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Search results

1000 results found for “Erythropoietin”

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  • View Data Sheet

    Name :

    ANKRA2 Human

    Description:

    Ankyrin Repeat Family A2 Human Recombinant

    Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.

    Product # :

    PRO-2062

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    Description

    ANKRA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313a.a) and having a molecular mass of 36.7kDa. ANKRA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ANKRA2 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ankyrin Repeat Family A2, also known as ANKRA2 contains 5 ANK repeats. ANKRA2 assist endocytosis by linking megalin to components of the cytoskeleton or endocytic machinery.

    • Synonyms

      Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.

    • 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 MGSMDTSTNL DIGAQLIVEE CPSTYSLTGM PDIKIEHPLD PNSEEGSAQG VAMGMKFILP NRFDMNVCSR FVKSLNEEDS KNIQDQVNSD LEVASVLFKA ECNIHTSPSP GIQVRHVYTP STTKHFSPIK QSTTLTNKHR GNEVSTTPLL ANSLSVHQLA AQGEMLYLAT RIEQENVINH TDEEGFTPLM WAAAHGQIAV VEFLLQNGAD PQLLGKGRES ALSLACSKGY TDIVKMLLDC GVDVNEYDWN GGTPLLYAVH GNHVKCVKML LESGADPTIE TDSGYNSMDL AVALGYRSVQ QVIESHLLKL LQNIKE.

    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.

    Ankra2 Human
  • View Data Sheet

    Name :

    FLRT3 Human, HEK

    Description:

    Fibronectin Leucine Rich Transmembrane Protein 3 Human Recombinant, HEK

    Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.

    Product # :

    PRO-2805

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    Description

    FLRT3 Human Recombinant is a single, glycosylated, polypeptide chain (29-528 a.a) containing a total of 506 amino acids and having a molecular mass of 57.3 kDa. FLRT3 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    FLRT3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    >40%.  Measured by the ability of the immobilized protein to support the adhesion of Neuro-2a neuroblast cells. When cells are added to human FLRT3 coated plates 5 ug/ml.

    More Info

    • Synonyms

      Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.

    • 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

      KSCPSVCRCD AGFIYCNDRF LTSIPTGIPE DATTLYLQNN QINNAGIPSD LKNLLKVERI YLYHNSLDEF PTNLPKYVKE LHLQENNIRT ITYDSLSKIP YLEELHLDDN SVSAVSIEEG AFRDSNYLRL LFLSRNHLST IPWGLPRTIE ELRLDDNRIS TISSPSLQGL TSLKRLVLDG NLLNNHGLGD KVFFNLVNLT ELSLVRNSLT AAPVNLPGTN LRKLYLQDNH INRVPPNAFS
      YLRQLYRLDM SNNNLSNLPQ GIFDDLDNIT QLILRNNPWY CGCKMKWVRD WLQSLPVKVN VRGLMCQAPE KVRGMAIKDL NAELFDCKDS GIVSTIQITT AIPNTVYPAQ GQWPAPVTKQ PDIKNPKLTK DHQTTGSPSR KTITITVKSV TSDTIHISWK LALPMTALRL SWLKLGHSPA FGSITETIVT GERSEYLVTA LEPDSPYKVC MVPMETSNLY LFDETPVCIE TETAPLRMYN
      PTTTLNREQE KEPYKNPNLP HHHHHH.

    • Background

      Fibronectin leucine-rich transmembrane protein 3, commonly known as FLRT3, stands as a molecular architect in the intricate landscape of neural development. Its roles, initially discovered in the embryonic nervous system, have expanded to encompass various physiological and pathological processes in both the brain and beyond. This research endeavors to unravel the enigma of FLRT3 protein, exploring its structural intricacies, physiological functions, and its far-reaching implications in neurobiology, embryogenesis, and disease. By delving into FLRT3's multifaceted roles, scientists aim to decipher the underlying mechanisms that govern its diverse functions and explore potential therapeutic avenues in the realms of neuroscience and beyond.

