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  • Aprotinin

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Search results

1000 results found for “Avidin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    GADD45B Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Beta Human Recombinant

    MYD118, GADD45BETA, GADD45B, Growth arrest and DNA-damage-inducible protein GADD45 beta, Myeloid differentiation primary response protein MyD118, Negative growth regulatory protein MyD118, DKFZp566B133.

    Product # :

    PRO-563

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    Description

    GADD45B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids and having a molecular mass of 17.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    The GADD45B protein solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GADD45B is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45B reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45B is involved in the regulation of growth and apoptosis. GADD45b takes part during chondrocyte terminal differentiation and mediates MMP-13 gene expression. GADD45 in B cells is induced by CD40 via a mechanism that involves NF-kappa B and that induction suppresses Fas-mediated killing. GADD45b is down-regulated in most cases of hepatocellular carcinoma (HCC), and is a molecular marker in the diagnosis of HCC and as a possible therapeutic target.

    • Synonyms

      MYD118, GADD45BETA, GADD45B, Growth arrest and DNA-damage-inducible protein GADD45 beta, Myeloid differentiation primary response protein MyD118, Negative growth regulatory protein MyD118, DKFZp566B133.

    • 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

      MTLEELVACD NAAQKMQTVT AAVEELLVAA QRQDRLTVGV YESAKLMNVD PDSVVLCLLA IDEEEEDDIA LQIHFTLIQS FCCDNDINIV
      RVSGMQRLAQ LLGEPAETQG TTEARDLHCL LVTNPHTDAW KSHGLVEVAS YCEESRGNNQ WVPYISLQER.

    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.

    Gadd45B Human
  • View Data Sheet

    Name :

    TNFRSF6B Human

    Description:

    Tumor Necrosis Factor Receptor Superfamily, Member 6b Human Recombinant

    Tumor Necrosis Factor Receptor Superfamily, Member 6b Decoy, Decoy Receptor For Fas Ligand, Decoy Receptor 3, DCR3, M68E, M68, TR6, DJ583P15.1.1, DcR3.

    Product # :

    CYT-799

    Price :

    Quantity :

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    Description

    TNFRSF6B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (30-300aa) and having a molecular mass of 32.1kDa.TNFRSF6B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFRSF6B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TNFRSF6B is a member of the Tumor necrosis factor receptor superfamily. TNFRSF6B performs as a decoy receptor which races against death receptors for ligand binding. TNFRSF6B has a regulatory role in suppressing FasL- and LIGHT-mediated cell death and T cell activation in addition to inducing angiogenesis via neutralization of TL1A.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily, Member 6b Decoy, Decoy Receptor For Fas Ligand, Decoy Receptor 3, DCR3, M68E, M68, TR6, DJ583P15.1.1, DcR3.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSVAETPTY PWRDAETGER LVCAQCPPGT FVQRPCRRDS PTTCGPCPPR HYTQFWNYLE RCRYCNVLCG EREEEARACH ATHNRACRCR TGFFAHAGFC LEHASCPPGA GVIAPGTPSQ NTQCQPCPPG TFSASSSSSE QCQPHRNCTA LGLALNVPGS SSHDTLCTSC TGFPLSTRVP GAEECERAVI DFVAFQDISI KRLQRLLQAL EAPEGWGPTP RAGRAALQLK LRRRLTELLG AQDGALLVRL LQALRVARMP GLERSVRERF LPVH.

    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.

    Tnfrsf6B Human
  • View Data Sheet

    Name :

    LCN2 Mouse

    Description:

    Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Mouse Recombinant

    Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.

    Product # :

    ENZ-875

    Price :

    Quantity :

    Shipping Method :

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    Description

    LCN2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (21-200 a.a) and having a molecular mass of 23.3kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCN2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
      They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

    • Synonyms

      Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.

    • 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 MGSQDSTQNL IPAPSLLTVP LQPDFRSDQF RGRWYVVGLA GNAVQKKTEG SFTMYSTIYE LQENNSYNVT SILVRDQDQG CRYWIRTFVP SSRAGQFTLG NMHRYPQVQS YNVQVATTDY NQFAMVFFRK TSENKQYFKI TLYGRTKELS PELKERFTRF AKSLGLKDDN IIFSVPTDQC IDN.

    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.

