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Search results

1000 results found for “Omentin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    TIPIN Human

    Description:

    TIMELESS Interacting Protein Human Recombinant

    TIMELESS Interacting Protein, CSM3 Homolog.

    Product # :

    PRO-1710

    Price :

    Quantity :

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    • source
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    • More Info

    Description

    TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.

    • Synonyms

      TIMELESS Interacting Protein, CSM3 Homolog.

    • 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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR

    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.

    Tipin Human
  • View Data Sheet

    Name :

    OSM Mouse

    Description:

    Oncostatin-M Mouse Recombinant

    Oncostatin-M, OSM, OncoM.

    Product # :

    CYT-168

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
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    • purity
    • biological activity
    • More Info

    Description

    OSM Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.4kDa.The OSM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of NIH-3T3 mouse embryonic fibroblast cells is < 1 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.

    More Info

    • Introduction

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

    • Synonyms

      Oncostatin-M, OSM, OncoM.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      NRGCSNSSSQ LLSQLQNQAN LTGNTESLLE PYIRLQNLNT PDLRAACTQH SVAFPSEDTL RQLSKPHFLS TVYTTLDRVL YQLDALRQKF LKTPAFPKLD SARHNILGIR NNVFCMARLL NHSLEIPEPT QTDSGASRST TTPDVFNTKI GSCGFLWGYH RFMGSVGRVF REWDDGSTRS R.

    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.

    Osm Mouse
  • View Data Sheet

    Name :

    STOM Antibody

    Description:

    Stomatin, Mouse Anti Human

    BND7, EPB7, EPB72, Erythrocyte band 7 integral membrane protein, Protein 7.2b, Stomatin, STOM.

    Product # :

    ANT-514

    Price :

    Quantity :

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    More Info

    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      Stomatin (STOM) is a part of a highly conserved family of integral membrane proteins. STOM is a membrane protein involved in regulation of monovalent cation transport through lipid membranes which regulates ACCN1 and ACCN3 gating. STOM is a major lipid-raft component of erythrocytes and epithelial cells, and an abundant platelet protein which acts as a cytoskeletal anchor.

    • Synonyms

      BND7, EPB7, EPB72, Erythrocyte band 7 integral membrane protein, Protein 7.2b, Stomatin, STOM.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human STOM mAb, clone PAT33F5AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human STOM protein 55-288 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT33F5AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

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

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

    Stom Antibody
  • View Data Sheet

    Name :

    MT I

    Description:

    Melanotan-I

    Melanotan-I, MT-I, Melanotan-1.

    Product # :

    HOR-306

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • formulation
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    • More Info

    Description

    Melanotan-I has the amino acid sequence of Ser-Tyr-Ser-Nle-Glu-His-D-Phe-Arg-Trp-Gly-Lys-Pro-Val and a molecular weight of 1647.4 Dalton.

    Formulation

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

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Synonyms

      Melanotan-I, MT-I, Melanotan-1.

    • Physical Appearance

      Sterile Filtered off-White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Melanotan-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MT-I 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 Melanotan-I in sterile 1% acetic acid not less than 100 µg/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.

    Melanotan I
  • View Data Sheet

    Name :

    OSTF1 Human

    Description:

    Osteoclast Stimulating Factor-1 Human Recombinant

    SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

    Product # :

    CYT-630

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    OSTF1 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 225 amino acids (1-217) and having a molecular mass of 25.1kDa. The OSTF1 is fused to an 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSTF1 protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH 8, 0.5mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.

    • Synonyms

      SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MSKPPPKPVK PGEGGQVKVF RALYTFEPRT PDELYFEEGD IIYITDMSDT NWWKGTSKGR TGLIPSNYVA EQAESIDNPL HEAAKRGNLS WLRECLDNRV GVNGLDKAGS TALYWACHGG HKDIVEMLFT QPNIELNQQN KLGDTALHAA AWKGYADIVQ LFLAKGARTD LRNIEKKLAF DMATNAACAS LLKKKQGTDA VRTLSNAEDY LDDEDSDLEH HHHHH.

