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Search results

1000 results found for “tubulin gamma”

Name

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  • View Data Sheet

    Name :

    TNFA Rat, His Active

    Description:

    Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active

    Tumor Necrosis Factor-alpha, TNF a His,  Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

    Product # :

    CYT-1057

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    Description

    TNFA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235 a.a) and having a molecular mass of 19.9kDa.TNFA Rat is expressed with an 25 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFA Rat protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D.
    The ED50 for this effect is ≤ to 0.2 ng/ml.

    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

      Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

    • Physical Appearance

      Sterile Filtered colorless liquid.

    • 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 MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.

    • Background

      Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active: An In-Depth Analysis

      Abstract:


      Tumor Necrosis Factor-alpha (TNF-α) is a cytokine that plays a significant role in various physiological and pathological processes. This human research paper provides an in-depth analysis of TNF-α Rat Recombinant with a His Tag, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the potential applications of TNF-α Rat Recombinant in human research.

      Introduction:


      TNF-α is a key mediator of inflammation and immune responses in humans. This research paper aims to provide a comprehensive analysis of TNF-α Rat Recombinant with a His Tag, highlighting its significance in human physiology and its potential applications in human research.

      Structure and Function of TNF-α:


      TNF-α is a homotrimeric protein that binds to two distinct receptors, TNFR1 and TNFR2, initiating downstream signaling cascades. It regulates immune cell activation, cytokine production, and cellular responses, influencing diverse biological processes.

      Signaling Pathways:


      Upon binding to its receptors, TNF-α activates various signaling pathways, including the NF-κB pathway, MAPK pathway, and cell death pathways. These pathways regulate gene expression and mediate cellular responses, impacting inflammation, apoptosis, and tissue homeostasis.

      Functions of TNF-α:


      TNF-α plays a crucial role in immune responses, inflammation, and tissue homeostasis. It regulates the activation and migration of immune cells, promotes cytokine production, and modulates cell survival and death. Dysregulation of TNF-α is implicated in the pathogenesis of various human diseases, making it an attractive target for research and therapeutic interventions.

      Applications in Human Research:


      TNF-α Rat Recombinant with a His Tag has diverse applications in human research. It can be used to investigate TNF-α signaling pathways, study its effects on immune cell functions, and explore its role in disease pathogenesis. Additionally, this recombinant protein can be utilized for in vitro and in vivo studies aimed at developing novel therapeutic strategies.

      Future Directions:


      Further research is necessary to unravel the intricate mechanisms of TNF-α signaling and its contributions to human diseases. Continued investigations will enable the development of targeted therapies and personalized medicine approaches. Future studies should also focus on optimizing the use of TNF-α Rat Recombinant in preclinical and clinical research settings.

    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.

    Tnfa Rat 2
  • View Data Sheet

    Name :

    GLUL Human, His Active

    Description:

    Glutamine Synthetase Human Recombinant, His Active

    GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    Product # :

    ENZ-984

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    Description

    GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLUL Human solution containing 20mM Tris-HCl pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,800 pmol/min/ug, and is defined as the amount of enzyme that convert 1.0 pmole of L-glutamate to L-glutamine per miunte at pH 7.5 at 37C in coupled system with PK/LDH.

    More Info

    • Introduction

      GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

    • Synonyms

      GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    • 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 MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.

    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.

    Glul Human His Active
  • View Data Sheet

    Name :

    GNAI1 Human

    Description:

    Guanine Nucleotide Binding Protein Alpha Inhibiting Activity 1 Human Recombinant

    Guanine nucleotide-binding protein G(i) subunit alpha-1, Adenylate cyclase-inhibiting G alpha protein, GNAI1, Gi.

    Product # :

    PRO-940

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    Description

    GNAI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 377 amino acids (1-354 a.a.) and having a molecular mass of 42.7kDa.GNAI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GNAI1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Guanine nucleotide binding proteins are heterotrimeric signal-transducing molecules comprising alpha, beta, and gamma subunits. GNAI1 represents the alpha subunit of an inhibitory complex. Guanine nucleotide-binding protein G(i) subunit alpha (GNAI1) functions to transmit information from cell surface receptors to intracellular effectors. GNAI1 binds guanine nucleotide, can hydrolyze GTP, and can interact with other proteins. GNAI1 is part of a complex that responds to beta-adrenergic signals by inhibiting adenylate cyclase. In addition, GNAI1 functions to open atrial potassium channels.