    Lcn2 Mouse
  • View Data Sheet

    Name :

    LECT1 Human

    Description:

    Leukocyte Cell Derived Chemotaxin 1 Human Recombinant

    BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    Product # :

    PRO-1846

    Price :

    Quantity :

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    Description

    LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 144 amino acids (214-334) and having a molecular mass of 16.3kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Leukocyte Cell Derived Chemotaxin 1, also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.

    • Synonyms

      BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    • 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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV.

    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.

    Lect1 Human
  • View Data Sheet

    Name :

    Leptin qA Human

    Description:

    Leptin Antagonist Quadruple Mutant Human Recombinant

    Product # :

    CYT-353

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    • More Info
    • Citations

    Description

    Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.Leptin Antagonist Quadruple Mutant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin Quadruple Antagonist Mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Quadruple Mutant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant 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-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.89 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 Qa Human
  • View Data Sheet

    Name :

    LGALS7 Mouse

    Description:

    Galectin-7 Mouse Recombinant

    Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.

    Product # :

    CYT-184

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    Description

    LGALS7 mouse Recombinant produced E. coli is a single polypeptide chain containing 159 amino acids (1-136) and having a molecular mass of 17.6kDa.LGALS7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LGALS7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    LGALS7 Mouse-SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.

    • Synonyms

      Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.

    • 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 MGSMSATQHK TSLPQGVRVG TVMRIRGMVP DQAGRFHVNL LCGEEQGADA ALHFNPRLDT SEVVFNTKEQ GKWGREERGT GIPFERGQPF EVLLIATEEG FKAVVGDDEY LHFHHRMPPA RVRLVEVGGD VQLHSVKIF.

    • Background

      What is the molecular weight/Mw of LGALS7 MOUSE Protein?
      LGALS7 MOUSE Protein has a total Mw of 17.6kDa.

      What is the source or expression system of LGALS7 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of LGALS7 MOUSE Protein?
      LGALS7 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS7 MOUSE Protein?
      The biological functionality of LGALS7 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of LGALS7 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMSATQHK TSLPQGVRVG TVMRIRGMVP DQAGRFHVNL LCGEEQGADA ALHFNPRLDT SEVVFNTKEQ GKWGREERGT GIPFERGQPF EVLLIATEEG FKAVVGDDEY LHFHHRMPPA RVRLVEVGGD VQLHSVKIF.

      What applications can LGALS7 MOUSE Protein be used in?
      LGALS7 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS7 MOUSE Protein?
      The endotoxin level is minimal, LGALS7 MOUSE Protein was purified using conventional chromatography techniques.


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

    Lgals7 Mouse
  • View Data Sheet

    Name :

    TXN2 Human

    Description:

    Thioredoxin-2 Human Recombinant

    Thioredoxin mitochondrial, Thioredoxin-2, TXN2, MTRX, TRX2, MT-TRX, TRX-2, TXN-2.

    Product # :

    PRO-625

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    Description

    MTRX Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 108 amino acids and having a molecular mass of 11 kDa.

    Source

    Escherichia Coli.

    Formulation

    TXN2 protein solution contains 1x PBS pH-7.4.

    Purity

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

    Biological Activity

    Specific activity is 3-4 A650/min/mg, obtained by measuring the increase of INS precipitation in absorbance at 650 nm resulting from the reduction of INS.

    Citations

    More Info

    • Introduction

      Thioredoxin-2 is a low molecular weight redox protein. TRX2 contains a redox active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The TXN2 is involved in the regulation of the mitochondrial membrane potential and in protection against oxidant-induced apoptosis. Upon stimulation of Fas, TXN2 mediates denitrosylation of mitochondria-associated caspase-3, a process required for caspase-3 activation, and promoted apoptosis.
      TRX2 is important at low oxidative stress conditions.
      MTRX is involved in the regulation of the mitochondrial membrane potential and cell death. Mitochondrial thioredoxin plays an important roles in protection against oxidant-induced apoptosis. Thioredoxin1 and thioredoxin2 have opposed regulatory functions on hypoxia-inducible factor-1alpha.

    • Synonyms

      Thioredoxin mitochondrial, Thioredoxin-2, TXN2, MTRX, TRX2, MT-TRX, TRX-2, TXN-2.

