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Search results

1000 results found for “natural coagulation factors”

Name

Description

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  • View Data Sheet

    Name :

    MOG

    Description:

    Myelin Oligodendrocyte Glycoprotein

    Myelin Oligodendrocyte Glycoprotein, MOG.

    Product # :

    PRO-371

    Price :

    Quantity :

    Shipping Method :

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    • formulation
    • purity
    • More Info

    Description

    Myelin Oligodendrocyte Glycoprotein is a single, non-glycosylated polypeptide chain containing 21 amino acids and having a molecular mass of 2581 Dalton, the molecular formula: C118H177N35O29S.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      MOG is a transmembrane protein expressed on the surface of oligodendrocyte cell and on the outermost surface of myelin sheaths. MOG comprises about 0.1% of total CNS myelin protein. The MOG gene is a member of the immunoglobulin gene superfamily and is found within the MHC. The MOG gene is found on chromosome 6p21.3-p22. Myelin Oligodendrocyte Glycoprotein is a glycoprotein thought to be significant in the process of myelinization of nerves in the central nervous system (CNS). MOG peptide (35-55) is highly encephalitogenic and can induce strong T and B cell responses. A single injection of this peptide produces a relapsing- remitting neurologic disease with extensive plaque-like demyelination. Because of the clinical, histophathologic, and immunologic similarities with multiple sclerosis (MS), the MOG induced demyelinating encephalomyelitis may serve as a model for investigating MS.

    • Synonyms

      Myelin Oligodendrocyte Glycoprotein, MOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-Met-Glu-Val-Gly-Trp-Tyr-Arg-Ser-Pro-Phe-Ser-Arg-Val-Val-His-Leu-Tyr-Arg-Asn-Gly-Lys-OH.

    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.

    Mog
  • View Data Sheet

    Name :

    TNF B Human, Sf9

    Description:

    Tumor Necrosis Factor-beta Human Recombinant, Sf9

    Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

    Product # :

    CYT-989

    Price :

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    • More Info

    Description

    Tumor Necrosis Factor-beta Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 180 amino acids (35-205a.a.) and having a molecular mass of 19.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).TNFB is fused with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFB protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cytotoxicity assay using L-929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is ≤ 1ng/ml.

    More Info

    • Introduction

      Lymphotoxin alpha, a member of the tumor necrosis factor family, is a cytokine produced by lymphocytes. LTA is highly inducible, secreted, and exists as homotrimeric molecule. LTA forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. LTA is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis.

    • Synonyms

      Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

    • 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

      ADPLPGVGLT PSAAQTARQH PKMHLAHSTL KPAAHLIGDP SKQNSLLWRA NTDRAFLQDG FSLSNNSLLV PTSGIYFVYS QVVFSGKAYS PKATSSPLYL AHEVQLFSSQ YPFHVPLLSS QKMVYPGLQE PWLHSMYHGA AFQLTQGDQL STHTDGIPHL VLSPSTVFFG AFALHHHHHH.

    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.

    Tnfb Human Sf9
  • View Data Sheet

    Name :

    FGF4 Human

    Description:

    Fibroblast Growth Factor-4 Human Recombinant

    HBGF4, FGF-4, FGF4, KFGF, HSTF1.

    Product # :

    CYT-312

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    Description

    FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa. The FGF4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF4 protein was lyophilized with 20mM sodium phosphate and 500mM NaCl pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.

    More Info

    • Introduction

      FGF4 holds s comprehensive mitogenic and cell survival activities and takes part in a range of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF4 possess oncogenic transforming activity. FGF4 and FGF3, oncogenic growth factors are localized on chromosome 11. Co-amplification of both factors was found in several kinds of human tumors. FGF4 functions in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway.

    • Synonyms

      HBGF4, FGF-4, FGF4, KFGF, HSTF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-4 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 FGF4 Human Recombinant sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.

