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1000 results found for “hint”

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  • View Data Sheet

    Name :

    Ornithine Aminotransferase Human

    Description:

    Ornithine Aminotransferase Human Recombinant

    DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.

    Product # :

    ENZ-472

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    Description

    Ornithine Aminotransferase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (33-439 a.a.) and having a molecular wieght of 45.2kDa.The Ornithine Aminotransferase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Ornithine Aminotransferase protein solution contains 20mM Tris, pH-8, and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ornithine Aminotransferase is a mitochondrial enzyme which is an important factor that converts arginine and ornithine into the major excitatory and inhibitory neurotransmitters glutamate and GABA. Ornithine Aminotransferase mutations result in a deficiency that cause the autosomal recessive eye disease Gyrate Atrophy.

    • Synonyms

      DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.

    • 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

      MTVQGPPTSD DIFEREYKYG AHNYHPLPVA LERGKGIYLW DVEGRKYFDF LSSYSAVNQG HCHPKIVNAL KSQVDKLTLT SRAFYNNVLG EYEEYITKLF NYHKVLPMNT GVEAGETACK LARKWGYTVK GIQKYKAKIV AAGNFWGRT LSAISSSTDP TSYDGFGPFM PGFDIIPYND LPALERALQD PNVAAFMVEP IQGEAGVVVP DPGYLMGVRE LCTRHQVLFI ADEIQTGLAR TGRWLAVDYE NVRPDIVLLG KALSGGLYPV SAVLCDDDIM LTIKPGEHGS TYGGNPLGCR VAIAALEVLE EENLAENADK LGIILRNELM KLPSDVVTAV RGKGLLNAIV IKETKDWDAW KVCLRLRDNG LLAKPTHGDI IRFAPPLVIK EDELRESIEI INKTILSF.

    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.

    Ornithine Aminotransferase Human
  • View Data Sheet

    Name :

    G CSF Human, PEG

    Description:

    Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    CYT-018

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    Description

    Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

    Purity

    Greater than 95.0% as determined by SEC-HPLC.

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Colorless, clear and transparent solution.

    • Stability

      G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.

    • Background

      What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

      What is the source or expression system of G CSF HUMAN, PEG Protein?
      Escherichia Coli.

      What is the Purity of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of G CSF HUMAN, PEG Protein?
      The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

      What is the amino acid sequence of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

      What is the endotoxin level for G CSF HUMAN, PEG Protein?
      The endotoxin level is minimal, G CSF HUMAN, PEG 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.

    G Csf Human Pegylated
  • View Data Sheet

    Name :

    MBP E.Coli, His

    Description:

    Maltose Binding Protein E.coli Recombinant, His Tag

    Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    Product # :

    PRO-2322

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    Description

    Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
      MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

    • Synonyms

      Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    • 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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.

    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.

    Mbp Ecoli His
  • View Data Sheet

    Name :

    CCNH Antibody

    Description:

    Cyclin-H, Mouse Anti Human

    CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    Product # :

    ANT-583

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.

    • Synonyms

      CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CCNH mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CCNH amino acids 1-323 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT3G6AT.

    • Applications

      CCNH antibody has been tested by ELISA, 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 starting dilution for Western blot analysis is 1:1000.

    • 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

      CCNH antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Ccnh Antibody
  • View Data Sheet

    Name :

    INHBC Human

    Description:

    Inhibin-Beta C Chain Human Recombinant

    Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.

    Product # :

    HOR-010

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    Description

    INHBC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (237-352) and having a molecular mass of 14.9kDa.INHBC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The INHBC solution (0.5mg/ml) 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

      INHBC, the beta C chain of inhibin, belongs to the TGF-beta superfamily. INHBC formulates heterodimers with beta A and beta B subunits. Other members of the TGF-beta superfamily are Actv's and Inhibins, hormones with contradictory roles which take part in pituitary, hypothalamic, and gonadal hormone secretion, as well as differentiation and growth of numerous cell types.

    • Synonyms

      Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.

    • 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 MGSGIDCQGG SRMCCRQEFF VDFREIGWHD WIIQPEGYAM NFCIGQCPLH IAGMPGIAAS FHTAVLNLLK ANTAAGTTGG GSCCVPTARR PLSLLYYDRD SNIVKTDIPD MVVEACGCS

    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.