    • 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

      MTTFNIQDGP DFQDRVVNSE TPVVVDFHAQ WCGPCKILGP RLEKMVAKQH GKVVMAKVDI DDHTDLAIEY EVSAVPTVLA MKNGDVVDKF VGIKDEDQLE AFLKKLIG.

    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.

    Txn2 Human
  • View Data Sheet

    Name :

    TXNDC17 Human

    Description:

    Thioredoxin Domain Containing 17 Human Recombinant

    Thioredoxin domain containing 17, Thioredoxin-like protein 5, Protein 42-9-9, thioredoxin (Trx)-related protein 14 kDa, TRP14, TXNL5, MGC14353.

    Product # :

    PRO-1055

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    Description

    TXNDC17 Human Recombinant produced in E. coli is a single polypeptide chain containing 147 amino acids (1-123) and having a molecular mass of 16.5kDa.TXNDC17 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TXNDC17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM Nacl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TXNDC17 is a disulfide reductase that takes part in several redox reactions using the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. TXNDC17 has peroxidase activity and assists to eliminate cellular hydrogen peroxide.

    • Synonyms

      Thioredoxin domain containing 17, Thioredoxin-like protein 5, Protein 42-9-9, thioredoxin (Trx)-related protein 14 kDa, TRP14, TXNL5, MGC14353.

    • 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 MGSHMARYEE VSVSGFEEFH RAVEQHNGKT IFAYFTGSKD AGGKSWCPDC VQAEPVVREG LKHISEGCVF IYCQVGEKPY WKDPNNDFRK NLKVTAVPTL LKYGTPQKLV ESECLQANLV EMLFSED

    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.

    Txndc17 Human
  • View Data Sheet

    Name :

    PVALB Human

    Description:

    Parvalbumin Human Recombinant

    Parvalbumin alpha, PVALB, D22S749, MGC116759.

    Product # :

    PRO-004

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    Description

    PVALB Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-110 a.a.) and having a molecular mass of 14.6kDa. The PVALB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PVALB solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Parvalbumin alpha (PVALB) is a member of a larger group of EF hand proteins. PVALB is a high affinity calcium ion-binding protein which is structurally and functionally similar to calmodulin and troponin C. Parvalbumin is expressed in a specific population of GABAergic interneurones which are believed to have a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus.

    • Synonyms

      Parvalbumin alpha, PVALB, D22S749, MGC116759.

    • 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 MGSHMSMTDL LNAEDIKKAV GAFSATDSFD HKKFFQMVGLKKKSADDVKK VFHMLDKDKS GFIEEDELGF ILKGFSPDAR DLSAKETKML MAAGDKDGDG KIGVDEFSTL VAES.

    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.

    Pvalb Human
  • View Data Sheet

    Name :

    VPS25 Human

    Description:

    Vacuolar Protein Sorting 25 Human Recombinant

    Vacuolar protein sorting 25 homolog (S. cerevisiae), vacuolar protein-sorting-associated protein 25, ELL-associated protein of 20 kDa, ESCRT-II complex subunit VPS25, Dermal papilla-derived protein 9, DERP9, EAP20, FAP20, MGC10540.

    Product # :

    PRO-1054

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    Description

    VPS25 Human Recombinant produced in E. coli is a single polypeptide chain containing 200 amino acids (1-176) and having a molecular mass of 23.3kDa.VPS25 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The VPS25 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      VPS25 contains the ESCRT-II complex (endosomal sorting complex required for transport II), that is needed for sorting of endosomal cargo proteins into MVBs and multivesicular body (MVB) formation. The MVB pathway facilitates transport of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex takes part in the recruitment of the ESCRT-III complex which is involved in transcription regulation, probably through its collaboration with ELL.

    • Synonyms

      Vacuolar protein sorting 25 homolog (S. cerevisiae), vacuolar protein-sorting-associated protein 25, ELL-associated protein of 20 kDa, ESCRT-II complex subunit VPS25, Dermal papilla-derived protein 9, DERP9, EAP20, FAP20, MGC10540.

    • 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 MGSHMAMSFE WPWQYRFPPF FTLQPNVDTR QKQLAAWCSL VLSFCRLHKQ SSMTVMEAQE SPLFNNVKLQ RKLPVESIQI VLEELRKKGN LEWLDKSKSS FLIMWRRPEE WGKLIYQWVS RSGQNNSVFT LYELTNGEDT EDEEFHGLDE ATLLRALQAL QQEHKAEIIT VSDGRGVKFF

    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.

