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Search results

1000 results found for “Osteopontin”

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  • View Data Sheet

    Name :

    NRP1 Rat

    Description:

    Neuropilin 1 Rat Recombinant

    Neuropilin-1, Vascular endothelial cell growth factor 165 receptor, CD304, Nrp1.

    Product # :

    CYT-973

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    Description

    NRP1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 842 amino acids (22-855 a.a.) and having a molecular mass of 94.8kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuropilin 1 (Nrp1) is a transmembrane glycoprotein which functions as a co-receptor for several extracellular ligands including class III/IV semaphorins, some isoforms of vascular endothelial growth factor and transforming growth factor beta. Nrp1 binds vascular endothelial growth factor (VEGF)-A and is believed to serve as a coreceptor for kinase insert domain-containing receptor (KDR) by connecting with KDR and enhancing VEGF signaling. Nrp1 is a marker of regulatory T cells.

    • Synonyms

      Neuropilin-1, Vascular endothelial cell growth factor 165 receptor, CD304, Nrp1.

    • 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

      FRSDKCGGTI KIENPGYLTS PGYPHSYHPS EKCEWLIQAP EPYQRIMINF NPHFDLEDRD CKYDYVEVID GENEGGRLWG KFCGKIAPSP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TAPTGVIKSP GFPEKYPNSL ECTYIIFAPK MSEIILEFES FDLEQDSNPP GGVFCRYDRL EIWDGFPEVG PHIGRYCGQK TPGRIRSSSG ILSMVFYTDS AIAKEGFSAN YSVLQSSISE DFKCMEALGM ESGEIHSDQI TASSQYGTNW SVERSRLNYP ENGWTPGEDS YREWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYRVD ISSNGEDWIT LKEGNKAIIF QGNTNPTDVV FGVFPKPLIT RFVRIKPASW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITASN QGDRNWMPEN IRLVTSRTGW ALPPSPHPYI NEWLQVDLGD EKIVRGVIIQ GGKHRENKVF MRKFKIAYSN NGSDWKMIMD DSKRKAKSFE GNNNYDTPEL RAFTPLSTRF IRIYPERATH SGLGLRMELL GCEVEVPTAG PTTPNGNPVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTIIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDSHAQL RWRVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQSSAHC MTFWYHMSGS HVGTLRVKLH YQKPEEYDQL VWMVVGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHIPQEDCAK PTDLDKKNTE IKIDETGSTP GYEEGKGDKN ISRKPGNVLK TLDPLEHHHH HH

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

    Nrp1 Rat
  • View Data Sheet

    Name :

    Leptin Dog

    Description:

    Leptin Dog Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-506

    Price :

    Quantity :

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    Description

    Leptin Dog Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 adjusted to pH 8-9, 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 Ala-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Dog
  • View Data Sheet

    Name :

    BMP 7 Human, Plant

    Description:

    Bone Morphogenetic Protein-7 Human Recombinant, Plant

    Osteogenic Protein 1, BMP-7.

    Product # :

    CYT-039

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    • More Info

    Description

    Bone Morphogenetic Protein-7 Human Recombinant produced in Plant is a monomeric, glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 16.5kDa, and fused to a 6xHis-tag at the N-terminus. The BMP-7 is purified by proprietary chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    BMP-7 was lyophilized from a solution containing Tris-HCl 0.05M buffer at pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of BMP-7 was measured by its ability to induce alkaline phosphatase production by ATDC5 cells, ED50 is less than 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

    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 BMP-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP 7 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

      Lyophilized BMP-7 protein should be reconstituted in distilled water to a concentration of 50 ng/µl.

    • Amino Acid Sequence

      HHHHHHSTGSKQRSQNRSKTPKNQEALRMANVAEN
      SSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAY
      YCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKP
      CCAPTQLNAISVLYFDDSSVILKKYRNMVVRACGCH.

    • Background

      Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, Plant, Monomer, HEK

      Abstract:

      Welcome to our research paper exploring the incredible world of Bone Morphogenetic Protein-7 Human Recombinant, Plant, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this study, we embark on a captivating journey to unravel the wonders of BMP-7 HR and its significance in cellular differentiation. As a key member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR plays a pivotal role in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells, while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).

