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Search results

1000 results found for “transforming growth factor”

Name

Description

Product #

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  • View Data Sheet

    Name :

    IL3 Mouse, sf9

    Description:

    Interleukin-3 Mouse Recombinant, sf9

    Interleukin-3, Interleukin-3, sf9, IL3 sf9, L-3, Hematopoietic growth factor, Mast cell growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor, Il3, Csfmu, Il-3, BPA, Csfmu, HCGF, Il-3, MCGF, PSF.

    Product # :

    CYT-922

    Price :

    Quantity :

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

    Description

    IL3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 148 amino acids (27-166 a.a.) and having a molecular mass of 16.7kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).IL3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 is Measured in a cell proliferation assay using TF-1 human erythroleukemic and is ≤ 0.1 ng/ml.

    More Info

    • Introduction

      Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
      IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.

    • Synonyms

      Interleukin-3, Interleukin-3, sf9, IL3 sf9, L-3, Hematopoietic growth factor, Mast cell growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor, Il3, Csfmu, Il-3, BPA, Csfmu, HCGF, Il-3, MCGF, PSF.

    • 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

      ASISGRDTHR LTRTLNCSSI VKEIIGKLPE PELKTDDEGP SLRNKSFRRV NLSKFVESQG EVDPEDRYVI KSNLQKLNCC LPTSANDSAL PGVFIRDLDD FRKKLRFYMV HLNDLETVLT SRPPQPASGS VSPNRGTVEC LEHHHHHH.

    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.

    Il3 Mouse Sf9
  • View Data Sheet

    Name :

    Protein A/G

    Description:

    Protein A/G Recombinant

    Product # :

    PRO-646

    Price :

    Quantity :

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    • description
    • source
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    Description

    The recombinant Protein A/G consists of 5 IgG-binding regions of protein A and 2 of protein G, which corresponds to the Protein A and G domains that are included in the recombinant sequence. Cell wall binding region, cell membrane binding region and albumin binding region have been removed from the recombinant Protein A/G to ensure the maximum specific IgG binding. The Protein A portion is from Staphylococcus aureus segments E, D, A, B and C. The Protein G portion is from Streptococcus segments C1 and C3. The fusion protein has a predicted molecular mass of 47.7kDa and containing 429 amino acids.

    Source

    Escherichia coli.

    Formulation

    Lyophilized white Powder containing no additives.

    Purity

    >97% as determined by SDS-PAGE and RP-HPLC.

    More Info

    • Introduction

      Recombinant Protein A/G fusion protein joins IgG binding domains of both Protein A and Protein G.
      Protein A/G includes four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50.4 kDa. The binding dependency to pH of Protein A/G lower than Protein A, but has the additive properties of Protein A and G together. Protein A/G binds to all subclasses of human IgG, making it helpful for purifying polyclonal or monoclonal IgG antibodies whose subclasses have not been identifieed. Protein A/G binds to IgA, IgE, IgM and IgD. Protein A/G binds to all subclasses of mouse IgG excluding mouse IgA, IgM or serum albumin. This permits Protein A/G to be used in purification and detection of mouse monoclonal IgG antibodies, with no interference from IgA, IgM and serum albumin. Mouse monoclonal antibodies normally have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G. Protein A/G also has been used for purification of macaque IgG.

    • Stability

      After reconstitution, aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTE.

    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.

    Protein A G
  • View Data Sheet

    Name :

    C1QTNF5 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 5 Human Recombinant

    CTRP5, MFRP.

    Product # :

    PRO-2599

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    C1QTNF5 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (16-243.a.a) and having a molecular mass of 26.4kDa. C1QTNF5 Human is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C1QTNF5 protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.5) containing 30% glycerol and 0.2M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement C1q Tumor Necrosis Factor-Related Protein 5 (C1QTNF5) encodes a short-chain collagen which is expressed mainly in sub-retinal pigment epithelium, ciliary epithelium and adipose tissue. C1QTNF5 is increased in mtDNA-depleted myocytes and stimulates the phosphorylation of AMP activated protein kinase. C1QTNF5 takespart in the adhesion of the retinal pigment epithelium (RPE) to the Bruch Membrane. Mutations in C1QTNF5 have been associated with late-onset retinal degeneration.

