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Search results

1000 results found for “EPH Receptor”

Name

Description

Product #

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  • View Data Sheet

    Name :

    MBP E.Coli, His

    Description:

    Maltose Binding Protein E.coli Recombinant, His Tag

    Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    Product # :

    PRO-2322

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    Description

    Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
      MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

    • Synonyms

      Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    • 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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.

    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.

    Mbp Ecoli His
  • View Data Sheet

    Name :

    TEK Mouse

    Description:

    TEK Tyrosine Kinase Endothelial Mouse Recombinant

    Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.

    Product # :

    PKA-083

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    Description

    TEK produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 730 amino acids (23-746 a.a.) and having a molecular mass of 81.6kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). TEK is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.

    • Synonyms

      Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.

    • 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

      AMDLILINSL PLVSDAETSL TCIASGWHPH EPITIGRDFE ALMNQHQDPL EVTQDVTREW AKKVVWKREK ASKINGAYFC EGRVRGQAIR IRTMKMRQQA SFLPATLTMT VDRGDNVNIS FKKVLIKEED AVIYKNGSFI HSVPRHEVPD ILEVHLPHAQ PQDAGVYSAR YIGGNLFTSA FTRLIVRRCE AQKWGPDCSR PCTTCKNNGV CHEDTGECIC PPGFMGRTCE KACEPHTFGR TCKERCSGPE GCKSYVFCLP DPYGCSCATG WRGLQCNEAC PSGYYGPDCK LRCHCTNEEI CDRFQGCLCS QGWQGLQCEK EGRPRMTPQI EDLPDHIEVN SGKFNPICKA SGWPLPTSEE MTLVKPDGTV LQPNDFNYTD RFSVAIFTVN RVLPPDSGVW VCSVNTVAGM VEKPFNISVK VLPEPLHAPN VIDTGHNFAI INISSEPYFG DGPIKSKKLF YKPVNQAWKY IEVTNEIFTL NYLEPRTDYE LCVQLARPGE GGEGHPGPVR RFTTASIGLP PPRGLSLLPK SQTALNLTWQ PIFTNSEDEF YVEVERRSLQ TTSDQQNIKV PGNLTSVLLS NLVPREQYTV RARVNTKAQG EWSEELRAWT LSDILPPQPE NIKISNITDS TAMVSWTIVD GYSISSIIIR YKVQGKNEDQ HIDVKIKNAT VTQYQLKGLE PETTYHVDIF AENNIGSSNP AFSHELRTLP HSPASADLGG GKMLHHHHHH.

    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.

    Tek Mouse
  • View Data Sheet

    Name :

    NCR3 Human

    Description:

    Natural Cytotoxicity Triggering Receptor 3 Human Recombinant

    Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    Product # :

    PRO-1886

    Price :

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    Description

    NCR3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (19-138 a.a) and having a molecular mass of 15.3kDa.NCR3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NCR3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytotoxicity Triggering Receptor 3 also known as NCR3 is a natural cytotoxicity receptor (NCR) which assists NK cells in the lysis of tumor cells. Moreover, NCR3 interacts with CD3-zeta (CD247), a T-cell receptor. A single nucleotide polymorphism in the 5' untranslated region of NCR3 has been related with mild malaria suceptibility. Three transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    • 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 MLWVSQPPEI RTLEGSSAFL PCSFNASQGR LAIGSVTWFR DEVVPGKEVR NGTPEFRGRL APLASSRFLH DHQAELHIRD VRGHDASIYV CRVEVLGLGV GTGNGTRLVV EKEHPQLGAG T

    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.

    Ncr3 Human
  • View Data Sheet

    Name :

    TSLPR Human

    Description:

    Thymic Stromal Lymphopoietin Receptor Human Recombinant

    CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.

    Product # :

    CYT-742

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    Description

    TSLPR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (23-231 a.a.) and having a molecular mass of 26.6kDa.TSLPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymic Stromal Lymphopoietin Receptor (TSLPR) is a member of the type I cytokine receptor family. TSLPR alongside the interleukin 7 receptor (IL7R) activate STAT3, STAT5, and JAK2 pathways, which is regulated processes such as cell proliferation and development of the hematopoietic system. Two transcript variants encoding dissimilar isoforms have been found for this gene. TSLPR is expressed in heart, skeletal muscle, kidney and adult and fetal liver.

    • Synonyms

      CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.

