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Search results

1000 results found for “Hepatitis E”

Name

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  • View Data Sheet

    Name :

    Anhui H7N9

    Description:

    Hemagglutinin-Influenza A Virus H7N9 Anhui 2013 Recombinant

    Hemagglutinin, Influenza A virus (A/Anhui/1-BALF_RG45/2013(H7N9) hemagglutinin, HA, Hemagglutinin HA1 chain, Hemagglutinin HA2 chain

    Product # :

    IHA-037

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    Description

    Anhui H7N9 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 330 amino acids (19-339 aa) and having a molecular mass of 36 kDa.Anhui H7N9 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Anhui H7N9 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Hemagglutinin-Influenza A Virus H7N9 Anhui 2013 (Anhui H7N9) is a part of the influenza viruses hemagglutinin family. H7N9 Anhui is anantigenic glycoprotein which is responsible for binding the virus to the infected cell. An H7N9 virus was firstreported to have infected humans in March 2013, in China. Although the risk is low, The H7N9 virus has thegreatest potential compared with other influenza A viruses to cause a pandemicbecause like other type A viruses, it is not easily transmitted between people in its current form.

    • Synonyms

      Hemagglutinin, Influenza A virus (A/Anhui/1-BALF_RG45/2013(H7N9) hemagglutinin, HA, Hemagglutinin HA1 chain, Hemagglutinin HA2 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

      ADLDKICLGH HAVSNGTKVN TLTERGVEVV NATETVERTN IPRICSKGKR TVDLGQCGLL GTITGPPQCD QFLEFSADLI IERREGSDVC YPGKFVNEEA LRQILRESGG IDKEAMGFTY SGIRTNGATS ACRRSGSSFY AEMKWLLSNT DNAAFPQMTK SYKNTRKSPA LIVWGIHHSV STAEQTKLYG SGNKLVTVGS SNYQQSFVPS PGARPQVNGL SGRIDFHWLM LNPNDTVTFS FNGAFIAPDR ASFLRGKSMG IQSGVQVDAN CEGDCYHSGG TIISNLPFQN IDSRAVGKCP RYVKQRSLLL ATGMKNVPEI PKGRHHHHHH

    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.

    H7N9 Anhui Influenza
  • View Data Sheet

    Name :

    CXCL12 Human alpha, His

    Description:

    Stromal Cell-Derived Factor-1 alpha Human Recombinant, His Tag

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.

    Product # :

    CHM-241

    Price :

    Quantity :

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    Description

    Stromal Cell-Derived Factor-1 alpha Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 78 amino acids, having a molecular mass of 9.2 kDa. The SDF-1a is fused to 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was filtered (0.4µm) and lyophilized from a concentrated (0.5mg/ml) solution containing 20mM Tris buffer pH-7.5 and 20mM sodium chloride.

    Purity

    Greater than 95.0% as determined SDS-PAGE.

    Citations

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
      The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SDF1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK.

    • Background

      What is the molecular weight/Mw of CXCL12 HUMAN ALPHA, HIS Protein?
      CXCL12 HUMAN ALPHA, HIS Protein has a total Mw of 9.2kDa.

      What is the source or expression system of CXCL12 HUMAN ALPHA, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL12 HUMAN ALPHA, HIS Protein?
      CXCL12 HUMAN ALPHA, HIS Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL12 HUMAN ALPHA, HIS Protein?
      The biological functionality of CXCL12 HUMAN ALPHA, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL12 HUMAN ALPHA, HIS Protein?
      MKHHHHHHAS KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK.

      What applications can CXCL12 HUMAN ALPHA, HIS Protein be used in?
      CXCL12 HUMAN ALPHA, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL12 HUMAN ALPHA, HIS Protein?
      The endotoxin level is minimal, CXCL12 HUMAN ALPHA, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL12 HUMAN ALPHA, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL12 HUMAN ALPHA, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Sdf 1A Human His
  • View Data Sheet

    Name :

    GCAT Human

    Description:

    Glycine C-Acetyltransferase Human Recombinant

    2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

    Product # :

    ENZ-705

    Price :

    Quantity :

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    Description

    GCAT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (22-419 a.a) and having a molecular mass of 45kDa.GCAT is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.

    • Synonyms

      2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

    • 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 MSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP.

    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.