    • Background

      What is the molecular weight/Mw of FGF4 HUMAN Protein?
      FGF4 HUMAN Protein has a total Mw of 19.8kDa.

      What is the source or expression system of FGF4 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FGF4 HUMAN Protein?
      FGF4 HUMAN Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF4 HUMAN Protein?
      The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.

      What is the amino acid sequence of FGF4 HUMAN Protein?
      MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.

      What applications can FGF4 HUMAN Protein be used in?
      FGF4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF4 HUMAN Protein?
      The endotoxin level is minimal, FGF4 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.

    Fgf4 Human
  • View Data Sheet

    Name :

    EIF3K (50-94) Human

    Description:

    Eukaryotic Translation Initiation Factor 3K (50-94 a.a.) Human Recombinant

    PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.

    Product # :

    PRO-2833

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    The EIF3KHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The EIF3KHis-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 45 amino acid residues of the EIF3KHuman, 50-94 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized EIF3Kat -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Background

      Eukaryotic Translation Initiation Factor 3K (EIF3K) is a part of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a few other subunits of the 40S ribosomal subunit and eIF3. EIF3K is found both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4. EIF3K is conserved among high eukaryotes, including mammals, plants and insects and is expressed in human tissues.

    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.

    Eif3K Protein
  • View Data Sheet

    Name :

    KLF4 Human

    Description:

    Kruppel-Like Factor 4 Human Recombinant

    Kruppel-like factor 4 (gut), EZF, GKLF, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor, endothelial Kruppel-like zinc finger protein.

    Product # :

    PRO-891

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    KLF4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 545 amino acids (11-395) and having a molecular mass of 58.1 kDa.The KLF4 is fused to a 159 amino acid His-CaM Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The KLF4 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      KLF4 is a transcription factor that performs as both an activator and repressor. KLF4 is expressed mainly in erythroid tissues and found mostly in gut. KLF4 is takes part in the differentiation of epithelial cells in addition to skeletal and kidney development.

    • Synonyms

      Kruppel-like factor 4 (gut), EZF, GKLF, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor, endothelial Kruppel-like zinc finger protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MAHHHHHHMA DQLTEEQIAE FKEAFSLFDK DGDGTITTKE LGTVMRSLGQ NPTEAELQDM INEVDADGNG TIDFPEFLTM MARKMKDTDS EEEIREAFRV FDKDGNGYIS AAELRHVMTN LGEKLTDEEV DEMIREADID GDGQVNYEEF VQMMTAKGSM AVSDALLPSF STFASGPAGR EKTLRQAGAP NNRWREELSH MKRLPPVLPG RPYDLAAATV ATDLESGGAG AACGGSNLAP LPRRETEEFN DLLDLDFILS NSLTHPPESV AATVSSSASA SSSSSPSSSG PASAPSTCSF TYPIRAGNDP GVAPGGTGGG LLYGRESAPP PTAPFNLADI NDVSPSGGFV AELLRPELDP VYIPPQQPQP PGGGLMGKFV LKASLSAPGS EYGSPSVISV SKGSPDGSHP VVVAPYNGGP PRTCPKIKQE AVSSCTHLGA GPPLSNGHRP AAHDFPLGRQ LPSRTTPTLG LEEVLSSRDC HPALPLPPGF HPHPGPNYPS FLPDQMQPQV PPLHYQELMP PGSCMPEEPK PKRGRRSWPR KRTAT

    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.

    Klf4 Human
  • View Data Sheet

    Name :

    EIF1AX Human

    Description:

    Eukaryotic Translation Initiation Factor 1 X-linked Human Recombinant

    eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.

    Product # :

    PRO-253

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    Description

    EIF1AX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-144a.a.) and having a molecular wieght of 18.6kDa. EIF1AX is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF1AX protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 5mM DTT, 200mM NaCl and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF1AX is an important eukaryotic translation initiation factor. EIF1AX is essential for the binding of the 43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5'' end of capped RNA. EIF1AP1 is needed for maximal rate of protein biosynthesis. EIF1AX increases ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA (I) to 40 S ribosomal subunits.