    • Synonyms

      Guanine nucleotide-binding protein G(i) subunit alpha-1, Adenylate cyclase-inhibiting G alpha protein, GNAI1, Gi.

    • 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 MGSMGCTLSA EDKAAVERSK MIDRNLREDG EKAAREVKLL LLGAGESGKS TIVKQMKIIH EAGYSEEECK QYKAVVYSNT IQSIIAIIRA MGRLKIDFGD SARADDARQL FVLAGAAEEG FMTAELAGVI KRLWKDSGVQ ACFNRSREYQ LNDSAAYYLN DLDRIAQPNY IPTQQDVLRT RVKTTGIVET HFTFKDLHFK MFDVGGQRSE RKKWIHCFEG VTAIIFCVAL SDYDLVLAED EEMNRMHESM KLFDSICNNK WFTDTSIILF LNKKDLFEEK IKKSPLTICY PEYAGSNTYE EAAAYIQCQF EDLNKRKDTK EIYTHFTCAT DTKNVQFVFD AVTDVIIKNN LKDCGLF.

    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.

    Gnai1 Human
  • View Data Sheet

    Name :

    LYG2 Human

    Description:

    Lysozyme G-Like 2 Human Recombinant

    Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.

    Product # :

    PRO-1245

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    Description

    LYG2 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (20-212) and having a molecular mass of 23.9 kDa. LYG2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The LYG2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      lysozyme G-like 2 and LYGH (LYG2), is a member of the glycosyl hydrolase 23 family. Lysozyme takes part in human innate immunity by causing bacterial cell lysis. LYG2 contains a SLT domain, a protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc).

    • Synonyms

      Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSSYPFSHS MKPHLHPRLY HGCYGDIMTM KTSGATCDAN SVMNCGIRGS EMFAEMDLRA IKPYQTLIKE VGQRHCVDPA VIAAIISRES HGGSVLQDGW DHRGLKFGLM QLDKQTYHPV GAWDSKEHLS QATGILTERI KAIQKKFPTW SVAQHLKGGL SAFKSGIEAI ATPSDIDNDF VNDIIARAKF YKRQSF.

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    Lyg2 Human
  • View Data Sheet

    Name :

    SNCA A30P/A53T Human

    Description:

    Alpha Synuclein A30P/A53T Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-160

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    Description

    A-Synuclein A30P/A53T Human Recombinant which is a Parkinson’s disease-related double mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.5kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A30P/A53T is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA A30P/A53T protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAP GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.

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    Snca A30P A53T Human
  • View Data Sheet

    Name :

    TAC3 Human

    Description:

    Tachykinin-3 Human Recombinant

    Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.

    Product # :

    PRO-716

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    Description

    TAC3 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (17-121 a.a.) and having a molecular mass of 13.8kDa.The TAC3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TAC3 solution contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Tachykinin-3 belongs to the substance P-related tachykinin family. Tachykinins are active peptides that stimulate neurons, induce behavioral responses, are effective vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. TAC3 and its receptor are essential switches of regulator of human puberty, regulated by the brain through the release of the GnRH which starts a chain of processes which eventually lead to the production of sex hormones.
      During pregnancy, the expression of TAC3 is restricted to the outer syncytiotrophoblast of the placenta, significant concentrations of TAC3 can be identified in plasma as early as week 9, and plasma concentrations of TAC3 are grossly elevated in pregnancy-induced hypertension and pre-eclampsia. Higher Tachykinin-3 concentrations in normotensive pregnant women may be caused by the advanced gestational age and/or the result of a negative interaction of other vasoactive substances. TAC3 has a role in the continuance of high placental blood flow in normal pregnancy.

    • Synonyms

      Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.

    • 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 QSFGAVCKEP QEEVVPGGGR SKRDPDLYQL LQRLFKSHSS LEGLLKALSQ ASTDPKESTS PEKRDMHDFF VGLMGKRSVQ PDSPTDVNQE NVPSFGILKY PPRAE.

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    Tac3 Human
  • View Data Sheet

    Name :

    GLUL Human

    Description:

    Glutamine Synthetase Human Recombinant

    GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    Product # :

    ENZ-544

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    Description

    GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLUL Human solution containing 20mM Tris-HCl pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

    • Synonyms

      GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    • 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 MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.

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    Glul Human
  • View Data Sheet

    Name :

    Thyroglobulin Human

    Description:

    Thyroglobulin Human Recombinant

    Thyroglobulin, TGN, AITD3, TG.

