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Search results

142 results found for “Pigment Epithelium-Derived Factor”

Name

Description

Product #

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  • View Data Sheet

    Name :

    PAFAH1B3 Human

    Description:

    Platelet-activating Factor Acetylhydrolase 1b, Catalytic Subunit 3 Human Recombinant

    Platelet-activating factor acetylhydrolase 1b catalytic subunit 3 (29kDa), PAF acetylhydrolase 29 kDa subunit, platelet-activating factor acetylhydrolase, isoform Ib gamma subunit (29kD), PAF-AH1b alpha 1 subunit, PAF-AH 29 kDa subunit, PAFAHG, PAFAH subunit gamma, EC 3.1.1.47.

    Product # :

    ENZ-641

    Price :

    Quantity :

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    Description

    PAFAH1B3 Human Recombinant produced in E. coli is a single polypeptide chain containing 254 amino acids (1-231) and having a molecular mass of 28.2 kDa.PAFAH1B3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PAFAH1B3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet-activating Factor Acetylhydrolase 1b Catalytic Subunit 3 (PAFAH1B3) is a member of the 'GDSL' lipolytic enzyme family. Acetylhydrolase catalyzes the elimination of an acetyl group from the glycerol backbone of platelet-activating factor. PAFAH1B3, which is a subunit of the platelet-activating factor cetylhydrolase isoform 1B complex, is comprised of the catalytic beta and gamma subunits and the regulatory alpha subunit. The PAFAH1B3 complex has an imperative role during the development of brain.

    • Synonyms

      Platelet-activating factor acetylhydrolase 1b catalytic subunit 3 (29kDa), PAF acetylhydrolase 29 kDa subunit, platelet-activating factor acetylhydrolase, isoform Ib gamma subunit (29kD), PAF-AH1b alpha 1 subunit, PAF-AH 29 kDa subunit, PAFAHG, PAFAH subunit gamma, EC 3.1.1.47.

    • 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 MGSMSGEENP ASKPTPVQDV QGDGRWMSLH HRFVADSKDK EPEVVFIGDS LVQLMHQCEI WRELFSPLHA LNFGIGGDGT QHVLWRLENG ELEHIRPKIV VVWVGTNNHG HTAEQVTGGI KAIVQLVNER QPQARVVVLG LLPRGQHPNP LREKNRQVNE LVRAALAGHP RAHFLDADPG FVHSDGTISH HDMYDYLHLS RLGYTPVCRA LHSLLLRLLA QDQGQGAPLL EPAP

    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.

    Pafah1B3 Human
  • View Data Sheet

    Name :

    PDGF CC Human

    Description:

    Platelet Derived Growth Factor-CC Human Recombinant

    Platelet Derived Growth Factor C, Spinal Cord-Derived Growth Factor, FALLOTEIN, PDGF-C, VEGF-E, SCDGF, Secretory Growth Factor-Like Protein, Platelet-Derived Growth Factor C, PDGFC.

    Product # :

    CYT-872

    Price :

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    • More Info

    Description

    PDGF-CC Human Recombinant (235-345) produced in E.Coli is a disulfide-linked homodimer containing 2x118 amino acids and having a total molecular mass of 26.8kDa.The PDGF-CC is fused to a 7 amino acid His tag [M-HHHHHH] at N-terminal and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 350ng/ml.

    More Info

    • Introduction

      Platelet Derived Growth Factor-CC (PDGF-CC) belongs to the PGDF family of growth factors. PDGF-CC binds with high-affinity to PDGF R-a and activates PDGF R-ab heterodimers. During development, PDGF-CC is involved in ductal morphogenesis, cardiovascular smooth muscle cell proliferation; also PDGF-CC is an angiogenic factor. Furthermore, PDGF-CC is expressed in numerous tumors and tumor cell lines, and may be linked with tumorigenesis.

