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Search results

1000 results found for “TSH”

Name

Description

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  • View Data Sheet

    Name :

    SAA1 Human, His

    Description:

    Serum Amyloid A Human Recombinant (APO-SAA1), His Tag

    Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.

    Product # :

    CYT-675

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    Quantity :

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    Description

    SAA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (19-122 a.a.) and having a total molecular mass of 13.9 kDa. SAA1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAA1 solution contains 20mM Tris buffer(pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SAA1 protein is an acute phase apolipoprotein reactant which is produced mostly by hepatocytes and under regulation of inflammatory cytokines. SAA1 (Serum amyloid A1) protein is produced mainly in the liver and circulates in low levels in the blood. The SAA1 seems to have a role in the immune system. SAA1 protein levels increase in the blood and other tissues under conditions of inflammation. SAA1 may facilitate the repair of injured tissues; it also acts as an antibacterial agent, and signals the migration of germ-fighting cells to sites of infection. SAA1 also functions as an apolipoprotein of the HDL complex.
      Elevated levels of SAA1 ultimately affect secondary amyloidosis, extracellular amassing of amyloid fibrils, resulting from a circulating precursor, in a variety of tissues and organs. The most widespread type of amyloidosis appears secondary to chronic inflammatory disease, mainly rheumatoid arthritis. The SAA1 cleavage product a designated amyloid protein A is deposited systemically as amyloid in vital organs such as the liver, spleen, and kidneys in chronic inflammatory diseases patients. These deposits are extremely insoluble and resistant to proteolysis; they disrupt tissue structure and compromise performance.

    • Synonyms

      Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.

    • 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 MRSFFSFLGE AFDGARDMWR AYSDMREANY IGSDKYFHAR GNYDAAKRGP GGVWAAEAIS DARENIQRFF GHGAEDSLAD QAANEWGRSG KDPNHFRPAG LPEKY.

    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.

    Saa1 Human
  • View Data Sheet

    Name :

    STYX Human (26-223)

    Description:

    Serine/Threonine/Tyrosine Interacting Protein (26-223 a.a.) Human Recombinant

    Serine/threonine/tyrosine-interacting protein.

    Product # :

    ENZ-590

    Price :

    Quantity :

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    Description

    STYX Human Recombinant produced in E. coli is a single polypeptide chain containing 221 amino acids (26-223) and having a molecular mass of 25.0kDa.STYX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The STYX solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      STYX is a member of the protein-tyrosine phosphatase family. STYX has a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. Nevertheless, the binding pocket is adequately preserved to bind phosphorylated substrates, and possibly protect them from phosphatases. STYX takes part in spermiogenesis.

    • Synonyms

      Serine/threonine/tyrosine-interacting protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH SHMRREMQEI LPGLFLGPYS SAMKSKLPVL QKHGITHIIC IRQNIEANFI KPNFQQLFRY LVLDIADNPV ENIIRFFPMT KEFIDGSLQM GGKVLVHGNA GISRSAAFVI AYIMETFGMK YRDAFAYVQE RRFCINPNAG FVHQLQEYEA IYLAKLTIQM MSPLQIERSL SVHSGTTGSL KRTHEEEDDF GTMQVATAQN G

    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.

    Styx Human 26 223
  • View Data Sheet

    Name :

    tPA Human, Sf9

    Description:

    Tissue Plasminogen Activator Human Recombinant, Sf9

    Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.

    Product # :

    ENZ-1011

    Price :

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    • description
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    Description

    tPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 545 amino acids (24-562 a.a) and having a molecular mass of 61.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).tPA is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    tPA protein solution (0.25mg/ml) containing 50mM MES buffer(pH 5.5 ), 40% glycerol, 5mM CaCl2, 1mM DTT and 0.5M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
      This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

    • Synonyms

      Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.