    Product # :

    PRO-2803

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    • sds-page

    Description

    Thyroglobulin Human produced in a mammalian cell line is a single, non-glycosylated polypeptide chain (1-2768 a.a.) and having a molecular mass of 304640 Dalton. Thyroglobulin Human is fused with GlyAlaProGly4SerHis10-tag at C-terminal and purified by proprietary chromatographic techniques.

    Source

    Mammalian cell line.

    Formulation

    Thyroglobulin was lyophilized from PBS, pH 7.4 and 5.4 % sucrose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    Thyroglobulin Recombinant Human SDS-PAGE - Product image 1

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    • Synonyms

      Thyroglobulin, TGN, AITD3, TG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Thyroglobulin, a glycoprotein primarily produced in the thyroid gland, stands at the center of thyroid hormone synthesis. Comprising a series of tyrosine residues, thyroglobulin serves as the scaffold upon which thyroid hormones are assembled. Beyond its pivotal role in thyroid physiology, thyroglobulin has garnered significant attention in the realm of thyroid disease diagnostics, offering valuable insights into thyroid function and disorders. This research delves into the intricacies of thyroglobulin human recombinant protein, exploring its biochemical properties, physiological significance, and its crucial applications in both clinical and research settings.

      Structural Complexity of Thyroglobulin:

      Thyroglobulin is a large, dimeric protein boasting an intricate structure composed of multiple domains. Within its structure lie tyrosine residues crucial for iodine incorporation, a process fundamental for thyroid hormone synthesis. Its size and complexity reflect the sophistication of thyroid hormone production, as thyroglobulin acts as a reservoir for thyroid hormones within the thyroid follicles.

      Physiological Significance in Thyroid Function:

      Thyroglobulin plays a central role in the synthesis of triiodothyronine (T3) and thyroxine (T4), the thyroid hormones essential for regulating metabolism and overall body homeostasis. During thyroid hormone synthesis, thyroglobulin is secreted into the follicular lumen, where it undergoes iodination and subsequent proteolysis, releasing T3 and T4. This process highlights the indispensable nature of thyroglobulin in thyroid hormone production, making it a key biomolecule in thyroid physiology.

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    Thyroglobulin Antigen
  • View Data Sheet

    Name :

    CD116 Human, sf9

    Description:

    GM-CSF Receptor Alpha Sf9 Human Recombinant

    Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX,  GMCSFR, CD116, SMDP4, GMR.                  

    Product # :

    CYT-1044

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    Description

    CSF2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 310 amino acids (20-320a.a.) and having a molecular mass of 35.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CSF2RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CSF2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

    More Info

    • Introduction

      GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.

    • Synonyms

      Colony Stimulating Factor 2 Receptor Alpha Subunit, Colony Stimulating Factor 2 Receptor, Alpha, Low-Affinity (Granulocyte-Macrophage), Alpha-GM-CSF Receptor, GM-CSF-R-Alpha, CD116 Antigen, GMCSFR-Alpha, GMR-Alpha, CDw116, CSF2RY, CSF2R, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, GM-CSF Receptor Alpha Subunit, AlphaGMR, CSF2RAX, CSF2RAY, CSF2RX, GMCSFR, CD116, SMDP4, GMR.

    • 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

      ADPLIPEKSD LRTVAPASSL NVRFDSRTMN LSWDCQENTT FSKCFLTDKK NRVVEPRLSN NECSCTFREI CLHEGVTFEV HVNTSQRGFQ QKLLYPNSGR EGTAAQNFSC FIYNADLMNC TWARGPTAPR DVQYFLYIRN SKRRREIRCP YYIQDSGTHV GCHLDNLSGL TSRNYFLVNG TSREIGIQFF DSLLDTKKIE RFNPPSNVTV RCNTTHCLVR WKQPRTYQKL SYLDFQYQLD VHRKNTQPGT ENLLINVSGD LENRYNFPSS EPRAKHSVKI RAADVRILNW SSWSEAIEFG SDDGHHHHHH

    • Background

      GM-CSF Receptor Alpha Human Recombinant: A Glimpse into Its Potential and Implications

      Abstract:

      Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) receptor alpha, a pivotal component in the GM-CSF signaling pathway, has been the focal point of numerous studies pertaining to hematopoiesis and immune responses. This paper provides an overview of the GM-CSF receptor alpha human recombinant, exploring its characteristics, production techniques, and potential therapeutic applications.