      Introduction:

      Step into the fascinating world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its crucial role in guiding cellular differentiation. Meet our trusted companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.

      BMP-7 HR Signaling in HEK Cells:

      Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, paving the way for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.

      Influential Role in Cellular Differentiation:

      BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatility, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.

      Interplay with Key Cytokines:

      Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.

      Therapeutic Implications and Tissue Regeneration:

      The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.

      Conclusion:

      As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR from plant sources opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.

      What is the molecular weight/Mw of BMP7 Protein?
      BMP7 Protein has a total Mw of 16.5kDa.

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

      What is the Purity of BMP7 Protein?
      BMP7 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP7 Protein?
      The biological activity of BMP-7 was measured by its ability to induce alkaline phosphatase production by ATDC5 cells, ED50 is less than 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

      What is the amino acid sequence of BMP7 Protein?
      HHHHHHSTGSKQRSQNRSKTPKNQEALRMANVAEN
      SSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAY
      YCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKP
      CCAPTQLNAISVLYFDDSSVILKKYRNMVVRACGCH.

      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 Plant
  • View Data Sheet

    Name :

    Thyroglobulin Human, Biotin

    Description:

    Thyroglobulin Human, Biotinylated

    Thyroglobulin, TGN, AITD3, TG.

    Product # :

    PRO-2563

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    Description

    Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).

    Source

    Native, Isolated from human thyroid glands.

    Formulation

    Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
      Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease.

    • Synonyms

      Thyroglobulin, TGN, AITD3, TG.

    • Physical Appearance

      Sterile Filtered solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

    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.

    Thyroglobulin Protein
  • View Data Sheet

    Name :

    MMP 8 Human

    Description:

    Matrix Metalloproteinase-8 Human Recombinant

    EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL-CL, HNC, CLG1.

    Product # :

    ENZ-301

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    Description

    Matrix Metalloproteinase-8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 75 kDa.The MMP-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MMP-8 protein solution (100 units/ml) in 0.05M Tris-HCl buffer, pH 7.6, 0.2M NaCl, 5mM CaCl2, 0.0025% NaN3 and 0.1% BSA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    100 units/ml after activation with APMA by solution assay method.
    One unit of collagenolytic activity is defined as the cleavage of 1µg of collagen per minute by the solution method.

    More Info

    • Introduction

      Full-length recombinant human neutrophil MMP-8, latent form.
      Matrix metalloproteinase 8 (MMP-8), degrades interstitial collagens, acting preferentially on collagen type I.
      Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
      MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.

    • Synonyms

      EC 3.4.24.34, Matrix metalloproteinase-8, MMP-8, PMNL-CL, HNC, CLG1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Applications

      Used as a standard for analyzing mammalian colagenase activity.

    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.

    Mmp8 Human
  • View Data Sheet

    Name :

    CRYZ Human

    Description:

    Crystallin Zeta Human Recombinant

    Quinone oxidoreductase, NADPH:quinone reductase, Zeta-crystallin, CRYZ, Quinone oxidoreductase isoform a, Crystallin, zeta (quinone reductase), Crystallin Zeta.

    Product # :

    PRO-2016

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    Description

    CRYZ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329 a.a.) and having a molecular mass of 37.6kDa.CRYZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Crystallin Zeta, also known as CRYZ, Binds NADP and participates in a one-electron transfer process. CRYZ takes part in the detoxification of xenobiotics and Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. CRYZ improves the mRNA coding for BCL2.

    • Synonyms

      Quinone oxidoreductase, NADPH:quinone reductase, Zeta-crystallin, CRYZ, Quinone oxidoreductase isoform a, Crystallin, zeta (quinone reductase), Crystallin Zeta.