      Structural Complexities of FLRT3:

      FLRT3 belongs to the FLRT family, characterized by extracellular leucine-rich repeats (LRRs) and a transmembrane domain. These structural motifs enable FLRT3 to participate in a myriad of interactions, including binding with cell adhesion molecules and guidance cues. Understanding the three-dimensional architecture of FLRT3 is fundamental for unraveling its molecular partnerships, biological activities, and its contributions to cell adhesion and signaling.

      Physiological Functions in Neural Development:

      In the developing nervous system, FLRT3 acts as a guidance molecule, steering growing axons and dendrites to their precise destinations. Through interactions with other cell surface receptors and ligands, FLRT3 modulates axon pathfinding, synapse formation, and neuronal migration. Its presence in growth cones and developing neural circuits underscores its significance in sculpting the intricate neural networks essential for proper brain function.

      Beyond Neural Development:

      Beyond its canonical roles in neurodevelopment, FLRT3 has emerged as a versatile player in various physiological processes. It participates in tissue morphogenesis, modulates cell adhesion, and influences immune responses. Recent studies have also implicated FLRT3 in cancer progression, highlighting its involvement in pathological conditions and making it a potential target for therapeutic interventions in cancer therapy.

      FLRT3 as a Therapeutic Target:

      The diverse roles of FLRT3 in neural development and diseases position it as an attractive target for therapeutic interventions. Modulating FLRT3 interactions offers novel avenues for neurological disorder treatments, including neurodevelopmental disorders and neurodegenerative diseases. Moreover, understanding FLRT3's involvement in cancer biology opens doors for innovative cancer therapies, making it a promising target for precision medicine approaches.

      FLRT3, with its intricate structural features and diverse functional roles, stands as a linchpin in the realms of neuroscience, embryogenesis, and disease. Its multifaceted contributions to neural development, tissue morphogenesis, and disease pathogenesis underscore its significance in both health and pathology. As researchers continue to unravel FLRT3’s complexities, they not only deepen our understanding of fundamental biological processes but also pave the way for groundbreaking discoveries in neuroscience and therapeutic interventions, ultimately shaping the future landscape of medicine and scientific inquiry.

    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.

    Flrt3 Protein
  • View Data Sheet

    Name :

    BMP 7 Human, HEK

    Description:

    Bone Morphogenetic protein-7 Human Recombinant, HEK

    Osteogenic Protein 1, BMP-7.

    Product # :

    CYT-082

    Price :

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    Shipped at Room temp

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    • More Info

    Description

    BMP-7 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 30-38kDa due to glycosylation.The BMP7 corresponds to amino acid residues 315 to 431 of the full-length BMP-7 precursor and is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The BMP7 was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

    More Info

    • Introduction

      The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

    • Synonyms

      Osteogenic Protein 1, BMP-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-7 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 BMP-7 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.

    • Background

      BMP-7 Bone Morphogenetic Protein-7 Human Recombinant: A Key Regulator of Osteogenesis and Beyond

      Abstract:

      BMP-7 (Bone Morphogenetic Protein-7), also known as Osteogenic Protein 1 or BMP-7, is a potent growth factor that plays a crucial role in various biological processes, particularly in osteogenesis and tissue regeneration.

      This research paper aims to comprehensively explore the molecular characteristics, signaling pathways, and diverse physiological functions of BMP-7.

      Additionally, it investigates the therapeutic implications of BMP-7 in different disorders. Synonyms such as Osteogenic Protein 1 and BMP-7 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a growth factor with multifaceted roles in osteogenesis, tissue regeneration, and disease. This section introduces BMP-7 and its synonyms, highlighting their significance and relevance in scientific research.

      Molecular Characteristics of BMP-7:

      This section explores the molecular characteristics of BMP-7, including its primary amino acid sequence, protein structure, post-translational modifications, and binding partners. The importance of these factors in determining BMP-7's biological activity and receptor specificity is discussed.