    Inhbc Human
  • View Data Sheet

    Name :

    S100A8 Human, His

    Description:

    S100 Calcium Binding Protein A8 Human Recombinant, His Tag

    Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    Product # :

    PRO-150

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    Description

    The Recombinant Human S100A8 produced in E.coli has a molecular mass of 12.08kDa containing 103 amino acid residues of the human S100A8 and fused to a 10 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    S100A8 was filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris and 100mM NaCl, pH 7.5.

    More Info

    • Introduction

      S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

    • Synonyms

      Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    • 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQEMLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.

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    S100A8 Human His
  • View Data Sheet

    Name :

    ENO2 Human, His

    Description:

    Enolase-2 Human Recombinant, His Tag

    Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    Product # :

    ENZ-298

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    Description

    Neuron Specific Enolase Human Recombinant is expressed in E. coli containing 433 amino acids 2-434 fused to an amino terminal hexahistidine tag.The NSE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Enolase 2 is supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    More Info

    • Introduction

      NSE is the ?? isoform of the glycolytic enzyme enolase and is expressed primarily in neurons, in normal and neoplastic neuroendocrine cells. NSE is a highly soluble cytoplasmic protein that is readily secreted into the CSF and serum following tissue damage. NSE shows neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons and binds in a calcium-dependent manner to cultured neocortical neurons promoting cell survival.

    • Synonyms

      Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles.

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    Eno2 Human His
  • View Data Sheet

    Name :

    OTOR Human, His

    Description:

    Otoraplin Human Recombinant, His Tag

    Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.

    Product # :

    CYT-884

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    Description

    OTOR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (26-128 a.a) and having a molecular mass of 14.3kDa. OTOR is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
      Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness.

    • Synonyms

      Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.

    • 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 MGSHMLASKK LCADDECVYT ISLASAQEDY NAPDCRFINV KKGQQIYVYS KLVKENGAGE FWAGSVYGDG QDEMGVVGYF PRNLVKEQRV YQEATKEVPT TDIDFFCE.

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    Otor Human His
  • View Data Sheet

    Name :

    Inhibin a Human

    Description:

    Inhibin Alpha Human Recombinant

    Product # :

    HOR-303

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    Description

    Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE analysis.

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      Alpha chain:
      STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.

      Beta Chain:
      GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
      GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    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.

    Inhibin A Human
  • View Data Sheet

    Name :

    IFIH1 Human

    Description:

    Interferon Induced With Helicase C Domain 1 Human Recombinant

    Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

    Product # :

    PRO-1505

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    Description

    IFIH1 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 152,000 Dalton. IFIH1 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    IFIH1 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.

    • Synonyms

      Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

    • 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.

    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.

    Ifih1 Human
  • View Data Sheet

    Name :

    IHH Human

    Description:

    Indian Hedgehog Human Recombinant

    Indian hedgehog protein, IHH, HHG-2, BDA1.

    Product # :

    CYT-195

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    Description

    IHH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.

    More Info

    • Introduction

      IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.

    • Synonyms

      Indian hedgehog protein, IHH, HHG-2, BDA1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.

    • Background

      What is the molecular weight/Mw of IHH HUMAN Protein?
      IHH HUMAN Protein has a total Mw of 19.8kDa.

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

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

      What is the Biological Activity of IHH HUMAN Protein?
      Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.

      What is the amino acid sequence of IHH HUMAN Protein?
      IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.

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

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

    Ihh Human
  • View Data Sheet

    Name :

    KRT20 Human, His

    Description:

    Cytokeratin 20 Human Recombinant, His Tag

    Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.

    Product # :

    PRO-1358

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    Description

    KRT20 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424 a.a) and having a molecular mass of 50.9kDa. KRT20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT20 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Recombinant Human Cytokeratin 20 His Tag (KRT20) belongs to the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins is comprised of acidic proteins that are organized in pairs of heterotypic keratin chains. KRT20 is a main cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa.

    • Synonyms

      Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.

