMILPNP LYHCLGSVAG TMMCLMYGAT LILASPIFNG KKALEAISRE RGTFLYGTPT MFVDILNQPD FSSYDISTMC GGVIAGSPAP PELIRAIINK INMKDLVVAY GTTENSPVTF AHFPEDTVEQ KAESVGRIMP HTEARIMNME AGTLAKLNTP GELCIRGYCV MLGYWGEPQK TEEAVDQDKW YWTGDVATMN EQGFCKIVGR SKDMIIRGGE NIYPAELEDF FHTHPKVQEV QVVGVKDDRM GEEICACIRL KDGEETTVEE IKAFCKGKIS HFKIPKYIVF VTNYPLTISG KIQKFKLREQ MERHLNL.

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    Acsf2 Human
  • View Data Sheet

    Name :

    CTDSPL Human

    Description:

    CTD Small Phosphatase-Like Human Recombinant

    CTD small phosphatase-like protein, CTDSP-like, Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3, NIF-like protein, Nuclear LIM interactor-interacting factor 1, NLI-interacting factor 1, Protein YA22, hYA22, RBSP3, Small C-terminal domain phosphatase 3, SCP3, Small CTD phosphatase 3, CTDSPL, C3orf8, NIF1, NIFL, SCP3, YA22, PSR1.

    Product # :

    ENZ-569

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    Description

    CTDSPL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (82-265) and having a molecular mass of 23.9kDa.CTDSPL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTDSPL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTD small phosphatase-like protein (CTDSPL) specially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the biggest RNA polymerase II subunit POLR2A. CTDSPL negatively regulates RNA polymerase II transcription, probably by directing the transition from initiation/capping to processive transcript elongation. CTDSPL is employed by REST to neuronal genes which contain RE-1 elements, directing to neuronal gene silencing in non-neuronal cells.

    • Synonyms

      CTD small phosphatase-like protein, CTDSP-like, Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3, NIF-like protein, Nuclear LIM interactor-interacting factor 1, NLI-interacting factor 1, Protein YA22, hYA22, RBSP3, Small C-terminal domain phosphatase 3, SCP3, Small CTD phosphatase 3, CTDSPL, C3orf8, NIF1, NIFL, SCP3, YA22, PSR1.

    • 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 MGSHMKYLLP EVTVLDYGKK CVVIDLDETL VHSSFKPISN ADFIVPVEID GTIHQVYVLK RPHVDEFLQR MGQLFECVLF TASLAKYADP VADLLDRWGV FRARLFRESC VFHRGNYVKD LSRLGRELSK VIIVDNSPAS YIFHPENAVP VQSWFDDMTD TELLDLIPFF EGLSREDDVY SMLHRLCNR.

    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.

    Ctdspl Human
  • View Data Sheet

    Name :

    S100P Human, His

    Description:

    S100 Calcium Binding Protein P Human Recombinant, His Tag

    Protein S100-E, S100E, Migration-Inducing Gene 9, MIG9.

    Product # :

    PRO-830

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    Description

    S100P Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 115 amino acids (1-95a.a.) and having a molecular mass of 12.6 kDa. S100P protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    S100P Human solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.05M NaCl & 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100P is a Ca2+ binding protein that is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are found in the cytoplasm and/or nucleus of a large range of cells, and participates in the regulation of a number of cellular function such as cell cycle progression and differentiation. S100P participates in numerous biological functions but the exact functions or mechanism of its action is still mostly unknown. Once S100P binds calcium ions it goes through a conformational change that results in an exposure of a hydrophobic surface which permits the interaction with specific target proteins.

    • Synonyms

      Protein S100-E, S100E, Migration-Inducing Gene 9, MIG9.

    • 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 MTELETAMGM IIDVFSRYSG SEGSTQTLTK GELKVLMEKE LPGFLQSGKD KDAVDKLLKD LDANGDAQVD FSEFIVFVAA ITSACHKYFE KAGLK.

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    S100P Human His
  • View Data Sheet

    Name :

    CTSS Human

    Description:

    Cathepsin-S Human Recombinant

    Cathepsin S, MGC3886, CTSS, Cathepsin-S.

    Product # :

    ENZ-686

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    Description

    CTSS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (17-331) and having a molecular mass of 38.1kDa. CTSS is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTSS 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

      Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.

    • Synonyms

      Cathepsin S, MGC3886, CTSS, Cathepsin-S.

    • 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 MQLHKDPTLD HHWHLWKKTY GKQYKEKNEE AVRRLIWEKN LKFVMLHNLE HSMGMHSYDL GMNHLGDMTS EEVMSLMSSL RVPSQWQRNI TYKSNPNWIL PDSVDWREKG CVTEVKYQGS CGACWAFSAV GALEAQLKLK TGKLVSLSAQ NLVDCSTEKY GNKGCNGGFM TTAFQYIIDN KGIDSDASYP YKAMDQKCQY DSKYRAATCS KYTELPYGRE DVLKEAVANK GPVSVGVDAR HPSFFLYRSG VYYEPSCTQN VNHGVLVVGY GDLNGKEYWL VKNSWGHNFG EEGYIRMARN KGNHCGIASF PSYPEI.

    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.