    • 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

      QEIHARFRRG ARSYQVICRD EKTQMIYQQH QSWLRPVLRS NRVEYCWCNS GRAQCHSVPV KSCSEPRCFN GGTCQQALYF SDFVCQCPEG FAGKCCEIDT RATCYEDQGI SYRGTWSTAE SGAECTNWNS SALAQKPYSG RRPDAIRLGL GNHNYCRNPD RDSKPWCYVF KAGKYSSEFC STPACSEGNS DCYFGNGSAY RGTHSLTESG ASCLPWNSMI LIGKVYTAQN PSAQALGLGK HNYCRNPDGD AKPWCHVLKN RRLTWEYCDV PSCSTCGLRQ YSQPQFRIKG GLFADIASHP WQAAIFAKHR RSPGERFLCG GILISSCWIL SAAHCFQERF PPHHLTVILG RTYRVVPGEE EQKFEVEKYI VHKEFDDDTY DNDIALLQLK SDSSRCAQES SVVRTVCLPP ADLQLPDWTE CELSGYGKHE ALSPFYSERL KEAHVRLYPS SRCTSQHLLN RTVTDNMLCA GDTRSGGPQA NLHDACQGDS GGPLVCLNDG RMTLVGIISW GLGCGQKDVP GVYTKVTNYL DWIRDNMRPHHHHHH.

    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.

    Tpa Human Sf9
  • View Data Sheet

    Name :

    UTI Human

    Description:

    Urinary Trypsin Inhibitor-Ulinastatin Human

    UTI, Ulinastatin, Urinary Trypsin Inhibitor.

    Product # :

    PRO-321

    Price :

    Quantity :

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    • description
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    Description

    Ulinastatin is derived from human urine.

    Source

    Human Urine.

    Formulation

    Lyophilized from a (1mg/ml) solution containing no additives.

    Biological Activity

    Human UTI has an activity of 2350IU/mg.

    Citations

    More Info

    • Introduction

      Urinary-Trypsin Inhibitor is a glucoprotein proteinase inhibitor which inhibits the activity of trypsin, chymotrypsin, lactate, lipase, hyaluronidase and various pancreatic enzymes. Ulinastatin is effective for acute pancreatitis, chronic recurrent pancreatitis and hemorrhagic, traumatic and endotoxic shocks. Ulinastatin is has strong inhibition effect to various protease, sugar and fat hydrolase. Ulinastatin precursor is proteolytically processed into distinct functioning proteins. Urinary trypsin inhibitor belongs to the superfamily of Kunitz-type protease inhibitors and plays an important role in many physiological and pathological processes. Uristatin gene is located on chromosome 9 in a cluster of lipocalin genes.
      High levels of Ulinastatin secretion is an early marker of renal tubular involvement and has radical scavenging activity. Bikunin localizes cell membrane.
      Free uristatin and bikunin pass readily into urine and are primarily bound to heavy chains that constitute the proinhibitor form in plasma. UTI has a calculated Mw of approx. 20kDa and 40kDa by SDS-PAGE analysis.
      Ulinastatin particularly interacts with ORF3 protein of hepatitis E virus and in charge for enhancing alpha microglobulin export from the hepatocyte.

    • Synonyms

      UTI, Ulinastatin, Urinary Trypsin Inhibitor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized UTI between 2-8°C, do not freeze. Upon reconstitution UTI 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 UTI in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Uti Human
  • View Data Sheet

    Name :

    CTSS Mouse

    Description:

    Cathepsin-S Mouse Recombinant

    Cathepsin S, Ctss, Cats.

    Product # :

    ENZ-954

    Price :

    Quantity :

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    Description

    CTSS Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 325 amino acids (24-340 a.a.) and having a molecular mass of 36.9kDa.CTSS is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Cathepsin S, Ctss, Cats.

    • 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

      EQLQRDP TLDYHWDLWK KTHEKEYKDK NEEEVRRLIW EKNLKFIMIH NLEYSMGMHT YQVGMNDMGD MTNEEISCRM GALRISRQSP KTVTFRSYSN RTLPDTVDWR EKGCVTEVKY QGSCGACWAF SAVGALEGQL KLKTGKLISL SAQNLVDCSN EEKYGNKGCG GGYMTEAFQY IIDNGGIEAD ASYPYKAMDE KCHYNSKNRA ATCSRYIQLP FGDEDALKEA VATKGPVSVG IDASHSSFFF YKSGVYDDPS CTGNVNHGVL VVGYGTLDGK DYWLVKNSWG LNFGDQGYIR MARNNKNHCG IASYCSYPEI LEHHHHHHDY WLVKNSWGLN FGDQGYIRMA RNNKNHCGIA
      SYCSYPEILE HHHHHH.

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    Ctss Mouse
  • View Data Sheet

    Name :

    TFF3 Human

    Description:

    Trefoil Factor-3 Human Recombinant

    TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.