    • 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 MGSMATGQKL MRAVRVFEFG GPEVLKLRSD IAVPIPKDHQ VLIKVHACGV NPVETYIRSG TYSRKPLLPY TPGSDVAGVI EAVGDNASAF KKGDRVFTSS TISGGYAEYA LAADHTVYKL PEKLDFKQGA AIGIPYFTAY RALIHSACVK AGESVLVHGA SGGVGLAACQ IARAYGLKIL GTAGTEEGQK IVLQNGAHEV FNHREVNYID KIKKYVGEKG IDIIIEMLAN VNLSKDLSLL SHGGRVIVVG SRGTIEINPR DTMAKESSII GVTLFSSTKE EFQQYAAALQ AGMEIGWLKP VIGSQYPLEK VAEAHENIIH GSGATGKMIL LL.

    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.

    Cryz Human
  • View Data Sheet

    Name :

    S100A8 Human

    Description:

    S100 Calcium Binding Protein A8 Human Recombinant

    Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    Product # :

    PRO-800

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    Description

    S100A8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (1-93 a.a.) and having a molecular mass of 10.8 kDa. The S100A8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A8 solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

    • Synonyms

      Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    • Physical Appearance

      Sterile Filtered clear 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

      MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.

    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.

    S100A8 Human
  • View Data Sheet

    Name :

    CTDSPL Human

    Description:

    CTD Small Phosphatase-Like Human Recombinant

    CTD small phosphatase-like protein, CTDSP-like, Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3, NIF-like protein, Nuclear LIM interactor-interacting factor 1, NLI-interacting factor 1, Protein YA22, hYA22, RBSP3, Small C-terminal domain phosphatase 3, SCP3, Small CTD phosphatase 3, CTDSPL, C3orf8, NIF1, NIFL, SCP3, YA22, PSR1.

    Product # :

    ENZ-569

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    Description

    CTDSPL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (82-265) and having a molecular mass of 23.9kDa.CTDSPL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTDSPL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CTD small phosphatase-like protein (CTDSPL) specially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the biggest RNA polymerase II subunit POLR2A. CTDSPL negatively regulates RNA polymerase II transcription, probably by directing the transition from initiation/capping to processive transcript elongation. CTDSPL is employed by REST to neuronal genes which contain RE-1 elements, directing to neuronal gene silencing in non-neuronal cells.

    • Synonyms

      CTD small phosphatase-like protein, CTDSP-like, Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3, NIF-like protein, Nuclear LIM interactor-interacting factor 1, NLI-interacting factor 1, Protein YA22, hYA22, RBSP3, Small C-terminal domain phosphatase 3, SCP3, Small CTD phosphatase 3, CTDSPL, C3orf8, NIF1, NIFL, SCP3, YA22, PSR1.

    • 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 MGSHMKYLLP EVTVLDYGKK CVVIDLDETL VHSSFKPISN ADFIVPVEID GTIHQVYVLK RPHVDEFLQR MGQLFECVLF TASLAKYADP VADLLDRWGV FRARLFRESC VFHRGNYVKD LSRLGRELSK VIIVDNSPAS YIFHPENAVP VQSWFDDMTD TELLDLIPFF EGLSREDDVY SMLHRLCNR.

    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.

    Ctdspl Human
  • View Data Sheet

    Name :

    MMP1 (24-207) Human

    Description:

    Matrix Metalloproteinase-1 (24-207 a.a) Human Recombinant, HEK

    nterstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.

    Product # :

    ENZ-1085

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    Description

    MMP1 (24-207) Human Recombinant is a single, glycosylated polypeptide chain containing 190 amino acids and having a molecular mass of 21.2kDa. MMP1 (24-207) is fused to a 6 a.a C-terminal His tag.

    Source

    HEK293 Cells.

    Formulation

    MMP1 (24-207) filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS, pH7.5 and 5% (w/v) Threalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IGFBP-3, IGFBP-5, casein, gelatin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

    • Synonyms

      nterstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.

    • 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.

    • Amino Acid Sequence

      CTCVPPHPQT AFCNSDLVIR AKFVGTPEVN QTTLYQRYEI KMTKMYKGFQ ALGDAADIRF VYTPAMESVC GYFHRSHNRS EEFLIAGKLQ DGLLHITTCS FVAPWNSLSL AQRRGFTKTY TVGCEECTVF PCLSIPCKLQ SGTHCLWTDQ LLQGSEKGFQ SRHLACLPRE PGLCTWQSLR SQIAHHHHHH.