    Ctss Human
  • View Data Sheet

    Name :

    NAA50 Human

    Description:

    N Alpha-Acetyltransferase 50, NatE Catalytic Subunit Human Recombinant

    N-alpha-acetyltransferase 50, N-acetyltransferase 13, N-acetyltransferase 5, hNAT5, N-acetyltransferase san homolog, hSAN, NatE catalytic subunit, NAA50, MAK3, NAT13, NAT5, SAN.

    Product # :

    ENZ-424

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    Description

    NAA50 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (1-169) and having a molecular mass of 21.9kDa.NAA50 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NAA50 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-alpha-acetyltransferase 50 (NAA50) consists of 169 amino acid cytoplasmic protein belonging to the acetyltransferase family and GNAT subfamily. NAA50 is a likely catalytic component of the ARD1A-NARG1 complex which displays alpha acetyltransferase activity. NAA50 has also been shown to interact with MAK10 and is encoded by a gene that maps to human chromosome 3q13.2.

    • Synonyms

      N-alpha-acetyltransferase 50, N-acetyltransferase 13, N-acetyltransferase 5, hNAT5, N-acetyltransferase san homolog, hSAN, NatE catalytic subunit, NAA50, MAK3, NAT13, NAT5, SAN.

    • 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 MGSHMKGSRI ELGDVTPHNI KQLKRLNQVI FPVSYNDKFY KDVLEVGELA KLAYFNDIAV GAVCCRVDHS QNQKRLYIMT LGCLAPYRRL GIGTKMLNHV LNICEKDGTF DNIYLHVQIS NESAIDFYRK FGFEIIETKK NYYKRIEPAD AHVLQKNLKV
      PSGQNADVQK TDN.

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    Naa50 Human
  • View Data Sheet

    Name :

    SHH Mouse, His

    Description:

    Sonic HedgeHog Mouse Recombinant, His Tag

    SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    Product # :

    CYT-711

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    Description

    SHH Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 183 amino acids (25-198 a.a.) and having a molecular mass of 20.8 kDa. SHH protein is fused to a 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SHH Mouse His Tag solution containing 20mM Trsi HCL pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

    • Synonyms

      SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MCGPGRGFGK RRHPKKLTPL AYKQFIPNVA EKTLGASGRY EGKITRNSER FKELTPNYNP DIIFKDEENT GADRLMTQRC KDKLNALAIS VMNQWPGVKL RVTEGWDEDG HHSEESLHYE GRAVDITTSD RDRSKYGMLA RLAVEAGFDW VYYESKAHIH CSVKAENSVA AKSGGLEHHH HHH.

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    Shh Mouse His
  • View Data Sheet

    Name :

    DSTN Human

    Description:

    Destrin Human Recombinant

    Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.

    Product # :

    PRO-1137

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    Description

    DSTN Human Recombinant produced in E. coli is a single polypeptide chain containing 173 amino acids (1-165) and having a molecular mass of 19.5 kDa.DSTN is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DSTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Actin depolymerizing factor (Destrin/DSTN) belongs to the ADF/Cofilin/destrin superfamily which has the ability to swiftly depolymerize F-Actin in a stoichiometric mode. The ADF family of proteins is responsible for enhancing the turnover rate of actin in vivo. Destrin is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. DSTN functions in a pH-independent manner. DSTN is found in a variety of epithelial and endothelial cells, however it is virtually nonexistent in adult mouse heart and skeletal muscle cells. Destrin shares a 71% sequence homology with Cofilin, however the 2 proteins vary in their interaction with Actin.

    • Synonyms

      Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.

    • 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

      MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPVLEHHH HHH

    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.

    Dstn Human
  • View Data Sheet

    Name :

    NEU1 Human

    Description:

    Sialidase 1 Human Recombinant

    Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

    Product # :

    ENZ-645

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NEU1 Human Recombinant produced in E. coli is a single polypeptide chain containing 393 amino acids (48-415) and having a molecular mass of 42.9 kDa.NEU1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NEU1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sialidase 1 (NEU1) is a lysosomal enzyme which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, the NEU1 enzyme is part of a heterotrimeric complex in cooperation with beta-galactosidase and cathepsin A. NEU1 gene mutations may lead to sialidosis, a lysosomal storage disease that can be the type 1 (cherry red -myoclonus syndrome or normosomatic type), which is late-onset, or the type 2 (the dysmorphic type), which takes place at an earlier age with increased acuteness.

    • Synonyms

      Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

    • 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 MGSHMENDFG LVQPLVTMEQ LLWVSGRQIG SVDTFRIPLI TATPRGTLLA FAEARKMSSS DEGAKFIALR RSMDQGSTWS PTAFIVNDGD VPDGLNLGAV VSDVETGVVF LFYSLCAHKA GCQVASTMLV WSKDDGVSWS TPRNLSLDIG TEVFAPGPGS GIQKQREPRK GRLIVCGHGT LERDGVFCLL SDDHGASWRY GSGVSGIPYG QPKQENDFNP DECQPYELPD GSVVINARNQ NNYHCHCRIV LRSYDACDTL RPRDVTFDPE LVDPVVAAGA VVTSSGIVFF SNPAHPEFRV NLTLRWSFSN GTSWRKETVQ LWPGPSGYSS LATLEGSMDG EEQAPQLYVL YEKGRNHYTE SISVAKISVY GTL

    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.

    Neu1 Human
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