    Gcat Human
  • View Data Sheet

    Name :

    DPP4 Human, HEK

    Description:

    Dipeptidyl-Peptidase 4 Human Recombinant, HEK

    CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

    Product # :

    ENZ-1187

    Price :

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    Description

    DPP4 Human Recombinant is a single, glycosylated polypeptide chain containing 977 amino acids (29-766a.a) and having a molecular mass of 112.1kDa (calculated). DPP4 is fused to a 239 amino acid hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    DPP4 protein solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

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

    Biological Activity

    Specific activity is > 15,000 pmol/min/ug in which one unit defined as the amount of enzyme that hydrolyze 1pmole of H-Gly-Pro-AMC.HBr to H-Gly-Pro and AMC per minute at pH 8.0 at 37℃.

     The ED50 range ≤250 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike S1 Subunit (CAT# sars-052)..

    The ED50 range ≤200 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike RBD (CAT# sars-054).

    The ED50 range ≤120 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike (CAT# sars-051).

    Citations

    More Info

    • Synonyms

      CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

    • 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

      DGSMNKGTDD ATADSRKTYT LTDYLKNTYR LKLYSLRWIS DHEYLYKQEN NILVFNAEYG NSSVFLENST FDEFGHSIND YSISPDGQFI LLEYNYVKQW RHSYTASYDI YDLNKRQLIT EERIPNNTQW VTWSPVGHKL AYVWNNDIYV KIEPNLPSYR ITWTGKEDII YNGITDWVYE EEVFSAYSAL WWSPNGTFLA YAQFNDTEVP LIEYSFYSDE SLQYPKTVRV PYPKAGAVNP TVKFFVVNTD SLSSVTNATS IQITAPASML IGDHYLCDVT WATQERISLQ WLRRIQNYSV MDICDYDESS GRWNCLVARQ HIEMSTTGWV GRFRPSEPHF TLDGNSFYKI ISNEEGYRHI CYFQIDKKDC TFITKGTWEV IGIEALTSDY LYYISNEYKG MPGGRNLYKI QLSDYTKVTC LSCELNPERC QYYSVSFSKE AKYYQLRCSG PGLPLYTLHS SVNDKGLRVL EDNSALDKML QNVQMPSKKL DFIILNETKF WYQMILPPHF DKSKKYPLLL DVYAGPCSQK ADTVFRLNWA TYLASTENII VASFDGRGSG YQGDKIMHAI NRRLGTFEVE DQIEAARQFS KMGFVDNKRI AIWGWSYGGY VTSMVLGSGS GVFKCGIAVA PVSRWEYYDS VYTERYMGLP TPEDNLDHYR NSTVMSRAEN FKQVEYLLIH GTADDNVHFQ QSAQISKALV DVGVDFQAMW YTDEDHGIAS STAHQHIYTH MSHFIKQCFS LPKLLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGK.

    • Background

      DPP4 protein, also known as Dipeptidyl peptidase-4 or CD26, is a cell surface protease with diverse functions in cell signaling and metabolism. This research aims to investigate the role of DPP4 protein in various physiological processes and its implications in disease pathogenesis. Understanding the biological significance of DPP4 can provide insights into its potential as a therapeutic target for several disorders.

      Function of DPP4 Protein:

      DPP4 protein is involved in the cleavage and regulation of several peptide hormones and chemokines, influencing their bioactivity and half-life. It is widely expressed in various tissues, including immune cells, endothelial cells, and epithelial cells. DPP4 can modulate immune responses, glucose metabolism, and neuropeptide signaling through enzymatic and non-enzymatic activities.

      Role of DPP4 Protein in Immune Regulation:

      DPP4 protein plays a role in immune cell activation and regulation. It is expressed on the surface of T cells, where it functions as a co-stimulatory molecule. DPP4 engagement on T cells promotes T cell activation, cytokine production, and adhesion to endothelial cells. Additionally, DPP4 can cleave and inactivate certain chemokines, thereby influencing chemotaxis and immune cell recruitment.

      Implications of DPP4 Protein in Metabolic Disorders:

      DPP4 protein is involved in glucose metabolism and insulin regulation. It cleaves incretin hormones, such as glucagon-like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP), which play crucial roles in glucose homeostasis. Inhibition of DPP4 activity can enhance the action of these incretin hormones, leading to improved glycemic control. Therefore, DPP4 inhibitors have been developed as antidiabetic drugs.

      Association of DPP4 Protein with Cardiovascular Diseases:

      DPP4 protein has been implicated in the pathogenesis of cardiovascular diseases. Elevated DPP4 levels have been observed in patients with heart failure, atherosclerosis, and hypertension. DPP4 can contribute to endothelial dysfunction, inflammation, and vascular remodeling, which are key factors in the development and progression of cardiovascular disorders. Inhibition of DPP4 activity has shown potential as a therapeutic strategy in preclinical studies.