      Introduction

      GM-CSF, a cytokine responsible for the differentiation and proliferation of white blood cells, functions by binding to its receptor, GM-CSF receptor. The alpha subunit (GM-CSFRα) of this receptor plays a crucial role in ligand binding and is essential for initiating cellular responses. Modern biotechnological advancements have led to the successful production of its human recombinant form, offering new avenues in medical research.

      Recombinant GM-CSFRα:

      Production and Features Recombinant GM-CSFRα is synthesized using cutting-edge recombinant DNA technologies, predominantly in bacterial or mammalian expression systems. This human recombinant form retains its ability to bind to GM-CSF, maintaining its biological functionality and providing myriad research opportunities.

      Therapeutic and Clinical Prospects

      1. Autoimmune Diseases: GM-CSF is often overexpressed in various autoimmune disorders. By utilizing recombinant GM-CSFRα as a potential decoy receptor, it's feasible to mitigate the effects of excessive GM-CSF, offering a new therapeutic strategy.
      2. Hematopoietic Disorders: Given its integral role in white blood cell development, recombinant GM-CSFRα might hold promise in treatments or as a diagnostic tool for certain hematological conditions.
      3. Research Paradigm: Beyond therapeutic applications, the recombinant GM-CSFRα can serve as an invaluable research tool to elucidate the nuances of GM-CSF signaling, aiding in the understanding of immune response mechanisms.

      Conclusion:

      GM-CSF receptor alpha human recombinant stands at the forefront of exciting research and therapeutic potential. While its full capabilities are yet to be realized, current insights underscore its significance in the realms of immunology and medicine.

      What is the molecular weight/Mw of CD116 Protein?
      CD116 Protein has a total Mw of 35.9kDa.

      What is the source or expression system of CD116 Protein?
      Sf9, Baculovirus cells.
      What is the Purity of CD116 Protein?
      CD116 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD116 Protein?
      Measured by its ability to inhibit GM-CSF dependent proliferation of TF1 human erythroleukemic cells. The ED50 for this effect is less or equal to 10ug/ml in the presence of 0.5ng/ml GM-CSF.

      What is the amino acid sequence of CD116 Protein?
      CD116 Protein is composed from 310 amino acids.

      What applications can CD116 Protein be used in?
      CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD116 Protein?
      The endotoxin level is minimal, CD116 Protein was purified using conventional chromatography techniques

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    Gmcsf Receptor
  • View Data Sheet

    Name :

    HMGA2 Human

    Description:

    High Mobility Group AT-Hook 2 Human Recombinant

    High Mobility Group AT-Hook 2, HMGIC, High-Mobility Group (Nonhistone Chromosomal) Protein Isoform I-C, High Mobility Group AT-Hook Protein, BABL, HMGI-C, LIPO, STQTL9, High Mobility Group Protein HMGI-C, HMGA2.

    Product # :

    PRO-1469

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    Description

    HMGA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (1-109 a.a) and having a molecular mass of 12.8kDa.HMGA2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HMGA2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 250mM Imidazole.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

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    • Introduction

      High Mobility Group AT-Hook 2 (HMGA2) is a member of the non-histone chromosomal high mobility group (HMG) family. HMG proteins perform as architectural factors and are necessary components of the enhancesome. Thisprotein contains structural DNA-binding domains and may function as a transcriptional regulating factor. In addition, identification ofthe deletion, amplification, and rearrangement of this gene that are associated with myxoid liposarcoma proposes arole in adipogenesis and mesenchymal differentiation. A gene knock out study of the mouse counterpartdemonstrated that this gene is implicated in diet-induced obesit.Among the Diseases associated with HMGA2 are diffuse lipomatosis, and 12q14 microdeletion syndrome.

    • Synonyms

      High Mobility Group AT-Hook 2, HMGIC, High-Mobility Group (Nonhistone Chromosomal) Protein Isoform I-C, High Mobility Group AT-Hook Protein, BABL, HMGI-C, LIPO, STQTL9, High Mobility Group Protein HMGI-C, HMGA2.

    • 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

      MSARGEGAGQ PSTSAQGQPA APAPQKRGRG RPRKQQQEPT GEPSPKRPRG RPKGSKNKSP SKAAQKKAEA TGEKRPRGRP RKWPQQVVQK KPAQEETEET SSQESAEEDL EHHHHHH.