    • 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 MGSQGGAAEG VQIQIIYFNL ETVQVTWNAS KYSRTNLTFH YRFNGDEAYD QCTNYLLQEG HTSGCLLDAE QRDDILYFSI RNGTHPVFTA SRWMVYYLKP SSPKHVRFSW HQDAVTVTCS DLSYGDLLYE VQYRSPFDTE WQSKQENTCN VTIEGLDAEK CYSFWVRVKA MEDVYGPDTY PSDWSEVTCW QRGEIRDACA ETPTPPKPKL SK.

    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.

    Tslpr Human
  • View Data Sheet

    Name :

    FOLR2 Human

    Description:

    Folate Receptor 2 Human Recombinant

    Folate receptor beta, FR-beta, Folate receptor 2, Folate receptor, fetal/placental, Placental folate-binding protein, BETA-HFR Protein, FBP/PL-1 Protein, FR-BETA Protein, FR-P3 Protein, FRbeta, FR-BETA, FBP/PL1, BETA-HFR, FBP, FOLR2

    Product # :

    PRO-2673

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    Description

    FOLR2 Human Recombinant is a single, glycosylated polypeptide chain containing 215 amino acids (22-230a.a) and having a molecular mass of 25.1kDa. FOLR2 is fused to a 6 a.a His tag at C-terminal, and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The FOLR2 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    ED50 Range is ≤ 5 ug/ml. The Biological activity is measured by the protein’s binding ability in a functional ELISA with Folic Acid-BSA.

    More Info

    • Introduction

      Folate Receptor 1, also known as FOLR1, is a part of the folate receptor family whose members bind folic acid. FOLR1 binds to folate and reduced folic acid derivatives and facilitates transfer of 5-methyltetrahydrofolate and folate analogs into the cells. FOLR1 is either attaches to membranes through a glycosyl-phosphatidylinositol linkage or exists in a soluble form. FOLR1 is also needed for embryonic development and normal cell proliferation.

    • Synonyms

      Folate receptor beta, FR-beta, Folate receptor 2, Folate receptor, fetal/placental, Placental folate-binding protein, BETA-HFR Protein, FBP/PL-1 Protein, FR-BETA Protein, FR-P3 Protein, FRbeta, FR-BETA, FBP/PL1, BETA-HFR, FBP, FOLR2

    • 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

      QDRTDLLNVC MDAKHHKTKP GPEDKLHDQC SPWKKNACCT ASTSQELHKD TSRLYNFNWD HCGKMEPACK RHFIQDTCLY ECSPNLGPWI QQVNQSWRKE RFLDVPLCKE DCQRWWEDCH TSHTCKSNWH RGWDWTSGVN KCPAGALCRT FESYFPTPAA LCEGLWSHSY KVSNYSRGSG RCIQMWFDSA QGNPNEEVAR FYAAAMHVNH HHHHH

    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.

    Folr2 Human
  • View Data Sheet

    Name :

    EGF (1-51), Human

    Description:

    Epidermal Growth Factor (1-51 a.a.)Human Recombinant

    Urogastrone, URG, EGF.

    Product # :

    CYT-1115

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    Description

    Epidermal Growth Factor (1-51 a.a.) Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.0kDa. The EGF is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.

    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 several epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

    • Background

      Exploring the Potential of Epidermal Growth Factor (1-51 a.a.) Human Recombinant: Novel Insights and Therapeutic Prospects

      Abstract:

      Epidermal Growth Factor (EGF) stands as a pivotal cytokine orchestrating essential cellular processes. This concise research paper delves into the unique realm of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, unveiling its intricate molecular dynamics, signaling cascades, and therapeutic promise. Employing cutting-edge methodologies encompassing in vitro assays and animal models, this study elucidates the multifaceted cellular responses sparked by this truncated EGF variant, paving the way for potential clinical applications.

      Introduction:

      The truncated form of EGF, spanning amino acids 1 to 51 (a.a.), carries distinct attributes that set it apart from the full-length counterpart. This paper centers on exploring the intriguing dimensions of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, offering new insights into its interactions and potential utility.

      Molecular Insights and Signaling Dynamics:

      At the heart of its function lies the interplay between EGF (1-51 a.a.) and the epidermal growth factor receptor (EGFR). High-resolution structural analyses unveil the nuances of their binding interface, initiating a cascade of phosphorylation events that trigger canonical and non-canonical signaling pathways. The MAPK pathway and the PI3K/Akt pathway, intricately modulated by EGF (1-51 a.a.), propel cellular processes like proliferation, migration, and evasion of apoptosis.

      In Vitro Profiling and Cellular Responses:

      In dissecting the cellular responses, diverse in vitro assays have been employed. These encompass cell viability assays, wound healing assays, and intricate fluorescence resonance energy transfer (FRET) studies. These assays converge to illuminate the dynamic orchestration of EGF-induced cellular behaviors, showcasing its role in promoting cellular migration, division, and wound closure.

