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Search results

1000 results found for “rassf”

Name

Description

Product #

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  • View Data Sheet

    Name :

    RELM b Human, His

    Description:

    RELM-Beta Human Recombinant, His Tag

    Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    Product # :

    CYT-454

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    Description

    RELM-beta Human Recombinant is a His-Tagged Fusion Protein which is 11 kDa protein containing 90 amino acid residues of the RELM-beta human and 12 additional amino acid residues - HisTag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
      RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
      The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.

    • Synonyms

      Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      Add 0.1M Acetate buffer pH-4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MGSTQCSLDS VMDKKIKDVL NSLEYSPSPI SKKLSCASVK SQGRPSSCPA GMAVTGCACG YGCGSWDVQLETTCHCQCSV VDWTTARCCH LTKLRSHHHH HH.

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

    Relm Beta Human
  • View Data Sheet

    Name :

    NARS Human

    Description:

    Asparaginyl-TRNA Synthetase Human Recombinant

    NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    Product # :

    ENZ-915

    Price :

    Quantity :

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    Description

    NARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-548 a.a) and having a molecular mass of 65.3kDa. NARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    NARS protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

    • Synonyms

      NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      GSSHHHHHH SSGLVPRGSH MGSMVLAELY VSDREGSDAT GDGTKEKPFK TGLKALMTVG KEPFPTIYVD SQKENERWNV ISKSQLKNIK KMWHREQMKS ESREKKEAED SLRREKNLEE AKKITIKNDP SLPEPKCVKI GALEGYRGQR VKVFGWVHRL RRQGKNLMFL VLRDGTGYLQ CVLADELCQC YNGVLLSTES SVAVYGMLNL TPKGKQAPGG HELSCDFWEL IGLAPAGGAD NLINEESDVD VQLNNRHMMI RGENMSKILK ARSMVTRCFR DHFFDRGYYE VTPPTLVQTQ VEGGATLFKL DYFGEEAFLT QSSQLYLETC LPALGDVFCI AQSYRAEQSR TRRHLAEYTH VEAECPFLTF DDLLNRLEDL VCDVVDRILK SPAGSIVHEL NPNFQPPKRP FKRMNYSDAI VWLKEHDVKK EDGTFYEFGE DIPEAPERLM TDTINEPILL CRFPVEIKSF YMQRCPEDSR LTESVDVLMP NVGEIVGGSM RIFDSEEILA GYKREGIDPT PYYWYTDQRK YGTCPHGGYG LGLERFLTWI LNRYHIRDVC LYPRFVQRCT P.

    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.

    Human Nars
  • View Data Sheet

    Name :

    LTF Holo Human

    Description:

    Lactoferrin Holo Human Recombinant

    Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    Product # :

    PRO-592

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Recombinant Human Holo Lactoferrin produced in Plant is a glycosylated mature polypeptide sequence having an approximate molecular mass of 80 kDa.The Human Holo Lactoferrin is purified by proprietary chromatographic techniques.

    Source

    Rice Flour.

    Formulation

    The Human Holo lactoferrin was lyophilized with no additives.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

    • Synonyms

      Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    • Physical Appearance

      Pink lyophilized powder.

    • Stability

      Recombinant Holo Lactoferrin although stable at room temperature for 5 days, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized LTF Holo Human in sterile water at 10mg/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.

    Lactoferrin Holo Human
  • View Data Sheet

    Name :

    MAVS Human

    Description:

    Mitochondrial Antiviral Signaling Protein Human Recombinant

    CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

    Product # :

    PRO-1351

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    MAVS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 536 amino acids (1-513) and having a molecular mass of 55.9 kDa. MAVS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAVS solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitochondrial antiviral signaling protein (MAVS) is vital for innate immune defense against viruses. MAVS is an intermediary protein essential in the virus-triggered IFN-beta signaling pathways. MAVS is involved in activation of transcription factors that regulate expression of IFN-beta and contributes to antiviral immunity.