    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.

    Mmp1 Protein
  • View Data Sheet

    Name :

    AITRL Human, His

    Description:

    AITRL Human Recombinant, His Tag

    Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

    Product # :

    CYT-317

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    Description

    AITRL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 50-177) containing a total of 137 amino acids and having a molecular mass of 15.6kDa. The AITRL protein is fused to a 9 aa His Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AITRL protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) & 10% glycerol.

    Purity

    Greater than 85.0% as determined bySDS-PAGE.

    More Info

    • Introduction

      Osteostat is the cytokine that binds to TNFRSF18/AITR/GITR and is important for interactions between activated T-lymphocytes and endothelial cells and may modulate T-lymphocyte survival in peripheral tissues. Osteostat is expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells after stimulation by lipopolysaccharides.
      Osteostat protein is detectable in human microvascular EC and is highly up-regulated by IFN-alpha and IFN-beta. Osteostat inhibit differentiation of osteoclasts from monocytic precursor cells. Osteostat suppresses the early stage of osteoclastogenesis via inhibition of macrophage colony-stimulating factorinduced receptor activator of NF-kappaB (RANK) expression in the osteoclast precursor cells. Osteostat does not inhibit lipopolysaccharide-induced RANK expression in monocytes and dendritic cells, or activation-induced RANK expression in T cells. Osteostat is a novel regulator of osteoclast generation and substantiate the major role played by the endothelium in bone physiology.

    • Synonyms

      Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

    • 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

      MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 15.6kDa.

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

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >85% 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 is the amino acid sequence of ADIPONECTIN Protein?
      MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH

      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.

    Gitrl Human
  • View Data Sheet

    Name :

    SERPINI1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade I Member 1 Human Recombinant

    Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    Product # :

    PRO-213

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    Description

    SERPINI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 394 amino acids and having a total molecular mass of 44.7kDa. SERPINI1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of rat C6 cells which is less than 0.5µg/ml, corresponding to a specific activity of >2000IU/mg.

    More Info

    • Introduction

      SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).

    • Synonyms

      Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPINI1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPINI1 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 SERPINI1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG
      STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN
      GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL
      VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM
      MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT
      LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF
      IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL
      YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL.

    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.

    Serpini1 Human
  • View Data Sheet

    Name :

    ASS1 Human

    Description:

    Argininosuccinate Synthase 1 Human Recombinant

    ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.

    Product # :

    ENZ-548

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    Description

    ASS1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 432 amino acids (1-412 a.a.) and having a molecular mass of 48.6 kDa. The ASS1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ASS1 Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASS1 is involved in the urea cycle, which is a sequence of chemical reactions that is localized in liver cells. The urea cycle processes excess nitrogen that is generated as the body uses proteins. The surplus nitrogen is used to create a molecule called urea, which is excreted from the body in urine.

    • Synonyms

      ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 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 MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK.

    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.

    Ass1 Human
  • View Data Sheet

    Name :

    ATP5O Human

    Description:

    ATP Synthase Subunit O, Mitochondrial Human Recombinant

    ATP synthase subunit O mitochondrial, Oligomycin sensitivity conferral protein, OSCP, ATP5O, ATPO.

    Product # :

    ENZ-043

    Price :

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    Description

    ATP5O Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 211 amino acids (24-213 a.a.) and having a molecular mass of 23.1kDa. The ATP5O is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ATP5O solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ATP synthase subunit O (ATP5O) localizes to the mitochondria and catalyzes ATP synthesis. ATP5O is a component of the F-type ATPase found in the mitochondrial matrix. F-type ATPases are composed of a catalytic core and a membrane proton channel. ATP5O seems to be part of the connector connecting these two components and may be involved in transmission of conformational changes or proton conductance.

    • Synonyms

      ATP synthase subunit O mitochondrial, Oligomycin sensitivity conferral protein, OSCP, ATP5O, ATPO.