      In Vivo Implications and Therapeutic Horizons:

      Translating these insights into tangible therapeutic possibilities, in vivo studies present a compelling narrative. In animal models, EGF (1-51 a.a.) emerges as a potent player in cutaneous wound healing, fostering accelerated tissue regeneration. Moreover, its potential extends to oncology, as it not only influences tumor microenvironments but also demonstrates anti-apoptotic effects, hinting at its role in tailored cancer interventions.

      Future Prospects and Challenges:

      While these discoveries hold immense promise, challenges persist. The intricate network of signaling events demands further scrutiny, considering potential cross-talk and off-target effects. Refining delivery mechanisms and dosing regimens is essential for realizing the clinical potential of EGF (1-51 a.a.).

      Conclusion:

      In a synthesis of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (1-51 a.a.) Human Recombinant emerges as a captivating subject. Its truncated structure and distinctive signaling cascades paint a canvas of cellular orchestration. As research advances, harnessing its therapeutic benefits could usher in novel interventions for wound healing and cancer therapy.

      What is the molecular weight/Mw of EGF Protein?
      EGF Protein has a total Mw of 6kDa.

      What is the source or expression system of EGF Protein?
      Saccharomyces cerevisiae

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

      What is the Biological Activity of EGF Protein?
      The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.

      What is the amino acid sequence of EGF Protein?
      NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

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

      What is the endotoxin level for EGF Protein?
      The endotoxin level is minimal, EGF 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 Protein
  • View Data Sheet

    Name :

    LAIR2 Human

    Description:

    Leukocyte-Associated Ig-Like Receptor 2 Human Recombinant

    Leukocyte-associated immunoglobulin-like receptor 2, LAIR-2, CD306, LAIR2.

    Product # :

    PRO-1081

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    Description

    LAIR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (22-135 a.a) and having a molecular mass of 15.2kDa.LAIR2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LAIR2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Leukocyte-associated immunoglobulin-like receptor 2 (LAIR2) is a secreted, 131 amino acids protein which contains one IglikeC2 type domain, rendering it a member of the Ig superfamily. Even though one is secreted and one is membrane bound, the 2 LAIR proteins are assumed to have evolved from a common gene ancestor and seem to share similar adhesion profiles, suggesting that LAIR2 may compete with LAIR1 for ligand binding. LAIR2 was discovered by its similarity to LAIR1, which is an inhibitory receptor present on mononuclear leukocytes. The LAIR2 gene maps to a region of 19q13.4, dubbed the leukocyte receptor cluster, which contains 29 genes in the immunoglobulin superfamily, including LAIR1. The function of the LAIR2 protein is unknown, though it is assumed to be secreted and may help modulate mucosal tolerance.

    • Synonyms

      Leukocyte-associated immunoglobulin-like receptor 2, LAIR-2, CD306, LAIR2.

    • 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 MGSHMQEGAL PRPSISAEPG TVISPGSHVT FMCRGPVGVQ TFRLEREDRA KYKDSYNVFR LGPSESEARF HIDSVSEGNA GLYRCLYYKP PGWSEHSDFL ELLVKGTVPG TEASGFDAP.

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    Lair2 Human
  • View Data Sheet

    Name :

    HERPUD1 Human

    Description:

    HERPUD1 Human Recombinant

    Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.

    Product # :

    PRO-2105

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    Description

    HERPUD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 31.6kDa.HERPUD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HERPUD1 solution (0.5mg/1ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      HERPUD1 is a multi-pass membrane protein which is a part of the endoplasmic reticulum quality control system. HERPUD1 owns 1 N-terminal ubiquitin-like domain and is expressed highly in the brain. HERPUD1 is also known as ER-associated degradation (ERAD) which takes part in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins.

    • Synonyms

      Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.

    • 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 MGSMESETEP EPVTLLVKSP NQRHRDLELS GDRGWSVGHL KAHLSRVYPE RPRPEDQRLI YSGKLLLDHQ CLRDLLPKQE KRHVLHLVCN VKSPSKMPEI NAKVAESTEE PAGSNRGQYP EDSSSDGLRQ REVLRNLSSP GWENISRPEA AQQAFQGLGP GFSGYTPYGW LQLSWFQQIY ARQYYMQYLA ATAASGAFVP PPSAQEIPVV SAPAPAPIHN QFPAENQPAN QNAAPQVVVN PGANQNLRMN AQGGPIVEED DEINRD.