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    Hmga2 Human
  • View Data Sheet

    Name :

    SKA1 Human

    Description:

    Spindle And Kinetochore Associated Complex Subunit 1 Human Recombinant

    Spindle and kinetochore-associated protein 1, SKA1, C18orf24, Spindle And Kinetochore Associated Complex Subunit 1.

    Product # :

    PRO-1896

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    Description

    SKA1 Human Recombinant produced in E. coli is a single polypeptide chain containing 278 amino acids (1-255) and having a molecular mass of 31.9 kDa.SKA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SKA1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

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    • Introduction

      Spindle And Kinetochore Associated Complex Subunit 1 (SKA1) is a part of the kinetochore-microtubule interface which associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. SKA1 is necessary for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint.

    • Synonyms

      Spindle and kinetochore-associated protein 1, SKA1, C18orf24, Spindle And Kinetochore Associated Complex Subunit 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

      MGSSHHHHHH SSGLVPRGSH MGSMASSDLE QLCSHVNEKI GNIKKTLSLR NCGQEPTLKT VLNKIGDEII VINELLNKLE LEIQYQEQTN NSLKELCESL EEDYKDIEHL KENVPSHLPQ VTVTQSCVKG SDLDPEEPIK VEEPEPVKKP PKEQRSIKEM PFITCDEFNG VPSYMKSRLT YNQINDVIKE INKAVISKYK ILHQPKKSMN SVTRNLYHRF IDEETKDTKG RYFIVEADIK EFTTLKADKK FHVLLNILRH CRRLSEVRGG GLTRYVIT.

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    Ska1 Human
  • View Data Sheet

    Name :

    CD105 (27-581) Mouse

    Description:

    Endoglin (27-581) Mouse Recombinant

    Endoglin, Cell surface MJ7/18 antigen, CD105, Eng, Edg.

    Product # :

    CYT-972

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    Description

    Endoglin Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 563 amino acids (27-581 a.a.) and having a molecular mass of 60.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).Endoglin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
      The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.

    • Synonyms

      Endoglin, Cell surface MJ7/18 antigen, CD105, Eng, Edg.

    • 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

      ERVGCDLQPV DPTRGEVTFT TSQVSEGCVA QAANAVREVH VLFLDFPGML SHLELTLQAS KQNGTETQEV FLVLVSNKNV FVKFQAPEIP LHLAYDSSLV IFQGQPRVNI TVLPSLTSRK QILDWAATKG AITSIAALDD PQSIVLQLGQ DPKAPFLCLP EAHKDMGATL EWQPRAQTPV QSCRLEGVSG HKEAYILRIL PGSEAGPRTV TVMMELSCTS GDAILILHGP PYVSWFIDIN HSMQILTTGE YSVKIFPGSK VKGVELPDTP QGLIAEARKL NASIVTSFVE LPLVSNVSLR ASSCGGVFQT TPAPVVTTPP KDTCSPVLLM SLIQPKCGNQ VMTLALNKKH VQTLQCTITG LTFWDSSCQA EDTDDHLVLS SAYSSCGMKV TAHVVSNEVI ISFPSGSPPL RKKVQCIDMD SLSFQLGLYL SPHFLQASNT IELGQQAFVQ VSVSPLTSEV TVQLDSCHLD LGPEGDMVEL IQSRTAKGSC VTLLSPSPEG DPRFSFLLRV YMVPTPTAGT LSCNLALRPS TLSQEVYKTV SMRLNIVSPD LSGKGLEHHH HHH

    • Background

      What is the molecular weight/Mw of CD105 Protein?
      CD105 Protein has a total Mw of 60.9kDa.

      What is the source or expression system of CD105 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CD105 Protein?
      CD105 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD105 Protein?
      The biological functionality of CD105 Protein will be determined in the future.

      What is the amino acid sequence of CD105 Protein?
      ERVGCDLQPV DPTRGEVTFT TSQVSEGCVA QAANAVREVH VLFLDFPGML SHLELTLQAS KQNGTETQEV FLVLVSNKNV FVKFQAPEIP LHLAYDSSLV IFQGQPRVNI TVLPSLTSRK QILDWAATKG AITSIAALDD PQSIVLQLGQ DPKAPFLCLP EAHKDMGATL EWQPRAQTPV QSCRLEGVSG HKEAYILRIL PGSEAGPRTV TVMMELSCTS GDAILILHGP PYVSWFIDIN HSMQILTTGE YSVKIFPGSK VKGVELPDTP QGLIAEARKL NASIVTSFVE LPLVSNVSLR ASSCGGVFQT TPAPVVTTPP KDTCSPVLLM SLIQPKCGNQ VMTLALNKKH VQTLQCTITG LTFWDSSCQA EDTDDHLVLS SAYSSCGMKV TAHVVSNEVI ISFPSGSPPL RKKVQCIDMD SLSFQLGLYL SPHFLQASNT IELGQQAFVQ VSVSPLTSEV TVQLDSCHLD LGPEGDMVEL IQSRTAKGSC VTLLSPSPEG DPRFSFLLRV YMVPTPTAGT LSCNLALRPS TLSQEVYKTV SMRLNIVSPD LSGKGLEHHH HHH