    • Synonyms

      eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.

    • 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 MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT FGPGDDDEIQ FDDIGDDDED IDDI

    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.

    Eif1Ax Human
  • View Data Sheet

    Name :

    MSR1 Human, sf9

    Description:

    Macrophage Scavenger Receptor 1, sf9 Human Recombinant

    Macrophage Scavenger Receptor 1, Macrophage Acetylated LDL Receptor I And II, Scavenger Receptor Class A Member 1, SCARA1, Macrophage Scavenger Receptor Type III, CD204 Antigen, CD204, PhSR1, PhSR2, SR-A, SRA.

    Product # :

    PRO-2318

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    Description

    MSR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 384 amino acids (77-451 a.a.) and having a molecular mass of 42.4kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). MSR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MSR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Macrophage Scavenger Receptor 1, also known as MSR1 is a member of the class A macrophage scavenger receptors, which comprises three different types 1, 2 and 3 generated by alternative splicing. Furthermore, these receptors or isoforms are macrophage-specific trimeric integral membrane glycoproteins and have been implicated in many macrophage-associated physiological as well as pathological processes which include atherosclerosis, Alzheimer's disease, and host defense.

    • Synonyms

      Macrophage Scavenger Receptor 1, Macrophage Acetylated LDL Receptor I And II, Scavenger Receptor Class A Member 1, SCARA1, Macrophage Scavenger Receptor Type III, CD204 Antigen, CD204, PhSR1, PhSR2, SR-A, SRA.

    • 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

      ADPKWETKNC SVSSTNANDI TQSLTGKGND SEEEMRFQEV FMEHMSNMEK RIQHILDMEA NLMDTEHFQN FSMTTDQRFN DILLQLSTLF SSVQGHGNAI DEISKSLISL NTTLLDLQLN IENLNGKIQE NTFKQQEEIS KLEERVYNVS AEIMAMKEEQ VHLEQEIKGE VKVLNNITND LRLKDWEHSQ TLRNITLIQG PPGPPGEKGD RGPTGESGPR GFPGPIGPPG LKGDRGAIGF PGSRGLPGYA GRPGNSGPKG QKGEKGSGNT LTPFTKVRLV GGSGPHEGRV EILHSGQWGT ICDDRWEVRV GQVVCRSLGY PGVQAVHKAA HFGQGTGPIW LNEVFCFGRE SSIEECKIRQ WGTRACSHSE DAGVTCTLHH HHHH.

    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.

    Msr1 Human Sf9
  • View Data Sheet

    Name :

    VEGF Rat, His

    Description:

    Vascular Endothelial Growth Factor Rat Recombinant, His Tag

    VEGF-A, Vascular permeability factor, VPF, VEGF.

    Product # :

    CYT-854

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    Description

    VEGF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (206-325 a.a) and having a molecular mass of 16.7kDa.VEGF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    VEGF protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      VEGF-A, Vascular permeability factor, VPF, VEGF.

    • 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 MGSHMAPTTE GEQKAHEVVK FMDVYQRSYC RPIETLVDIF QEYPDEIEYI FKPSCVPLMR CAGCCNDEAL ECVPTSESNV TMQIMRIKPH QSQHIGEMSF LQHSRCECRP KKDRTKPEKC DKPRR

    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.

    Vegf Rat His
  • View Data Sheet

    Name :

    NAA10 Human

    Description:

    N Alpha-Acetyltransferase 10, NatA Catalytic Subunit Human Recombinant

    N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.

    Product # :

    ENZ-158

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    Description

    NAA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (1-235 a.a.) and having a molecular mass of 28.6kDa (the molecular weight on SDS-PAGE will appear higher).NAA10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAA10 is a member of the acetyltransferase family. NAA10 interacts with NAA15, HIF-1 and with the ribosome. In its binding to HIF-1, NAA10 functions as a protein acetyltransferase by regulating its stability. In various cell lines, NAA10 is downregulated in response to hypoxia. NAA10 is expressed during the course of the development of the brain.