    • Synonyms

      CTRP5, MFRP.

    • 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 MGSHMSPPLD DNKIPSLCPG HPGLPGTPGH HGSQGLPGRD
      GRDGRDGAPG APGEKGEGGR PGLPGPRGDP GPRGEAGPAG PTGPAGECSV PPRSAFSAKR
      SESRVPPPSD APLPFDRVLV NEQGHYDAVT GKFTCQVPGV YYFAVHATVY RASLQFDLVK
      NGESIASFFQ FFGGWPKPAS LSGGAMVRLE PEDQVWVQVG VGDYIGIYAS IKTDSTFSGF LVYSDWHSSP VFA.

    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.

    C1Qtnf5 Human
  • View Data Sheet

    Name :

    SDF2 Human, sf9

    Description:

    Stromal Cell-Derived Factor 2, Sf9 Human Recombinant

    Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-2 

    Product # :

    CHM-034

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    SDF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 202 amino acids (19-211a.a.) and having a molecular mass of 22.3kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SDF2 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SDF2 protein solution (0.25mg/ml) contains 50mM Tris-HCl (pH 8.0), 10% glycerol, 0.1M NaCl 0.1mM PMSF and 0.5mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stromal Cell-Derived Factor 2 (SDF2) is a secretory protein which is partly similar to the hydrophilic segments of yeast mannosyltransferases. SDF2 protein’s expression is ubiquitous and the gene is rather conserved among mammals. SDF2 is a protein-coding gene whose alternative splicing results in coding and non-coding variants.

    • Synonyms

      Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-2

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAELHHHH HH

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

    Sdf 2 Human
  • View Data Sheet

    Name :

    EIF3I Human, Sf9

    Description:

    Eukaryotic Translation Initiation Factor 3I Human Recombinant, Sf9

    eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiationfactor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta.

    Product # :

    PRO-2611

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    EIF3I Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (1-325 a.a) and having a molecular mass of 37.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).EIF3I is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EIF3I protein solution (0.25mg/ml) 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% Glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic translation initiation factor 3, subunit I (EIF3I) is part of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is essential for numerous steps in the initiation of protein synthesis. The eIF-3 complex links with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2: GTP: methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also essential for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3I are clonorchiasis, and tonsillitis.

    • Synonyms

      eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiation
      factor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta.

    • 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

      MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA
      DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC
      FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV
      LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN
      YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY SSGGEDGYVR IHYFDPQYFE FEFEAHHHHH H.

    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.

    Eif3I Protein
  • View Data Sheet

    Name :

    TNFRSF14 Human, His

    Description:

    HVEM Human Recombinant, His Tag

    Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

    Product # :

    CYT-800

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    Description

    TNFRSF14 Human Recombinant produced in E. Coli is a single, glycosylated polypeptide chain containing 187 amino acids (39-202) and having a molecular mass of 19.7kDa.TNFRSF14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TNFRSF14 solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

    • 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 MGSLPSCKED EYPVGSECCP KCSPGYRVKE ACGELTGTVC EPCPPGTYIA HLNGLSKCLQ CQMCDPAMGL RASRNCSRTE NAVCGCSPGH FCIVQDGDHC AACRAYATSS PGQRVQKGGT ESQDTLCQNC PPGTFSPNGT LEECQHQTKC SWLVTKAGAG TSSSHWV.

    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.

    Tnfrsf14 Human His
  • View Data Sheet

    Name :

    TEK Human Fc

    Description:

    TEK Tyrosine Kinase Endothelial Fc Chimera Human Recombinant

    Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.

    Product # :

    PKA-248

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    Description

    Soluble TEK Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a monomeric, glycosylated, polypeptide containing 730 amino acids and having a total molecular mass of 250 kDa. Human TIE-2/Fc monomer has a calculated molecular mass of approximately 125 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 140 kDa protein in SDS-PAGE under reducing conditions.The TEK Fc Chimera is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    TEK Fc Chimera was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.