    • Synonyms

      Platelet Derived Growth Factor C, Spinal Cord-Derived Growth Factor, FALLOTEIN, PDGF-C, VEGF-E, SCDGF, Secretory Growth Factor-Like Protein, Platelet-Derived Growth Factor C, PDGFC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MHHHHHHVVD LNLLTEEVRL YSCTPRNFSV SIREELKRTD TIFWPGCLLV KRCGGNCACC LHNCNECQCV PSKVTKKYHE VLQLRPKTGV RGLHKSLTDV ALEHHEECDC VCRGSTGG.

    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.

    Pdgf Cc Human
  • View Data Sheet

    Name :

    PGRN Human

    Description:

    Progranulin Human Recombinant

    GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.

    Product # :

    CYT-524

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    Progranulin Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 1-593 amino acids and having a molecular mass of 74kDa. The Progranulin is purified by standard chromatographic techniques.

    Source

    HEK 293 cells.

    Formulation

    The protein contains 1xPBS.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Activates phospho-ERK1/2 in neuronal mouse P19 cells and regulates food intake and body weight.

    More Info

    • Introduction

      A 88-kDa progranulin, also called proepithelin and PC cell-derived growth factor, is a single precursor protein of granulins which are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin/epithelin motif. Granulins are a variety of active, 6 kDa peptides and named granulin A (epithelin 1), granulin B (epithelin 2), granulin C, etc. Both the peptides and intact progranulin protein regulate cell growth. However, different members of the granulin protein family may act as inhibitors, stimulators, or have dual actions on cell growth. Granulin family members are important in normal development, wound healing, and tumorigenesis.

    • Synonyms

      GRN, PGRN, granulin, Acrogranin, propithelin, PC cell derived growth Factor, GEP, GP88, PEPI, PCDGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

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

    Progranulin Human
  • View Data Sheet

    Name :

    TFF1 Human, His

    Description:

    Trefoil Factor-1 Human Recombinant, His Tag

    TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    Product # :

    CYT-610

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TFF-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids (25-84) which includes a 10 amino acid His Tag and having a total molecular mass of 7.9 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF1 His Tag protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5 and 20mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.

    • Synonyms

      TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF1 His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 His Tag should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS EAQTETCTVA PRERQNCGFP GVTPSQCANK GCCFDDTVRG VPWCFYPNTI DVPPEEECEF.

    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.

    Tff1 Human His
  • View Data Sheet

    Name :

    EIF4E Mouse

    Description:

    Eukaryotic Translation Initiation Factor 4E Recombinant Mouse

    eIF-4E, eIF4E, mRNA cap-binding protein, eIF-4F 25 kDa subunit, Eif4e.

    Product # :

    PRO-2411

    Price :

    Quantity :

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    Description

    EIF4E Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 241 amino acids (1-217 a.a) and having a molecular mass of 27.6kDa. EIF4E is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EIF4E protein solution (1mg/ml) 20mM Tris-HCl Buffer (pH8.0), 10% glycerol, 1mM DTT, 0.1M NaCl and 0.1mM PMSF.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.

    • Synonyms

      eIF-4E, eIF4E, mRNA cap-binding protein, eIF-4F 25 kDa subunit, Eif4e.

    • 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 MGSHMATVEP ETTPTTNPPP AEEEKTESNQ EVANPEHYIK HPLQNRWALW FFKNDKSKTW QANLRLISKF DTVEDFWALY NHIQLSSNLM PGCDYSLFKD GIEPMWEDEK NKRGGRWLIT LNKQQRRSDL DRFWLETLLC LIGESFDDYS DDVCGAVVNV RAKGDKIAIW TTECENRDAV THIGRVYKER LGLPPKIVIG YQSHADTATK SGSTTKNRFV V

    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.

    Eif4E Mouse
  • View Data Sheet

    Name :

    EDAR Human, Sf9

    Description:

    Ectodysplasin A Receptor Human Recombinant, Sf9

    Ectodysplasin A Receptor, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Downless Homolog, EDA-A1 Receptor, DL, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, Ectodysplasin-A Receptor, ECTD10A, ECTD10B, EDA-A1R, EDA1R, ED1R, EDA3, HRM1, ED5, ED3.