      Given its involvement in various biological processes and disease pathogenesis, DPP4 protein has emerged as a potential therapeutic target. DPP4 inhibitors, which prevent the enzymatic activity of DPP4, have been developed for the treatment of type 2 diabetes. These inhibitors enhance the action of incretin hormones, leading to improved glycemic control. Additionally, ongoing research aims to explore the therapeutic potential of DPP4 inhibitors in other conditions, such as immune-mediated disorders and cardiovascular diseases.

      Conclusion:

      The investigation of DPP4 protein provides insights into its diverse functions in cell signaling, immune regulation, and metabolism. Understanding the role of DPP4 in disease pathogenesis opens avenues for the development of targeted therapies for conditions such as diabetes, cardiovascular diseases, and immune-mediated disorders. Further research on DPP4 protein and its associated pathways may uncover new therapeutic opportunities and improve patient outcomes.

    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.

    Dpp4 Human Hek
  • View Data Sheet

    Name :

    MMP 1 Human, HEK

    Description:

    Matrix Metalloproteinase-1 Human Recombinant, HEK

    Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.

    Product # :

    ENZ-099

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    Description

    MMP-1 Human Recombinant produced in HEK293 cells is a proform of the Human MMP1 (Met1-Asn469) and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa. MMP-1 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The MMP-1 is supplied as a 0.2µm filtered solution in MES, NaCl, Glycerol and Brij35.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The activity was measured by its ability to cleave fluorogenic peptide substrate, Mca-KPLGL-Dpa-AR-NH2, The specific activity is > 400 pmoles/min/µg.
    Recombinant Human MMP-1 protein pro form needs to be activated with p-aminophenylmercuric acetate (APMA).
    Activation Protocol:
    1. Dilute MMP1 to 50µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
    2. Activate MMP1 by adding APMA to a final concentration of 1mM. (Sigma, Catalog # A9563) and 100mM stock in DMSO.
    3. Incubate at 37°C for 2 hours.

    sds-page

    mmp1 human hek sds-page - Product image 1

    Citations

    More Info

    • Introduction

      MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

    • Synonyms

      Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.

    • 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.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.

    Mmp 1 Human
  • View Data Sheet

    Name :

    HK2 Antibody

    Description:

    Hexokinase-2, Mouse Anti Human

    Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.

    Product # :

    ANT-378

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    Formulation

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

    Citations

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    • Introduction

      Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.

    • Synonyms

      Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.

    • Immunogen

      Anti-human Hexokinase-2 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Hexokinase-2 amino acids 1-917 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P1A7AT.

    • Applications

      Hexokinase-2 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 1:1,000 ~ 3,000. Recommended starting dilution is 1:2,000.

    • 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

      Hexokinase-2 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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    Hk2 Antibody
  • View Data Sheet

    Name :

    Tamm Horsfall

    Description:

    Recombinant Human Tamm Horsfall Glycoprotein

    Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.


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    ENZ-1206

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    Description

    Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.

    Source

    HEK293

    Formulation

    The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE analysis.

    SDS-PAGE

    Tamm Horsfall-SDS-PAGE - Product image 1

    Citations

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    • Introduction

      Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
      Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
      Reduced Uromodulin levels is associated with chronic kidney disease.
      UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.

    • Synonyms

      Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD should be stored at 4C between 2-7 days and for future use below -18C.
      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
      Please prevent freeze-thaw cycles.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5mg/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

      DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH

    • Background

      Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

      What is the molecular weight/Mw of UMOD Protein?
      UMOD Protein has a total Mw of 65kDa.

      What is the source or expression system of UMOD Protein?
      HEK293.

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

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

      What is the amino acid sequence of UMOD Protein?
      UMOD Protein is composed from 595 amino acids.

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

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

    Tamm Horsfall
  • View Data Sheet

    Name :

    ARMC10 Human

    Description:

    Armadillo Repeat Containing 10 Human Recombinant

    Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    Product # :

    PRO-1453

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    Description

    ARMC10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (28-308 a.a) and having a molecular mass of 33.6 kDa.ARMC10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARMC10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.