      Signaling Pathways Activated by BMP-7 :

      BMP-7 activates specific signaling pathways upon binding to its receptors, leading to diverse cellular responses. This section focuses on the canonical BMP signaling pathway, highlighting the activation of Smad-dependent and Smad-independent pathways. The downstream effectors and transcriptional regulators involved in mediating BMP-7's cellular responses are also discussed.

      Physiological Functions of BMP-7 :

      BMP-7 plays critical roles in various physiological processes, particularly in osteogenesis and tissue regeneration. This section provides an in-depth analysis of BMP-7's contributions to these processes, emphasizing its role in promoting bone formation, cartilage development, renal function, and wound healing.

      Therapeutic Implications of BMP-7 :

      The unique properties of BMP-7 make it a promising therapeutic candidate for various disorders. This section discusses the potential applications of BMP-7 in bone regeneration, cartilage repair, kidney disease, and tissue engineering. The challenges and future directions in utilizing BMP-7 as a therapeutic agent are also explored.

      BMP-7 in Disease Progression:

      BMP-7 is implicated in the progression of certain diseases, including fibrosis, cancer, and cardiovascular disorders. This section examines the role of BMP-7 in tissue fibrosis, tumor progression, angiogenesis, and cardiac remodeling. The therapeutic implications and targeting of BMP-7 in disease management are also discussed.

      Conclusion:

      BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a critical growth factor involved in osteogenesis, tissue regeneration, and disease progression. Understanding the molecular characteristics, signaling pathways, and physiological functions of BMP-7 contributes to the exploration of its therapeutic potential in various disorders.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 38kDa.

      What is the source or expression system of BMP7 Protein?
      HEK.

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.

      What is the amino acid sequence of BMP7 Protein?
      DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.


      What applications can BMP7 Protein be used in?
      BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP7 Protein?
      The endotoxin level is minimal, BMP7 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.

    Bmp 7 Human Hek
  • View Data Sheet

    Name :

    PF4 Bovine

    Description:

    Platelet Factor-4 (CXCL4) Bovine Recombinant

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-039

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    Description

    Platelet Factor-4 (CXCL4) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 88 amino acid and having a molecular mass of approximately 9.5kDa.PF4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-100ng/ml.

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets.PF4’s major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Furthermore, it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Platelet Factor-4 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Platelet Factor-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ESSFPATFVP LPADSEGGED EDLQCVCLKT TSGINPRHIS SLEVIGAGTH CPSPQLLATK KTGRKICLDQ QRPLYKKILK KLLDGDES.

    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.

    Cxcl4 Bovine
  • View Data Sheet

    Name :

    PI3 Human

    Description:

    Peptidase Inhibitor 3 Human Recombinant

    Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.

    Product # :

    PRO-1627

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    Description

    PI3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (23-117) and having a molecular mass of 12.0kDa.PI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PI3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      PI3 is an elastase-specific protease inhibitor, which contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. PI3 belongs to the centromeric cluster.

    • Synonyms

      Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.

    • 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 MGSAVTGVPV KGQDTVKGRV PFNGQDPVKG QVSVKGQDKV KAQEPVKGPV STKPGSCPII LIRCAMLNPP NRCLKDTDCP GIKKCCEGSC GMACFVPQ

    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.

    Pi3 Human
  • View Data Sheet

    Name :

    MCL1 Human

    Description:

    Myeloid Cell Leukemia Sequence 1 Human Recombinant

    Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.

    Product # :

    PRO-1202

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    Description

    MCL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (1-327) and having a molecular mass of 37.2 kDa.MCL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MCL1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MCL1 is a member of the Bcl-2 family. MCL1 takes part in the control of apoptosis against cell existence, and in the preservation of viability but not of proliferation. Alternative splicing happens at this locus and two transcript variants encoding different isoforms are known. Isoform 1 is the longer gene product and it increases cell existence by inhibiting apoptosis. Isoform 2 is a shorter gene product which indorses apoptosis and is death-inducing.

    • Synonyms

      Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.

    • 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 MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR TKRDWLVKQR GWDGFVEFFH VEDLEGG.

    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.