    Product # :

    PRO-2510

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    Description

    EDAR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (27-187a.a.) and having a molecular mass of 45.6kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).EDAR is expressed with a 249 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.

    • Synonyms

      Ectodysplasin A Receptor, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Downless Homolog, EDA-A1 Receptor, DL, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, Ectodysplasin-A Receptor, ECTD10A, ECTD10B, EDA-A1R, EDA1R, ED1R, EDA3, HRM1, ED5, ED3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPEYSNCGE NEYYNQTTGL CQECPPCGPG EEPYLSCGYG TKDEDYGCVP CPAEKFSKGG YQICRRHKDC EGFFRATVLT PGDMENDAEC GPCLPGYYML ENRPRNIYGM VCYSCLLAPP NTKECVGATS GASANFPGTS GSSTLSPFQH AHKELSGQGH LATAAAAFES ACSLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

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    Edar Protein
  • View Data Sheet

    Name :

    PCOLCE Human, Sf9

    Description:

    Procollagen C-Endopeptidase Enhancer Human Recombinant, Sf9

    Procollagen C-endopeptidase enhancer 1,  Procollagen COOH-terminal proteinase enhancer 1,  PCPE-1,  Procollagen C-proteinase enhancer 1,  Type 1 procollagen C-proteinase enhancer protein,  Type I procollagen COOH-terminal proteinase enhancer,  PCOLCE,  PCPE1,  Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase, Enhancer 1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1.

    Product # :

    ENZ-1075

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    Description

    PCOLCE produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 433 amino acids (26-449 a.a.) and having a molecular mass of 46.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PCOLCE is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.

    • Synonyms

      Procollagen C-endopeptidase enhancer 1, Procollagen COOH-terminal proteinase enhancer 1, PCPE-1, Procollagen C-proteinase enhancer 1, Type 1 procollagen C-proteinase enhancer protein, Type I procollagen COOH-terminal proteinase enhancer, PCOLCE, PCPE1, Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase, Enhancer 1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 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

      ADPQTPNYTR PVFLCGGDVK GESGYVASEG FPNLYPPNKE CIWTITVPEG QTVSLSFRVF DLELHPACRY DALEVFAGSG TSGQRLGRFC GTFRPAPLVA PGNQVTLRMT TDEGTGGRGF LLWYSGRATS GTEHQFCGGR LEKAQGTLTT PNWPESDYPP GISCSWHIIA PPDQVIALTF EKFDLEPDTY CRYDSVSVFN GAVSDDSRRL GKFCGDAVPG SISSEGNELL VQFVSDLSVT ADGFSASYKT LPRGTAKEGQ GPGPKRGTEP KVKLPPKSQP PEKTEESPSA PDAPTCPKQC RRTGTLQSNF CASSLVVTAT VKSMVREPGE GLAVTVSLIG AYKTGGLDLP SPPTGASLKF YVPCKQCPPM KKGVSYLLMG QVEENRGPVL PPESFVVLHR PNQDQILTNL SKRKCPSQPV RAAASQDHHH 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.

    Pcolce Protein
  • View Data Sheet

    Name :

    BDNF Human, CHO

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant, CHO

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-1262

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    • sds-page

    Description

    Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    CHO Cells

    Formulation

    The protein was lyophilized with 5% trehalose and 1x PBS

    Purity

    Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

    Biological Activity

    BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

    sds-page

    bdnf human cho sds-page - Product image 1

    More Info

    • Introduction

      BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
      BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

      What is the source or expression system of BDNF Protein?
      CHO Cells

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

      What is the Biological Activity of BDNF Protein?
      BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.

      What is the amino acid sequence of BDNF Protein?
      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • References

      Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
      Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
      Link:BDNF prospec publication

    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.