    • Synonyms

      N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.

    • 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 MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS.

    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.

    Naa10 Human
  • View Data Sheet

    Name :

    Fibronectin Recombinant, Oryza

    Description:

    Fibronectin, Oryza Human Recombinant

    Product # :

    PRO-2841

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    Description

    Fibronectin Human Recombinant is a single, non-glycosylated polypeptide chain having a molecular mass of 216kDa. The Fibronectin is purified by proprietary chromatographic techniques.

    Source

    Oryza sativa (rice).

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism mainly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.

    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.

    Fibronectin Human Protein
  • View Data Sheet

    Name :

    ARF5 Human

    Description:

    ADP-Ribosylation Factor 5 Human Recombinant

    ADP-ribosylation factor 5, ARF5.

    Product # :

    PRO-245

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    Description

    ARF5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (1-180 a.a) and having a molecular mass of 22.6kDa.ARF5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARF5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-ribosylation factor 5 (ARF5) is a small guanine nucleotide-binding protein which enhances the enzymatic activities of cholera toxin. ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the connection of actin to the golgi via rho family-dependent G-protein localization and WASP/Arp2/3 complexes. ARF5 is involved in vesicular transport and functioning via phospholipase D activation.

    • Synonyms

      ADP-ribosylation factor 5, ARF5.

    • 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 MGLTVSALFS RIFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV QESADELQKM LQEDELRDAV LLVFANKQDM PNAMPVSELT DKLGLQHLRS RTWYVQATCA
      TQGTGLYDGL DWLSHELSKR.

    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.

    Arf5 Human
  • View Data Sheet

    Name :

    Cor a 1.0103

    Description:

    Major pollen allergen Cor a 1 Recombinant

    Major pollen allergen Cor a 1 isoforms 5, 6, 11 and 16, Allergen Cor a I, Cor a 1, Cor a 1.0103.

    Product # :

    PRO-2285

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    Description

    Recombinant Major pollen allergen Cor a 1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 17,470 Dalton. Cor a 1.0103 purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Cor a 1.0103 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Major pollen allergen Cor a 1 (Cor a 1.0103) causes an allergic reaction in human. The Cor a 1 isoforms exhibit different antigenic and allergenic properties.

    • Synonyms

      Major pollen allergen Cor a 1 isoforms 5, 6, 11 and 16, Allergen Cor a I, Cor a 1, Cor a 1.0103.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Cor A 10103
  • View Data Sheet

    Name :

    TCEA2 Human

    Description:

    Transcription Elongation Factor A (SII)-2 Human Recombinant

    Transcription elongation factor A protein 2, Testis-specific S-II, Transcription elongation factor S-II protein 2, Transcription elongation factor TFIIS.l, TCEA2, TFIIS, Transcription Elongation Factor A (SII) 2.

    Product # :

    PRO-1489

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    Description

    TCEA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a) and having a molecular mass of 36kDa.TCEA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TCEA2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.25M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription Elongation Factor A (SII)- 2 (TCEA2) is located in the nucleus, where it serves as an SII class transcription elongation factor. Elongation factors in this class are responsible for discharging RNA polymerase II ternary complexes from transcriptional arrest at template-encoded arresting sites. TCEA2 interacts with general transcription factor IIB, a basal transcription factor.