    Product # :

    CYT-005

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    Description

    TFF-3 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 59 amino acid chains which includes a 40 amino acid trefoil motif containing 3 conserved interamolecular disulfide bonds and having a total molecular mass of 13.2kDa. TFF-3 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of > 100IU/mg.

    Citations

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    • Introduction

      Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains. TFF3 induces ciliogenesis and promotes airway epithelial ciliated cell differentiation, relatively through an epidermal growth factor receptor-dependent pathway. TFF3 overexpression is crucial for progression in mouse and human hepatocellular carcinogenesis. TFF-3 is normally expressed in hepatocellular carcinoma and its expression associates with tumor grade.

    • Synonyms

      TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF3 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 TFF3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EEYVGLSANQ CAVPAKDRVD CGYPHVTPKE CNNRGCCFDS RIPGVPWCFK PLQEAECTF.

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    Tff3 Human
  • View Data Sheet

    Name :

    HA Monoclonal Antibody

    Description:

    HA Mouse Antibody

    Product # :

    ANT-225

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    Description

    Monoclonal antibodies are produced by immunizing mouse with synthetic peptide (YPYDVPDYA) coupled to KLH.

    Formulation

    1×PBS & 50% glycerol.

    Citations

    More Info

    • Physical Appearance

      Sterile filtered colorless solution.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      PHASHG.

    • Applications

      Western Blot, Immunoprecipitation.

    • Titer

      Western Blotting: 1µg/ml.

    • Type

      Mouse Antibody 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.

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    Ha Antibody
  • View Data Sheet

    Name :

    LH Porcine

    Description:

    Luteinizing Hormone Porcine

    Product # :

    HOR-310

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    Description

    Porcine Luteinizing Hormone is a glycosylated, heterodimer polypeptide chain which stimulates maturation of follicle, induces ovulation, accelerates formation of corpus luteum and secretion of pregnanolone. Porcine Luteinizing Hormone delays ovulation and ovarian cyst.

    Source

    Porcine.

    Formulation

    The LH was lyophilized with no additives.

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Porcine LH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LH 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 Porcine LH in sterile 18M-cm H2O at 100IU/4ml, which can then be further diluted to other aqueous solutions.

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    Lh Porcine
  • View Data Sheet

    Name :

    HTLV-1 p24

    Description:

    HTLV-1 p24 Recombinant

    Product # :

    HIV-003

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    Description

    HTLV-1 p24 Recombinant produced in E.Coli covers full length of HTLV-1 p24 and contains 188 amino acids having a molecular size 21kDa. HTLV-1 p24 is purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    HTLV-1 p24 protein solution containing PBS, pH-7.4.

    Purity

    Protein is >95% pure as determined by 12% SDS-PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

      Human T-lymphotropic virus (HTLV) is a human, single-stranded RNA retrovirus that causes
      T-cell leukemia and T-cell lymphoma. The virus activates a subset of T-helper cellscalled Th1cells. The result is a proliferation of Th1 cells and overproduction of Th1 related cytokines (mainly IFN-gamma and TNF-alpha). Feedback mechanisms of these cytokines cause a suppression of the Th2 lymphocytes and a reduction of Th2 cytokine production (mainly
      IL-4, IL-5, IL-10 and IL-13). The end result is a reduction in the ability of the infected host to mount an adequate immune response to invading organisms that require a predominantly
      Th2 dependant response (these include parasitic infections and production of mucosal and humoral antibodies).
      HTLV-1 p24 is usually used for clinical diagnosis and forms both monomer and dimer on
      SDS-PAGE gel but the majority of protein is a dimer.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      HTLV-1 p24 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

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    Htlv 1 P24
  • View Data Sheet

    Name :

    DBH Human

    Description:

    DBH Human Recombinant

    EC 1.14.17.1, DBM, DBH.

    Product # :

    ENZ-891

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    Description

    DBH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 599 amino acids (40-617 a.a) and having a molecular mass of 67.2kDa.DBH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DBH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DBH catalyzes the chemical reaction. DBH is an oxidoreductase which belongs to the copper type II, ascorbate-dependent monooxygenase family, in particular those performing on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated can not be derived from O2 with reduced ascorbate as one donor, as well as incorporation of one ato of oxygen into the other donor.