    • Synonyms

      Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized sTIE-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TEK 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 TIE-2 Fc Chimera in sterile water 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.

    Tie 2 Human Fc
  • View Data Sheet

    Name :

    BMF Human

    Description:

    Bcl2 Modifying Factor, Isoform 3 Human Recombinant

    Bcl-2-modifying factor, FLJ00065, BMF.

    Product # :

    PRO-700

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    Description

    Bcl2 modifying factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids (1-129 a.a.) and having a molecular mass of 15.6 kDa.The Bcl2 modifying factor is fused to 15 amino acid His Tag at Nterminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Bcl2 modifying factor solution contains 20mM Tris pH-7.5, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Bcl2 modifying factor, is a member of the Bcl2 protein family of apoptosis mediators. Bcl2 modifying factor is widely expressed in many tissues.
      Bcl2 modifying factor contains a single Bcl2 homology domain 3 (BH3), and binds Bcl2 proteins and functions as an apoptotic activator. Also, Bcl2 modifying factor is important for histone deacetylase (HDAC) inhibitors which alters the balance between acetylation and deacetylation, significantly increasing histone acetylation, while strongly inducing apoptosis in a variety of cancer cell types. Bcl2 modifying factor supports Bim in regulating cell death processes in response to many stimuli. A synergistic role for bim and Bcl2 modifying factor in an apoptotic pathway leading to the clearance of Neisseria gonorrhoeae -infected cells.

    • Synonyms

      Bcl-2-modifying factor, FLJ00065, BMF.

    • 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

      MASMTGGQQM GRGSHMEPSQ CVEELEDDVF QPEDGEPVTQ PGSLLSADLF AQSLLDCPLS RLQLFPLTHC CGPGLRPTSQ EDKATQTLSPASPSQGVMLP CGVTEEPQRL FYAPAEPKSC VVADPPLPAQ PCFEWRREQE RGRP.

    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.

    Bcl2 Modifying Factor Human
  • View Data Sheet

    Name :

    Leptin Bovine

    Description:

    Leptin Bovine Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-502

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    • source
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    Description

    Leptin Bovine 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) Gel filtration analysis.
    (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 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 0.2 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 Bovine
  • View Data Sheet

    Name :

    PIP Human

    Description:

    Prolactin-Induced Protein Human

    Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, PIP, GCDFP15, GPIP4.

    Product # :

    CYT-779

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    Description

    The Prolactin-Induced Protein produced from Human Seminal Plasma has a molecular mass of 13.52kDa (calculated without glycosylation) containing 118 amino acid residues.

    Source

    Human Seminal Plasma.

    Formulation

    PIP protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prolactin inducible protein (PIP) is a 17kDa glycoprotein existing in human seminal plasma. PIP is synthesized as a 146 amino acid long polypeptide exhibiting high sequence similarity with mouse submaxillary gland with a single glycosylation site. The precise biological functions of PIP are still ambiguous but various functions have been assigned to PIP due its existence at high concentration in biological fluids. PIP binds to various proteins such as fibrinogen, actin, keratin, myosin and tropomyosin. PIP is also expressed in pathological conditions of the mammary gland and in some exocrine tissues, such as the lacrimal, salivary and sweat glands. Due to PIP’s association with secretory cell differentiation, it has been used in diagnostic evaluation of tumors of breast, salivary gland, and skin.

    • Synonyms

      Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, PIP, GCDFP15, GPIP4.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      QDNTRKIIIK NFDIPKSVRP NDEVTAVLAV QTELKECMVV KTYLISSIPL QGAFNYKYTA CLCDDNPKTF YWDFYTNRTV QIAAVVDVIR ELGICPDDAA VIPIKNNRFY TIEILKVE.

    • Human Virus Test

      Samples from each donor have been tested and found negative for HBsAg, HIV1+2, HCV, syphilis, aHBc, RRR.

    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.

    Pip Human
  • View Data Sheet

    Name :

    Leptin qA Rat, PEG

    Description:

    Leptin Quadruple Antagonist, Pegylated Rat Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1241

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    Description

    Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Rat Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.