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    Herpud1 Human
  • View Data Sheet

    Name :

    EIF4E Human

    Description:

    Eukaryotic Translation Initiation Factor 4E Human Recombinant

    CBP, EIF4E1, EIF4EL1, EIF4F.

    Product # :

    PRO-530

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    Description

    EIF4E Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular weight of 27.2kDa. The EIF4E is fused to a 20 aa His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF4E 0.5mg/ml protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.

    • Synonyms

      CBP, EIF4E1, EIF4EL1, EIF4F.

    • 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 MATVEPETTP TPNPPTTEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL RLISKFDTVE
      DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG
      DKIAIWTTEC ENREAVTHIG RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV.

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    Eif4E Human
  • View Data Sheet

    Name :

    SPRED1 Human

    Description:

    Sprouty-Related EVH1 Domain Containing 1 Human Recombinant

    Sprouty-Related EVH1 Domain Containing 1, SPRED1, Spred-1, hSpred1, NFLS.

    Product # :

    PRO-2107

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    Description

    SPRED1 Human Recombinant produced in E. coli is a single polypeptide chain containing 467 amino acids (1-444) and having a molecular mass of 52.9kDa.SPRED1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPRED1 solution (0.5mg/1ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

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    • Introduction

      Sprouty-Related EVH1 Domain Containing 1, also known as SPRED1, is a part of the Sprouty family of proteins and is phosphorylated by tyrosine kinase. SPRED1 inhibits growth-factor-mediated activation of MAP kinase. SPRED1 plays a role as a homodimer or as a heterodimer with SPRED2 to regulate activation of the MAP kinase cascade. SPRED1 is a negative regulator of hematopoiesis of bone marrow.

    • Synonyms

      Sprouty-Related EVH1 Domain Containing 1, SPRED1, Spred-1, hSpred1, NFLS.

    • 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 MGSMSEETAT SDNDNSYARV RAVVMTRDDS SGGWLPLGGS GLSSVTVFKV PHQEENGCAD FFIRGERLRD KMVVLECMLK KDLIYNKVTP TFHHWKIDDK KFGLTFQSPA DARAFDRGIR RAIEDISQGC PESKNEAEGA DDLQANEEDS SSSLVKDHLF QQETVVTSEP YRSSNIRPSP FEDLNARRVY MQSQANQITF GQPGLDIQSR SMEYVQRQIS KECGSLKSQN RVPLKSIRHV SFQDEDEIVR INPRDILIRR YADYRHPDMW KNDLERDDAD SSIQFSKPDS KKSDYLYSCG DETKLSSPKD SVVFKTQPSS LKIKKSKRRK EDGERSRCVY CQERFNHEEN VRGKCQDAPD PIKRCIYQVS CMLCAESMLY HCMSDSEGDF SDPCSCDTSD DKFCLRWLAL VALSFIVPCM CCYVPLRMCH RCGEACGCCG GKHKAAG.

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    Spred1 Human
  • View Data Sheet

    Name :

    CDH1 Human, Sf9

    Description:

    E-Cadherin Human Recombinant, Sf9

    Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-1.

    Product # :

    PRO-2265

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    Description

    CDH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 694 amino acids (24-709a.a.) and having a molecular mass of 76.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70kDa). CDH1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CDH1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. It plays an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Numerous studies have demonstrated that reduction and/or loss of Ecadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis.

    • Synonyms

      Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-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

      EPEPCHPGFD AESYTFTVPR RHLERGRVLG RVNFEDCTGR QRTAYFSLDT RFKVGTDGVI TVKRPLRFHN PQIHFLVYAW DSTYRKFSTK VTLNTVGHHH RPPPHQASVS GIQAELLTFP NSSPGLRRQK RDWVIPPISC PENEKGPFPK NLVQIKSNKD KEGKVFYSIT GQGADTPPVG VFIIERETGW LKVTEPLDRE RIATYTLFSH AVSSNGNAVE DPMEILITVT DQNDNKPEFT QEVFKGSVME GALPGTSVME VTATDADDDV NTYNAAIAYT ILSQDPELPD KNMFTINRNT GVISVVTTGL DRESFPTYTL VVQAADLQGE GLSTTATAVI TVTDTNDNPP IFNPTTYKGQ VPENEANVVI TTLKVTDADA PNTPAWEAVY TILNDDGGQF VVTTNPVNND GILKTAKGLD FEAKQQYILH VAVTNVVPFE VSLTTSTATV TVDVLDVNEA PIFVPPEKRV EVSEDFGVGQ EITSYTAQEP DTFMEQKITY RIWRDTANWL EINPDTGAIS TRAELDREDF EHVKNSTYTA LIIATDNGSP VATGTGTLLL ILSDVNDNAP IPEPRTIFFC ERNPKPQVIN IIDADLPPNT SPFTAELTHG ASANWTIQYN DPTQESIILK PKMALEVGDY KINLKLMDNQ NKDQVTTLEV SVCDCEGAAG VCRKAQPVEA GLQIPALEHH HHHH.