    • Synonyms

      Transcription elongation factor A protein 2, Testis-specific S-II, Transcription elongation factor S-II protein 2, Transcription elongation factor TFIIS.l, TCEA2, TFIIS, Transcription Elongation Factor A (SII) 2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMMGKEEE IARIARRLDK MVTKKSAEGA MDLLRELKAM PITLHLLQST RVGMSVNALR KQSSDEEVIA LAKSLIKSWK KLLDASDAKA RERGRGMPLP TSSRDASEAP DPSRKRPELP RAPSTPRITT FPPVPVTCDA VRNKCREMLT AALQTDHDHV AIGADCERLS AQIEECIFRD VGNTDMKYKN RVRSRISNLK DAKNPDLRRN VLCGAITPQQ IAVMTSEEMA SDELKEIRKA MTKEAIREHQ MARTGGTQTD LFTCGKCRKK NCTYTQVQTR SSDEPMTTFV VCNECGNRWK FC.

    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.

    Tcea2 Human
  • View Data Sheet

    Name :

    CFB-a Human

    Description:

    Complement Factor B Fragment a Human

    Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    Product # :

    PRO-2735

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    Description

    CFB-a Human produced in Human Plasma having a molecular mass of 33 kDa.

    Source

    Human Plasma.

    Formulation

    CFB-a solution (1mg/ml) contains Phosphate-buffered saline, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

    • Synonyms

      Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFB-a Human is stable at 4°C if entire vial will be used within 2-4 weeks. Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

    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.

    Cfb Protein
  • View Data Sheet

    Name :

    OSM Mouse

    Description:

    Oncostatin-M Mouse Recombinant

    Oncostatin-M, OSM, OncoM.

    Product # :

    CYT-168

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    • 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 :

    Cytochrome-C Bovine

    Description:

    Cytochrome-C Bovine

    CYCS, CYC, cyt c

    Product # :

    PRO-2810

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    Description

    Cytochrome-C Bovine is a natural native protein.

    Source

    Bovine.

    Formulation

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

    Purity

    Greater than 99.0%.

    More Info

    • Synonyms

      CYCS, CYC, cyt c

    • Physical Appearance

      Reddish or dark brown crystalline powder.

    • Stability

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

    • Background

      Bovine Cytochrome c in Health and Disease:

      Understanding the behavior of Cytochrome c in bovine systems has implications for veterinary medicine and livestock health. Alterations in mitochondrial function, reflected in changes in Cytochrome c dynamics, may be indicative of metabolic disorders, oxidative stress, or other pathological conditions. Bovine Cytochrome c studies contribute to our knowledge of mitochondrial dysfunction in diseases affecting cattle, potentially paving the way for diagnostic and therapeutic strategies.

      Challenges and Future Directions:

      While the study of Cytochrome c in bovine systems provides a wealth of insights, challenges persist. Fine-tuning experimental methodologies, exploring the interplay with other mitochondrial components, and deciphering the specificities in bovine systems are critical considerations for advancing our understanding. Additionally, linking changes in Cytochrome c behavior to specific physiological outcomes in cattle poses a challenge, requiring comprehensive investigations in diverse contexts.

      Bovine Cytochrome c emerges as a sentinel player in the intricate dance of cellular respiration, offering a window into the energetic dynamics of bovine mitochondria. Its structural insights, functional significance, and implications in health and disease position it as a central focus in understanding cellular bioenergetics in cattle. As researchers continue to unravel the molecular intricacies of bovine Cytochrome c, they not only deepen our understanding of mitochondrial function but also contribute to advancements in veterinary medicine and the optimization of livestock health, shaping the future of sustainable and healthy cattle farming practices.

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    Cytochrome C Bovine
  • View Data Sheet

    Name :

    CSTF1 Human, sf9

    Description:

    Cleavage Stimulation Factor 1 Human Recombinant, sf9

    Cleavage Stimulation Factor Subunit 1, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kD, Cleavage Stimulation Factor 50 KDa Subunit, CF-1 50 KDa Subunit, CSTF 50 KDa Subunit, CstF-50, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kDa, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, CstFp50.

    Product # :

    PRO-2436

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    Description

    CSTF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 437 amino acids (1-431a.a.) and having a molecular mass of 49.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CSTF1 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CSTF1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.