    Vps25 Human
  • View Data Sheet

    Name :

    RELM g Mouse

    Description:

    RELM-Gamma Mouse Recombinant

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

    Product # :

    CYT-1035

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    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.

    Citations

    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
  • View Data Sheet

    Name :

    RGS19 Human

    Description:

    Regulator of G-Protein Signaling 19 Human Recombinant

    GAIP, Regulator of G-protein signalling 19, G alpha interacting protein, GNAI3IP.

    Product # :

    PRO-037

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    Description

    RGS19 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217a.a.) and having a molecular mass of 26.7kDa.RGS19 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RGS19 protein solution (0.5mg/1ml) is formulated in Phosphate Buffered Saline (pH7.4) and 10% Glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RGS19 is a member of RGS (regulator of G protein signaling) family and negatively regulates G protein coupled receptor signaling. RGS19 protein specifically cooperates with heterotrimeric GTP-binding protein G alpha i3 (GAI3).

    • Synonyms

      GAIP, Regulator of G-protein signalling 19, G alpha interacting protein, GNAI3IP.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPTPHEAEKQ ITGPEEADRP PSMSSHDTAS PAAPSRNPCC LCWCCCCSCS WNQERRRAWQ ASRESKLQPL PSCEVCATPS PEEVQSWAQS FDKLMHSPAG RSVFRAFLRT EYSEENMLFW LACEELKAEA NQHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINKKMQ EPSAHTFDDA QLQIYTLMHR DSYPRFLSSP TYRALLLQGP SQSSSEA

    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.

    Rgs19 Human
  • View Data Sheet

    Name :

    GDF15 Mouse

    Description:

    Growth and Differentiation factor 15 Mouse Recombinant

    Growth/differentiation factor 15, GDF-15.

    Product # :

    CYT-857

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    Description

    GDF15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (189-303 a.a) and having a molecular mass of 14.9kDa. GDF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF15 protein solution (1.0mg/ml) containing 20mM Phosphate buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    GDF15 Mouse - Product image 1

    Citations

    More Info

    • Introduction

      GDF15 is part of the TGF-Beta superfamily which is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.

    • Synonyms

      Growth/differentiation factor 15, GDF-15.

    • 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 MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.

    • Background

      What is the molecular weight/Mw of GDF15 MOUSE Protein?
      GDF15 MOUSE Protein has a total Mw of 14.9kDa.

      What is the source or expression system of GDF15 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of GDF15 MOUSE Protein?
      GDF15 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 MOUSE Protein?
      The biological functionality of GDF15 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of GDF15 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.

      What applications can GDF15 MOUSE Protein be used in?
      GDF15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF15 MOUSE Protein?
      The endotoxin level is minimal, GDF15 MOUSE Protein was purified using conventional chromatography techniques.

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

    Gdf15 Mouse
  • View Data Sheet

    Name :

    AP1AR Human

    Description:

    Adaptor-Related Protein Complex 1 Associated Regulatory Protein Human Recombinant

    AP-1 complex-associated regulatory protein, 2c18, Adapter-related protein complex 1-associated regulatory protein, Gamma-1-adaptin brefeldin A resistance protein, GBAR, Gamma-BAR, Gamma-A1-adaptin and kinesin interactor, Gadkin, AP1AR, C4orf16, PRO0971.

    Product # :

    PRO-1696

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    Description

    AP1AR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-302) and having a molecular mass of 36.4 kDa.AP1AR is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AP1AR solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adaptor-related protein complex 1 associated regulatory protein (AP1AR) is essential for AP-1 dependent transport between the trans-Golgi network and endosomes. AP1AR regulates the membrane association of AP1G1/Gamma1-adaptin which is one of the subunits of the AP-1 adapter complex. AP1AR plays a role as effector of AP-1 in calcium-induced endo-lysosome secretion. The interaction with AP1G1/Gamma1-adaptin attenuates the release of the AP-1 complex from membranes.

    • Synonyms

      AP-1 complex-associated regulatory protein, 2c18, Adapter-related protein complex 1-associated regulatory protein, Gamma-1-adaptin brefeldin A resistance protein, GBAR, Gamma-BAR, Gamma-A1-adaptin and kinesin interactor, Gadkin, AP1AR, C4orf16, PRO0971.