    • 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 MGSMDFSRRS FHRSLSSSLQ APVVSTVGMQ RLGTTPSVYG GAGGRGIRIS NSRHTVNYGS DLTGGGDLFV GNEKMAMQNL NDRLASYLEK VRTLEQSNSK LEVQIKQWYE TNAPRAGRDY SAYYRQIEEL RSQIKDAQLQ NARCVLQIDN AKLAAEDFRL KYETERGIRL TVEADLQGLN KVFDDLTLHK TDLEIQIEEL NKDLALLKKE HQEEVDGLHK HLGNTVNVEV DAAPGLNLGV IMNEMRQKYE VMAQKNLQEA KEQFERQTAV LQQQVTVNTE ELKGTEVQLT ELRRTSQSLE IELQSHLSMK ESLEHTLEET KARYSSQLAN LQSLLSSLEA QLMQIRSNME RQNNEYHILL DIKTRLEQEI ATYRRLLEGE DVKTTEYQLS TLEERDIKKT RKIKTVVQEV VDGKVVSSEV KEVEENI.

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    Krt20 Human His
  • View Data Sheet

    Name :

    LDHA Antibody

    Description:

    Lactate Dehydrogenase A, Mouse Anti Human

    LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.

    Product # :

    ANT-004

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    Formulation

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

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    • Introduction

      LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.

    • Synonyms

      LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.

    • Immunogen

      Anti-human LDHA mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human LDHA amino acids 1-332 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT1A4AT.

    • Applications

      LDHA antibody has been tested by ELISA, Western blot and Immunofluorescence 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 and Immunofluorescence is 1:500 ~ 8,000.
      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

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

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

    Ldha Antibody
  • View Data Sheet

    Name :

    Lysostaphin

    Description:

    Lysostaphin Recombinant

    Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    Product # :

    ENZ-269

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    Description

    Lysostaphin Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 26.92 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized without any additives.

    Purity

    98% as determined by RP-HPLC.

    Biological Activity

    Assessed by the decrease in turbidity of a suspension of heat-killed Staphylococcus aureus at pH-8, 30°C.  Lysostaphin is a zinc enzyme therefore EDTA is an inhibitory factor.

    More Info

    • Introduction

      Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.

    • Synonyms

      Lysostaphin, EC 3.4.24.75, Glycyl-glycine endopeptidase.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Lyophilized Lysostaphin although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution Lysostaphin can be stored at 4°C up to 3 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Lysostaphin in 20mM sodium acetate, pH 4.5 for optimal stability, which can then be further diluted.

    • Protein content

      Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis RP-HPLC, using a calibrated solution of Lysostaphin as a Reference standard.

    • Specific Activity

      Determined to be 3,540 units/mg.

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    Lysostaphin
  • View Data Sheet

    Name :

    His Tag Antibody

    Description:

    Polyhistidine Tag, Mouse Antibody

    Product # :

    ANT-753

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    Description

    Monoclonal antibodies are produced by immunizing mouse with synthesized polypeptide 6 x His. This antibody was purified via protein-A affinity chromatography.

    Formulation

    1mg/ml in PBS (pH 7.4) 0.02% Sodium Azide & 10% Glycerol

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    • Introduction

      His tag peptide also called polyhistidine-tag is chain of amino acids that are attached to proteins and consist of at least six histidine (6xHis, Hexa Histidine) residues, often at the N- or C-terminus of the protein. Polyhistidine-tags are used for affinity purification of genetically engineered proteins.

    • Physical Appearance

      Sterile Filtered solution.

    • Ig Subclass

      Kappa IgG1.

    • Clone

      PAT1D6AT.

    • Applications

      ELISA and W.B. The researcher should titrate to obtain optimal results.

    • Type

      Mouse Antibody Monoclonal.

    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.

    His Tag Antibody
  • View Data Sheet

    Name :

    MIOX Human

    Description:

    Myo-Inositol Oxygenase Human Recombinant

    Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.

    Product # :

    ENZ-812

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    Description

    MIOX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Trp285) containing 295 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 34.2kDa.

    Source

    Escherichia Coli.

    Formulation

    MIOX was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl and 5% (w/v) trehalose, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inositol oxygenase is a non-heme di-iron enzyme which oxidizes myo-inositol to glucuronic acid. In addition, inositol oxygenase oxidizes the less abundant chiro isomer of inositol. MIOX enzyme is a component of the only known pathway for the catabolism of inositol in humans. MIOX is expressed mostly in the kidneys. Reduction of Inositol Oxygenase and accumulation of polyols, such as inositol and xylitol, have been implicated as contributing factors in complications linked with diabetes.