    • Synonyms

      EC 1.14.17.1, DBM, DBH.

    • 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 MSAPRESPLP YHIPLDPEGS LELSWNVSYT QEAIHFQLLV RRLKAGVLFG MSDRGELENA DLVVLWTDGD TAYFADAWSD QKGQIHLDPQ QDYQLLQVQR TPEGLTLLFK RPFGTCDPKD YLIEDGTVHL VYGILEEPFR SLEAINGSGL QMGLQRVQLL KPNIPEPELP SDACTMEVQA PNIQIPSQET TYWCYIKELP KGFSRHHIIK YEPIVTKGNE ALVHHMEVFQ CAPEMDSVPH FSGPCDSKMK PDRLNYCRHV LAAWALGAKA FYYPEEAGLA FGGPGSSRYL RLEVHYHNPL VIEGRNDSSG IRLYYTAKLR RFNAGIMELG LVYTPVMAIP PRETAFILTG YCTDKCTQLA LPPSGIHIFA SQLHTHLTGR KVVTVLVRDG REWEIVNQDN HYSPHFQEIR MLKKVVSVHP GDVLITSCTY NTEDRELATV GGFGILEEMC VNYVHYYPQT QLELCKSAVD AGFLQKYFHL INRFNNEDVC TCPQASVSQQ FTSVPWNSFN RDVLKALYSF APISMHCNKS SAVRFQGEWN LQPLPKVIST LEEPTPQCPT SQGRSPAGPT VVSIGGGKG

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    Dbh Human
  • View Data Sheet

    Name :

    Myostatin Propeptide Human, HEK

    Description:

    Myostatin Propeptide Human Recombinant, HEK

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-936

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    Description

    Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Arg266) containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa. Myostatin Propetide is fused to a 10 aa C-terminal His tag.

    Source

    HEK 293.

    Formulation

    Myostatin Propetide solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • Physical Appearance

      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

      NENSEQKENV EKEGLCNACT WRQNTKSSRI EAIKIQILSK LRLETAPNIS KDVIRQLLPK APPLRELIDQ YDVQRDDSSD GSLEDDDYHA TTETIITMPT ESDFLMQVDG KPKCCFFKFS SKIQYNKVVK AQLWIYLRPV ETPTTVFVQI LRLIKPMKDG TRYTGIRSLK LDMNPGTGIW QSIDVKTVLQ NWLKQPESNL GIEIKALDEN GHDLAVTFPG PGEDGLNPFL EVKVTDTPKR SRR HHHHHHH HHH.

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    Myostatin Propeptide Human Hek
  • View Data Sheet

    Name :

    TREM2 Human, HEK

    Description:

    Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant, HEK

    Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    Product # :

    PRO-2773

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    Description

    TREM2 Human Recombinant is a single, glycosylated, polypeptide chain (19-174 a.a) containing a total of 162 amino acids, having a molecular mass of 18.2 kDa. TREM2 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The TREM2 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

    • Synonyms

      Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    • 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

      HNTTVFQGVA GQSLQVSCPY DSMKHWGRRK AWCRQLGEKG PCQRVVSTHN LWLLSFLRRW NGSTAITDDT LGGTLTITLR NLQPHDAGLY QCQSLHGSEA DTLRKVLVEV LADPLDHRDA GDLWFPGESE SFEDAHVEHS ISRSLLEGEI PFPPTSHHHH HH.

    • Background

      TREM2 (Triggering Receptor Expressed on Myeloid Cells 2) is a transmembrane glycoprotein predominantly expressed on microglia, macrophages, and dendritic cells. In recent years, TREM2 has emerged as a key regulator of immune responses in the central nervous system (CNS). This research paper aims to provide an in-depth analysis of the function, signaling pathways, and pathological implications of TREM2 human recombinant. Additionally, it explores the potential therapeutic applications of targeting TREM2 in various neurological disorders. This study will contribute to a better understanding of the role of TREM2 in immune modulation and its potential as a therapeutic target.

      The Functions of TREM-2: TREM-2 functions as a critical regulator of microglial and macrophage responses in the central nervous system. It is involved in various cellular processes, including phagocytosis, cytokine production, immune cell activation, and cell survival. Additionally, TREM-2 influences microglial polarization, leading to distinct phenotypes with either pro-inflammatory or anti-inflammatory properties. Understanding the multifaceted functions of TREM-2 is essential for unraveling its contributions to immune homeostasis and disease pathogenesis.