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

    Ostf1 Human
  • View Data Sheet

    Name :

    L Selectin Human

    Description:

    L-selectin Human Recombinant

    L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.

    Product # :

    PRO-381

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    L-Selectin Human Recombinant is expressed in E. coli containing 294 amino acids 39-332 fused to an amino terminal hexahistidine tag, having a total molecular weight of 37.55kDa.

    Source

    Escherichia Coli.

    Formulation

    L-Sel is supplied in 1x PBS and 50% Glycerol.

    Purity

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

    More Info

    • Introduction

      L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
      L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
      L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.

    • Synonyms

      L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Applications

      L-Selectin can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    L Selectin Human
  • View Data Sheet

    Name :

    ASMT Human

    Description:

    Acetylserotonin O-Methyltransferase Human Recombinant

    HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    Product # :

    ENZ-664

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    Description

    ASMT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298 a.a) and having a molecular mass of 35.3kDa.ASMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASMT is a member of the methyltransferase superfamily. ASMT participates in melatonin biosynthesis. ASMT Expressed in brain, retina and pineal gland, ASMT utilities to catalyze the final reaction in the synthesis of melatonin, particularly the conversion of S-adenosyl-L-methionine and N-acetylserotonin to S-adenosyl-Lhomocysteine and melatonin.

    • Synonyms

      HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.

    • 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 MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGDF FKDPLPEADL YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD EDRRGPLLTQ LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK

    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.

    Asmt Human
  • View Data Sheet

    Name :

    Intein Bacillus Circulans

    Description:

    Intein Bacillus Circulans Recombinant

    Intein-CBD

    Product # :

    PRO-958

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    Description

    Intein Bacillus Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 533 amino acids (3-518) and having a molecular mass of 59.4 kDa.Intein is fused to a 16 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Intein is a section of a protein which can remove itself and return the remaining segment with a peptide bond. In addition, Inteins hold an endonuclease domain which takes part in Intein proliferation. Actually, various genes have unrelated intein-coding segments inserted at altered positions and they were found in all three domains of life (eukaryotes, bacteria, and archaea) and in viruses.

    • Synonyms

      Intein-CBD

    • 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

      MKIEEGKLVI GSLEGCFAKG TNVLMADGSI ECIENIEVGN KVMGKDGRPR EVIKLPRGRE TMYSVVQKSQ HRAHKSDSSR EVPELLKFTC NATHELVVRT PRSVRRLSRT IKGVEYFEVI TFEMGQKKAP DGRIVELVKE VSKSYPISEG PERANELVES YRKASNKAYF EWTIEARDLS LLGSHVRKAT YQTYAPILYE NDHFFDYMQK SKFHLTIEGP KVLAYLLGLW IGDGLSDRAT FSVDSRDTSL MERVTEYAEK LNLCAEYKDR KEPQVAKTVN LYSKVVRGAS TNPGVSAWQV NTAYTAGQLV TYNGKTYKCL QPHTSLAGWE PSNVPALWQL QGGHGGIRNN LNTENPLWDA IVGLGFLKDG VKNIPSFLST DNIGTRETFL AGLIDSDGYV TDEHGIKATI KTIHTSVRDG LVSLARSLGL VVSVNAEPAK VDMNVTKHKI SYAIYMSGGD VLLNVLSKCA GSKKFRPAPA AAFARECRGF YFELQELKED DYYGITLSDD SDHQFLLGSQ VVVQNLEHHH HHH

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

    Intein Bacillus Circulans
  • View Data Sheet

    Name :

    Leptin Receptor Chicken

    Description:

    Leptin Receptor Chicken Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    Product # :

    CYT-509

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    Description

    Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    • Physical Appearance

      Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.

    • Stability

      Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of Leptin Binding Domain as a Reference Standard.

    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.

    Leptin Receptor Chicken
  • View Data Sheet

    Name :

    OCT Human

    Description:

    Octreotide Human

    Product # :

    HOR-265

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    Description

    Octreotide Human Synthetic is a single, non-glycosylated, polypeptide chain containing 8 amino acids, having a molecular mass of 1019.26 Dalton and a molecular formula of C49H66N10O10S2.Octreotide is purified by proprietary chromatographic techniques.