    • Synonyms

      CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

    • 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 MGSMPFAEDK TYKYICRNFS NFCNVDVVEI LPYLPCLTAR DQDRLRATCT LSGNRDTLWH LFNTLQRRPG WVEYFIAALR GCELVDLADE VASVYQSYQP RTSDRPPDPL EPPSLPAERP GPPTPAAAHS IPYNSCREKE PSYPMPVQET QAPESPGENS EQALQTLSPR AIPRNPDGGP LESSSDLAAL SPLTSSGHQE QDTELGSTHT AGATSSLTPS RGPVSPSVSF QPLARSTPRA SRLPGPTGSV VSTGTSFSSS SPGLASAGAA EGKQGAESDQ AEPIICSSGA EAPANSLPSK VPTTLMPVNT VALKVPANPA SVSTVPSKLP TSSKPPGAVP SNALTNPAPS KLPINSTRAG MVPSKVPTSM VLTKVSASTV PTDGSSRNEE TPAAPTPAGA TGGSSAWLDS SSENRGLGSE LSKPGVLASQ VDSPFSGCFE DLAISASTSL GMGPCHGPEE NEYKSEGTFG IHVAENPSIQ LLEGNPGPPA DPDGGPRPQA DRKFQEREVP CHRPSP.

    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.

    Mavs Human
  • View Data Sheet

    Name :

    CYTH3 Human

    Description:

    Cytohesin 3 Human Recombinant

    Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.

    Product # :

    PRO-1951

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    Description

    CYTH3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (1-399) and having a molecular mass of 48.7 kDa.CYTH3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CYTH3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Cytohesin 3 (CYTH3) belongs to the PSCD family, whose members have identical structural organization which consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain, and seem to mediate the regulation of protein sorting and membrane trafficking. CYTH3 is involved in the regulation of Golgi structure and function, and it might have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.

    • Synonyms

      Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.

    • 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 MGSMDEDGGG EGGGVPEDLS LEEREELLDI RRRKKELIDD IERLKYEIAE VMTEIDNLTS VEESKTTQRN KQIAMGRKKF NMDPKKGIQF LIENDLLQSS PEDVAQFLYK GEGLNKTVIG DYLGERDEFN IKVLQAFVEL HEFADLNLVQ ALRQFLWSFR LPGEAQKIDR MMEAFASRYC LCNPGVFQST DTCYVLSFAI IMLNTSLHNH NVRDKPTAER FIAMNRGINE GGDLPEELLR NLYESIKNEP FKIPEDDGND LTHTFFNPDR EGWLLKLGGR VKTWKRRWFI LTDNCLYYFE YTTDKEPRGI IPLENLSIRE VEDPRKPNCF ELYNPSHKGQ VIKACKTEAD GRVVEGNHVV YRISAPSPEE KEEWMKSIKA SISRDPFYDM LATRKRRIAN KK.

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    Cyth3 Human
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    Name :

    ART4 Human

    Description:

    ADP-Ribosyltransferase 4 Human Recombinant

    ARTC4, DOK1, CD297 Antigen, Dombrock Blood Group, ADP-Ribosyltransferase 4, Ecto-ADP-Ribosyltransferase 4.

    Product # :

    ENZ-1072

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    Description

    ART4 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 248 amino acids (47-285 a.a.) and having a molecular mass of 28.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). ART4 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ART4 protein solution (0.25mg/ml) contains Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Ecto-ADP-Ribosyltransferase 4 or ART4 is typed as a glycosylphosphatidylinositol (GPI)-linked membrane protein which carries Dombrock blood group antigens. The development of this protein takes place at the highest levels in the fetal liver. the process of the ART4 development is regulated while the erythroid differentiation process occurs. ART4 is a is part of the Ribosyltransferase family.

    • Synonyms

      ARTC4, DOK1, CD297 Antigen, Dombrock Blood Group, ADP-Ribosyltransferase 4, Ecto-ADP-Ribosyltransferase 4.