    • Synonyms

      Cleavage Stimulation Factor Subunit 1, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kD, Cleavage Stimulation Factor 50 KDa Subunit, CF-1 50 KDa Subunit, CSTF 50 KDa Subunit, CstF-50, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kDa, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, CstFp50.

    • 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

      MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DHHHHHH.

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    Cstf1 Human Sf9
  • View Data Sheet

    Name :

    SULT1C4 Human

    Description:

    Sulfotransferase Family, Cytosolic 1C, Member 4 Human Recombinant

    Sulfotransferase 1C4, SULT1C, SULT1C2, Sulfotransferase Family, Cytosolic 1C, Member 4, SULT1C4, ST1C4, Sulfotransferase 1C2, SULT1C#2.

    Product # :

    ENZ-710

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    Description

    SULT1C4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-302 a.a) and having a molecular mass of 37.6kDa. SULT1C4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SULT1C4 protein solution (1mg/ml) containing 0.1M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sulfotransferase 1C4 (SULT1C4) is a member of the SULT subfamily. SULT1C4 is responsible for transferring a sulfo moiety from PAPS to phenol-containing compounds. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. Sulfotransferase enzymes are different in their tissue distributions and substrate specificities. SULT1C4 catalyzes the sulfonation of p-nitrophenol and N-hydroxy-2-acetylaminofluorene.

    • Synonyms

      Sulfotransferase 1C4, SULT1C, SULT1C2, Sulfotransferase Family, Cytosolic 1C, Member 4, SULT1C4, ST1C4, Sulfotransferase 1C2, SULT1C#2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MALHDMEDFT FDGTKRLSVN YVKGILQPTD TCDIWDKIWN FQAKPDDLLI STYPKAGTTW TQEIVELIQN EGDVEKSKRA PTHQRFPFLE MKIPSLGSGL EQAHAMPSPR ILKTHLPFHL LPPSLLEKNC KIIYVARNPK DNMVSYYHFQ RMNKALPAPG TWEEYFETFL AGKVCWGSWH EHVKGWWEAK DKHRILYLFY EDMKKNPKHE IQKLAEFIGK KLDDKVLDKI VHYTSFDVMK QNPMANYSSI PAEIMDHSIS PFMRKGAVGD WKKHFTVAQN ERFDEDYKKK MTDTRLTFHF QF.

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    Sult1C4 Human
  • View Data Sheet

    Name :

    EGF Rat Protein

    Description:

    Epidermal Growth Factor Rat

    Urogastrone, URG, EGF.

    Product # :

    CYT-556

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    Description

    Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.

    Source

    Adult Male Rat Submandibular Glands.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

    Purity

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

    More Info

    • Introduction

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

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Background

      Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential

      Abstract:

      This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.

      Introduction:

      Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.

      Protein Expression and Purification:

      The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.

      Receptor Binding Assays and Ligand Interaction:

      Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.

      Cellular Signaling Pathways and Responses:

      In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.

      Bioinformatics Insights and Structural Modeling:

      Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.

      Therapeutic Implications and Future Prospects:

      EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.

      Challenges and Future Directions:

      Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.

      Conclusion:

      A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.

      What is the molecular weight/Mw of EGF RAT Protein?
      EGF RAT Protein has a total Mw of 6.15kDa.

      What is the source or expression system of EGF RAT Protein?
      Adult Male Rat Submandibular Glands.

      What is the Purity of EGF RAT Protein?
      EGF RAT Protein is >99% pure as determined by SDS-PAGE.

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

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

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

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

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

    Egf Rat
  • View Data Sheet

    Name :

    FOLH1 Mouse

    Description:

    Folate Hydrolase 1 Mouse Recombinant

    Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.

    Product # :

    ENZ-957

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    Description

    FOLH1 Mouse Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 717 amino acids (45-752a.a) and having a molecular mass of 80.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). FOLH1 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The FOLH1 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Folate Hydrolase 1 (Folh1) is a single pass type 2 membrane protein which is expressed mainly in prostate epithelium. Folh1 which is a part of the peptidase M28 family and M28B subfamily has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase activity. Folh1 can be found in urinary bladder, kidney, testis, ovary, stomach, small intestine colon, and the capillary endothelium of various tumors. Therefore, Folh1 plays a role in directed imaging and therapy of recurrent of metastatic disease.