    Formulation

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

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Octreotide acetate is a longer acting synthetic octapeptide analog of naturally occurring somatostatin. It inhibits the secretion of gastro-entero-pancreatic peptide hormones and the release of growth hormone.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Octreotide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Octreotide 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 Octreotide 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-Phe-Cys-Phe-D-Trp-Lys-Thr-Cys-L-threoninol.

    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.

    Octreotide Human
  • View Data Sheet

    Name :

    Leptin Protein

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

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    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin 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 95.0% as determined by:
    (a) Analysis by Gel filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile water or 0.4% NaHCO3 pH-8-9, 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 Ala-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Human
  • View Data Sheet

    Name :

    IGF1 Gilthead Seabream

    Description:

    IGF1 Gilthead Seabream Recombinant

    Somatomedin C, IGF-I, IGFI.

    Product # :

    CYT-295

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    Description

    IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.IGF-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.

    More Info

    • Introduction

      The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.

    • Synonyms

      Somatomedin C, IGF-I, IGFI.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK

    • Protein content

      Somatomedin C quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.60 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IGF1 as a Reference Standard.

    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.

    Igf 1 Denis
  • View Data Sheet

    Name :

    Leptin Rabbit

    Description:

    Leptin Rabbit Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-507

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    Description

    Leptin Rabbit Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 adjusted to pH-8-9, 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 Ala-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.505 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Rabbit
  • View Data Sheet

    Name :

    OmpA

    Description:

    Outer Membrane Protein-A Bacterial Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-571

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    Description

    The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.

    More Info

    • Introduction

      The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.

    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.

    Outer Membrane Protein A
  • View Data Sheet

    Name :

    Follistatin Human

    Description:

    Follistatin Human Recombinant

    FST, FS

    Product # :

    CYT-232

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    Description

    Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

    More Info

    • Introduction

      Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

    • Synonyms

      FST, FS

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin 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 Gly-Asn-Cys-Trp-Leu.

    • Background

      What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
      FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.

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

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

      What is the Biological Activity of FOLLISTATIN HUMAN Protein?
      The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

      What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.

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

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

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

    Follistatin Human
  • View Data Sheet

    Name :

    UMOD Porcine

    Description:

    Uromodulin Porcine

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

    Product # :

    ENZ-733

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    Description

    Porcine Uromodulin is a 97kDa glycoprotein which is produced in the thick ascending limb of Henle´s loop and early distal convoluted tubules of the nephron.

    Source

    Porcine Urine.

    Formulation

    The UMOD protein was lyophilized from 0.4µm filtered solution at a concentration of 0.5mg/ml containing deionized water.

    More Info

    • Introduction

      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.

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      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.

    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.

    Umod Porcine
  • View Data Sheet

    Name :

    OPG Human, His

    Description:

    Osteoprotegerin Human Recombinant, His Tag

    TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

    Product # :

    CYT-290

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    Description

    Recombinant Human OCIF produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing amino acids 201-401 and having a molecular mass of 31 kDa which includes a 4 kDa His tag.The OPG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

    Purity

    Greater than 80.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Osteoprotegerin, which is a member of the tumor necrosis factor receptor superfamily and is involved in the regulation of bone metabolism. OPGand its ligand (OPGL) are cytokines regulating osteoclasto-genesis. OPGL binds to receptors on the surface of preosteoclasts and stimulates their differentiation into active osteoclasts. This leads to osteoresorption. OPG inhibits this osteoclasto-genesis (OPG is secreted by osteoblasts, and binds to OPGL, thus inhibiting maturation of osteoclasts and osteoresorption). The degree and activity of osteoresorption depend mainly on the balance between OPG and its ligand (OPGL); factors increasing OPGL expression mostly reduce OPG expression and vice versa.

    • Synonyms

      TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      1. Positive control for Western blot.
      2. Antibody production.
      3. Protein assay.