    • 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

      ADPSEVAIKI DFDFAPGSFD DQYQGCSKQV MEKLTQGDYF TKDIEAQKNY FRMWQKAHLA WLNQGKVLPQ NMTTTHAVAI LFYTLNSNVH SDFTRAMASV ARTPQQYERS FHFKYLHYYL TSAIQLLRKD SIMENGTLCY EVHYRTKDVH FNAYTGATIR FGQFLSTSLL KEEAQEFGNQ TLFTIFTCLG APVQYFSLKK EVLIPPYELF KVINMSYHPR GDWLQLRSTG NLSTYNCQLL KAHHHHHH.

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    Art4 Human
  • View Data Sheet

    Name :

    TNF a Human, His

    Description:

    Tumor Necrosis Factor-Alpha Human Recombinant, His Tag

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

    Product # :

    CYT-494

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    Description

    Tumor Necrosis Factor-α Human Recombinant His produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids fragment and having a molecular mass of 18.3kDa with an N-terminal hexahistidine tag. The TNF-alpha His is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.0.

    Purity

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

    Biological Activity

    The ED50 was determined in the presence of actinomycin D by a cytotoxicity assay using murine L929 cells is <0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107IU/mg.

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

    • Amino Acid Sequence

      MHHHHHHVRS SSRTPSDKPV AHVVANPQAE GQLQWLNRRA NALLANGVEL RDNQLVVPSE GLYLIYSQVL FKGQGCPSTH VLLTHTISRI AVSYQTKVNL LSAIKSPCQR ETPEGAEAKP WYEPIYLGGV FQLEKGDRLS AEINRPDYLD FAESGQVYFG IIAL.

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    Tnf Alpha Human His
  • View Data Sheet

    Name :

    TNF a Mutant Human

    Description:

    Tumor Necrosis Factor-Alpha Mutant Human Recombinant

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

    Product # :

    CYT-384

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    Description

    Tumor Necrosis Factor-a Variant Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 151 amino acids and having a molecular mass of 16598 Dalton. The TNF-alpha Variant is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized after extensive dialysis against 0.5x PBS pH -7.

    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 cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 units/mg.

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    • Introduction

      The clinical use of the potent anti-tumor activity of TNF-a has been limited by the proinflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-a mutants with low systemic toxicity has been an intense pharmacological interest. Human TNF-a, which binds to the murine TNF-R55 but not to the mouse TNF-R75, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-a, which binds to both murine TNF receptors. Based on these results, many TNF-? mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro, and exhibited lower systemic toxicity in vivo.
      Recombinant Human TNF-a Variant/Mutant compared with the wild-type, has an amino acid sequence deletion from a.a. 1-7, and the following a.a. substitutes Arg8, Lys9, Arg10 and Phe157 which is proven tohave more activity and with less inflammatory side effect in vivo.

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

    • Amino Acid Sequence

      MRKRKPVAHV VANPQAEGQL QWLNRRANAL LANGVELRDN
      QLVVPSEGLY LIYSQVLFKG QGCPSTHVLL THTISRIAVS YQTKVNLLSA IKSPCQRETP EGAEAKPWYE PIYLGGVFQL EKGDRLSAEI NRPDYLDFAE SGQVYFGIIAF.

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    Tnf Alpha Mutant Human
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    Name :

    TNFSF8 Human, Sf9

    Description:

    CD30 Ligand Human Recombinant, Sf9

    Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.

    Product # :

    CYT-954

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    Description

    TNFSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 181 amino acids (63-234a.a.) and having a molecular mass of 20.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). TNFSF8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.

    • Synonyms

      Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.

    • 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

      ADPQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSDHHHHH H.

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    Tnfsf8 Human Sf9
  • View Data Sheet

    Name :

    NKIRAS2 Human

    Description:

    NFKB Inhibitor Interacting Ras-Like 2 Human Recombinant

    NF-kappa-B inhibitor-interacting Ras-like protein 2, I-kappa-B-interacting Ras-like protein 2, Kappa B-Ras protein 2, KappaB-Ras2, NKIRAS2, KBRAS2.