    • Synonyms

      Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.

    • 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

      ADPKPSNEAT GNVSHSGMKK EFLHELKAEN IKKFLYNFTR TPHLAGTQNN FELAKQIHDQ WKEFGLDLVE LSHYDVLLSY PNKTHPNYIS IINEDGNEIF KTSLSEQPPP GYENISDVVP PYSAFSPQGT PEGDLVYVNY ARTEDFFKLE REMKISCSGK IVIARYGKVF RGNMVKNAQL AGAKGMILYS DPADYFVPAV KSYPDGWNLP GGGVQRGNVL NLNGAGDPLT PGYPANEHAY RHELTNAVGL PSIPVHPIGY DDAQKLLEHM GGPAPPDSSW KGGLKVPYNV GPGFAGNFST QKVKMHIHSY TKVTRIYNVI GTLKGALEPD RYVILGGHRD AWVFGGIDPQ SGAAVVHEIV RSFGTLKKKG RRPRRTILFA SWDAEEFGLL GSTEWAEEHS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVYNLTK ELQSPDEGFE GKSLYDSWKE KSPSPEFIGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWKTNKVSSY PLYHSVYETY ELVVKFYDPT FKYHLTVAQV RGAMVFELAN SIVLPFDCQS YAVALKKYAD TIYNISMKHP QEMKAYMISF DSLFSAVNNF TDVASKFNQR LQELDKSNPI LLRIMNDQLM YLERAFIDPL GLPGRPFYRH IIYAPSSHNK YAGESFPGIY DALFDISSKV NASKAWNEVK RQISIATFTV QAAAETLREV AHHHHHH.

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    Folh1 Mouse
  • View Data Sheet

    Name :

    NTH E.Coli

    Description:

    Endonuclease-III E.Coli Recombinant

    DNA-(apurinic or apyrimidinic site) lyase, b1633, JW1625.

    Product # :

    ENZ-132

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    Description

    NTH E.Coli Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 231 amino acids (1-211a.a.) and having a molecular mass of 25.7kDa. The NTH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NTH solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT, 0.1mM PMSF and 40% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Endonuclease III (nth) is a DNA repair enzyme which has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases numerous damaged pyrimidines from DNA by cleaving the N-glycosidic bond and leaving an AP (apurinic/apyrimidinic) site. This AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, thus leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

    • Synonyms

      DNA-(apurinic or apyrimidinic site) lyase, b1633, JW1625.

    • 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 MNKAKRLEIL TRLRENNPHP TTELNFSSPF ELLIAVLLSA QATDVSVNKA TAKLYPVANT PAAMLELGVE GVKTYIKTIG LYNSKAENII KTCRILLEQH NGEVPEDRAA LEALPGVGRK TANVVLNTAF GWPTIAVDTH IFRVCNRTQF APGKNVEQVE EKLLKVVPAE FKVDCHHWLI LHGRYTCIAR KPRCGSCIIE DLCEYKEKVD I.

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    Nth Ecoli
  • View Data Sheet

    Name :

    TPST2 Human

    Description:

    Tyrosylprotein Sulfotransferase 2 Human Recombinant

    Protein-tyrosine sulfotransferase 2, EC 2.8.2.20, Tyrosylprotein sulfotransferase 2, TPST-2, TPST2, TANGO13B.

    Product # :

    ENZ-707

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    Description

    TPST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (26-377) and having a molecular mass of 41kDa.TPST2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPST2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosylprotein Sulfotransferase 2 (TPST2) is a member of the protein sulfotransferase family. TPST2 is a widely expressed protein, which catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The TPST2 protein is a type II integral membrane protein located in the Golgi body.