    More Info

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Rat Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    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 Rat Peg Qa
  • View Data Sheet

    Name :

    SPP1 Human, HEK

    Description:

    Osteopontin Human Recombinant, HEK

    Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    Product # :

    CYT-047

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    Description

    Osteopontin Human Recombinant is a single, glycosylated, polypeptide chain produced in HEK293 cells, is a full length protein (amino acids 17-314) fused with a polyhistidine tag at the C-terminus, having a total calculated molecular mass of 34.5kDa (The actual molecular mass may be approximately 60-65kDa in SDS-PAGE under reducing conditions due to glycosylation).Osteopontin is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
      Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

    • Synonyms

      Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized SPP1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETL
      PSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDEL
      VTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDIT
      SHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRK
      ANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDS
      ASSEVNVDHHHHHH.

    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.

    Spp1 Human Hek
  • View Data Sheet

    Name :

    F8 Human

    Description:

    Coagulation Factor-VIII Human

    Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.

    Product # :

    PRO-317

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    • More Info

    Description

    Human Factor VIII produced from Human Plasma contains 2332 amino acids and having a molecular mass of 330kDa. Factor-VIII is effective in the correction and prevention of severe bleeding episodes attributed to Factor VIII deficiency. The Factor-VIII is purified by proprietary chromatographic techniques.

    Source

    Human Plasma.

    Formulation

    The lyophilized protein 200IU/ml was lyophilized from a sterile solution containing 1.5% Glycine, 160mM Calcium chloride and 25mM NaCitrate and 25mM NaCl.

    Biological Activity

    The potency was found to be 10 Units/mg.

    More Info

    • Introduction

      Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.

    • Synonyms

      Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Factor-VIII although stable at room temperature for 1 week, should be stored desiccated between 2-8°C. Upon reconstitution Factor-VIII should be stored at 4°C.

    • Solubility

      It is recommended to reconstitute the lyophilized Factor-VIII in sterile 18MΩ-cm H2O at a concentration of 200IU/ml, which can then be further diluted to other aqueous solutions.

      Make sure that the vial has reached room temperature prior to its reconstitution, otherwise it might precipitate.

    • Human Virus Test

      The plasma is collected from donors with Hepatitis B vaccinated. Each unit of plasma has been tested for HBsAg, Anti-HIV-1/2 plus O and Anti-HCV by using the imported kits which are approved by Federal Drug Administration (FDA).

    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.

    Factor Viii
  • View Data Sheet

    Name :

    TNFRSF6B Human

    Description:

    Tumor Necrosis Factor Receptor Superfamily, Member 6b Human Recombinant

    Tumor Necrosis Factor Receptor Superfamily, Member 6b Decoy, Decoy Receptor For Fas Ligand, Decoy Receptor 3, DCR3, M68E, M68, TR6, DJ583P15.1.1, DcR3.

    Product # :

    CYT-799

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    • More Info

    Description

    TNFRSF6B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (30-300aa) and having a molecular mass of 32.1kDa.TNFRSF6B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFRSF6B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF6B is a member of the Tumor necrosis factor receptor superfamily. TNFRSF6B performs as a decoy receptor which races against death receptors for ligand binding. TNFRSF6B has a regulatory role in suppressing FasL- and LIGHT-mediated cell death and T cell activation in addition to inducing angiogenesis via neutralization of TL1A.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily, Member 6b Decoy, Decoy Receptor For Fas Ligand, Decoy Receptor 3, DCR3, M68E, M68, TR6, DJ583P15.1.1, DcR3.

    • 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 MGSVAETPTY PWRDAETGER LVCAQCPPGT FVQRPCRRDS PTTCGPCPPR HYTQFWNYLE RCRYCNVLCG EREEEARACH ATHNRACRCR TGFFAHAGFC LEHASCPPGA GVIAPGTPSQ NTQCQPCPPG TFSASSSSSE QCQPHRNCTA LGLALNVPGS SSHDTLCTSC TGFPLSTRVP GAEECERAVI DFVAFQDISI KRLQRLLQAL EAPEGWGPTP RAGRAALQLK LRRRLTELLG AQDGALLVRL LQALRVARMP GLERSVRERF LPVH.