    Mcl1 Human
  • View Data Sheet

    Name :

    Adiponectin Mouse, Trimeric

    Description:

    Adiponectin Mouse Recombinant, Trimeric form

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-247

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    Description

    Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.

    Purity

    Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
      In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      Filtered white lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse 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 deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293

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

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

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

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

    Adiponectin Mouse Trimeric
  • View Data Sheet

    Name :

    PTHrP N15 Human

    Description:

    Parathyroid Hormone Related Protein N15 Labeled Human Recombinant

    Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.

    Product # :

    HOR-005

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    Description

    PTHrP N15 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids, having an MW of 10033 Da labeled by the stable isotope N15.The PTHrP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PthRp N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS,
    pH 7.4.

    Purity

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

    More Info

    • Introduction

      PTHrP is a powerful and discriminating agonist of PTH2R which takes part in adenyl cyclase activation and intracellular calcium levels elevation. PTHrP encourages protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. Additionally, PTHrP inhibits cell proliferation through its contribution to PTH2R activation, activates nociceptors and nociceptive circuits and acts as a neuropeptide in spermatogenesis.

    • Synonyms

      Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PTHrP N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTHrP N15 should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      AVSEHQLLHD KGKSIQDLRR RFFLHHLIAE IHTAEIRATS EVSPNSKPSP NTKNHPVRFG SDDEGRYLTQ ETNKVETYKE QPLKTP.

    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.

    Pthrp N15 Human
  • View Data Sheet

    Name :

    IL15 Human, HEK

    Description:

    Interleukin-15 Human Recombinant, HEK

    IL-15, IL15, Interleukin-15, MGC9721.

    Product # :

    CYT-967

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    Description

    Interleukin-15 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight of 12.8kDa.The IL15 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The IL-15 protein was lyophilized from 1842µl filtered (0.2µm) solution in PBS, pH 7.4 and 10% Trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity was determined by the dose dependent stimulation of the proliferation of CTLL-2 cells, the ED50 is typically less than 0.5ng/ml, corresponding to a specific activity of >2 x 106 Unit/mg.

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.

    • Synonyms

      IL-15, IL15, Interleukin-15, MGC9721.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL15 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 IL15 with 2500µl PBS to a stock solution of 400µg/ml.

    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.

    Il15 Human Hek
  • View Data Sheet

    Name :

    Transthyretin Human

    Description:

    Prealbumin Human Recombinant

    TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.

    Product # :

    PRO-771

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    Description

    Transthyertin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (21-147 a.a.) and having a molecular weight of 13.8kDa. The Transthyertin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Transthyertin protein solution contains 1x PBS, pH-7.4, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prealbumin is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. Prealbumin is a carrier protein which transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. Transthyretin consists of a tetramer of identical subunits and is dominantly produced in the liver. Mutations in Prealbumin are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, and carpal tunnel syndrome. Prealbumin is an indicator of protein-energy malnutrition since it has a circulating half life of 2 days and reacts swiftly to changes in nutritional status.

    • Synonyms

      TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.

    • 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

      MGPTGTGESK CPLMVKVLDA VRGSPAINVA VHVFRKAADD TWEPFASGKT SESGELHGLT TEEEFVEGIY KVEIDTKSYW KALGISPFHE HAEVVFTAND SGPRRYTIAA LLSPYSYSTT AVVTNPKE.

    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.

    Prealbumin Human
  • View Data Sheet

    Name :

    IL 11 Human, Pichia

    Description:

    Interleukin-11 Human Recombinant, Pichia

    Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    Product # :

    CYT-013

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    Description

    IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    IL11 was Lyophilized from a 0.2 µm filtered concentrated solution of 20mM PB, pH7.2 and 2% Glycine buffer.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 Interleukin -11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

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

    Il 11 Human Pichia
  • View Data Sheet

    Name :

    IL 12 p35 Human

    Description:

    Interleukin-12 p35 Human Recombinant

    NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.

    Product # :

    CYT-487

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    Description

    Interleukin-12 p35 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 197 amino acids fragment (57-253) with an amino-terminal hexahistidine tag. The IL-12 p35 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-12 p35 His-Tag is supplied in 1xPBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.