    • Synonyms

      Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.

    • 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 0.5mg/ml and let the lyophilized pellet dissolve completely. MIOX is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASMKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL AMLPWVREFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW.

    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.

    Miox Human
  • View Data Sheet

    Name :

    HIBCH Human

    Description:

    3-Hydroxyisobutyryl-CoA Hydrolase Human Recombinant

    3-hydroxyisobutyryl-coenzyme A hydrolase mitochondrial, HIBYL-CoA-H, HIB-CoA hydrolase, EC 3.1.2.4

    Product # :

    ENZ-594

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    Description

    HIBCH Recombinant produced in E. coli is a single polypeptide chain containing 379 amino acids (33-386) and having a molecular mass of 42.1kDa.HIBCH is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      HIBCH enzyme is in charge of hydrolysis of both HIBYL-CoA and beta-hydroxypropionyl-CoA. Damages in the HIBCH gene linked to 3-hyroxyisobutyryl-CoA hydrolase deficiency. Multiple transcript variants exist as a result of alternative splicing.

    • Synonyms

      3-hydroxyisobutyryl-coenzyme A hydrolase mitochondrial, HIBYL-CoA-H, HIB-CoA hydrolase, EC 3.1.2.4

    • 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 MGSHMDAAEE VLLEKKGCTG VITLNRPKFL NALTLNMIRQ IYPQLKKWEQ DPETFLIIIK GAGGKAFCAG GDIRVISEAE KAKQKIAPVF FREEYMLNNA VGSCQKPYVA LIHGITMGGG VGLSVHGQFR VATEKCLFAM PETAIGLFPD VGGGYFLPRL QGKLGYFLAL TGFRLKGRDV YRAGIATHFV DSEKLAMLEE DLLALKSPSK ENIASVLENY HTESKIDRDK SFILEEHMDK INSCFSANTV EEIIENLQQD GSSFALEQLK VINKMSPTSL KITLRQLMEG SSKTLQEVLT MEYRLSQACM RGHDFHEGVR AVLIDKDQSP KWKPADLKEV TEEDLNNHFK SLGSSDLKF.

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    Hibch Human
  • View Data Sheet

    Name :

    Omentin Human, His

    Description:

    Omentin Human Recombinant, His Tag

    Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    Product # :

    CYT-551

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    Description

    Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.

    Purity

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

    More Info

    • Introduction

      Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

    • Synonyms

      Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.

    • Applications

      Elisa
      Western blot.

    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.

    Omentin Human His
  • View Data Sheet

    Name :

    IMPDH2 Human

    Description:

    IMP Dehydrogenase 2 Human Recombinant

    Inosine-5'-monophosphate dehydrogenase 2, IMP dehydrogenase 2, IMPD 2, IMPDH 2, IMPDH-II, IMPDH2, IMPD2.

    Product # :

    ENZ-187

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    Description

    IMPDH2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 534 amino acids (1-514) and having a molecular mass of 58kDa.IMPDH2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IMPDH2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 150mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      IMPDH2 is a member of the IMPDH/GMPR family. IMPDH2 catalyzes the NAD-dependent oxidation of inosine-5'-monophosphate into xanthine-5'-monophosphate, which is afterward converted into guanosine-5'-monophosphate. IMPDH2 is the rate-limiting enzyme in the de novo guanine nucleotide biosynthesis. IMPDH2 is consequently involved in maintaining cellular guanine deoxy- and ribonucleotide pools required for DNA and RNA synthesis. In addition, IMPDH1 and IMPDH2 are targets for the important immunosuppressive drug, MPA. Furthermore, the IMPDH2 gene is up-regulated in some neoplasms, suggesting it may have a role in malignant transformation.

    • Synonyms

      Inosine-5'-monophosphate dehydrogenase 2, IMP dehydrogenase 2, IMPD 2, IMPDH 2, IMPDH-II, IMPDH2, IMPD2.