    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.

    Tnfrsf6B Human
  • View Data Sheet

    Name :

    IL 3 Human, His

    Description:

    Interleukin-3 Human Recombinant, His Tag

    MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    Product # :

    CYT-482

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    Description

    Interleukin-3 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 154 amino acids fragment (20-152) and having a total molecular mass of 17.3kDa and fused with a 20 aa N-terminal His tag. The IL3 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-3 His (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH 8.0), 0.2mM PMSF and 10% glycerol.

    Purity

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

    Biological Activity

    The ED50 for this effect is <0.53ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.

    More Info

    • Introduction

      Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells. IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.

    • Synonyms

      MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    • 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 MAPMTQTTSL KTSWVNCSNM IDEIITHLKQ PPLPLLDFNN LNGEDQDILM ENNLRRPNLE AFNRAVKSLQ NASAIESILK NLLPCLPLAT AAPTRHPIHI KDGDWNEFRR KLTFYLKTLE NAQAQQTTLS LAIF.

    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.

    Il 3 Human His
  • View Data Sheet

    Name :

    SF20 Human

    Description:

    MYDGF Human Recombinant

    C19orf10, Interleukin-25, IL-25, IL25, IL27, IL-27, IL27w, IL-27w, Stromal cell-derived growth factor SF20, UPF0556 protein C19orf10, chromosome 19 open reading frame 10.

    Product # :

    CYT-622

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    • sds-page

    Description

    SF20 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 162 amino acids fragment (33-173) and having a total molecular mass of 18 kDa. C9orf10 is fused to 20 amino acids His tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    C9orf10 is supplied in 20mM Tris HCL pH-8 and 20% glycerol.

    Purity

    Greater than 95.0% by SDS-PAGE.

    sds-page

    SF20 Human SDS-PAGE - Product image 1

    More Info

    • Introduction

      SF20 plays a role in proliferation of lymphoid cells and is considered an interleukin. SF20 was initially identified as a product of bone marrow-derived stromal cells.

    • Synonyms

      C19orf10, Interleukin-25, IL-25, IL25, IL27, IL-27, IL27w, IL-27w, Stromal cell-derived growth factor SF20, UPF0556 protein C19orf10, chromosome 19 open reading frame 10.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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

    Sf20 Human
  • View Data Sheet

    Name :

    HIF1A Human (85 a.a.)

    Description:

    Hypoxia-Inducible Factor-1 Alpha (85 a.a.) Human Recombinant

    Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

    Product # :

    PRO-258

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    Description

    HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-85 a.a.) and having a molecular mass of 11.8 kDa. The HIF1A is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HIF1A Human (0.25mg/ml) solution containing 20mM Tris buffer(pH 8.0), 20% glycerol, 1mM DTT, 0.2M NaCl and 1mM EDTA.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.

    • Synonyms

      Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

    • 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 MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM RLTISYLRVR KLLDAGDLDI EDDMK.

    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.

    Hif1A Human 85 Aa
  • View Data Sheet

    Name :

    CNTF Rat, His

    Description:

    Ciliary Neurotrophic Factor Rat Recombinant, His Tag

    Ciliary neurotrophic factor, CNTF, Cntf.

    Product # :

    CYT-926

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    Description

    CNTF Rat Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-200a.a) and having a molecular mass of 25.2kDa.CNTF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNTF protein solution (0.5mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      Ciliary neurotrophic factor, CNTF, Cntf.

    • 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 MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.

    • Background

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 25.2kDa.