    • 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 MFAKLVRPPV QVYGIEGRYA TALYSAASKQ NKLEQVEKEL LRVAQILKEP KVAASVLNPY VKRSIKVKSL NDITAKERFS PLTTNLINLL AENGRLSNTQ GVVSAFSTMM SVHRGEVPCT VTSASPLEEA TLSELKTVLK SFLSQGQVLK LEAKTDPSIL GGMIVRIGEK YVDMSVKTKI QKLGRAMREI V.

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

    Atp5O Human
  • View Data Sheet

    Name :

    C17ORF49 Human

    Description:

    Chromosome 17 Open Reading Frame 49 Human Recombinant

    Chromosome 17 open reading frame 49, BPTF-associated protein of 18 kDa, chromatin complexes subunit BAP18, MLL1/MLL complex subunit C17orf49, MGC49942, BAP18.

    Product # :

    PRO-1192

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    Description

    C17ORF49 Human Recombinant produced in E. coli is a single polypeptide chain containing 195 amino acids (1-172) and having a molecular mass of 20.3 kDa.C17ORF49 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The C17ORF49 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      C17ORF49 is a component of chromatin complexes such as the MLL1/MLL and NURF complexes.

    • Synonyms

      Chromosome 17 open reading frame 49, BPTF-associated protein of 18 kDa, chromatin complexes subunit BAP18, MLL1/MLL complex subunit C17orf49, MGC49942, BAP18.

    • 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 MGSMTSASTK VGEIFSAAGA AFTKLGELTM QLHPVADSSP AGAKWTETEI EMLRAAVKRF GDDLNHISCV IKERTVAQIK ATVKRKVYED SGIPLPAESP KKGPKKVASG VLSPPPAAPP PSSSSVPEAG GPPIKKQKAD VTLSALNDSD ANSDVVDIEG LGETPPAKKL NFDQA

    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.

    C17Orf49 Human
  • View Data Sheet

    Name :

    FGF 18 Mouse

    Description:

    Fibroblast Growth Factor-18 Mouse Recombinant

    Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

    Product # :

    CYT-064

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    • sds-page

    Description

    FGF-18 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 21kDa.The FGF-18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-18 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

    sds-page

    fgf18 mouse sds-page - Product image 1

    More Info

    • Introduction

      Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a heparin binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.

    • Synonyms

      Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG.

    • Background

      What is the molecular weight/Mw of FGF18 Protein?
      FGF18 Protein has a total Mw of 21kDa.

      What is the source or expression system of FGF18 Protein?
      Escherichia Coli.

      What is the Purity of FGF18 Protein?
      FGF18 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF18 Protein?
      The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

      What is the amino acid sequence of FGF18 Protein?
      EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG.

      What applications can FGF18 Protein be used in?
      FGF18 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF18 Protein?
      The endotoxin level is minimal, FGF18 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 18 Mouse
  • View Data Sheet

    Name :

    CALB2 Human

    Description:

    Calbindin-2 Human Recombinant

    Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.

    Product # :

    PRO-401

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    Description

    CALB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa.The CALB2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CALB2 1mg/ml protein solution contains 20mM Tris-HCl buffer pH-8 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

    • Synonyms

      Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.

    • 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 MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSST EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M.

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    Calb2 Human
  • View Data Sheet

    Name :

    CAMK2N2 Human

    Description:

    Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 2 Human Recombinant

    Calcium/calmodulin-dependent protein kinase II inhibitor 2, CAMK2N2, CaM-KII inhibitory protein, CaM-KIIN, CAMKIIN, Calcium/calmodulin-dependent protein kinase II.

    Product # :

    PKA-311

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    Description

    CAMK2N2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (1-79a.a) and having a molecular mass of 11kDa.CAMK2N2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CAMK2N2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calcium/Calmodulin-Dependent Protein Kinase II Inhibitor 2 (CAMK2N2) is a protein coding gene which regulates cell growth when overexpressed in colon adenocarcinoma LoVo cells. CAMK2N2 plays a role as a cellular inhibitor of CaM-kinase II (CAMK2).