      Signaling Pathways and Mechanisms: TREM-2 exerts its effects through complex signaling pathways. Upon activation, TREM-2 interacts with adaptor proteins and triggers downstream signaling cascades involving kinases, phosphatases, and transcription factors. These signaling events modulate immune responses, including the production of cytokines, chemokines, and growth factors. Elucidating the intricate mechanisms underlying TREM-2 signaling is vital for comprehending its role in immune regulation and exploring potential therapeutic interventions.

      Implications in Neurodegenerative Diseases: TREM-2 has emerged as a key player in neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. Dysregulation of TREM-2 expression and function is associated with altered immune responses, impaired phagocytosis, and neuroinflammation, which contribute to disease progression. Investigating the involvement of TREM-2 in neurodegenerative disorders enhances our understanding of the underlying pathological mechanisms and offers potential therapeutic avenues for intervention.

      Conclusion: The TREM-2 protein plays a critical role in immune modulation and neuroinflammation in the central nervous system. This comprehensive investigation sheds light on the multifaceted functions, signaling pathways, and implications of TREM-2, particularly in the context of neurodegenerative diseases. Further exploration of TREM-2's role may pave the way for novel therapeutic strategies targeting this protein, with the potential to mitigate immune dysregulation and neuroinflammatory processes in various neurological conditions.

      Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on TREM-2 for a comprehensive list of references and sources.

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    Trem2 Human Hek
  • View Data Sheet

    Name :

    GSTM1 Mouse

    Description:

    Glutathione S-Transferase M1 Mouse Recombinant

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

    Product # :

    ENZ-397

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    Description

    GSTM1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 218 amino acids and having a molecular mass of 25.9 kDa.The GTM1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM1 solution contains PBS pH-7.4 & 5mM glutathione.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is 3 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK.

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    Gstm1 Mouse
  • View Data Sheet

    Name :

    GSTM3 Human

    Description:

    Glutathione S-Transferase MU 3 Human Recombinant

    Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.

    Product # :

    ENZ-592

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    Description

    GSTM3 Recombinant produced in E. coli is a single polypeptide chain containing 249 amino acids (1-225) and having a molecular mass of 29.1kDa.GSTM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GSTM3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl,
    1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GSTM3 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The mu type of enzymes takes part in the detoxification of electrophilic compounds, including therapeutic drugs, carcinogens, environmental toxins and products of oxidative stress, by conjugation with glutathione.

    • Synonyms

      Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione
      S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMSCESS MVLGYWDIRG LAHAIRLLLE FTDTSYEEKR YTCGEAPDYD RSQWLDVKFK LDLDFPNLPY LLDGKNKITQ SNAILRYIAR KHNMCGETEE EKIRVDIIEN QVMDFRTQLI RLCYSSDHEK LKPQYLEELP GQLKQFSMFL GKFSWFAGEK LTFVDFLTYD ILDQNRIFDP KCLDEFPNLK AFMCRFEALE KIAAYLQSDQ FCKMPINNKM AQWGNKPVC

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    Gstm3 Human
  • View Data Sheet

    Name :

    DTD1 Human

    Description:

    D-Tyrosyl-tRNA Deacylase 1 Human Recombinant

    bA379J5.3, bA555E18.1, C20orf88, DUEB, HARS2, pqn-68, D-tyrosyl-tRNA(Tyr) deacylase 1, DNA-unwinding element-binding protein B.

    Product # :

    ENZ-671

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    Description

    DTD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-209a.a.) and having a molecular mass of 25.9kDa.DTD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DTD1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      D-Tyrosyl-tRNA Deacylase 1 (DTD1) is a member of the DTD family. DTD1 hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). DTD1 may be a defense mechanism against a damaging effect of D-tyrosine. DTD1 is an ATPase involved in DNA replication, which may facilitate loading of CDC45 onto pre-replication complexes. The DTD1 protein localizes to the DUE (DNA unwinding elements) of active replication origins. DTD1 is expressed in numerous adult and fetal tissues, with the highest levels in the testis, ovary, spleen and in the adult and fetal brain. DTD1 might be a risk factor for AIA (aspirin-intolerant asthma) by catalyzing the hydrolysis of D-tryptophan and interacting with the tyrosyl-tRNA synthetase (tyrRS) enzyme that promotes a pro-inflammatory phenotype.