    Bdnf Human Cho
  • View Data Sheet

    Name :

    TRAIL Human

    Description:

    TRAIL / APO2 Ligand Human Recombinant

    Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    Product # :

    CYT-443

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    Description

    TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. The sTRAIL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a filtered (0.2µm) solution containing 20mM Tris-HCl pH 8.0 and 150mM NaCl.

    Purity

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

    Biological Activity

    The activity is determined by the cytolysis of Murine L929 cells in the presence of Actinomycin D, ED50 for this effect is less than 2ng/ml, corresponding to a specific activity of 5,000,000IU/mg.

    More Info

    • Introduction

      TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
      In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized APO 2 Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL 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 TRAIL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MRERGPQRVA AHITGTRGRS NTLSSPNSKN EKALGRKINS WESSRSGHSF LSNLHLRNGE LVIHEKGFYY IYSQTYFRFQ EEIKENTKND KQMVQYIYKY TSYPDPILLM KSARNSCWSK DAEYGLYSIY QGGIFELKEN DRIFVSVTNE HLIDMDHEAS FFGAFLVG.

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    Apo2L Human
  • View Data Sheet

    Name :

    Recombinant EGFR Antibody

    Description:

    Recombinant Anti Human Epidermal Growth Factor Receptor

    Product # :

    ANT-600

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    Description

    Recombinant Anti Human Epidermal Growth Factor Receptor monoclonal antibody produced in CHO is a glycosylated dimer containing 1326 amino acids and having a molecular mass of 187.2 kDa.

    Source

    CHO.

    Formulation

    The protein 15.6mg/ml solution contains 20mmol/L Na2HPO4- NaH2PO4, 0.005% Tween 80, pH7.0.

    Purity

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

    Biological Activity

    Compared with reference standard, the range of biological activity was found to be 86%.

    More Info

    • Introduction

      The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.

    • Physical Appearance

      Sterile filtered colorless liquid formulation.

    • Stability

      Recombinant EGFR Antibody should be stored between 2-8°C. Please do not freeze.

    • Amino Acid Sequence

      Heavy chain
      QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYNTP
      FTSRLSINKDNSKSQVFFKMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAASTKG
      PSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSS
      VVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPK
      PKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTV
      LHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVK
      GFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEAL
      HNHYTQKSLSLSPGK.
      Light chain
      DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPSRF
      SGSGSGTDFTLSINSVESEDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPPSDEQ
      LKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADY
      EKHKVYACEVTHQGLSSPVTKSFNRGEC.

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    Recombinant Egfr Antibody
  • 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 :

    HB-EGF Human, His

    Description:

    Proheparin-Binding EGF-like Growth Factor Human Recombinant, His Tag

    Proheparin-binding EGF-like growth factor, HBEGF, DTR, DTS, HEGFL, HB-EGF, Heparin-binding EGF-like growth factor, Diphtheria toxin receptor, DT-R, DTSF.

    Product # :

    CYT-761

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    Description

    HB-EGF His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (63-148) and having a molecular mass of 12.1kDa.HB-EGF His is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HB-EGF His solution (0. 5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind heparin and heparin sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

    • Synonyms

      Proheparin-binding EGF-like growth factor, HBEGF, DTR, DTS, HEGFL, HB-EGF, Heparin-binding EGF-like growth factor, Diphtheria toxin receptor, DT-R, DTSF.

    • 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 MGSDLQEADL DLLRVTLSSK PQALATPNKE EHGKRKKKGK GLGKKRDPCL RKYKDFCIHG ECKYVKELRA PSCICHPGYH GERCHGLSL.

    • Background

      What is the molecular weight/Mw of HB-EGF Protein?
      HB-EGF Protein has a total Mw of 12.1kDa.