    Product # :

    PRO-1091

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    Description

    NKIRAS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids (1-191 a.a) and having a molecular mass of 24kDa.NKIRAS2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NKIRAS2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      NFKB inhibitor interacting Ras-like 2 (NKIRAS2) is an inhibitor of the transcription factor NF-kappaB. NKIRAS2 is similar to the Ras-like small GTPases which associate with IkappaB. The Ras-like proteins- NKIRAS1 and NKIRAS2, interact with the PEST domains of I?B? and I?B? and reduce their rate of degradation. NKIRAS2 is an atypical Ras-like protein which functions as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more impervious to degradation.

    • Synonyms

      NF-kappa-B inhibitor-interacting Ras-like protein 2, I-kappa-B-interacting Ras-like protein 2, Kappa B-Ras protein 2, KappaB-Ras2, NKIRAS2, KBRAS2.

    • 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 MGSHMGKSCK VVVCGQASVG KTSILEQLLY GNHVVGSEMI ETQEDIYVGS IETDRGVREQ VRFYDTRGLR DGAELPRHCF SCTDGYVLVY STDSRESFQR VELLKKEIDK SKDKKEVTIV VLGNKCDLQE QRRVDPDVAQ HWAKSEKVKL WEVSVADRRS
      LLEPFVYLAS KMTQPQSKSA FPLSRKNKGS GSLDG.

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    Nkiras2 Human
  • View Data Sheet

    Name :

    FGFR1OP Human (1-80)

    Description:

    FGFR1 Oncogene Partner (1-80 a.a.) Human Recombinant

    FGFR1 oncogene partner, FGFR1OP, FOP.

    Product # :

    PKA-138

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    Description

    The FGFR1O PHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FGFR1OP His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 80 amino acid residues of the FGFR1OP Human, 1-80 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.

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    • Synonyms

      FGFR1 oncogene partner, FGFR1OP, FOP.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized FGFR1OP at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/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.

    • Amino Acid Sequence

      L MAATAAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE SLRKFLNTKD GRLVASLVA

    • Background

      FGFR1 oncogene partner also known as FGFR1OP is a leucine-rich member of the FGFR1OP family. The ensuing chimeric protein contains the N-terminal leucine-rich region of the FGFR1OP protein fused to the catalytic domain of FGFR1. The FGFR1OP plays a main role in normal proliferation and differentiation of the erythroid lineage.

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    Fgfr1Op Protein
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    Name :

    SARS Nucleocapsid Monoclonal

    Description:

    SARS-Nucleocapsid, Monoclonal Antibody

    Product # :

    ANT-759

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    Formulation

    Lyophilized from 1mg/ml in PBS

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    • Introduction

      SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SARS-Nucleocapsid Monoclonal Antibody although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution store at 4°C between 2-7 days and for future use below -18°C.Please avoid freeze thaw cycles.

    • Solubility

      Reconstitute Mouse Anti SARS Nucleocapsid antibody at a conc. of 0.5mg/ml in sterile PBS.

    • Immunogen

      SARS Antibody was developed by immunizing mice with a protein fragment amino acids 1-49 from the human SARS Nucleocapsid coronavirus (Genbank accession no. NP_828858). SARS-Nucleocapsid, Monoclonal Antibody is protein-G purified.

    • Applications

      Western Blot 1:1000, ELISA, Immunocytochemistry/Immunofluorescence.

      SARS-Nucleocapsid, Monoclonal Antibody detects CoV-2 & SARS Coronavirus Nucleoprotein in direct ELISA. S-Species cross reactivity based on immunogen sequence homology: COV-2 (84%)

    • Type

      Mouse antibody Monoclonal.

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    Anti Sars Nucleocapsid
  • View Data Sheet

    Name :

    BRMS1 Human

    Description:

    Breast Cancer Metastasis Suppressor 1 Human Recombinant

    Breast Cancer Metastasis Suppressor 1.