    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.

    Osteoprotegerin Human His
  • View Data Sheet

    Name :

    TMEFF1 Human

    Description:

    TMEFF1 Human Recombinant

    C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.

    Product # :

    PRO-1429

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    Description

    TMEFF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 314 amino acids (40-330) and having a molecular mass of 33.9kDa. TMEFF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TMEFF1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TMEFF1 is a type I transmembrane glycoprotein which includes 2 follistatin modules and an EGF domain in its extracellular domain, a transmembrane domain and a short cytoplasmic tail. The extracellular domain of TMEFF1 can be released as a soluble protein. TMEFF1 is primarily expressed in brain, but is downregulated in brain neoplasms. TMEFF1 selectively regulates nodal but not activin signaling through direct binding to the nodal co-receptor, Cripto. TMEFF inhibits NODAL and BMP signaling through neural patterning and also a possible tumor suppressor in brain cancers.

    • Synonyms

      C9orf2, CT120.1, H7365, TR-1, Tomoregulin-1, Transmembrane protein with EGF-like and one follistatin-like domain, TMEFF1.

    • 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 MGSSNQPPGG GGGSGGDCPG GKGKSINCSE LNVRESDVRV CDESSCKYGG VCKEDGDGLK CACQFQCHTN YIPVCGSNGD TYQNECFLRR AACKHQKEIT VIARGPCYSD NGSGSGEGEE EGSGAEVHRK HSKCGPCKYK AECDEDAENV GCVCNIDCSG YSFNPVCASD GSSYNNPCFV REASCIKQEQ IDIRHLGHCT DTDDTSLLGK KDDGLQYRPD VKDASDQRED VYIGNHMPCP ENLNGYCIHG KCEFIYSTQK ASCRCESGYT GQHCEKTDFS ILYVVPSRQK LTHV.

    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.

    Tmeff1 Human
  • View Data Sheet

    Name :

    ODC1 antibody

    Description:

    Ornithine Decarboxylase 1, Mouse Anti Human

    ODC, Ornithine decarboxylase 1, EC 4.1.1.17.

    Product # :

    ANT-739

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    • More Info

    Formulation

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

    More Info

    • Introduction

      Ornithine decarboxylase is the preliminary and rate-limiting enzyme in the biosynthetic pathway of polyamines and it takes part in the alteration of ornithine to putrescine. ODC1 is a key member of various biological processes, such as cell growth, transformation, differentiation and apoptosis. Overexpression of the ODC1 gene has a vital part in cell proliferation and the progress of cancer.

    • Synonyms

      ODC, Ornithine decarboxylase 1, EC 4.1.1.17.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human ODC1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human ODC1 amino acids 1-461 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT9B3AT.

    • Applications

      ODC1 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      ODC1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Odc1 Antibody
  • View Data Sheet

    Name :

    Secretin Human

    Description:

    Secretin Human

    Product # :

    HOR-273

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    Description

    Secretin has a molecular formula of C130H220N44O41, a.a. sequence of H-His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg- Asp-Ser-Ala-Arg-Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 and having an Mw of 3055.4 Dalton.

    Formulation

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

    Purity

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

    More Info

    • Introduction

      Human Secretin stimulates the secretion of bicarbonate by the pancreas and inhibits the production of gastrin and acid production in the stomach. It also potentiates the release of digestive enzymes from the pancreas triggered by cholecystokinin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Secretin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secretin 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 Secretin in sterile 18MΩ-cm H2O not less than 100 µg/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.

    Secretin Human
  • View Data Sheet

    Name :

    SCRN1 Human

    Description:

    Secernin 1 Human Recombinant

    Secernin-1, SES1, KIAA0193, Secernin 1.

    Product # :

    PRO-2212

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    Description

    SCRN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414 a.a) and having a molecular mass of 48.8kDa. SCRN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SCRN1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) , 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Secernin 1 (SCRN1) which is a member of the peptidase C69 family, regulates exocytosis in mast cells. SCRN1 increases both the level of secretion and the sensitivity of mast cells to stimulation with calcium.