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

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

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

      What is the amino acid sequence of CNTF Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMAFAEQT PLTLHRRDLC SRSIWLARKI RSDLTALMES YVKHQGLNKN INLDSVDGVP VASTDRWSEM TEAERLQENL QAYRTFQGML TKLLEDQRVH FTPTEGDFHQ AIHTLMLQVS AFAYQLEELM VLLEQKIPEN EADGMPATVG DGGLFEKKLW GLKVLQELSQ WTVRSIHDLR VISSHQMGIS ALESHYGAKD KQM.
      What applications can CNTF Protein be used in?
      CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Cntf Rat His
  • View Data Sheet

    Name :

    NUTF2 Human

    Description:

    Nuclear Transport Factor 2 Human Recombinant

    Nuclear transport factor 2, NTF-2, Placental protein 15, PP15, NUTF2, NTF2.

    Product # :

    PRO-844

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    Description

    NUTF2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids (1-127 a.a.) and having a molecular mass of 16.6 kDa. The NUTF2 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUTF2 Human solution containing 20mM Tris HCL pH-8, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NUTF2 assists in protein transport into the nucleus and interacts with the nucleoporin p62 and with Ran. NUTF2 plays a role at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. NUTF2 is part of a multicomponent system of cytosolic factors that come together at the pore complex during nuclear import.

    • Synonyms

      Nuclear transport factor 2, NTF-2, Placental protein 15, PP15, NUTF2, NTF2.

    • 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 MGDKPIWEQI GSSFIQHYYQ LFDNDRTQLG AIYIDASCLT WEGQQFQGKA AIVEKLSSLP FQKIQHSITA QDHQPTPDSC IISMVVGQLK ADEDPIMGFH QMFLLKNIND AWVCTNDMFR LALHNFG.

    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.

    Nutf2 Human
  • View Data Sheet

    Name :

    TSTD1 Human

    Description:

    Thiosulfate Sulfurtransferase Like Domain Containing 1 Human Recombinant

    Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 1, TSTD1, KAT.

    Product # :

    ENZ-094

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    Description

    TSTD1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids (1-115 a.a.) and having a molecular mass of 14.6kDa.TSTD1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TSTD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thiosulfate sulfurtransferase like domain containing 1 (TSTD1) is a member of a family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. TSTD1 is localized around the nuclear membranes. TSTD1 is expressed in a number of human tissues, including the kidney, liver, skeletal muscle, heart, colon, thymus, spleen, placenta and lung. TSTD1 may participate in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes.

    • Synonyms

      Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 1, TSTD1, KAT.

    • 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 MAGAPTVSLP ELRSLLASGR ARLFDVRSRE EAAAGTIPGA LNIPVSELES ALQMEPAAFQ ALYSAEKPKL EDEHLVFFCQ MGKRGLQATQ LARSLGYTGA RNYAGAYREW LEKES.

    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.

    Tstd1 Human
  • View Data Sheet

    Name :

    CNTF Mouse

    Description:

    Ciliary-Neurotrophic Factor Mouse Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-139

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    • More Info

    Description

    Ciliary Neurotrophic Factor Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.6kDa. The CNTF 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:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of TF-1 cells is less than 35ng/ml, corresponding to a Specific Activity of 3.0×104 IU/mg.

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      HCNTF, CNTF, Ciliary Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAFAEQSPLT LHRRDLCSRS IWLARKIRSD LTALMESYVK HQGLNKNISL DSVDGVPVAS TDRWSEMTEA ERLQENLQAY RTFQGMLTKL LEDQRVHFTP TEGDFHQAIH TLTLQVSAFA YQLEELMALL EQKVPEKEAD GMPVTIGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRVIS SHHMGISAHE SHYGAKQM

    • Background

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 22.6kDa.

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

      What is the Purity of CNTF Protein?
      CNTF Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CNTF Protein?
      Fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of TF-1 cells is less than 35ng/ml, corresponding to a Specific Activity of 3.0×104 IU/mg.

      What is the amino acid sequence of CNTF Protein?
      MAFAEQSPLT LHRRDLCSRS IWLARKIRSD LTALMESYVK HQGLNKNISL DSVDGVPVAS TDRWSEMTEA ERLQENLQAY RTFQGMLTKL LEDQRVHFTP TEGDFHQAIH TLTLQVSAFA YQLEELMALL EQKVPEKEAD GMPVTIGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRVIS SHHMGISAHE SHYGAKQM

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

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

    Cntf Mouse
  • View Data Sheet

    Name :

    TIAF1 Human

    Description:

    TGFB1-Induced Anti-Apoptotic Factor 1 Human Recombinant

    TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.