    • Synonyms

      Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    • 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 MGSTRGRRRG DRELGIRSSK SAEDLTDGSY DDVLNAEQLQ KLLYLLESTE DPVIIERALI TLGNNAAFSV NQAIIRELGG IPIVANKINH SNQSIKEKAL NALNNLSVNV ENQIKIKIYI SQVCEDVFSG PLNSAVQLAG LTLLTNMTVT NDHQHMLHSY ITDLFQVLLT GNGNTKVQVL KLLLNLSENP AMTEGLLRAQ VDSSFLSLYD SHVAKEILLR VLTLFQNIKN CLKIEGHLAV QPTFTEGSLF FLLHGEECAQ KIRALVDHHD AEVKEKVVTI IPKI.

    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.

    Armc10 Human
  • View Data Sheet

    Name :

    GSTO1 Human Mutant

    Description:

    Glutathione S-Transferase Omega 1 Mutant Human Recombinant

    Glutathione S-transferase omega-1, GSTO 1-1, GSTO1, GSTTLP28, P28, DKFZp686H13163.

    Product # :

    ENZ-435

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    Description

    Several polymorphisms in the coding regions of the human GSTO1 have been identified. A polymorphism causing an alanine-to-aspartate (A140D) substitution in amino acid 140 produces a variant with lowered enzyme activities in the arsenic biotransformation.GSTO1 Variant Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 241 amino acids fragment (1-241) having a total molecular mass of 36kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The GSTO1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTO1 protein is supplied in 1x PBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      GSTO1 belongs to the theta class glutathione S-transferase-like (GSTTL) protein family. GSTO1 is expressed in a broad array of human tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities as well as catalyzing the reduction of monomethylarsonate which is an intermediate in the pathway of arsenic biotransformation. Furthermore, GSTO1 shields from oxidative stress which is a risk factor for Alzheimer disease, vascular dementia and stroke. GSTO1 is abundant in alveolar macrophages and airway secretions, with the levels reduced in chronic obstructive pulmonary disease patients. In mouse, the GSTO1 protein acts as a small stress response protein, probably involved in cellular redox homeostasis.

    • Synonyms

      Glutathione S-transferase omega-1, GSTO 1-1, GSTO1, GSTTLP28, P28, DKFZp686H13163.

    • 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.

    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.

    Gsto1 Human Mutant
  • View Data Sheet

    Name :

    ICAM1 Human HEK

    Description:

    Intercellular Adhesion Molecule-1 Human Recombinant HEK

    Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.

    Product # :

    PRO-1643

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    Description

    ICAM1 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 461 amino acids (28-480). ICAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    ICAM1 was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

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    • Introduction

      ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues.
      ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH.
      Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions.

    • Synonyms

      Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ICAM1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ICAM1 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized ICAM1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQE
      DSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANL
      TVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAP
      YQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGN
      DSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEV
      TVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELR
      VLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYL
      CRARSTQGEVTRKVTVNVLSPRYEVDHHHHHH.

    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.

    Icam1 Human Hek
  • View Data Sheet

    Name :

    HTF Bovine

    Description:

    Holo Transferrin Bovine

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    Product # :

    PRO-510

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    Description

    Bovine Holo Transferrin is a glycoprotein of approximately 80 kDa.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by Cellulose Acetate.

    Citations

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bovine HTF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bovine HTF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Bovine HTF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG, HBc, ALT and Syphilis.Viral inactivation by pasteurization (60°C for 10 hours) has been validated using three different test viruses, with removal of 8-14.5 logs of virus documented. The purification process has also been found to remove significant additional quantities of virus.

    • Applications

      Bovine Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    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.

    Holo Transferrin Bovine
  • View Data Sheet

    Name :

    MHC Class I, H-2K Antibody, Biotin

    Description:

    MHC Class I, (H-2K) Mouse Antibody, Biotin

    Product # :

    ANT-266

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    Formulation

    1mg/ml in PBS (after reconstitution).

    Citations

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    • Introduction

      MHC Class I is a membrane spanning molecule consisting of 2 proteins. MHC Class I is just about 350 amino acids in length, with roughly 75 amino acids at the carboxylic end comprising the transmembrane and cytoplasmic portions. The remaining 270 amino acids, are divided into three globular domains labeled Alpha-1, Alpha-2 and Alpha-3 prime, with Alpha-1 being closest to the amino terminus and Alpha-3 closest to the membrane. The second portion of the molecule is a small globular protein called Beta-2 Microglobulin. It links primarily with the Alpha-3 prime domain and is essential for MHC stability.
      The MHC ability to show a vast range of antigenic peptides for T cell recognition needs a compromise between broad specificity and high affinity. Both MHC class I and MHC class II show an exceptional structure while the peptide main chain is tightly bound and peptide side chains show less restrictive interactions. It is primarily the peptide side-chain contacts and conformational variability that ensures that the peptide-MHC complex presents an antigenically unique surface to T cell receptors.