    Product # :

    PRO-1828

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    Description

    BRMS1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 261 amino acids (1-246) and having a molecular mass of 29.9 kDa. BRMS1 is fused to a 15 amino acid T7-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The BRMS1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

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    • Introduction

      BRMS1 protein, a member of the mSin3a family of HDAC (histone deacetylase complexes), is mainly restricted to the nucleus. BRMS1 holds two coiled-coil motifs and a few imperfect leucine zipper motifs. BRMS1 reduces the metastatic potential, but not the tumorogenicity, of melanoma cell lines and human breast cancer. Alternative splicing creates two transcript variants encoding different isoforms.

    • Synonyms

      Breast Cancer Metastasis Suppressor 1.

    • 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

      MASMTGGQQM GRGSHMPVQP PSKDTEEMEA EGDSAAEMNG EEEESEEERS GSQTESEEES SEMDDEDYER RRSECVSEML DLEKQFSELK EKLFRERLSQ LRLRLEEVGA ERAPEYTEPL GGLQRSLKIR IQVAGIYKGF CLDVIRNKYE CELQGAKQHL ESEKLLLYDT LQGELQERIQ RLEEDRQSLD LSSEWWDDKL HARGSSRSWD SLPPSKRKKA PLVSGPYIVY MLQEIDILED WTAIKKARAA VSPQKRKSDG P

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    Brms1 Human
  • View Data Sheet

    Name :

    Exodus-2 Mouse, Sf9

    Description:

    Exodus-2 (CCL21) Mouse Recombinant, Sf9

    Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    Product # :

    CHM-043

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    Description

    Exodus-2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (24-133aa) and having a molecular mass of 13.1kDa.Exodus-2 is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Exodus-2 solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Exodus-2 protein or CCL21 is a cytokine, part of the CC chemokines subgroup. Because of its 6 conserved residues of the cysteine amino acid (instead of the 4 residues we usually see in chemokines), the protein is also named 6Ckine and SLC (secondary lymphoid-tissue chemokine). The gene that codes for this protein is located on chromosome 9 in humans. The Exodus-2 is binding to the CCR7 receptor, which is a chemokine receptor located to the cell’s surface.

    • Synonyms

      Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    • 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

      ADPSDGGGQD CCLKYSQKKI PYSIVRGYRK QEPSLGCPIP AILFSPRKHS KPELCANPEE GWVQNLMRRL DQPPAPGKQS PGCRKNRGTS KSGKKGKGSK GCKRTEQTQP SRGHHHHHH

    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.

    Exodus 2 Mouse
  • View Data Sheet

    Name :

    ProNGF Human

    Description:

    Pro-Nerve Growth Factor Human Recombinant

    Human Pro-NGF, ProNGF, NGFB.

    Product # :

    CYT-426

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    Description

    Pro-NGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 25 kDa.ProNGF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ProNGF was lyophilized from a 0.2 μM filtered solution of 20m Tris-HCL, 0.5M NaCl, 5% Trehalose, 5% Mannitol. 0.01% Tween-80 and 1mM EDTA pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Human Pro-NGF, ProNGF, NGFB.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ProNGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProNGF 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 ProNGF in distilled water to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
      TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
      SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
      KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
      VCVLSRKAVRRA.

    • Background

      Pro-Nerve Growth Factor Human Recombinant: Unveiling its Potential in Neuroregulation and Disease Pathogenesis

      Abstract:

      Pro-Nerve Growth Factor (Pro-NGF) human recombinant is a crucial precursor protein involved in neuronal development, survival, and degenerative processes. This research paper aims to provide a comprehensive analysis of Pro-NGF, including its characteristics, processing mechanisms, and implications in neuroregulation and disease pathogenesis. Additionally, innovative methodologies for the production and manipulation of Pro-NGF human recombinant are proposed, highlighting its potential as a therapeutic target for neurological disorders and neurodegenerative diseases.