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

      What is the Purity of HB-EGF Protein?
      HB-EGF Protein is >85% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of HB-EGF Protein?
      MGSSHHHHHH SSGLVPRGSH MGSDLQEADL DLLRVTLSSK PQALATPNKE EHGKRKKKGK GLGKKRDPCL RKYKDFCIHG ECKYVKELRA PSCICHPGYH GERCHGLSL.

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

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

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

    Hb Egf Human His
  • View Data Sheet

    Name :

    proBDNF Human

    Description:

    Precursor Brain-Derived Neurotrophic Factor Human Recombinant

    proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

    Product # :

    CYT-014

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    Description

    proBDNF Human Recombinant produced in E.Coli is a single, non-glycosylated, non-covalently linked homodimer with each polypeptide chain containing 229 amino acids and having a molecular mass of 52kDa. The proBDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    proBDNF was lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH 8.0 and 500mM NaCl.

    Purity

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

    More Info

    • Introduction

      proBDNF (the precursor form of Brain-derived neurotrophic factor) interacts preferentially with p75NTR (the pan-neurotrophin receptor p75) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, while the mature BDNF selectively binds with great affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. Since proneurotrophins and mature neurotrophins bring forth opposite biological effects, proBDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. proBDNF has an important role in negative regulation of neurotrophic actions in the brain.

    • Synonyms

      proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.

    • Background

      Precursor Brain-Derived Neurotrophic Factor Human Recombinant: Unveiling the Potential of a Key Neurotrophic Factor

      Abstract:

      Precursor Brain-Derived Neurotrophic Factor (proBDNF) human recombinant is a pivotal neurotrophic factor that plays a critical role in neuronal development, survival, and synaptic plasticity. This research paper provides a comprehensive overview of proBDNF, including its characteristics, processing mechanisms, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of proBDNF human recombinant are proposed, highlighting its future implications in the field of neuroregenerative medicine.

      Introduction:

      Understanding the intricate processes underlying neuronal development and function is crucial for advancing neuroregenerative strategies. Neurotrophic factors, such as proBDNF, have garnered significant attention due to their pivotal roles in supporting neuronal growth and survival. This paper delves into the unique features of proBDNF and presents novel approaches for its production and optimization.

      Characteristics and Processing Mechanisms:

      proBDNF is a precursor protein consisting of 247 amino acids and is processed into mature brain-derived neurotrophic factor (mBDNF) through proteolytic cleavage. The ratio between proBDNF and mBDNF is tightly regulated and determines the balance between neuronal survival and apoptosis. Additionally, proBDNF exerts distinct biological functions through its receptor interactions, modulating synaptic plasticity and neuronal activity.

      Production of proBDNF Human Recombinant:

      Efficient production methodologies are essential to harness the therapeutic potential of proBDNF human recombinant. Various expression systems, including bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents unique advantages and challenges, necessitating careful selection to achieve high yields and protein quality. Optimization strategies, such as codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality proBDNF recombinant.

      Potential Therapeutic Applications:

      proBDNF human recombinant holds immense promise for neuroregenerative medicine. Its role in promoting neuronal survival, axonal growth, and synaptic plasticity positions it as a valuable therapeutic agent for neurodegenerative disorders, spinal cord injuries, and stroke. Additionally, the balance between proBDNF and mBDNF presents a potential therapeutic target for fine-tuning neuronal processes and restoring proper brain function.

      Conclusion:

      proBDNF human recombinant represents a crucial neurotrophic factor with diverse therapeutic applications in neuroregenerative medicine. Optimizing production methodologies and further understanding its processing mechanisms will enhance its clinical utility. With its potential implications in neurodegenerative disorders and neuronal repair, proBDNF human recombinant holds immense promise as a transformative tool for promoting neural health and regeneration.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 52kDa.

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

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

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

      What is the amino acid sequence of BDNF Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.

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

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

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    Probdnf Human
  • View Data Sheet

    Name :

    LIF Human, Sf9

    Description:

    Leukemia Inhibitory Factor Human Recombinant, Sf9

    Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.