    • Solubility

      Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Purified mouse LN cells (C57Bl/6 anti-BALB/c).

    • Ig Subclass

      Mouse IgG2b.

    • Clone

      NYRmH-2K.

    • Applications

      Cytotoxic and staining antibody. For staining, use 10ml/1,000,000 cells. Titer for cytotoxicity should be determined by the investigator.

    • Specificity

      Recognizes most mouse H-2K haplotypes (k,p,q,r,s). Does NOT react with H-2kd.

    • Available Conjugates

      This antibody is also available as unconjugated antibody and conjugated to FITC.

    • Type

      Mouse Antibody Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Ion exchange column.

    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.

    Mhc Class I H 2K Antibody Biotin
  • View Data Sheet

    Name :

    HBZ Mouse

    Description:

    Hemoglobin-Zeta Mouse Recombinant

    Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.

    Product # :

    PRO-2517

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    Description

    HBZ Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-142 a.a) and having a molecular mass of 18.3kDa.HBZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HBZ protein solution (0.25mg/ml) containing 20mM MES(pH6.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Hemoglobin Subunit Zeta (Hbz) or Hba-x is a alpha-like hemoglobin and part of the globin family. The protein is expressed and produced in the the yolk sac in early stages of embryonic development. Hemoglobin subunit zeta has 2 pseudogenes and 5 functional genes.

    • Synonyms

      Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.

    • 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).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSLMKNERAI IMSMWEKMAA QAEPIGTETL ERLFCSYPQT KTYFPHFDLH HGSQQLRAHG FKIMTAVGDA VKSIDNLSSA LTKLSELHAY ILRVDPVNFK LLSHCLLVTM AARFPADFTP EVHEAWDKFM SILSSILTEK YR.

    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.

    Hemoglobin Zeta Mouse
  • View Data Sheet

    Name :

    EGF (Leu 21) Human

    Description:

    Epidermal Growth Factor (Leu-21) Human Recombinant

    Urogastrone, URG, EGF.

    Product # :

    CYT-466

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    Description

    EGF 21-Leu Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6205 Dalton.The EGF 21-Leu is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

    Citations

    More Info

    • Introduction

      Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu 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 Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu.

    • Background

      Deciphering the Potential of Epidermal Growth Factor (Leu-21) Human Recombinant: Unveiling Novel Insights and Therapeutic Implications

      Abstract:

      This concise research paper delves into the enigmatic landscape of Epidermal Growth Factor (Leu-21) Human Recombinant, illuminating its intricate molecular characteristics, signaling pathways, and promising therapeutic avenues. Through a combination of advanced methodologies, including structural analysis, cellular assays, and in vivo studies, this investigation sheds light on the multifaceted cellular responses driven by this specific EGF variant, presenting new avenues for clinical applications.

      Introduction:

      Central to cellular processes, Epidermal Growth Factor (EGF) stands as a pivotal cytokine. This paper uniquely focuses on Epidermal Growth Factor (Leu-21) Human Recombinant, with a specific spotlight on its molecular properties and potential clinical relevance.

      Molecular Insights and Signaling Dynamics:

      The crux of its functionality lies in the interaction between Epidermal Growth Factor (Leu-21) and its cognate receptor, initiating a cascade of intracellular events. Through high-resolution structural analyses, we unveil the intricate binding interface, which sets the stage for signaling cascades that include both canonical and non-canonical pathways. These pathways, particularly the MAPK and PI3K/Akt routes, orchestrate cellular responses such as proliferation, migration, and evasion of apoptosis.

      Experimental Profiling and Cellular Responses:

      In decoding the cellular ramifications, a repertoire of in vitro assays has been meticulously employed. These encompass cell viability assessments, wound healing analyses, and sophisticated fluorescence resonance energy transfer (FRET) studies. These endeavors collectively unravel the dynamic choreography of cellular behaviors, underlining the role of Epidermal Growth Factor (Leu-21) in fostering cellular migration, division, and wound closure.

      In Vivo Implications and Therapeutic Prospects:

      Translating these in vitro insights to clinical potential, in vivo investigations present a compelling narrative. Within animal models, Epidermal Growth Factor (Leu-21) emerges as a potent driver of cutaneous wound healing, promoting accelerated tissue regeneration. Furthermore, its reach extends to oncology, where it not only influences tumor microenvironments but also exerts anti-apoptotic effects, offering tantalizing possibilities for targeted cancer interventions.