    • Synonyms

      NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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

    Il 12 P35 Human His
  • View Data Sheet

    Name :

    IL 13 Variant Human

    Description:

    Interleukin-13 Variant Human Recombinant

    Interleukin-13, NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.

    Product # :

    CYT-682

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    Description

    Interleukin-13 Variant Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids, with a substitution of Q for R at position 112 compared with the wild type IL-13, having a molecular mass of 12.5 kDa. The IL-13 Variant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.2, containing 5% trehalose.

    Purity

    Greater than 95% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the dose dependent prolifiration of TF-1 cells and was found to be < 1ng/ml, corresponding to a specific activity of >1,000,000 units/mg. This analog has also been shown to exhibit increased in vivo activity compared to wild type IL-13.

    More Info

    • Introduction

      IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.

    • Synonyms

      Interleukin-13, NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-13 Variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 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 Interleukin 13 Variant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPGPVPPSTA LRELIEELVN ITQNQKAPLC NGSMVWSINL TAGMYCAALE SLINVSGCSA IEKTQRMLSG FCPHKVSAGQ FSSLHVRDTK IEVAQFVKDL LLHLKKLFRE GQFN.

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

    Il 13 Variant Human
  • View Data Sheet

    Name :

    CEA Human

    Description:

    Carcinoembryonic Antigen Human Recombinant

    CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    Product # :

    PRO-287

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    Description

    CEA Human Recombinant is glycosylated with N-linked sugars and produced using baculovirus vectors in insect cells. CEA is a well-known tumor marker corresponding to the full length human CEA which is approximately 120,000 Dalton.

    Source

    Baculovirus Insect Cells.

    Formulation

    The sterile protein solution contains 10mM NaH2PO4, pH 7 and 150mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
      There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
      The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
      CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
      The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
      Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed.

    • Synonyms

      CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    • Physical Appearance

      Sterile Filtered colourless solution.

    • Stability

      CEA should be stored at 2-8°C.Avoid freezing.

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    Carcinoembryonic Antigen
  • View Data Sheet

    Name :

    MLF1 Human

    Description:

    Myeloid Leukemia Factor 1 Human Recombinant

    Myeloid leukemia factor 1, Myelodysplasia-myeloid leukemia factor 1, MLF1.

    Product # :

    PRO-100

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    Description

    MLF1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 288 amino acids (1-268 a.a.) and having a molecular mass of 32.8kDa (Molecular weight on SDS-PAGE will appear higher). The MLF1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MLF1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 5mM DTT and 200mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myeloid leukemia factor 1 (MLF1) is a member of the MLF family, and is a widely expressed negative regulator of cell cycle progression functioning upstream of the tumor suppressor p53. MLF1 hinders the erythropoietin-induced erythroid terminal differentiation by averting cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. MLF1 generally functions in multi-potent progenitor cells, and its dysregulation may be to some extent responsible for leukemogenesis. Translocations between the MLF1 gene and nucleophosmin are linked to myelodysplastic syndrome and acute myeloid leukemia.

    • Synonyms

      Myeloid leukemia factor 1, Myelodysplasia-myeloid leukemia factor 1, MLF1.

    • 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 MFRMLNSSFE DDPFFSESIL AHRENMRQMI RSFSEPFGRD LLSISDGRGR AHNRRGHNDG EDSLTHTDVS SFQTMDQMVS NMRNYMQKLE RNFGQLSVDP NGHSFCSSSV MTYSKIGDEP PKVFQASTQT RRAPGGIKET RKAMRDSDSG LEKMAIGHHI HDRAHVIKKS KNKKTGDEEV NQEFINMNES DAHAFDEEWQ SEVLKYKPGR HNLGNTRMRS VGHENPGSRE LKRREKPQQS PAIEHGRRSN VLGDKLHIKG SSVKSNKK.

    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.