    • Synonyms

      Calcium/calmodulin-dependent protein kinase II inhibitor 2, CAMK2N2, CaM-KII inhibitory protein, CaM-KIIN, CAMKIIN, Calcium/calmodulin-dependent protein kinase II.

    • 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 MGSMSEILPY SEDKMGRFGA DPEGSDLSFS CRLQDTNSFF AGNQAKRPPK LGQIGRAKRV VIEDDRIDDV LKGMGEKPPS GV.

    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.

    Camk2N2 Human
  • View Data Sheet

    Name :

    FIBP Human

    Description:

    FGF-1 Intracellular-Binding Protein Human Recombinant

    FGFIBP, FIBP-1, Acidic fibroblast growth factor intracellular-binding protein, aFGF intracellular-binding protein, FGF-1 intracellular-binding protein, FIBP.

    Product # :

    CYT-758

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    • sds-page

    Description

    FIBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 387amino acids (1-364) and having a molecular mass of 44.3kDa. The FIBP is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    FIBP protein (0.5mg/ml) is supplied in 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    sds-page

    FIBP Human - Product image 1

    More Info

    • Introduction

      FGF-1 Intracellular-Binding Protein (FIBP) which is a member of Fibroblast growth factors (FGFs) binds to internalized FGF-1 and is thought to be involved in mitogenic function of FGF-1. FGF activity effects development, adult tissue homeostasis, angiogenesis and cancer progression. FIBP localizes to the nucleus and is greatly expressed in heart, skeletal muscle and pancreas and at lower levels in brain, placenta, liver and kidney.

    • Synonyms

      FGFIBP, FIBP-1, Acidic fibroblast growth factor intracellular-binding protein, aFGF intracellular-binding protein, FGF-1 intracellular-binding protein, FIBP.

    • 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 MGSMTSELDI FVGNTTLIDE DVYRLWLDGY SVTDAVALRV RSGILEQTGA TAAVLQSDTM DHYRTFHMLE RLLHAPPKLL HQLIFQIPPS RQALLIERYY AFDEAFVREV LGKKLSKGTK KDLDDISTKT GITLKSCRRQ FDNFKRVFKV VEEMRGSLVD NIQQHFLLSD RLARDYAAIV FFANNRFETG KKKLQYLSFG DFAFCAELMI QNWTLGAVGE APTDPDSQMD DMDMDLDKEF LQDLKELKVL VADKDLLDLH KSLVCTALRG KLGVFSEMEA NFKNLSRGLV NVAAKLTHNK DVRDLFVDLV EKFVEPCRSD HWPLSDVRFF LNQYSASVHS LDGFRHQALW DRYMGTLRGC LLRLYHD.

    • Background

      What is the molecular weight/Mw of FIBP Protein?
      FIBP Protein has a total Mw of 44.3kkDa.

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

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

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

      What is the amino acid sequence of FIBP Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMTSELDI FVGNTTLIDE DVYRLWLDGY SVTDAVALRV RSGILEQTGA TAAVLQSDTM DHYRTFHMLE RLLHAPPKLL HQLIFQIPPS RQALLIERYY AFDEAFVREV LGKKLSKGTK KDLDDISTKT GITLKSCRRQ FDNFKRVFKV VEEMRGSLVD NIQQHFLLSD RLARDYAAIV FFANNRFETG KKKLQYLSFG DFAFCAELMI QNWTLGAVGE APTDPDSQMD DMDMDLDKEF LQDLKELKVL VADKDLLDLH KSLVCTALRG KLGVFSEMEA NFKNLSRGLV NVAAKLTHNK DVRDLFVDLV EKFVEPCRSD HWPLSDVRFF LNQYSASVHS LDGFRHQALW DRYMGTLRGC LLRLYHD.
      What applications can FIBP Protein be used in?
      FIBP Protein can probably be used in western blot, ELISA and Lateral Flow.