    • 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 MGNCCWTQCF GLLRKEAGRL QRVGGGGGSK YFRTCSRGEH LTIEFENLVE SDEGESPGSS HRPLTEEEIV DLRERHYDSI AEKQKDLDKK IQKELALQEE KLRLEEEALY AAQREAARAA KQRKLLEQER QRIVQQYHPS NNGEYQSSGP EDDFESCLRN MKSQYEVFRS SRLSSDATVL TPNTESSCDL MTKTKSTSGN DDSTSLDLEW EDEEGMNRML PMRERSKTEE DILRAALKYS NKKTGSNPTS ASDDSNGLEW ENDFVSAEMD DNGNSEYSGF VNPVLELSDS GIRHSDTDQQ TR.

    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.

    Ap1Ar Human
  • View Data Sheet

    Name :

    FLT1 Human

    Description:

    Vascular Endothelial Growth Factor Receptor-1 Human Recombinant

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-240

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    • description
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    Description

    Soluble FLT1 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 687 amino acids and having a molecular mass of 96 kDa. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity of FLT1 was determined by its ability to inhibit the VEGF (165)-induced proliferation of HUVECs.

    Citations

    More Info

    • Introduction

      Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 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 FLT1 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRGEHC NKKAVFSRIS KFKSTRNDCT TQSNVKH

    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.

    Flt1 Human
  • View Data Sheet

    Name :

    FSTL1 Human

    Description:

    Follistatin Like 1 Human Recombinant

    Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.

    Product # :

    CYT-792

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    Description

    FSTL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 309 amino acids (21-308) and having a molecular mass of 34.9 kDa.FSTL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The FSTL1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    FSTL1  Human-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      FSTL1 protein resembles follistatin, an ACTV-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.

    • Synonyms

      Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.

    • 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 MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.

    • Background

      What is the molecular weight/Mw of FSTL1 HUMAN Protein?
      FSTL1 HUMAN Protein has a total Mw of 34.9kDa.

      What is the source or expression system of FSTL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FSTL1 HUMAN Protein?
      FSTL1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of FSTL1 HUMAN Protein?
      The biological functionality of FSTL1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of FSTL1 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.

      What applications can FSTL1 HUMAN Protein be used in?
      FSTL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FSTL1 HUMAN Protein?
      The endotoxin level is minimal, FSTL1 HUMAN Protein was purified using conventional chromatography techniques.

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

    Fstl1 Human
  • View Data Sheet

    Name :

    MAPKAPK3 Human

    Description:

    Mitogen-Activated Protein Kinase-Activated Protein Kinase 3 Human Recombinant

    3PK, MAPKAP-K3, MAPKAP3, MAPKAPK-3, MK-3, MAP kinase-activated protein kinase 3, MAPK-activated protein kinase 3, MAPKAP kinase 3,MAPKAPK-3, MK-3,MAPKAPK3.

    Product # :

    PKA-045

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    Description

    MAPKAPK3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 405 amino acids (1-382 a.a) and having a molecular mass of 45.4kDa. MAPKAPK3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    MAPKAPK3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MAP kinase-activated protein kinase 3 (MAPKAPK3) is involved in inflammatory Reaction by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally. MAPKAPK3 phosphorylates AU-rich elements (AREs)-binding proteins, like TTP/ZFP36, leading to control of stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36 (a major post-transcriptional regulator of TNF), promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity resulting in inhibition of dependent degradation of ARE-containing transcript. MAPKAPK3 is activated by growth inducers and stress stimulation of cells.

    • Synonyms

      3PK, MAPKAP-K3, MAPKAP3, MAPKAPK-3, MK-3, MAP kinase-activated protein kinase 3, MAPK-activated protein kinase 3, MAPKAP kinase 3,MAPKAPK-3, MK-3,MAPKAPK3.

    • 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 MGSMDGETAE EQGGPVPPPV APGGPGLGGA PGGRREPKKY AVTDDYQLSK QVLGLGVNGK VLECFHRRTG QKCALKLLYD SPKARQEVDH HWQASGGPHI VCILDVYENM HHGKRCLLII MECMEGGELF SRIQERGDQA FTEREAAEIM RDIGTAIQFL HSHNIAHRDV KPENLLYTSK EKDAVLKLTD FGFAKETTQN ALQTPCYTPY YVAPEVLGPE KYDKSCDMWS LGVIMYILLC GFPPFYSNTG QAISPGMKRR IRLGQYGFPN PEWSEVSEDA KQLIRLLLKT DPTERLTITQ FMNHPWINQS MVVPQTPLHT ARVLQEDKDH WDEVKEEMTS ALATMRVDYD QVKIKDLKTS NNRLLNKRRK KQAGSSSASQ GCNNQ.