    Mlf1 Human
  • View Data Sheet

    Name :

    CAPSL Human

    Description:

    Calcyphosine-Like Human Recombinant

    Calcyphosine-like protein, CAPSL, MGC26610.

    Product # :

    PRO-185

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    Description

    CAPSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-208) and having a molecular mass of 26.3 kDa.The CAPSL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CAPSL protein at 1mg/ml in 20mM Tris-HCL, pH-8, 0.2M NaCl, 5mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CAPSL is a calcium-binding protein holding two conserved calcium-binding motifs (EF-hands) which are found in a superfamily of calcium sensors and calcium signal modulators. In addition, the CAPSL gene is in the same linkage disequilibrium (LD) block as the IL7R gene and there is well known association between the CAPSL-IL7R locus and type 1 diabetes.

    • Synonyms

      Calcyphosine-like protein, CAPSL, MGC26610.

    • Physical Appearance

      CAPSL is supplied as a 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 MAGTARHDRE MAIQAKKKLT TATDPIERLR LQCLARGSAG IKGLGRVFRI MDDDNNRTLD FKEFMKGLND YAVVMEKEEV EELFQRFDKD GNGTIDFNEF LLTLRPPMSR ARKEVIMQAF RKLDKTGDGV ITIEDLREVY NAKHHPKYQN GEWSEEQVFR KFLDNFDSPY DKDGLVTPEE FMNYYAGVSA SIDTDVYFII MMRTAWKL

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    Capsl Human
  • View Data Sheet

    Name :

    Vaspin Human, His

    Description:

    Vaspin Human Recombinant, His Tag

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-459

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Liquid Vaspin although stable at 10°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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.

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    Vaspin Human
  • View Data Sheet

    Name :

    CPE Human

    Description:

    Carboxypeptidase-E Human Recombinant

    Carboxypeptidase E, Carboxypeptidase H, CPH, CPE, CPE Human, Enkephalin convertase, Prohormone-processing carboxypeptidase.

    Product # :

    ENZ-687

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    Description

    CPE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (43-476 a.a.) and having a molecular mass of 51.4kDa. CPE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CPE protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carboxypeptidase-E (CPE ) is a carboxypeptidase that cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters. CPE is a peripheral membrane protein. CPE specifically connects regulated secretory pathway proteins, including prohormones, but constitutively secreted proteins. Mutations in CPE are implicated in type II diabetes.

    • Synonyms

      Carboxypeptidase E, Carboxypeptidase H, CPH, CPE, CPE Human, Enkephalin convertase, Prohormone-processing carboxypeptidase.

    • 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 MGSLQQEDGI SFEYHRYPEL REALVSVWLQ CTAISRIYTV GRSFEGRELL VIELSDNPGV HEPGEPEFKY IGNMHGNEAV GRELLIFLAQ YLCNEYQKGN ETIVNLIHST RIHIMPSLNP DGFEKAASQP GELKDWFVGR SNAQGIDLNR NFPDLDRIVY VNEKEGGPNN HLLKNMKKIV DQNTKLAPET KAVIHWIMDI PFVLSANLHG GDLVANYPYD ETRSGSAHEY SSSPDDAIFQ SLARAYSSFN PAMSDPNRPP CRKNDDDSSF VDGTTNGGAW YSVPGGMQDF NYLSSNCFEI TVELSCEKFP PEETLKTYWE DNKNSLISYL EQIHRGVKGF VRDLQGNPIA NATISVEGID HDVTSAKDGD YWRLLIPGNY KLTASAPGYL AITKKVAVPY SPAAGVDFEL ESFSERKEEE KEELMEWWKM MSETLNF.

    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.