      What applications can CD105 Protein be used in?
      CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD105 Protein?
      The endotoxin level is minimal, CD105 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.

    Endoglin 27 581 Mouse
  • View Data Sheet

    Name :

    LGALS16 Human

    Description:

    Galectin-16 Human Recombinant

    Lectin Galactoside Binding Soluble 16, Galectin16, Galectin-16, LGALS-16, LGALS16.

    Product # :

    CYT-993

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    Description

    LGALS16 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 16kDa.The LGALS16 also appears as a homodimer and therefore a 32kDa band is observed as well. LGALS16 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    1x PBS and 25mM arginine.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Galectin-16 (LGALS16) binds lactose with high affinity. LGALS16 is a strong inducer of T-cell apoptosis.

    • Synonyms

      Lectin Galactoside Binding Soluble 16, Galectin16, Galectin-16, LGALS-16, LGALS16.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      The Recombinant LGALS16 protein although stable at 4°C for 1 week, should be stored 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.

    • Background

      What is the molecular weight/Mw of LGALS16 HUMAN Protein?
      LGALS16 HUMAN Protein has a total Mw of 16kDa.

      What is the source or expression system of LGALS16 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS16 HUMAN Protein?
      LGALS16 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS16 HUMAN Protein?
      The biological functionality of LGALS16 HUMAN Protein will be determined in the future.


      What applications can LGALS16 HUMAN Protein be used in?
      LGALS16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS16 HUMAN Protein?
      The endotoxin level is minimal, LGALS16 HUMAN Protein was purified using conventional chromatography techniques.

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

    Lgals16 Human
  • View Data Sheet

    Name :

    sRANKL Human

    Description:

    RANK Ligand Soluble Human Recombinant

    Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    Product # :

    CYT-334

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    • HPLC, SDS-PAGE

    Description

    sRANKL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19.7kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Sodium phosphate, pH-7.5.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The activity of RAW-Blue was measured to be 46.96 ng/ml, corresponding to a specific activity of 2.1x104 units/mg.

    HPLC, SDS-PAGE

    sRANKL Human HPLC - Product image 1
    sRANKL Human SDS PAGE - Product image 2

    More Info

    • Introduction

      RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

    • Synonyms

      Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANKL 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 sRANKL in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EKAMVDGSW LDLAKRSKLE AQPFAHLTIN ATDIPSGSHK VSLSSWYHDR GWAKISNMTF SNGKLIVNQD GFYYLYANIC FRHHETSGDL ATEYLQLMVY VTKTSIKIPS SHTLMKGGST KYWSGNSEFH FYSINVGGFF KLRSGEEISI EVSNPSLLDP DQDATYFGAF KVRDID.

    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.

    Rankl Human
  • View Data Sheet

    Name :

    GM-CSF Mouse

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Mouse Recombinant

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

    Product # :

    CYT-222

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14285.35 Dalton.GM-CSF Mouse is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GM-CSF Mouse was lyophilized with no additives.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GM-CSF 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 Granulocyte Macrophage Colony Stimulating Factor in sterile 20mM AcOH (acetic Acid) 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-Thr-Arg.

    • Background

      What is the molecular weight/Mw of GM-CSF MOUSE Protein?
      GM-CSF MOUSE Protein has a total Mw of 14.28kDa.

      What is the source or expression system of GM-CSF MOUSE Protein?
      Escherichia Coli.

      What is the Purity of GM-CSF MOUSE Protein?
      GM-CSF MOUSE Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

      What is the amino acid sequence of GM-CSF MOUSE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.

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

      What is the endotoxin level for GM-CSF MOUSE Protein?
      The endotoxin level is minimal, GM-CSF MOUSE Protein was purified using conventional chromatography techniques.