    • Synonyms

      bA379J5.3, bA555E18.1, C20orf88, DUEB, HARS2, pqn-68, D-tyrosyl-tRNA(Tyr) deacylase 1, DNA-unwinding element-binding protein B.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMKAVVQR VTRASVTVGG EQISAIGRGI CVLLGISLED TQKELEHMVR KILNLRVFED ESGKHWSKSVMDKQYEILCV SQFTLQCVLK GNKPDFHLAM PTEQAEGFYN SFLEQLRKTY RPELIKDGKF GAYMQVHIQN DGPVTIELES PAPGTATSDP KQLSKLEKQQ QRKEKTRAKG PSESSKERNT PRKEDRSASS GAEGDVSSER EP.

    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.

    Dtd1 Human
  • View Data Sheet

    Name :

    TNNI3 Human, (1-210)

    Description:

    Cardiac Troponin-I Human Recombinant (1-210 a.a.)

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    Product # :

    PRO-2591

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    Description

    TNNI3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 26.4 kDa.TNNI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNNI3 protein solution (0.25mg/ml) contains 30% glycerol, 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl, 0.1mMPMSF & 1mM DTT.

    Purity

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

    Citations

    More Info

    • Introduction

      Troponin I (TnI), troponin T (TnT) and troponin C (TnC) form the troponin complex of the thin filaments of striated muscle. TnI acts as the inhibitory subunit by blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains 3 genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. The TNNI3 gene encodes the TnI-cardiac protein and isexpressed solely in cardiac muscle tissues. Mutations in the TNNI3 gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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 MGSMADGSSD AAREPRPAPA PIRRRSSNYR AYATEPHAKK KSKISASRKL QLKTLLLQIA KQELEREAEERRGEKGRALS TRCQPLELAG LGFAELQDLC RQLHARVDKV DEERYDIEAK VTKNITEIAD LTQKIFDLRG KFKRPTLRRV RISADAMMQALLGARAKESL DLRAHLKQVK KEDTEKENRE VGDWRKNIDA LSGMEGRKKK FES

    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.

    Cardiac Troponin I
  • View Data Sheet

    Name :

    ProInsulin Human

    Description:

    ProInsulin C-Peptide Analogue Human Recombinant

    Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN. 

    Product # :

    CYT-1120

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    Description

    ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Citations

    More Info

    • Introduction

      Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

    • Synonyms

      Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.

    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.

    Proinsulin C Peptide
  • View Data Sheet

    Name :

    LTA4H Human

    Description:

    Leukotriene A4 Hydrolase Human Recombinant

    Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.

    Product # :

    ENZ-869

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    Description

    LTA4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 634 amino acids (1-611 a.a) and having a molecular mass of 71.7kDa.LTA4H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LTA4H protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Leukotriene A-4 hydrolase (LTA4H) is a bifunctional enzyme that converts leukotriene A4 to leukotriene B4 and functions as an aminopeptidase. The LTA4H enzyme is a member of the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). LTA4H participates in arachidonic acid metabolism.

    • Synonyms

      Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.

    • 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 MGSMPEIVDT CSLASPASVC RTKHLHLRCS VDFTRRTLTG TAALTVQSQE DNLRSLVLDT KDLTIEKVVI NGQEVKYALG ERQSYKGSPM EISLPIALSK NQEIVIEISF ETSPKSSALQ WLTPEQTSGK EHPYLFSQCQ AIHCRAILPC QDTPSVKLTY TAEVSVPKEL VALMSAIRDG ETPDPEDPSR KIYKFIQKVP IPCYLIALVV GALESRQIGP RTLVWSEKEQ VEKSAYEFSE TESMLKIAED LGGPYVWGQY DLLVLPPSFP YGGMENPCLT FVTPTLLAGD KSLSNVIAHE ISHSWTGNLV TNKTWDHFWL NEGHTVYLER HICGRLFGEK FRHFNALGGW GELQNSVKTF GETHPFTKLV VDLTDIDPDV AYSSVPYEKG FALLFYLEQL LGGPEIFLGF LKAYVEKFSY KSITTDDWKD FLYSYFKDKV DVLNQVDWNA WLYSPGLPPI KPNYDMTLTN ACIALSQRWI TAKEDDLNSF NATDLKDLSS HQLNEFLAQT LQRAPLPLGH IKRMQEVYNF NAINNSEIRF RWLRLCIQSK WEDAIPLALK MATEQGRMKF TRPLFKDLAA FDKSHDQAVR TYQEHKASMH PVTAMLVGKD LKVD.