    • 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 MADYLISGGT SYVPDDGLTA QQLFNCGDGL TYNDFLILPG YIDFTADQVD LTSALTKKIT LKTPLVSSPM DTVTEAGMAI AMALTGGIGF IHHNCTPEFQ ANEVRKVKKY EQGFITDPVV LSPKDRVRDV FEAKARHGFC GIPITDTGRM GSRLVGIISS RDIDFLKEEE HDCFLEEIMT KREDLVVAPA GITLKEANEI LQRSKKGKLP IVNEDDELVA IIARTDLKKN RDYPLASKDA KKQLLCGAAI GTHEDDKYRL DLLAQAGVDV VVLDSSQGNS IFQINMIKYI KDKYPNLQVI GGNVVTAAQA KNLIDAGVDA LRVGMGSGSI CITQEVLACG RPQATAVYKV SEYARRFGVP VIADGGIQNV GHIAKALALG ASTVMMGSLL AATTEAPGEY FFSDGIRLKK YRGMGSLDAM DKHLSSQNRY FSEADKIKVA QGVSGAVQDK GSIHKFVPYL IAGIQHSCQD IGAKSLTQVR AMMYSGELKF EKRTSSAQVE GGVHSLHSYE KRLF.

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    Impdh2 Human
  • View Data Sheet

    Name :

    MIF Mouse, His

    Description:

    Macrophage Migration Inhibitor Factor Mouse Recombinant, His Tag

    Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    Product # :

    CYT-896

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    Description

    MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa. MIF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    • 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 MGSMPMFIVN TNVPRASVPE GFLSELTQQL AQATGKPAQY IAVHVVPDQL MTFSGTNDPC ALCSLHSIGK IGGAQNRNYS KLLCGLLSDR LHISPDRVYI NYYDMNAANV GWNGSTFA.

    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.

    Mif Mouse His
  • View Data Sheet

    Name :

    KRT8 Human, His

    Description:

    Cytokeratin 8 Human Recombinant, His Tag

    Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.

    Product # :

    PRO-1567

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    Description

    KRT8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 506 amino acids (1-483 a.a) and having a molecular mass of 56kDa. KRT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 8 (KRT8) belongs to the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. KRT8 typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. KRT8 has a role in retaining cellular structural integrity and also functions in signal transduction and cellular differentiation. KRT8 gene mutations cause cryptogenic cirrhosis.

    • Synonyms

      Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.

    • 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 MGSMSIRVTQ KSYKVSTSGP RAFSSRSYTS GPGSRISSSS FSRVGSSNFR GGLGGGYGGA SGMGGITAVT VNQSLLSPLV LEVDPNIQAV RTQEKEQIKT LNNKFASFID KVRFLEQQNK MLETKWSLLQ QQKTARSNMD NMFESYINNL RRQLETLGQE KLKLEAELGN MQGLVEDFKN KYEDEINKRT EMENEFVLIK KDVDEAYMNK VELESRLEGL TDEINFLRQL YEEEIRELQS QISDTSVVLS MDNSRSLDMD SIIAEVKAQY EDIANRSRAE AESMYQIKYE ELQSLAGKHG DDLRRTKTEI SEMNRNISRL QAEIEGLKGQ RASLEAAIAD AEQRGELAIK DANAKLSELE AALQRAKQDM ARQLREYQEL MNVKLALDIE IATYRKLLEG EESRLESGMQ NMSIHTKTTS GYAGGLSSAY GGLTSPGLSY SLGSSFGSGA GSSSFSRTSS SRAVVVKKIE TRDGKLVSES SDVLPK.

    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.

    Krt8 Human His
  • View Data Sheet

    Name :

    HNMT Human, Active

    Description:

    Histamine N-Methyltransferase Human Recombinant, Active

     HMT, HNMT-S1, HNMT-S2, MRT51.

    Product # :

    ENZ-1071

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    Description

    HNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-292 a.a) and having a molecular mass of 37.4kDa. HNMT is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HNMT protein solution (1mg/ml) containing 20mM, Tris-Hcl (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 200 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37°C.

    More Info

    • Introduction

      Histamine N-Methyltransferase or HNMT, is located in the cell cytosol. Sadenosyl-L-methionine acts as a methyl donor for HNMT which inactivates histamine. By inactivation of histamine, it affects the immune system’s response. HNMT acts on histamine in body tissues such as kidney, central nervous system and bronchus. The protein has a crucial part in the airway response to histamine & histamine degradation process and regulation.