      Future Challenges and Prospects:

      While these discoveries hold immense promise, challenges linger. The intricate web of signaling events necessitates deeper scrutiny, considering potential cross-talk and off-target effects. In parallel, refining delivery mechanisms and optimal dosing regimens will be pivotal for harnessing the clinical potential of Epidermal Growth Factor (Leu-21).

      Conclusion:

      In a symphony of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (Leu-21) Human Recombinant emerges as a captivating enigma. Its unique structural attributes and intricate signaling pathways paint a canvas of cellular choreography. As the landscape of research advances, unlocking its therapeutic virtues could pave the way for groundbreaking interventions in wound healing and cancer therapy.

      What is the molecular weight/Mw of EGF Protein?
      EGF Protein has a total Mw of 6.2kDa.

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

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

      What is the Biological Activity of EGF Protein?
      The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

      What is the amino acid sequence of EGF Protein?
      EGF Protein is composed from 53 amino acids.

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

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

    Egf 21 Leu Human
  • View Data Sheet

    Name :

    ADAL Human

    Description:

    Adenosine Deaminase-Like Human Recombinant

    Adenosine Deaminase-Like, Adenosine Deaminase-Like Protein, EC 3.5.4.-, EC 3.5.4, ADAL.

    Product # :

    ENZ-788

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    Description

    ADAL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 292 amino acids (1-267) and having a molecular mass of 32.7kDa.ADAL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ADAL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adenosine deaminase-like protein (ADAL) is a putative nucleoside deaminase. ADAL catalyzes the hydrolytic deamination of adenosine or some similar substrate and has a role in purine metabolism.

    • Synonyms

      Adenosine Deaminase-Like, Adenosine Deaminase-Like Protein, EC 3.5.4.-, EC 3.5.4, ADAL.

    • 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 MGSEFMIEAE EQQPCKTDFY SELPKVELHA HLNGSISSHT MKKLIAQKPD LKIHDQMTVI DKGKKRTLEE CFQMFQTIHQ LTSSPEDILM VTKDVIKEFA DDGVKYLELR STPRRENATG MTKKTYVESI LEGIKQSKQE NLDIDVRYLI AVDRRGGPLV AKETVKLAEE FFLSTEGTVL GLDLSGDPTV GQAKDFLEPL LEAKKAGLKL ALHLSEIPNQ KKETQILLDL LPDRIGHGTF LNSGEGGSLD LVDFVRQHRI PLGKAWSFRS SR.

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    Adal Human
  • View Data Sheet

    Name :

    DHFR Human

    Description:

    Dihydrofolate Reductase Human Recombinant

    Dihydrofolate reductase, DHFR, DHFRP1.

    Product # :

    ENZ-443

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    Description

    DHFR Human Recombinant fused with a 20 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.6kDa.The DHFR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DHFR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 2mM DTT and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >2000 pmol/min/ug  is defined as the amount of enzyme that converts 1.0 pmole of dihydrofolic acid to tetrahydrofolic acid per minute at pH 6.5 at 25C.

    sds-page

    dhfr-human-sds-page - Product image 1

    Citations

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    • Introduction

      Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes.
      DHFR deficiency is associated with megaloblastic anemia.
      DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid.
      DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.

    • Synonyms

      Dihydrofolate reductase, DHFR, DHFRP1.

    • 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 MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL VIMGKKTWFS IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL TEQPELANKV DMVWIVGGSS VYKEAMNHPG HLKLFVTRIM QDFESDTFFP EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF EVYEKND.

    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.

    Dhfr Human
  • View Data Sheet

    Name :

    EEF1A1 Human

    Description:

    Eukaryotic Translation Elongation Factor 1 Alpha 1 Human Recombinant

    Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.

    Product # :

    PRO-1910

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    Description

    EEF1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (1-462 a.a) and having a molecular mass of 50kDa.

    Source

    Escherichia Coli.

    Formulation

    EEF1A1 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.

    Citations

    More Info

    • Introduction

      EEF1A1 is an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible forthe enzymatic release of aminoacyl tRNAs to the ribosome. EEF1A1 is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. EEF1A1 is recognized as an autoantigen in 66% of patients with Felty syndrome. EEF1A1 has multiple copies on numerous chromosomes, part of them, if not all, symbolize different pseudogenes. Among the diseases associated with EEF1A1 are tinea nigra and andcervical cancer.