      Introduction:

      Neuroregulation and maintenance of neuronal health are intricate processes governed by a network of signaling molecules. Pro-NGF, the precursor form of Nerve Growth Factor (NGF), acts as a key player in neuronal development, synaptic plasticity, and cell survival. This paper delves into the distinctive features of Pro-NGF and presents novel approaches for the production and manipulation of Pro-NGF human recombinant, aiming to unravel its role in neuroregulation and disease pathogenesis.

      Characteristics and Processing Mechanisms:

      Pro-NGF is initially synthesized as an inactive precursor, requiring proteolytic cleavage for conversion into mature NGF. The processing of Pro-NGF involves the action of proteases, such as furin, and the formation of distinct protein complexes. The balance between Pro-NGF and mature NGF levels plays a critical role in modulating neuronal function and fate, influencing processes such as neuronal survival, axonal growth, and synaptic plasticity.

      Production and Manipulation of Pro-NGF Human Recombinant:

      Efficient production methodologies and manipulation strategies are crucial for studying the role of Pro-NGF in neuroregulation and disease pathogenesis. Recombinant protein expression systems, including mammalian cell culture and bacterial expression systems, have been employed to produce functional Pro-NGF human recombinant. Techniques such as mutagenesis, protein purification, and specific inhibitors targeting Pro-NGF processing pathways enable the manipulation of Pro-NGF levels and investigation of its downstream effects.

      Implications in Neuroregulation and Disease Pathogenesis:

      Pro-NGF human recombinant holds significant potential in understanding the intricate mechanisms underlying neuroregulation and disease pathogenesis. Dysregulation of Pro-NGF processing and altered Pro-NGF/mature NGF ratios have been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and ischemic stroke. Manipulating Pro-NGF levels and the balance between its mature form may offer therapeutic strategies for modulating neurotrophic signaling and promoting neuronal health in these conditions.

      Conclusion:

      Pro-NGF human recombinant emerges as a key regulator in neuroregulation and disease pathogenesis, offering promising avenues for therapeutic intervention. Enhancing our understanding of Pro-NGF processing mechanisms and its downstream signaling cascades will provide valuable insights into neurodevelopment, neurodegeneration, and potential therapeutic strategies. Targeting Pro-NGF as a therapeutic intervention may hold immense promise in treating neurological disorders and promoting neuronal health.

      What is the molecular weight / Mw of ProNGF Protein?
      ProNGF Protein has a total Mw of 25kDa.

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

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


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

      What is the amino acid sequence of ProNGF Protein?
      MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
      TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
      SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
      KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
      VCVLSRKAVRRA

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

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

    Pro Ngf 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 :

    PPARG Human (1-477)

    Description:

    Peroxisome Proliferator Activated Receptor Gamma Human Recombinant, (1-477 a.a)

    Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.

    Product # :

    PKA-334

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    Description

    PPARG Human Recombinant encoding amino acids 1-477 expressed in E.coli, is fused to a GST tag and it is antibody reactive.The PPARG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPARG at 0.1mg/ml in 50mM Tris-HCl and 10mM L-glutathione (reduced).

    More Info

    • Introduction

      Peroxisome proliferators are non-genotoxic carcinogens which are purported to exert their effect on cells through their interaction with members of the nuclear hormone receptor family termed peroxisome proliferators activated receptors (PPARs). Nuclear hormone receptors are ligand-dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate ligand. Studies indicate that PPARs are activated by peroxisome proliferators such as clofibric acid, nafenopin, and WY-14,643, as well as by some fatty acids.

    • Synonyms

      Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Avoid multiple freeze-thaw cycles.

    • Applications

      ELISA.
      Inhibition Assays.
      Western Blotting.

    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.

    Pparg Human 477 Aa
  • View Data Sheet

    Name :

    SCF Human, Sf9

    Description:

    Stem Cell Factor Human Recombinant, Sf9

    Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.

    Product # :

    CYT-421

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    Description

    Stem Cell Factor Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18409 Dalton. The SCF is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect Cells.

    Formulation

    The protein is supplied in 1xPBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of Human TF-1 cells is typically 1-5 ng/ml.