    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.

    Lta4H Human
  • View Data Sheet

    Name :

    Kisspeptin-10

    Description:

    Kisspeptin-10

    Product # :

    HOR-044

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    Description

    Kisspeptin-10 Synthetic is a single, non-glycosylated polypeptide chain containing 10 amino acids, having a molecular mass of 1302 Dalton and a Molecular formula of C63H83N17O14 .

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Kisspeptin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kisspeptin-10 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 Kisspeptin-10 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2.

    • Background

      Kisspeptin-10, a peptide derived from the Kisspeptin gene (KISS1), has emerged as a key player in the regulation of reproductive physiology. The peptide is known for its potent ability to stimulate the release of gonadotropin-releasing hormone (GnRH), a crucial factor in the control of the hypothalamic-pituitary-gonadal axis. The pivotal role of kisspeptin-10 in orchestrating the onset of puberty and the regulation of the menstrual cycle highlights its significance in reproductive health. This research aims to delve into the multifaceted functions of kisspeptin-10, shedding light on its physiological roles and potential applications in reproductive disorders.

      The primary objective of this study is to comprehensively explore the effects of kisspeptin-10 on the reproductive system. In vitro and in vivo assays will be conducted to investigate the impact of kisspeptin-10 on GnRH release and subsequent gonadotropin secretion. The interactions between kisspeptin-10 and its receptor, G protein-coupled receptor 54 (GPR54), will be explored using binding assays, potentially unraveling novel signaling pathways activated by this interaction.

      The second objective is to investigate the potential therapeutic applications of kisspeptin-10 in reproductive disorders. Clinical studies and animal models will be utilized to assess the efficacy of kisspeptin-10 in stimulating ovulation, particularly in cases of infertility caused by hypothalamic dysfunction. Furthermore, the potential of kisspeptin-10 in regulating conditions like polycystic ovary syndrome (PCOS) and hypogonadotropic hypogonadism will be explored.

      The third objective is to elucidate the molecular mechanisms underlying the actions of kisspeptin-10. Transcriptomic and proteomic analyses will be employed to identify genes and proteins regulated by kisspeptin-10 stimulation. This information could reveal novel downstream effectors of kisspeptin-10 signaling, contributing to a more comprehensive understanding of its role in reproductive physiology.

      By delving into the complexities of kisspeptin-10, this research aims to provide insights into its multifunctional roles in reproductive health and expand its potential therapeutic applications. The findings from this study may pave the way for the development of targeted interventions for reproductive disorders, potentially improving the quality of life for individuals affected by these conditions.

    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.

    Kisspeptin 10
  • View Data Sheet

    Name :

    GH Ovine

    Description:

    Growth Hormone Ovine Recombinant

    GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-237

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    Description

    Growth Hormone Ovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21833 Dalton. The GH Ovine Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    The activity as determined by the dose-dependant stimulation of the proliferation FDCP13B9 cells.

    Citations

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH Ovine 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 Growth Hormone in sterile 0.4% NaHCO3 or water adjusted to pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      1 afpamslsgl fanavlraqh lhqlaadtfk efertyipeg qrysiqntqv 51 afcfsetipa ptgkneaqqk sdlellrisl lliqswlgpl qflsrvftns 101 lvfgtsdrvy eklkdleegi lalmreledv tpragqilkq tydkfdtnmr 151 sddallknyg llscfrkdlh ktetylrvmk crrfgeasca f

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

    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.

    Growth Hormone Ovine
  • View Data Sheet

    Name :

    TARS Human

    Description:

    Threonyl-tRNA Synthetase Human Recombinant

    Threonine--tRNA ligase, cytoplasmic, Threonyl-tRNA synthetase, ThrRS, TARS.

    Product # :

    ENZ-571

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    Description

    TARS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 743 amino acids (1-723) and having a molecular mass of 85.6kDa.TARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Threonyl-tRNA synthetase, cytoplasmic (TARS) is a member of the class-II aminoacyl-tRNA synthetase family. The main role of TARS is in tRNA aminoacylation. The N-terminal domain of the TARS enzyme is responsible for the competition with the ribosome whereas the catalytic and the C-terminal domain are involved in binding the 2 anticodon arm-like structures in the operator.