    Cpe Human
  • View Data Sheet

    Name :

    IL34 Human

    Description:

    Interleukin-34 Human Recombinant

    Interleukin 34, C16orf77, MGC34647, IL34

    Product # :

    CYT-1198

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    Description

    IL34 Human Recombinant produced in CHO cells is a glycosylated homodimeric polypeptide chain containing 228 amino acids and having a total molecular mass of 26kDa.IL34 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    Lyophilized from a sterile (0.2µ) filtered solution containing phosphate buffered saline (PBS).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin 34 (IL34) is a cytokine that promotes the differentiation and viability of monocytes and macrophages through the colony-stimulating factor-1 receptor and is a part of a group of cytokines called interleukins. IL34 increases growth or survival of immune cells known as monocytes. IL34 protein obtains its activity by binding the Colony stimulating factor 1 receptor. Interleukin 34 has also a potential part in viral infection, the adaptive immune response and bone marrow cell proliferation. Furthermore, IL34 plays an important role in innate immunity and in inflammatory processes.

    • Synonyms

      Interleukin 34, C16orf77, MGC34647, IL34

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL34 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL34 Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL34 in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NEPLEMWPLT QNEECTVTGF LRDKLQYRSR LQYMKHYFPI NYKISVPYEG VFRIANVTRLQRAQVSEREL RYLWVLVSLS ATESVQDVLL EGHPSWKYLQ EVETLLLNVQ QGLTDVEVSPKVESVLSLLN APGPNLKLVR PKALLDNCFR VMELLYCSCC KQSSVLNWQD CEVPSPQSCSPEPSLQYAAT QLYPPPPWSP SSPPHSTGSV RPVRAQGEGL LPHHHHHH

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

    Il 34 Human
  • View Data Sheet

    Name :

    GLP-1 Human (31 a.a.)

    Description:

    Glucagon Like Peptide-1 (31 a.a.) Human Recombinant

    GLP1, GLP2, GRPP.

    Product # :

    HOR-236

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    Description

    Glucagon Like Peptide-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 31 amino acids and having a molecular mass of 3.3 kDa. The GLP-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Recombinant GLP-1 concentrated solution (1mg/ml) was lyophilized after extensive dialyses against 0.1mg sodium phosphate monobasic & 1.6mg sodium phosphate dibasic.

    Purity

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

    More Info

    • Introduction

      Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
      GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
      GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety.

    • Synonyms

      GLP1, GLP2, GRPP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Glucagon Like Peptide-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP-1 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 Glucagon Like Peptide-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HAEGTFTSDV SSYLEGQAAK EFIAWLVKGR G.

    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.

    Glucagon Like Peptide 1 Human
  • View Data Sheet

    Name :

    ING2 Human

    Description:

    Inhibitor of Growth Family, Member 2 Human Recombinant

    Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

    Product # :

    PRO-1739

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    Description

    ING2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 35.2kDa.ING2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ING2 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.

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    • Introduction

      Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).

    • Synonyms

      Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

    • 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 MGSMLGQQQQ QLYSSAALLT GERSRLLTCY VQDYLECVES LPHDMQRNVS VLRELDNKYQ ETLKEIDDVY EKYKKEDDLN QKKRLQQLLQ RALINSQELG DEKIQIVTQM LELVENRARQ MELHSQCFQD PAESERASDK AKMDSSQPER SSRRPRRQRT SESRDLCHMA NGIEDCDDQP PKEKKSKSAK KKKRSKAKQE REASPVEFAI DPNEPTYCLC NQVSYGEMIG CDNEQCPIEW FHFSCVSLTY KPKGKWYCPK CRGDNEKTMD KSTEKTKKDR RSR.

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    Ing2 Human
  • View Data Sheet

    Name :

    FGF19 Human, HEK

    Description:

    Fibroblast Growth Factor-19 Human Recombinant, HEK

    fibroblast growth factor 19, FGF19.

    Product # :

    CYT-1180

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    Description

    FGF19 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 23-216) containing 205 amino acids and having a molecular mass of 23.0 kDa.FGF19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    FGF19 protein (0.5mg/ml) contains 20mM Tris-HCl(pH8.0), 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Fibroblast Growth Factor-19 (FGF-19) is a member of the FGF family. FGF-19 interacts with FGFR1, FGFR2, FGFR3 and FGFR4. T FGF-19 takes part in the suppression of bile acid biosynthesis through downregulation of CYP7A1 expression, following positive regulation of the JNK and EPK1/2 cascades. FGF-19 stimulates glucose uptake in adiposytes and is a high affinity, heparin dependent ligand for FGFR4.