    More Info

    • Introduction

      Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
      SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).

    • Synonyms

      Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 Stem Cell Factor in 10mM acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.52 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 standard solution of Stem Cell Factor 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.

    Scf Human Sf9
  • View Data Sheet

    Name :

    CLCF1 Human

    Description:

    Neurotrophin-1 Human Recombinant

    Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.

    Product # :

    CYT-869

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    Description

    Neurotrophin-1 Human Recombinant (28-225) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 199 amino acids and having a molecular mass of 22kDa.The NNT-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NNT-1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.

    More Info

    • Introduction

      Cardiotrophin-like cytokine (CLC/ NNT-1) belongs to the IL-6 family of cytokines. All family members share the receptor subunit gp130, which belongs to the type I cytokine receptor superfamily. NNT1 is a trophic factor for motor neurons, a stimulator of ACTH release from corticotrophs, and an inducer of IgE synthesis and B cell proliferation. Cells expressing NNT-1 include embryonic muscle, lung epithelium, and mesenchyme. NNT1 binds to and activates the ILST/gp130 receptor.

    • Synonyms

      Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Neurotrophin-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NNT1 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 NNT1 in sterile 18M-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

    • Background

      What is the molecular weight/Mw of CLCF Protein?
      CLCF Protein has a total Mw of 22kDa.

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

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

      What is the Biological Activity of CLCF Protein?
      The ED50, as measured in a cell proliferation assay using human TF?1 cells transfected with human CNTF R?, is less than 15ng/ml.

      What is the amino acid sequence of CLCF Protein?
      MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

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

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

    Nnt1 Human
  • View Data Sheet

    Name :

    NT 3 Mouse

    Description:

    Neurotrophin-3 Mouse Recombinant

    Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.

    Product # :

    CYT-688

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    Description

    Neurotrophin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids and having a molecular mass of 13.6kDa. The NT-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 0.02% TFA.

    Purity

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

    Biological Activity

    The activity, as determined by the dose-dependent proliferation of BaF3 cells transfected with the TrkB receptor, is typically in the range of 1-10 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

    More Info

    • Introduction

      NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.

    • Synonyms

      Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      YAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

    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.

    Neurotrophin 3 Mouse
  • View Data Sheet

    Name :

    NTRK3 Mouse

    Description:

    Neurotrophic Receptor Tyrosine Kinase 3 Mouse Recombinant

    NT-3 growth factor receptor, GP145-TrkC, Trk-C, Neurotrophic tyrosine kinase receptor type 3, TrkC tyrosine kinase, Ntrk3, TrkC, AW125844, Ntrk3_tv3

    Product # :

    CYT-1163

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    Description

    NTRK3 Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 404 amino acids (32-429 aa) and having a molecular mass of 45.4kDa.NTRK3 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NTRK3 protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neurotrophic Receptor Tyrosine Kinase 3 (NTRK3)belongs to the receptor tyrosine kinases family and is a high affinity catalytic receptor of neurotrophin NT-3. NTRK3 mediates multiple effects of this neurotrophic factor, which includes neuronal differentiation and survival. NTRK3 inducesvarious pleiotorpic responses in malignant cells, including enhanced tumor cell invasiveness and chemotoxis.Increased NTRK3 expression was observed in neuroblastoma, medulloblastoma, and in neuroectodermal brain tumors.

    • Synonyms

      NT-3 growth factor receptor, GP145-TrkC, Trk-C, Neurotrophic tyrosine kinase receptor type 3, TrkC tyrosine kinase, Ntrk3, TrkC, AW125844, Ntrk3_tv3