    • Synonyms

      Protein-tyrosine sulfotransferase 2, EC 2.8.2.20, Tyrosylprotein sulfotransferase 2, TPST-2, TPST2, TANGO13B.

    • 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 MGSQQVLECR AVLAGLRSPR GAMRPEQEEL VMVGTNHVEY RYGKAMPLIF VGGVPRSGTT LMRAMLDAHP EVRCGEETRI IPRVLAMRQA WSKSGREKLR LDEAGVTDEV LDAAMQAFIL EVIAKHGEPA RVLCNKDPFT LKSSVYLSRL FPNSKFLLMV RDGRASVHSM ITRKVTIAGF DLSSYRDCLT KWNKAIEVMY AQCMEVGKEK CLPVYYEQLV LHPRRSLKLI LDFLGIAWSD AVLHHEDLIG KPGGVSLSKI ERSTDQVIKP VNLEALSKWT GHIPGDVVRD MAQIAPMLAQ LGYDPYANPP NYGNPDPFVI NNTQRVLKGD YKTPANLKGY FQVNQNSTSS HLGSS.

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    Tpst2 Human
  • View Data Sheet

    Name :

    HAGH Human

    Description:

    Hydroxyacylglutathione Hydrolase Human Recombinant

    GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.

    Product # :

    ENZ-034

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    Description

    HAGH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-260a.a.) and having a molecular mass of 31.4kDa.HAGH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HAGH protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl Buffer (pH 8.5) and 10% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      HAGH is a part of the glyoxalase family and a thiolesterase which hydrolyses S-lactoyl-glutathione to reduced glutathione and D-lactate. HAGH protein is a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73 and serves as a pro-survival factor of the p53 family. HAGH appears only as a monomer and binds two zinc ions per subunit.

    • Synonyms

      GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.

    • 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 MGSHMKVEVL PALTDNYMYL VIDDETKEAA IVDPVQPQKV VDAARKHGVK LTTVLTTHHH WDHAGGNEKL VKLESGLKVY GGDDRIGALT HKITHLSTLQ VGSLNVKCLA TPCHTSGHIC YFVSKPGGSE PPAVFTGDTL FVAGCGKFYE GTADEMCKAL LEVLGRLPPD TRVYCGHEYT INNLKFARHV EPGNAAIREK LAWAKEKYSI GEPTVPSTLA EEFTYNPFMR VREKTVQQHA GETDPVTTMR AVRREKDQFK MPRD.

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    Hagh Human
  • View Data Sheet

    Name :

    TNFRSF8 igG-His Human

    Description:

    CD30 Ligand Receptor, IgG-His Tag Human Recombinant

    Tumor Necrosis Factor Receptor Superfamily Member 8, Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1.

    Product # :

    CYT-983

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    Description

    TNFRSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 613 amino acids (19-379 a.a.) and having a molecular mass of 66.7kDa (Molecular size on SDS-PAGE will appear at approximately 25-100kDa). TNFRSF8 is expressed with a 252 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 8, Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-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

      ADPFPQDRPF EDTCHGNPSH YYDKAVRRCC YRCPMGLFPT QQCPQRPTDC RKQCEPDYYL DEADRCTACV TCSRDDLVEK TPCAWNSSRV CECRPGMFCS TSAVNSCARC FFHSVCPAGM IVKFPGTAQK NTVCEPASPG VSPACASPEN CKEPSSGTIP QAKPTPVSPA TSSASTMPVR GGTRLAQEAA SKLTRAPDSP SSVGRPSSDP GLSPTQPCPE GSGDCRKQCE PDYYLDEAGR CTACVSCSRD DLVEKTPCAW NSSRTCECRP GMICATSATN SCARCVPYPI CAAETVTKPQ DMAEKDTTFE APPLGTQPDC NPTPENGEAP ASTSPTQSLL VDSQASKTLP IPTSAPVALS STGKAAAFES RACSLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH 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.

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