    Product # :

    PRO-1211

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    Description

    TIAF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 152 amino acids (1-115) and having a molecular mass of 16.6 kDa.TIAF1 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TIAF1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TGFB1-induced anti-apoptotic factor 1 (TIAF1) hinders the cytotoxic effects of TNF-alpha and overexpressed TNF receptor adapters TRADD, FADD, and RIPK1. The TIAF1 protein is involved in TGF-beta1 inhibition of IkappaB-alpha expression and suppression of TNF-mediated IkappaB-alpha degradation. TIAF1 is not detected in normal kidney and liver. TIAF1 is up-regulated in chronic and acute allograft rejection: expressed in the inflammatory infiltrate and in tubular epithelial cells.

    • Synonyms

      TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSS PSSPFREQSF LCAAGDAGEE SRVQVLKNEV RRGSPVLLGW VEQAYADKCV CGPSAPPAPT PPSLSQRVMC NDLFKVNPFQ LQQFRADPST ASLLLCPGGL DHKLNLRGKA WG

    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.

    Tiaf1 Human
  • View Data Sheet

    Name :

    LGALS10 Human

    Description:

    Charcot-Leyden Crystal Protein Human Recombinant

    Eosinophil lysophospholipase, Charcot-Leyden crystal protein, CLC, Galectin-10, Gal-10, Lysolecithin acylhydrolase, GAL10, LGALS10, LGALS10A.

    Product # :

    PRO-744

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    Description

    LGALS10 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 18.6kDa.LGALS10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eosinophil lysophospholipase (CLC) acts on biological membranes to regulate the multifunctional lysophospholipids. CLC is a lysophospholipase expressed in eosinophils and basophils. CLC hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. The CLC protein may possess carbohydrate or IgE-binding activities. CLC is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. CLC may be linked with inflammation and some myeloid leukemias.

    • Synonyms

      Eosinophil lysophospholipase, Charcot-Leyden crystal protein, CLC, Galectin-10, Gal-10, Lysolecithin acylhydrolase, GAL10, LGALS10, LGALS10A.

    • 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 MSLLPVPYTE AASLSTGSTV TIKGRPLACF LNEPYLQVDF HTEMKEESDI VFHFQVCFGR RVVMNSREYG AWKQQVESKN MPFQDGQEFE LSISVLPDKY QVMVNGQSSY TFDHRIKPEA VKMVQVWRDI SLTKFNVSYL KR.

    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.

    Lgals10 Human
  • View Data Sheet

    Name :

    RANGRF Human

    Description:

    RAN Guanine Nucleotide Release Factor Human Recombinant

    Ran guanine nucleotide release factor, RanGNRF, Ran-binding protein MOG1, RANGRF, MOG1, HSPC165, HSPC236, MDS5.

    Product # :

    PRO-1149

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    Description

    RANGRF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-186 a.a) and having a molecular mass of 23kDa.RANGRF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RANGRF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RANGRF is a protein which acts as a guanine nucleotide release factor in mouse and regulates the expression and function of the Nav1.5 cardiac sodium channel in human. RANGRF also controls the intracellular trafficking of RAN. In cardiac cells, the RANGRF appears to regulate the cell surface localization of SCN5A.

    • Synonyms

      Ran guanine nucleotide release factor, RanGNRF, Ran-binding protein MOG1, RANGRF, MOG1, HSPC165, HSPC236, MDS5.

    • 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 MGSHMEPTRD CPLFGGAFSA ILPMGAIDVS DLRPVPDNQE VFCHPVTDQS LIVELLELQA HVRGEAAARY HFEDVGGVQG ARAVHVESVQ PLSLENLALR GRCQEAWVLS GKQQIAKENQ QVAKDVTLHQ ALLRLPQYQT DLLLTFNQPP PDNRSSLGPE NLSPAPWSLG DFEQLVTSLT LHDPNIFGPQ.

    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.

    Rangrf Human
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