    • 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

      CPANCVCSKT EINCRRPDDG NLFPLLEGQD SGNSNGNASI NITDISRNIT SIHIENWRGL HTLNAVDMEL YTGLQKLTIK NSGLRNIQPR AFAKNPHLRY INLSSNRLTT LSWQLFQTLS LRELRLEQNF FNCSCDIRWM QLWQEQGEAR LDSQSLYCIS ADGSQLPLFR MNISQCDLPE ISVSHVNLTV REGDNAVITC NGSGSPLPDV DWIVTGLQSI NTHQTNLNWT NVHAINLTLV NVTSEDNGFT LTCIAENVVG MSNASVALTV YYPPRVVSLV EPEVRLEHCI EFVVRGNPTP TLHWLYNGQP LRESKIIHMD YYQEGEVSEG CLLFNKPTHY NNGNYTLIAK NALGTANQTI NGHFLKEPFP ESTDFFDFES DASPTPPITV THKPEEDTHH 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.

    Ntrk3 Mouse
  • View Data Sheet

    Name :

    SSX1 Human

    Description:

    Synovial Sarcoma, X Breakpoint 1 Human Recombinant

    Synovial Sarcoma X Breakpoint 1, Cancer/Testis Antigen 5.1, CT5.1, SSRC Sarcoma Synovial X-Chromosome-Related 1, Cancer/Testis Antigen Family 5 Member 1, Cancer/Testis Antigen Family 5, Protein SSX1, Member 1, SSX1.

    Product # :

    PRO-1379

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    Description

    SSX1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (1-188 a.a) and having a molecular mass of 24.3kDa.SSX1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SSX1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Synovial Sarcoma, X Breakpoint 1 (SSX1) is a member of a family of highly homologous synovial sarcoma X (SSX) breakpoint proteins. SSX proteins are localized to the nucleus and expressed in testis and some types of cancers and, hence, they are classified as C/T (cancer/testis) antigens. These proteins may serve as transcriptional repressors. SSX1 genes are involved in the t (X;18) translocation typically found in all synovial sarcomas. This translocation leads to the fusion of the synovial sarcoma translocation gene on chromosome 18 to one of the SSX genes on chromosome X. These hybrid proteins are most likely responsible for transforming activity.

    • Synonyms

      Synovial Sarcoma X Breakpoint 1, Cancer/Testis Antigen 5.1, CT5.1, SSRC Sarcoma Synovial X-Chromosome-Related 1, Cancer/Testis Antigen Family 5 Member 1, Cancer/Testis Antigen Family 5, Protein SSX1, Member 1, SSX1.

    • 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 MGSMNGDDTF AKRPRDDAKA SEKRSKAFDD IATYFSKKEW KKMKYSEKIS YVYMKRNYKA MTKLGFKVTL PPFMCNKQAT DFQGNDFDND HNRRIQVEHP QMTFGRLHRI IPKIMPKKPA EDENDSKGVS EASGPQNDGK QLHPPGKANI SEKINKRSGP KRGKHAWTHR LRERKQLVIY EEISDPEEDD E.

    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.

    Ssx1 Human
  • View Data Sheet

    Name :

    TACI Human, Sf9

    Description:

    Tumor Necrosis Factor Receptor 13B Human Recombinant, Sf9

    Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.

    Product # :

    CYT-982

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TACI produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 407 amino acids (1-165a.a.) and having a molecular mass of 45.8kDa (Molecular size on SDS-PAGE will appear at approximately 25-50kDa). TACI is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    TACI a protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.

    • 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

      ADLMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYSLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

    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.

    Taci Human Sf9
  • View Data Sheet

    Name :

    GMFB Mouse

    Description:

    Glia Maturation Factor Beta Mouse Recombinant

    Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.

    Product # :

    CYT-006

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    Shipped at Room temp

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    Description

    Glia Maturation Factor-Beta (GMF-Beta) Mouse Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.6kDa. GMF-Beta, Mouse Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GMF-beta protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.

    • Synonyms

      Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
      VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
      MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.

    • Background

      What is the molecular weight/Mw of GMFB MOUSE Protein?
      GMFB MOUSE Protein has a total Mw of 16.6kDa.

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

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

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

      What is the amino acid sequence of GMFB MOUSE Protein?
      SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
      VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
      MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.

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

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

    Gmfb Mouse
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