    • Synonyms

      HMT, HNMT-S1, HNMT-S2, MRT51.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASS MRSLFSDHGK YVESFRRFLN HSTEHQCMQE FMDKKLPGII GRIGDTKSEI KILSIGGGAG EIDLQILSKV QAQYPGVCIN NEVVEPSAEQ IAKYKELVAK TSNLENVKFA WHKETSSEYQ SRMLEKKELQ KWDFIHMIQM LYYVKDIPAT LKFFHSLLGT NAKMLIIVVS GSSGWDKLWK KYGSRFPQDD LCQYITSDDL TQMLDNLGLK YECYDLLSTM DISDCFIDGD ENGDLLWDFL TETCNFNATA PPDLRAELGK DLQEPEFSAK KEGKVLFNNT LSFIVIEA.

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    Hnmt Protein
  • View Data Sheet

    Name :

    NMNAT1 Mouse

    Description:

    Nicotinamide Nucleotide Adenylyltransferase 1 Mouse Recombinant

    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.

    Product # :

    ENZ-1049

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    Description

    NMNAT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285 a.a) and having a molecular mass of 34.7kDa. NMNAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMNAT1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

    • Synonyms

      Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.

    • Physical Appearance

      Sterile filtered colourless 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 MGSMDSSKKT EVVLLACGSF NPITNMHLRL FELAKDYMHA TGKYSVIKGI ISPVGDAYKK KGLIPAHHRI IMAELATKNS HWVEVDTWES LQKEWVETVK VLRYHQEKLA TGSCSYPQSS PALEKPGRKR KWADQKQDSS PQKPQEPKPT GVPKVKLLCG ITNDISSTKI RRALRRGQSI RYLVPDLVQE YIEKHELYNT ESEGRNAGVT LAPLQRNAAE AKHNHSTL.

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    Nmnat1 Mouse
  • View Data Sheet

    Name :

    BLMH Mouse

    Description:

    Bleomycin Hydrolase Mouse Recombinant

    BMH, BH, BLM hydrolase, Bleomycin Hydrolase.

    Product # :

    ENZ-1109

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    Description

    BLMH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 478 amino acids (1-455 aa) and having a molecular mass of 54.9 kDa.BLMH is fused to a 23 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BLMH solution (0.25 mg/ml) contains 1mM DTT, 30% Glycerol, 20mM Tris-HCl(pH8.0) and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,500 pmole/min/ug. Measured by hydrolysis of 1pmole of Met-AMC to Methionine and AMC per minute at pH7.5 at 37C˚.

    More Info

    • Introduction

      BLMH is affiliate to the papain superfamily of the cysteine protease and the peptidase C1 family. BLMH is a cytoplasmic cysteinepeptidase usually found as a homohexamer. BLMH shields normal and malignant cells from the glycopeptide antitumor drug BLM. BLMH catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and in addition demonstrates general aminopeptidase activity.

    • Synonyms

      BMH, BH, BLM hydrolase, Bleomycin Hydrolase.

    • 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 MGSMNNAGLN SEKVSALIQK LNSDPQFVLA QNVGTTHDLL
      DICLRRATVQ GAQHVFQHVV PQEGKPVTNQ KSSGRCWIFS CLNVMRLPFM KKFNIEEFEF
      SQSYLFFWDK VERCYFFLNA FVDTAQKKEP EDGRLVQYLL MNPTNDGGQW DMLVNIVEKY
      GVVPKKCFPE SHTTEATRRM NDILNHKMRE FCIRLRNLVH SGATKGEISS TQDAMMEEIF
      RVVCICLGNP PETFTWEYRD KDKNYHKIGP ITPLQFYKEH VKPLFNMEDK ICFVNDPRPQ
      HKYNKLYTVD YLSNMVGGRK TLYNNQPIDF LKKMVAASIK DGEAVWFGCD VGKHFNGKLG
      LSDMNVYDHE LVFGVSLKNM NKAERLAFGE SLMTHAMTFT AVSEKDNQEG TFVKWRVENS
      WGEDHGHKGY LCMTDEWFSE YVYEVVVDKK HVPEEVLAVL EQEPIVLPAW DPMGALAE

    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.

    Blmh Mouse
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