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

    Fibp Human
  • View Data Sheet

    Name :

    GM-CSF Human, His

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, His Tag

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    Product # :

    CYT-477

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    Description

    GMCSF Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids fragment (18-144) and having a molecular mass of 18.98kDa with an amino-terminal hexahistidine tag. GM-CSF Human Recombinant His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Granulocyte Macrophage Colony Stimulating Factor-His is supplied in 20mM Tris HCl (pH 8) and 50% glycerol.

    Purity

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

    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. Granulocyte Macrophage Colony Stimulating Factor is a potent species-specific growth factor produced by a variety of cell types including T cells, B cells, macrophages, mast cells and endothelial cells. GM-CSF is produced in response to cytokine or immune stimulation and has been shown to stimulate the proliferation, maturation and function of hematopoietic cells.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    • 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.

    • Background

      What is the molecular weight/Mw of GM-CSF HUMAN, HIS Protein?
      GM-CSF HUMAN, HIS Protein has a total Mw of 18.98kDa.

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

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

      What is the Biological Activity of GM-CSF HUMAN, HIS Protein?
      The biological functionality of GM-CSF HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of GM-CSF HUMAN, HIS Protein?
      GM-CSF HUMAN, HIS Protein is composed from 127 amino acids.

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

      What is the endotoxin level for GM-CSF HUMAN, HIS Protein?
      The endotoxin level is minimal, GM-CSF HUMAN, HIS 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.

    Gm Csf Human His
  • View Data Sheet

    Name :

    TWF1 Human

    Description:

    Twinfilin-1 Human Recombinant

    Twinfilin-1, Protein A6, Protein tyrosine kinase 9, TWF1, PTK9.

    Product # :

    PRO-1003

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    Description

    TWF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-252 a.a.) and having a molecular mass of 31.5kDa. TWF1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TWF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Twinfilin (TWF1) is a ubiquitous actin-monomer-binding protein which is composed of two ADF-homology domains. Twinfilin forms a 1:1 complex with ADP-actin-monomers, prevents nucleotide exchange on actin monomers and blocks assembly of the monomer into filaments. TWF1 is composed of 2 ADF/cofilin-like (ADF-H) domains joined by a short linker region and followed by a C-terminal tail of approximately 20 residues. The 2 ADF-H domains are approximately 20% homologous to ADF/cofilin and to each other. TWF1 protein may be an actin monomer-binding protein, and its localization to cortical G-actin-rich structures might be regulated by the small GTPase RAC1.

    • Synonyms

      Twinfilin-1, Protein A6, Protein tyrosine kinase 9, TWF1, PTK9.

    • 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 MGSHMMLYAA TRATLKKEFG GGHIKDEVFG TVKEDVSLHG YKKYLLSQSS PAPLTAAEEE LRQIKINEVQ TDVGVDTKHQ TLQGVAFPIS REAFQALEKL NNRQLNYVQL EIDIKNEIII LANTTNTELK DLPKRIPKDS ARYHFFLYKH SHEGDYLESI VFIYSMPGYT CSIRERMLYS SCKSRLLEIV ERQLQMDVIR KIEIDNGDEL TADFLYEEVH PKQHAHKQSF AKPKGPAGKR GIRRLIRGPA ETEATTD.

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    Twf1 Human
  • View Data Sheet

    Name :

    PRRT2 Human

    Description:

    Proline-Rich Transmembrane Protein 2 Human Recombinant

    Proline-Rich Transmembrane Protein 2, Infantile Convulsions And Paroxysmal Choreoathetosis, Dispanin Subfamily B Member 3, DSPB3, BFIC2, BFIS2, DYT10, EKD1, PKC, FICCA, IFITMD1, ICCA.

    Product # :

    PRO-1852

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    Description

    PRRT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 291 amino acids (1-268) and having a molecular mass of 29.7 kDa. PRRT2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The PRRT2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transmembrane protein PRRT2 holds a proline-rich domain in its N-terminal half. PRRT2 is known to be primarily expressed in brain and spinal cord in embryonic and postnatal stages. Alterations in this gene are the cause for paroxysmal kinesigenic dyskinesia. PRRT2 mutations were found in nearly 30% of sporadic PKC patients.