    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.

    Mapkapk3 Human
  • View Data Sheet

    Name :

    Thymosin beta 4

    Description:

    Thymosin β4

    Thymosin beta-4. TB500, TB-500

    Product # :

    HOR-275

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    Description

    Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    Citations

    More Info

    • Introduction

      Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.

    • Synonyms

      Thymosin beta-4. TB500, TB-500

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.

    • Background

      What is the molecular weight/Mw of THYMOSIN BETA 4 Protein?
      THYMOSIN BETA 4 Protein has a total Mw of 4.96kDa.

      What is the Purity of THYMOSIN BETA 4 Protein?
      THYMOSIN BETA 4 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of THYMOSIN BETA 4 Protein?
      The biological functionality of THYMOSIN BETA 4 Protein will be determined in the future.

      What is the amino acid sequence of THYMOSIN BETA 4 Protein?
      Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.
      What applications can THYMOSIN BETA 4 Protein be used in?
      THYMOSIN BETA 4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for THYMOSIN BETA 4 Protein?
      The endotoxin level is minimal, THYMOSIN BETA 4 Protein was purified using conventional chromatography techniques.

      Who supplies THYMOSIN BETA 4 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of THYMOSIN BETA 4?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Thymosin Beta 4
  • View Data Sheet

    Name :

    LECT1 (214-333) Human

    Description:

    Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.) Human Recombinant

    BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    Product # :

    PRO-1857

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    Description

    LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 143 amino acids (214-333) and having a molecular mass of 16.2kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.), also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.

    • Synonyms

      BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    • 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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQEGESMT FDPRLDHEGI CCIECRRSYT HCQKICEPLG GYYPWPYNYQ GCRSACRVIM PCSWWVARIL GMV.

    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.

    Lect1 214 333 Human
  • View Data Sheet

    Name :

    SERPINA9 Mouse

    Description:

    Serpin Peptidase Inhibitor, Clade A Mouse Recombinant

    Serpin A9, Serpina9, SERPINA9.

    Product # :

    PRO-2366

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    Description

    SERPINA9 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 401 amino acids (26-418 a.a) and having a molecular mass of 45.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).SERPINA9 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SERPINA9 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Serpin Peptidase Inhibitor, Clade A Member 9, also known as serpin A9, belongs to the Serpin superfamily of serine protease inhibitors. Serpins are the most extensively distributed superfamily of protease inhibitors which use a conformational modification to inhibit target enzymes. Serpins are known to inhibit serine proteases as well as inhibiting caspases in addition to papain-like cysteine proteases. Serpins are conformational labile and numerous of the disease-linked mutations of serpins outcome in misfolding or in pathogenic, inactive polymers. serpin A9 demonstrates inhibition towards trypsin, thrombin, as well as plasmin and binds DNA and heparin.

    • Synonyms

      Serpin A9, Serpina9, SERPINA9.

    • 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

      NPYNQESSHL PSMKKNPASQ VSPSNTRFSF LLYQRLAQEN PGQNILFSPV SISTSLAMLS LGARSATKTQ ILRTLGFNFT WVSEPTIHMG FEYLVRSLNK CHQGRELRMG SVLFIRKELQ LQATFLDRVK KLYGAKVFSE DFSNAATAQA QINSYVEKET KGKVVDVIQD LDSQTAMVLV NHIFFKANWT QPFSTANTNK SFPFLLSKGT TVHVPMMHQT ESFAFGVDKE LGCSILQMDY RGDAVAFFVL PGKGKMRQLE KSLSARRLRK WSRSLQKRWI KVFIPKFSIS ASYNLETILP KMGIRDAFNS NADFSGITKT HFLQVSKAAH KAVLDVSEEG TEAAAATTTK LIVRSRDTPS SIIAFKEPFL ILLLDKNTES VLFLGKVENP RKMLEHHHHH H

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    Serpina9 Mouse
  • 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.