    Product # :

    CYT-1003

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    Description

    LIF Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 189 amino acids (23-202a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). LIF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LIF 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

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 0.5 ng/ml.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.

    • 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

      ADPSPLPITP VNATCAIRHP CHNNLMNQIR SQLAQLNGSA NALFILYYTA QGEPFPNNLD KLCGPNVTDF PPFHANGTEK AKLVELYRIV VYLGTSLGNI TRDQKILNPS ALSLHSKLNA TADILRGLLS NVLCRLCSKY HVGHVDVTYG PDTSGKDVFQ KKKLGCQLLG KYKQIIAVLA
      QAFHHHHHH.

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    Lif Human Sf9
  • View Data Sheet

    Name :

    VEGF Mouse

    Description:

    Vascular Endothelial Growth Factor Mouse Recombinant

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-336

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    Description

    Vascular Endothelial Growth Factor Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, double polypeptide chains containing 165 amino acids and having a molecular mass of 38.8kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered solution with PBS, pH 7.4.

    Purity

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

    Biological Activity

    The biological activity is determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 5.0 ng/ml corresponding to a specific activity of 200,000IU/mg.

    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

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

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    Vegf Mouse
  • View Data Sheet

    Name :

    VEGF Mouse, His

    Description:

    Vascular Endothelial Growth Factor Mouse Recombinant, His Tag

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, Vegf120, Vegf164, Vegf188, Vegfa.

    Product # :

    CYT-680

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    Description

    VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (205-324 a.a.) and having a total molecular mass of 16.3kDa. Mouse VEGF is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Mouse VEGF contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using NIH-3T3 mouse embryonic fibroblast. The ED50 for this effect is 0.5-1.5ng/ml.

    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/macrophage migration, 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 mitogenesis and 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 is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, Vegf120, Vegf164, Vegf188, Vegfa.

    • 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 MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKPR R.

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    Vegf Mouse His
  • View Data Sheet

    Name :

    PPIF Human

    Description:

    Cyclophilin-F Human Recombinant

    Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

    Product # :

    ENZ-385

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    Description

    PPIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids (30-207) and having a molecular mass of 21 kDa. The PPIF is fused to a 20 amino acid His tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPIF solution containing 20mM Tris-HCl pH-7.5, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 250 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

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    • Introduction

      PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

    • Synonyms

      Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

    • 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 CSKGSGDPSS SSSSGNPLVY LDVDANGKPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FTLKHVGPGV LSMANAGPNT NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGRTSKKIV ITDCGQLS.

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    Ppif Human
  • View Data Sheet

    Name :

    NAIF1 Human

    Description:

    Nuclear Apoptosis Inducing Factor 1 Human Recombinant

    bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    Product # :

    PRO-1978

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    Description

    NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.

    • Synonyms

      bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    • 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 MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.

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    Naif1 Human
  • View Data Sheet

    Name :

    TGFB2 Human

    Description:

    Transforming Growth Factor Beta 2 Human Recombinant

    Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    Product # :

    CYT-441

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    Description

    TGFB2 Human Recombinant produced in plants is a homodimeric polypeptide chain containing 2 x 118 amino acids and having a total molecular mass of 27.08kDa. The TGFB2 is fused to 6xHis Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of TGFB2 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 < 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

    More Info

    • Introduction

      TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-β (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.

    • Synonyms

      Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB2 Human 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 TGFB2 in sterile 18M-cm H2O not less than 1µg/40µl, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIH
      EPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASAS
      PCCVSQDLEPLTI LYYIGKTPKIEQLSNMIVKSCKCS.

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    Tgfb2 Human
  • View Data Sheet

    Name :

    TGFB2 Human, HEK

    Description:

    Transforming Growth Factor-Beta 2 Human Recombinant, HEK

    Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    Product # :

    CYT-112

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    Description

    TGF-b 2 Human Recombinant produced in HEK cells is a non-glycosylated homodimer, having a total molecular weight of 25kDa.The TGF-b 2 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    TGF-b 2 was lyophilized from a 0.2µm filtered solution containing 50mM sodium acetate pH 4.5.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2), the ED50 is 0.16ng/ml.