    • Synonyms

      Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK ITKSAQKAQK AK

    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.

    Eef1A1 Human
  • View Data Sheet

    Name :

    ENO1 Human

    Description:

    Enolase-1 Human Recombinant

    NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    Product # :

    ENZ-452

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    Description

    The ENO1 Human Recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 47.1kDa and containing 434 amino acids (1-434 a.a.).

    Source

    Escherichia Coli.

    Formulation

    The ENO1 protein solution (1mg/ml) is formulated in 20mM Tris-HCl pH-7.5 1mM MgSO4 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20,000pmol/min/ug, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.

    Citations

    More Info

    • Introduction

      ENO1 is a homodimeric soluble protein that encodes a smaller monomeric structural lens protein, tau-crystallin. ENO1 is a glycolytic enzyme expressed in mainly all tissues. ENO1 isoenzyme full length protein is found in the cytoplasm. The shorter protein is formed from another translation start that is restricted to the nucleus, and binds to a component in the c-myc promoter. ENO1 is involved in anaerobic metabolism under hypoxic conditions and plays a role as a cell surface plasminogen receptor during tissue invasion. Irregular expression of Enolase-1 is linked with tumor progression in several cases of breast and lung cancer. Enolase-1 is as an auto antigen associated with Hashimoto's encephalopathy and severe asthma. ENO1 is the target protein of serum anti-endothelial antibody in Behcet's disease.

    • Synonyms

      NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    • 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

      MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK AKFAGRNFRN PLAK.

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    Eno1 Human
  • View Data Sheet

    Name :

    TANK Human (1-119)

    Description:

    TRAF Family Member-Associated NFKB Activator Human Recombinant (1-119 a.a.)

    TRAF2, I-TRAF, TANK, TRAF family member-associated NF-kappa-B activator, TRAF-interacting protein, ITRAF.

    Product # :

    PRO-685

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    Description

    TANK produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (1-119 a.a.) and having a molecular mass of 13.6 kDa.TANK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TANK protein solution contains 20mM Tris, pH-8.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TRAF2 protein is related with transduce signals from members of the TNFR superfamily. TRAF2 is located in the cytoplasm binds to TRAF1, TRAF2, or TRAF3, thus inhibiting TRAF function by sequestering the TRAFs in a suppressed state in the cytoplasm. Overexpression of TANK inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and inhibits LMP1-mediated NF-kappa-B activation by blocking the association of TRAF2 with LMP1. TRAF2 is necessary for the cellular response to TNF-alpha by connecting upstream signalling molecules to the IKKs and p65.

    • Synonyms

      TRAF2, I-TRAF, TANK, TRAF family member-associated NF-kappa-B activator, TRAF-interacting protein, ITRAF.

    • 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

      MDKNIGEQLN KAYEAFRQAC MDRDSAVKEL QQKTENYEQR IREQQEQLSL QQTIIDKLKS QLLLVNSTQD NNYGCVPLLE DSETRKNNLT LDQPQDKVIS GIAREKLPKV DIASAESSI.

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    Traf2 Human
  • View Data Sheet

    Name :

    YAE1D1 Human

    Description:

    Yae1 Domain Containing 1 Human Recombinant

    Yae1 domain containing 1, C7orf361, GK003, Yae1 domain-containing protein 1, YAE1D1.

    Product # :

    PRO-1516

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    Description

    YAE1D1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 249 amino acids (1-226) and having a molecular mass of 27.7 kDa.YAE1D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YAE1D1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      Yae1 domain containing 1, C7orf361, GK003, Yae1 domain-containing protein 1, YAE1D1.

    • 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 MGSMSWVQAA SLIQGPGDKG DVFDEEADES LLAQREWQSN MQRRVKEGYR DGIDAGKAVT LQQGFNQGYK KGAEVILNYG RLRGTLSALL SWCHLHNNNS TLINKINNLL DAVGQCEEYV LKHLKSITPP SHVVDLLDSI EDMDLCHVVP AEKKIDEAKD ERLCENNAEF NKNCSKSHSG IDCSYVECCR TQEHAHSENP SPTWILEQTA SLVKQLGLSV DVLQHLKQL.

    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.