    Citations

    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 :

    ANKRD54 Human

    Description:

    Ankyrin Repeat Domain 54 Protein Human Recombinant

    LIAR, Lyn-interacting ankyrin repeat protein.

    Product # :

    PRO-1480

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    Description

    ANKRD54 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a.) and having a molecular mass of 34.9kDa.ANKRD54 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ANKRD54 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ankyrin Repeat Domain 54 (ANKRD54), which is also known as LIAR contains 4 ANK repeats. ANKRD54 plays a vital role in regulating intracellular signaling events related with erythroid terminal differentiation. ANKRD54 interacts with LYN through ankyrin repeat region and the SH3-domain in an activation-independent status of LYN. ANKRD54 creates a multiprotein complex with LYN and HCLS1.

    • Synonyms

      LIAR, Lyn-interacting ankyrin repeat protein.

    • 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 MGSMAAAAGD ADDEPRSGHS SSEGECAVAP EPLTDAEGLF SFADFGSALG GGGAGLSGRA SGGAQSPLRY LHVLWQQDAE PRDELRCKIP AGRLRRAARP HRRLGPTGKE VHALKRLRDS ANANDVETVQ QLLEDGADPC AADDKGRTAL HFASCNGNDQ IVQLLLDHGA DPNQRDGLGN TPLHLAACTN HVPVITTLLR GGARVDALDR AGRTPLHLAK SKLNILQEGH AQCLEAVRLE VKQIIHMLRE YLERLGQHEQ RERLDDLCTR LQMTSTKEQV DEVTDLLASF TSLSLQMQSM EKR.

    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.

    Ankrd54 Human
  • View Data Sheet

    Name :

    NEUROG3 Human

    Description:

    Neurogenin 3 Human Recombinant

    Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.

    Product # :

    CYT-811

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    Description

    NEUROG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-214) and having a molecular mass of 25.1 kDa. NEUROG3 is fused to a 20 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The NEUROG3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NEUROG3 is a common helix-loop-helix (bHLH) transcription factor which takes part in neurogenesis. NEUROG3 functions as a heterodimer with another bHLH protein. Mutations in this gene can result in congenital malabsorptive diarrhea 4 (DIAR4).

    • Synonyms

      Neurogenin 3, Class A Basic Helix-Loop-Helix Protein 7, Protein Atonal Homolog 5, BHLHA7, Math4B, NGN3, Atoh5.

    • 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 MTPQPSGAPT VQVTRETERS FPRASEDEVT CPTSAPPSPT RTRGNCAEAE EGGCRGAPRK LRARRGGRSR PKSELALSKQ RRSRRKKAND RERNRMHNLN SALDALRGVL PTFPDDAKLT KIETLRFAHN YIWALTQTLR IADHSLYALE PPAPHCGELG SPGGSPGDWG SLYSPVSQAG SLSPAASLEE RPGLLGATSS ACLSPGSLAF SDFL

    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.

    Neurog3 Human
  • View Data Sheet

    Name :

    EGF Mouse, Biotin

    Description:

    Epidermal Growth Factor Mouse Recombinant, Biotin

    Urogastrone, URG, EGF.

    Product # :

    CYT-841

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

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

    Description

    EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.

    Source

    Escherichia Coli.

    Formulation

    The protein (0.5mg/ml) solution contains sterile PBS.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

    Citations

    More Info

    • Introduction

      Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Should be stored at 4°C.Please do not freeze.

    • Amino Acid Sequence

      MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

    • Background

      Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential

      Abstract:

      This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.

      Introduction:

      Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.

      Protein Engineering and Biotin Conjugation:

      EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.

      Cellular Signaling Amplification:

      The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.

      Cellular Assays and Functional Responses:

      In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.

      Tailored Delivery Strategies:

      The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.

      Regenerative Medicine and Targeted Therapy:

      The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.

      Future Prospects and Challenges:

      While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.

      Conclusion:

      In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.

      What is the molecular weight/Mw of MEGF, BIOTIN Protein?
      MEGF, BIOTIN Protein has a total Mw of 7kDa.

      What is the source or expression system of MEGF, BIOTIN Protein?
      Escherichia Coli.

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

      What is the Biological Activity of MEGF, BIOTIN Protein?
      The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

      What is the amino acid sequence of MEGF, BIOTIN Protein?
      MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

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

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

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

    Egf Mouse Biotin
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