    • Synonyms

      fibroblast growth factor 19, FGF19.

    • 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

      DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH

    • Background

      What is the molecular weight/Mw of FGF19 HUMAN,HEK Protein?
      FGF19 HUMAN,HEK Protein has a total Mw of 23kDa.

      What is the source or expression system of FGF19 HUMAN,HEK Protein?
      HEK293 cells.

      What is the Purity of FGF19 HUMAN,HEK Protein?
      FGF19 HUMAN,HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF19 HUMAN,HEK Protein?
      The biological functionality of FGF19 HUMAN,HEK Protein will be determined in the future.

      What is the amino acid sequence of FGF19 HUMAN,HEK Protein?
      DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH

      What applications can FGF19 HUMAN,HEK Protein be used in?
      FGF19 HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF19 HUMAN,HEK Protein?
      The endotoxin level is minimal, FGF19 HUMAN,HEK 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.

    Fgf 19 Human
  • View Data Sheet

    Name :

    M CSF Rat HEK

    Description:

    Macrophage Colony Stimulating Factor Rat Recombinant HEK

    CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-046

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    Quantity :

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    Shipped at Room temp

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    More Info

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

    Description

    MCSF Rat Recombinant produced in HEK-293 cells is a secreted protein (amino acids Glu33-Arg254). M-CSF is disulfide-linked homodimer containing 2 x 222 a.a chains.

    Source

    HEK293

    Formulation

    The recombinant MCSF was lyophilized after extensive dialysis against PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of mouse M-NFS-60 cells.

    More Info

    • Introduction

      Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 MCSF in sterile PBS not less than 100 µg/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.

    M Csf Rat
  • View Data Sheet

    Name :

    MED7 Human

    Description:

    Mediator Complex Subunit 7 Human Recombinant

    Mediator complex subunit 7, cofactor required for Sp1 transcriptional activation subunit 9 33kDa, Activator-recruited cofactor 34 kDa component, Transcriptional coactivator CRSP33, RNA polymerase transcriptional regulation mediator subunit 7 homolog, mediator of RNA polymerase II transcription subunit 7, CRSP complex subunit 9, CRSP33, CRSP9, ARC34, hMED7.

    Product # :

    PRO-1319

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
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    • More Info

    Description

    MED7 Human Recombinant produced in E. coli is a single polypeptide chain containing 256 amino acids (1-233) and having a molecular mass of 29.7 kDa.MED7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MED7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      MED7 is a member of the Mediator complex subunit 7 family. The activation of gene transcription is a multistep course which is initiated by factors which identify transcriptional enhancer sites in DNA and collaborate with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The gene encode a subunit of the CRSP (cofactor required for SP1 activation) complex, that, together with TFIID, is needed for effective activation by SP1. Additionally, MED7 is also an element of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins that cooperate with TR and enables TR function on DNA templates in conjunction with initiation factors and cofactors.

    • Synonyms

      Mediator complex subunit 7, cofactor required for Sp1 transcriptional activation subunit 9 33kDa, Activator-recruited cofactor 34 kDa component, Transcriptional coactivator CRSP33, RNA polymerase transcriptional regulation mediator subunit 7 homolog, mediator of RNA polymerase II transcription subunit 7, CRSP complex subunit 9, CRSP33, CRSP9, ARC34, hMED7.

    • 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 MGSMGEPQQV SALPPPPMQY IKEYTDENIQ EGLAPKPPPP IKDSYMMFGN QFQCDDLIIR PLESQGIERL HPMQFDHKKE LRKLNMSILI NFLDLLDILI RSPGSIKREE KLEDLKLLFV HVHHLINEYR PHQARETLRV MMEVQKRQRL ETAERFQKHL ERVIEMIQNC LASLPDDLPH SEAGMRVKTE PMDADDSNNC TGQNEHQREN SGHRRDQIIE KDAALCVLID EMNERP

    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.

    Med7 Human
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