    • Synonyms

      Threonine--tRNA ligase, cytoplasmic, Threonyl-tRNA synthetase, ThrRS, TARS.

    • 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 MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW PEYIYTRLEM YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE NGFYYDMYLE EGGVSSNDFS SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP
      GSCFFLPKGA YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE EEF.

    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.

    Tars Human
  • View Data Sheet

    Name :

    Prolactin Human

    Description:

    Prolactin Human Recombinant

    Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    Product # :

    CYT-267

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    Description

    Prolactin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 23007 Dalton. The Prolactin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of rat lymphoma, Nb2-11 was found to be < 0.065ng/ml corresponding to a Specific Activity of 15,385,000IU/mg.

    Citations

    More Info

    • Introduction

      Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

    • Synonyms

      Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin 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 Prolactin 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 Met-Leu-Pro-Ile-Cys.

    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.

    Prolactin Human
  • View Data Sheet

    Name :

    Elamipretide

    Description:

    Elamipretide

    SS-31, MTP-131, Bendavia.

    Product # :

    HOR-040

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    Description

    Elamipretide Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 639.79 Dalton and a Molecular formula of C32H49N9O5
    .

    Source

    Synthetic Peptide

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    HPLC, MS

    Elamipretide hplc - Product image 1
    elamipretide mass spec - Product image 2

    Citations

    More Info

    • Synonyms

      SS-31, MTP-131, Bendavia.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-D-Arg-(2',6'-dimethyl-Tyr)-Lys-Phe-NH2

    • Background

      What is the molecular weight/Mw of Elamipretide Protein?
      Elamipretide Protein has a total Mw of 639Da.
      What is the source or expression system of Elamipretide Protein?
      Synthetic peptide

      What is the Purity of Elamipretide Protein?

      Elamipretide Protein is >97% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of Elamipretide Protein?
      H-D-Arg-(2',6'-dimethyl-Tyr)-Lys-Phe-NH2

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

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

      Elamipretide (also known as SS-31) is a novel mitochondrial-targeted peptide with immense promise as a therapeutic agent in mitochondrial dysfunction-related disorders. This research paper aims to provide a comprehensive analysis of Elamipretide, delving into its biochemical properties, mechanisms of action, and potential applications in various disease conditions.

      Elamipretide, a mitochondria-targeting tetrapeptide, has garnered attention for its unique ability to protect mitochondria from oxidative stress and attenuate mitochondrial dysfunction (Siegel et al., 2013). This paper endeavors to explore Elamipretide's biochemical basis and its potential as a therapeutic agent in various diseases linked to mitochondrial impairment.

      Elamipretide selectively accumulates within the inner mitochondrial membrane, where it exerts its cytoprotective effects. By reducing reactive oxygen species (ROS) production and enhancing electron transport chain efficiency, Elamipretide plays a crucial role in mitochondrial homeostasis (Kloner et al., 2015).

      The mitochondrial protective actions of Elamipretide arise from its interaction with cardiolipin, a phospholipid predominantly localized in the inner mitochondrial membrane. By binding to cardiolipin, Elamipretide stabilizes mitochondrial cristae, improves membrane integrity, and enhances oxidative phosphorylation (Minkler et al., 2015).

      Elamipretide's potential applications extend to a myriad of disease conditions characterized by mitochondrial dysfunction. In preclinical studies, Elamipretide has shown promise in mitigating tissue damage following ischemia-reperfusion injury, preserving cardiac function after myocardial infarction, and ameliorating neurodegenerative processes (Birk et al., 2017; Cho et al., 2015).

      As the research on Elamipretide progresses, further investigation is warranted to better understand its pharmacokinetics, long-term safety, and potential off-target effects. Clinical trials exploring its therapeutic efficacy in human diseases offer exciting prospects for the future.

      Elamipretide, a mitochondria-targeting peptide, emerges as a promising candidate in combating mitochondrial dysfunction-related disorders. Its unique ability to stabilize mitochondrial membranes and enhance cellular bioenergetics positions Elamipretide as a novel therapeutic option for a diverse range of diseases.

    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.

    Elamipretide
  • 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
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