    • Protein content

      GM-CSF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.765 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 GM-CSF 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.

    Gm Csf Mouse
  • View Data Sheet

    Name :

    SCGB1A1 Human, His

    Description:

    Uteroglobin Human Recombinant, His Tag

    Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

    Product # :

    CYT-752

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    Description

    Uteroglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 9.2kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.

    • Synonyms

      Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SCGB1A1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASEICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.

    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.

    Scgb1A1 Human His
  • View Data Sheet

    Name :

    UBE2K Human

    Description:

    Ubiquitin-Conjugating Enzyme E2K Human Recombinant

    HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.

    Product # :

    ENZ-339

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    Description

    UBE2K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-200a.a.) and having a molecular mass of 26.5kDa.UBE2K is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 50mM NaCl, and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      UBE2K belongs to the ubiquitin-conjugating enzymes family which take part in many cellular processes such as selective protein degradation, DNA repair, cell cycle control, and sporulation. In this mechanism, the ATP-coupled activation and subsequent ligation of ubiquitin are catalyzed by separate enzymes functionally linked by ubiquitin carrier protein UBC1. In addition, UBE2K is involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with amyloid-?, huntingtin, and MHC-heavy chain proteins.

    • Synonyms

      HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMANI AVQRIKREFK EVLKSEETSK NQIKVDLVDE NFTELRGEIA GPPDTPYEGG RYQLEIKIPE TYPFNPPKVR FITKIWHPNI SSVTGAICLD ILKDQWAAAM TLRTVLLSLQ ALLAAAEPDD PQDAVVANQY KQNPEMFKQT ARLWAHVYAG APVSSPEYTK KIENLCAMGF DRNAVIVALS SKSWDVETAT ELLLSN.

    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.

    Ube2K Human
  • View Data Sheet

    Name :

    TYMS Antibody

    Description:

    Thymidylate Synthetase, Mouse Anti Human

    TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.

    Product # :

    ANT-002

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    More Info

    • Introduction

      Thymidylate synthase catalyzes the methylation of deoxyuridylate to deoxythymidylate using 5,10-methylenetetrahydrofolate as a cofactor which maintains the dTMP (thymidine-5-prime monophosphate) pool vital for DNA replication and repair. Thymidylate synthase plays an important role as a cancer chemotherapeutic agent. Thymidylate synthase is the primary site of action for 5-fluorouracil, 5-fluoro-2-prime-deoxyuridine, and several folate analogs.

    • Synonyms

      TMS, EC 2.1.1.45, HST422, Thymidylate synthase, TSase, TS, TYMS, MGC88736.

    • Immunogen

      Anti-human TYMS mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human TYMS amino acids 1-313 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT1S5AT.

    • Applications

      TYMS antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot and Immunofluorescence analysis is 1:500 ~ 1000. Recommended starting dilution is 1:500.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      TYMS antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Tyms Antibody
  • View Data Sheet

    Name :

    TPM3 Human

    Description:

    Tropomyosin-3 Human Recombinant

    Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.

    Product # :

    PRO-1020

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    Description

    TPM3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a.) and having a molecular mass of 31.6kDa. TPM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPM3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tropomyosin alpha-3 chain (TPM3) belongs to the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins which polymerize end-to-end along the major groove in most actin filaments. Tropomyosins give stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, tropomyosins regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.

    • Synonyms

      Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.

    • 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 MGSHMAGITT IEAVKRKIQV LQQQADDAEE RAERLQREVE GERRAREQAE AEVASLNRRI QLVEEELDRA QERLATALQK LEEAEKAADE SERGMKVIEN RALKDEEKME LQEIQLKEAK HIAEEADRKY EEVARKLVII EGDLERTEER AELAESRCRE MDEQIRLMDQ NLKCLSAAEE KYSQKEDKYE EEIKILTDKL KEAETRAEFA ERSVAKLEKT IDDLEDKLKC TKEEHLCTQR MLDQTLLDLN EM.

    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.

    Tpm3 Human
  • View Data Sheet

    Name :

    GNG4 Human

    Description:

    Guanine Nucleotide Binding Protein Gamma 4 Human Recombinant

    Guanine Nucleotide Binding Protein (G Protein) Gamma 4, Guanine Nucleotide-Binding Protein G(I)/G(S)/G(O) Subunit Gamma-4, GNGT4.