    • Synonyms

      Proline-Rich Transmembrane Protein 2, Infantile Convulsions And Paroxysmal Choreoathetosis, Dispanin Subfamily B Member 3, DSPB3, BFIC2, BFIS2, DYT10, EKD1, PKC, FICCA, IFITMD1, ICCA.

    • 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 MGSMAASSSE ISEMKGVEES PKVPGEGPGH SEAETGPPQV LAGVPDQPEA PQPGPNTTAA PVDSGPKAGL APETTETPAG ASETAQATDL SLSPGGESKA NCSPEDPCQE TVSKPEVSKE ATADQGSRLE SAAPPEPAPE PAPQPDPRPD SQPTPKPALQ PELPTQEDPT PEILSESVGE KQENGAVVPL QAGDGEEGPA PEPHSPPSKK SPPANGAPPR VLQQLVEEDR MRRAHSGHPG SPRGSLSRHP SSQLAGPGVE GGEGTQKPRD Y.

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    Prrt2 Human
  • View Data Sheet

    Name :

    ULBP2 Human

    Description:

    UL16 Binding Protein 2 Human Recombinant

    UL16 binding protein 2, retinoic acid early transcript 1 H, NKG2D ligand 2, Retinoic acid early transcript 1H, ALCAN-alpha, N2DL-2, RAET1H.

    Product # :

    PRO-1134

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    Description

    ULBP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (26-216) and having a molecular mass of 24.3 kDa.ULBP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ULBP2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M urea, 0.2M NaCl, 2mM DTT and 30% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ULBP2 is a member of the MHC class I family. ULBP2 is ligand for the NKG2D receptor, composed with at least ULBP1 and ULBP3. ULBPs promote multiple signaling pathways in primary NK cells, triggering the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D encourages calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, ULBP2 cooperates with soluble CMV glycoprotein UL16. This cooperation is blocked with the NKG2D receptor, providing a mechanism in which CMV infected cells can escape the immune system. Additionally, UL16 causes ULBP2 to be held in the ER and cis-Golgi apparatus so that it does not reach the cell surface.

    • Synonyms

      UL16 binding protein 2, retinoic acid early transcript 1 H, NKG2D ligand 2, Retinoic acid early transcript 1H, ALCAN-alpha, N2DL-2, RAET1H.

    • 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 MGSHMGRADP HSLCYDITVI PKFRPGPRWC AVQGQVDEKT FLHYDCGNKT VTPVSPLGKK LNVTTAWKAQ NPVLREVVDI LTEQLRDIQL ENYTPKEPLT LQARMSCEQK AEGHSSGSWQ FSFDGQIFLL FDSEKRMWTT VHPGARKMKE KWENDKVVAM SFHYFSMGDC IGWLEDFLMG MDSTLEPSAG APLAMS

    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.

    Ulbp2 Human
  • View Data Sheet

    Name :

    MAP1LC3B Mouse

    Description:

    Microtubule-Associated Protein 1 Light Chain 3 Beta Mouse Recombinant

    Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    Product # :

    PRO-2482

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    MAP1LC3B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (1-120 a.a.) and having a molecular mass of 16.7kDa. MAP1LC3B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAP1LC3B protein solution (0.25mg/ml) containing 20mM MES(pH6.0), 0.1M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.

    • Synonyms

      Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    • 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 MGSHMPSEKT FKQRRSFEQR VEDVRLIREQ HPTKIPVIIE RYKGEKQLPV LDKTKFLVPD HVNMSELIKI IRRRLQLNAN QAFFLLVNGH SMVSVSTPIS EVYESERDED GFLYMVYASQ ETFG.

    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.

    Map1Lc3B Mouse
  • View Data Sheet

    Name :

    RELM g Mouse

    Description:

    RELM-Gamma Mouse Recombinant

    Resistin-like gamma, RELMgamma,RELM-γ, RELM-g. 

    Product # :

    CYT-1035

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    RELM g Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 18.9kDa. The RELM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.

    • Synonyms

      Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.

    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.

    Mouse Relm Gamma
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