    • Synonyms

      Secernin-1, SES1, KIAA0193, Secernin 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

      GSSHHHHHH SSGLVPRGSH MGSMAAAPPS YCFVAFPPRA KDGLVVFGKN SARPRDEVQE VVYFSAADHE PESKVECTYI SIDQVPRTYA IMISRPAWLW GAEMGANEHG VCIANEAINT REPAAEIEAL LGMDLVRLGL ERGETAKEAL DVIVSLLEEH GQGGNYFEDA NSCHSFQSAY LIVDRDEAWV LETIGKYWAA EKVTEGVRCI CSQLSLTTKM DAEHPELRSY AQSQGWWTGE GEFNFSEVFS PVEDHLDCGA GKDSLEKQEE SITVQTMMNT LRDKASGVCI DSEFFLTTAS GVSVLPQNRS SPCIHYFTGT PDPSRSIFKP FIFVDDVKLV PKTQSPCFGD DDPAKKEPRF QEKPDRRHEL YKAHEWARAI IESDQEQGRK LRSTMLELEK QGLEAMEEIL TSSEPLDPAE VGDLFYDCVD TEIKFFK.

    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.

    Scrn1 Human
  • View Data Sheet

    Name :

    UMOD Feline

    Description:

    Uromodulin Feline

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

    Product # :

    ENZ-732

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    • More Info

    Description

    Feline Uromodulin is a 95kDa glycoprotein which is produced in the thick ascending limb of Henle´s loop and early distal convoluted tubules of the nephron.

    Source

    Feline Urine.

    Formulation

    The UMOD protein was lyophilized from 0.4µm filtered solution at a concentration of 0.5mg/ml containing deionized water.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      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.

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      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.

    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.

    Umod Feline
  • View Data Sheet

    Name :

    PCMT1 Human

    Description:

    Protein-L-Isoaspartate O-Methyltransferase Human Recombinant

    EC 2.1.1.77, PIMT, PCMT1, Protein-beta-aspartate methyltransferase, Protein L-isoaspartyl/D-aspartyl methyltransferase, L-isoaspartyl protein carboxyl methyltransferase.

    Product # :

    ENZ-522

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    • More Info

    Description

    PCMT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-227 a.a.) and having a molecular mass of 28.8 kDa. The PCMT1 is fused to a 36 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PCMT1 Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PCMT1 enzyme catalyses the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. PCMT1 is involved in the repair and/or degradation of damaged proteins.

    • Synonyms

      EC 2.1.1.77, PIMT, PCMT1, Protein-beta-aspartate methyltransferase, Protein L-isoaspartyl/D-aspartyl methyltransferase, L-isoaspartyl protein carboxyl methyltransferase.

    • 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

      RGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAWK SGGASHSELI HNLRKNGIIK TDKVFEVMLA TDRSHYAKCN PYMDSPQSIG FQATISAPHM HAYALELLFD QLHEGAKALD VGSGSGILTA CFARMVGCTG KVIGIDHIKE LVDDSINNVR KDDPTLLSSG RVQLVVGDGR MGYAEEAPYD AIHVGAAAPV VPQALIDQLK PGGRLILPVG PAGGNQMLEQ YDKLQDGSIK MKPLMGVIYV PLTDKEKQWS RWK.

    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.

    Pcmt1 Human
  • View Data Sheet

    Name :

    E Selectin Human

    Description:

    E-selectin Human Recombinant

    E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    Product # :

    PRO-380

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    • description
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    • More Info

    Description

    E-Selectin Human Recombinant is expressed in E. coli containing amino acids 179-557 fused to an amino terminal hexahistidine tag, having a total molecular weight of 45.22 kDa.

    Source

    Escherichia Coli.

    Formulation

    E-Selectin is supplied in 1x PBS and 50% Glycerol.

    Purity

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

    More Info

    • Introduction

      E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.

    • Synonyms

      E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    • Physical Appearance

      Sterile Filtered liquid formulation.

    • Stability

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

    E Selectin Human
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