    More Info

    • Introduction

      TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-beta (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.

    • Synonyms

      Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGF-b 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 2 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 TGF-b 2 in sterile solution containing 20% ethanol, 50mM sodium acetate and 75mM acetic acid.

    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.

    Tgf B 2 Human Hek
  • View Data Sheet

    Name :

    SERF2 Human

    Description:

    Small EDRK-Rich Factor 2 Human Recombinant

    Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.

    Product # :

    PRO-1730

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    Description

    SERF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 82 amino acids (1-59 a.a) and having a molecular mass of 9.3kDa.SERF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SERF2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SERF2 (small EDRK-rich factor 2) is a member of the SERF family. SERF2 is a protein-coding gene. Among the diseases associated with SERF2 are spinal muscular atrophy, and muscular atrophy.

    • Synonyms

      Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.

    • 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 MGSMTRGNQR ELARQKNMKK QSDSVKGKRR DDGLSAAARK QRDSEIMQQK QKKANEKKEE PK

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    Serf2 Human
  • View Data Sheet

    Name :

    TNF a Mouse

    Description:

    Tumor Necrosis Factor-Alpha Mouse Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-252

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    Description

    Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (c) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL

    • Background

      Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.

      TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.

      In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.

      However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.

      In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.

      In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-a as a Reference Standard.

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

    Tnf Alpha Mouse
  • View Data Sheet

    Name :

    PBLD Human

    Description:

    Phenazine Biosynthesis-Like Protein Domain Containing Human Recombinant

    Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.

    Product # :

    PRO-010

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PBLD Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 308 amino acids (1-288 a.a.) and having a molecular mass of 33.9kDa. The PBLD is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PBLD solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PBLD is member of the phenazine biosynthesis-like protein (PhzF) family. PBLD which is expressed in most tissues is the only representative of the PhzF family in the human genome. PBLD participates in the MAPK signaling pathway. PBLD is involved in multiple basic cellular functions, its expression is elevated in several disease processes, including folate deficiency and hypotension.

    • Synonyms

      Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.

    • 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 MKLPIFIADA FTARAFRGNP AAVCLLENEL DEDMHQKIAR EMNLSETAFI RKLHPTDNFA QSSCFGLRWF TPASEVPLCG HATLASAAVL FHKIKNMNST LTFVTLSGEL RARRAEDGIV LDLPLYPAHP QDFHEVEDLI KTAIGNTLVQ DICYSPDTQK LLVRLSDVYN RSFLENLKVN TENLLQVENT GKVKGLILTL KGEPGGQTQA FDFYSRYFAP WVGVAEDPVT GSAHAVLSSY WSQHLGKKEM HAFQCSHRGG ELGISLRPDG RVDIRGGAAV VLEGTLTA.

    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.

    Pbld Human
  • View Data Sheet

    Name :

    TNFRSF8 Mouse

    Description:

    CD30 Ligand Receptor Mouse Recombinant

    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-1165

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    • description
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    Description

    TNFRSF8 Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 479 amino acids (19-258 aa) and having a molecular mass of 52.2kDa.TNFRSF8 is fused to a 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF8 protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% 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, 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

      FPTDRPLKTT CAGDLSHYPG EAARNCCYQC PSGLSPTQPC PRGPAHCRKQ CAPDYYVNED GKCTACVTCL PGLVEKAPCS GNSPRICECQ PGMHCCTPAV NSCARCKLHC SGEEVVKSPG TAKKDTICEL PSSGSGPNCS NPGDRKTLTS HATPQAMPTL ESPANDSARS LLPMRVTNLV QEDATELVKV PESSSSKARE PSPDPGNAEK NMTLELPSPG TLPDISTSEN SKEPASTAST LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

    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.

    Cd30 Mouse
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