    Product # :

    PRO-1842

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    Description

    GNG4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (1-72) and having a molecular mass of 10.4 kDa. GNG4 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The GNG4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNG4 belongs to a multigene family and is involved in defining the specificity of receptor-G protein interaction. In mammals, G protein alpha, beta and gamma polypeptides are encoded by no less than 16, 4 and 7 genes, respectively. It is a well-known fact that different G protein complexes expressed in different tissues carry structurally distinct members of the alpha beta and gamma subunits and that privileged connotation between members of subunit families rise G protein functional diversity.

    • Synonyms

      Guanine Nucleotide Binding Protein (G Protein) Gamma 4, Guanine Nucleotide-Binding Protein G(I)/G(S)/G(O) Subunit Gamma-4, GNGT4.

    • 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 MGSMKEGMSN NSTTSISQAR KAVEQLKMEA CMDRVKVSQA AADLLAYCEA HVREDPLIIP VPASENPFRE KKFFC

    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.

    Gng4 Human
  • View Data Sheet

    Name :

    CXCL3 Rat alpha

    Description:

    GRO-Gamma Rat Recombinant (CXCL3), CINC-2 alpha

    Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.

    Product # :

    CHM-258

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    Description

    GRO-g Rat Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa. The CXCL3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Rat CXCL3 lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.

    • Synonyms

      Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 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 GRO-gamma in sterile 18Mcm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.

    • Background

      What is the molecular weight/Mw of CXCL3 RAT ALPHA Protein?
      CXCL3 RAT ALPHA Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CXCL3 RAT ALPHA Protein?
      Escherichia Coli.

      What is the Purity of CXCL3 RAT ALPHA Protein?
      CXCL3 RAT ALPHA Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL3 RAT ALPHA Protein?
      Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.

      What is the amino acid sequence of CXCL3 RAT ALPHA Protein?
      RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.

      What applications can CXCL3 RAT ALPHA Protein be used in?
      CXCL3 RAT ALPHA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL3 RAT ALPHA Protein?
      The endotoxin level is minimal, CXCL3 RAT ALPHA 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.

    Gro G Rat Cinc 2A
  • View Data Sheet

    Name :

    SCGB1A1 Human

    Description:

    Uteroglobin Human Recombinant

    Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

    Product # :

    CYT-743

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    Shipped at Room temp

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

    Description

    Uteroglobin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 15.8kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.

    More Info

    • Introduction

      Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.

    • Synonyms

      Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.

    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.

    Scgb1A1 Human
  • View Data Sheet

    Name :

    CD3G Human

    Description:

    CD3G Human Recombinant

    T-cell surface glycoprotein CD3 gamma chain, CD3-GAMMA, T3G, CD3G.

    Product # :

    PRO-1392

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    Description

    CD3G Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (23-116a.a.) and having a molecular mass of 13.1kDa. CD3G is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CD3G protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD3-gamma polypeptide is encoded by CD3 Gamma (CD3G) which together with CD3-epsilon, -delta and -zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, configures the T-cell receptor-CD3 complex. The T-cell receptor-CD3 complex takes part in coupling antigen recognition to numerous intracellular signal-transduction pathways. The genes encoding the epsilon, gamma and delta polypeptides are located in the same cluster on chromosome 11. Deficiencies in this gene are associated with T cell immunodeficiency.

    • Synonyms

      T-cell surface glycoprotein CD3 gamma chain, CD3-GAMMA, T3G, CD3G.

    • 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 MGSQSIKGNH LVKVYDYQED GSVLLTCDAE AKNITWFKDG KMIGFLTEDK KKWNLGSNAK DPRGMYQCKG SQNKSKPLQV YYRMCQNCIE LNAATIS.

    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.

    Cd3G Human
  • View Data Sheet

    Name :

    YWHAG Antibody

    Description:

    YWHAG Mouse Anti Human

    14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3 monooxygenase/tryptophan 5-monooxygenase activation protein gamma polypeptide.

    Product # :

    ANT-539

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    Quantity :

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    • formulation
    • More Info
    • Western Blot, ICC/IF

    Formulation

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

    Western Blot, ICC/IF

    YWHAG Antibody Western Blot - Product image 1
    YWHAG Antibody ICC-IF - Product image 2

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

    • Synonyms

      14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3 monooxygenase/tryptophan 5-monooxygenase activation protein gamma polypeptide.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human YWHAG mAb, clone PAT4B9AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human YWHAG protein 1-247 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT4B9AT.

    • Applications

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

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

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

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

    Ywhag Pat4B9At Antibody
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