    Yae1D1 Human
  • View Data Sheet

    Name :

    RNF181 Human

    Description:

    Ring Finger Protein 181 Human Recombinant

    Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    Product # :

    PRO-1218

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    Description

    RNF181 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 20.3 kDa.RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RNF181 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      E3 ubiquitin-protein ligase RNF181 (RNF181) accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the thioester form and subsequently directly transfers the ubiquitin to targeted substrates. RNF181 is widely expressed, with the highest levels in the liver and heart and the lowest levels in the brain and skeletal muscle. RNF181 is also expressed in platelets (at protein level).

    • Synonyms

      Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    • 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 MGSMASYFDE HDCEPSDPEQ ETRTNMLLEL ARSLFNRMDF EDLGLVVDWD HHLPPPAAKT VVENLPRTVI RGSQAELKCP VCLLEFEEEE TAIEMPCHHL FHSSCILPWL SKTNSCPLCR YELPTDDDTY EEHRRDKARK QQQQHRLENL HGAMYT.

    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.

    Rnf181 Human
  • View Data Sheet

    Name :

    Borrelia p100

    Description:

    Borrelia Burgdorferi p100 Recombinant

    Product # :

    BOR-003

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    Description

    Recombinant Borrelia Burgdorferi p100 (p100/p83) produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 77,813 Dalton. Borrelia p100 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Borrelia p100 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • 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.

    • Applications

      Western blot with Lyme positive plasma.

    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.

    Borrelia P100
  • View Data Sheet

    Name :

    IDH3G Human

    Description:

    Isocitrate Dehydrogenase 3 (NAD+) Gamma Human Recombinant

    Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial, Isocitric dehydrogenase subunit gamma, NAD(+)-specific ICDH subunit gamma, IDH3G, H-IDHG.

    Product # :

    ENZ-205

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    Description

    IDH3G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (40-393) and having a molecular mass of 41.1kDa.IDH3G is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IDH3G solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Isocitrate dehydrogenase [NAD] subunit gamma (IDH3G) mitochondrial is a member of the isocitrate and isopropylmalate dehydrogenases family. Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. The IDH3G is a gamma subunit of one isozyme of isocitrate dehydrogenase which belongs to a distinct subclass, which utilizes NAD(+) as the electron acceptor, and is restricted to the mitochondrial matrix.

    • Synonyms

      Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial, Isocitric dehydrogenase subunit gamma, NAD(+)-specific ICDH subunit gamma, IDH3G, H-IDHG.

    • 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 MFSEQTIPPS AKYGGRHTVT MIPGDGIGPE LMLHVKSVFR HACVPVDFEE VHVSSNADEE DIRNAIMAIR RNRVALKGNI ETNHNLPPSH KSRNNILRTS LDLYANVIHC KSLPGVVTRH KDIDILIVRE NTEGEYSSLE HESVAGVVES LKIITKAKSL RIAEYAFKLA QESGRKKVTA VHKANIMKLG DGLFLQCCRE VAARYPQITF ENMIVDNTTM QLVSRPQQFD VMVMPNLYGN IVNNVCAGLV GGPGLVAGAN YGHVYAVFET ATRNTGKSIA NKNIANPTAT LLASCMMLDH LKLHSYATSI RKAVLASMDN ENMHTPDIGG QGTTSEAIQD VIRHIRVING RAVEA.

    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.

    Idh3G Human
  • View Data Sheet

    Name :

    NME1 Human, Active

    Description:

    Non-Metastatic Cells 1 Human Recombinant, BioActive

    Non-metastatic cells 1, Nucleoside diphosphate kinase A, NDP kinase A, AWD, GAAD, NB, NBS, NDPK-A, NM23, NM23-H1.

    Product # :

    PRO-2639

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    Description

    NME1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (1-152 a.a.) and having a molecular mass of 17.1kDa.

    Source

    E.coli.

    Formulation

    The NME1 solution (1mg/ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 7.5) and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,200unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.

    Citations

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    • Introduction

      Non-metastatic cells 1 or NME1 is a protein, found at first as a suppressor gene for candidate metastasis. The protein can be found in various types of tumor, potential of metastatic may increase or decrease as the protein’s levels changes. When the protein’s concentration is low, an aggressive carcinoma (colon, breast, gastric and melanoma) appears. High levels of NME1 have been linked to advanced thyroid cancer.

    • Synonyms

      Non-metastatic cells 1, Nucleoside diphosphate kinase A, NDP kinase A, AWD, GAAD, NB, NBS, NDPK-A, NM23, NM23-H1.

    • 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

      MANCERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF MQASEDLLKE HYVDLKDRPF FAGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS DSVESAEKEI GLWFHPEELV DYTSCAQNWI YE

    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.

    Nme1 Protein
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