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    Cdh1 Human Sf9
  • View Data Sheet

    Name :

    EPHX1 Antibody

    Description:

    Epoxide hydrolase 1, Mouse Anti Human

    Epoxide hydrolase 1, Microsomal epoxide hydrolase, Epoxide hydratase, EPHX1, EPHX, EPOX, MEH.

    Product # :

    ANT-440

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    Formulation

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

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    • Introduction

      Epoxide hydrolase is a vital biotransformation enzyme which converts epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase functions in both the activation and detoxification of epoxides. Mutations in the EPHX1 gene cause preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.

    • Synonyms

      Epoxide hydrolase 1, Microsomal epoxide hydrolase, Epoxide hydratase, EPHX1, EPHX, EPOX, MEH.

    • Immunogen

      Anti-human EPHX1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EPHX1 amino acids 21-455 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and κ light chain.

    • Clone

      PAT2E5AT.

    • Applications

      EPHX1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1000 ~ 2000. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      EPHX1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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    Ephx1 Antibody
  • View Data Sheet

    Name :

    EDN2 Human

    Description:

    Endothelin-2 Human Recombinant

    ET2, PPET2, Endothelin-2, ET-2, Preproendothelin-2, EDN2.

    Product # :

    HOR-006

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    Description

    EDN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (25-178 a.a.) and having a molecular mass of 19.9kDa. EDN2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    EDN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Endothelin-2 is a Hypoxia-induced Autocrine Survival Factor for Breast Tumor Cells. The synthesis of EDN2 by human kidney carcinoma cells is decreased by EGF. EDN2 is a chemoattractant for macrophages and THP-1 monocytic cells. Chemotaxis towards EDN2 is via the MAPK pathway: p44 and p42 are phosphorylated when THP-1 cells are stimulated with EDN2. Migration to EDN2 is inhibited by hypoxia and by pertussis toxin. EDN2 leads to activation of macrophages. EDN2 shares a similar peptide sequence with chemokines and may signal via a similar receptor and MAPK-mediated pathway. Furthermore, EDN2 expression by tumors may modulate the behavior of macrophages such that activated cells accumulate in areas of hypoxia.

    • Synonyms

      ET2, PPET2, Endothelin-2, ET-2, Preproendothelin-2, EDN2.

    • 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 MGSQAAATLE QPASSSHAQG THLRLRRCSC SSWLDKECVY FCHLDIIWVN TPEQTAPYGL GNPPRRRRRS LPRRCQCSSA RDPACATFCL RRPWTEAGAV PSRKSPADVF QTGKTGATTG ELLQRLRDIS TVKSLFAKRQ QEAMREPRST HSRWRKR.

    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.

    Edn2 Human His
  • View Data Sheet

    Name :

    EIF3F Human

    Description:

    Eukaryotic Translation Initiation Factor 3F Human Recombinant

    Eukaryotic Translation Initiation Factor 3, Subunit F, EIF3S5 , Eukaryotic Translation Initiation Factor 3, Subunit 5 (Epsilon, 47kD), EC 3.4.19.12, Deubiquitinating Enzyme EIF3f, eIF3f, eIF-3-epsilon, EIF3 P47, Eukaryotic Translation Initiation Factor 3 Subunit 5, eIF3-p47, Eukaryotic Translation Initiation Factor 3, Subunit 5 Epsilon, 47kDa.

    Product # :

    PRO-1722

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    Description

    EIF3F Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-357 a.a) and having a molecular mass of 40kDa. EIF3F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EIF3F protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic Translation Initiation Factor 3F, also known as EIF3F belongs to the eIF-3 subunit F family. EIF3F is a component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which isessential for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosomeand facilitates the recruitment of eIF-1, eIF-1A, eIF 2: GTP: methionyl-tRNAi and eIF-5 to form the 43S preinitiationcomplex (43S PIC). In addition, the eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA forAUG recognition. The eIF-3 complex is also necessary for disassembly and recycling of post termination ribosomalcomplexes and subsequently prevents premature union of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3F are intrahepatic cholangiocarcinoma, and cholangiocarcinoma.

    • Synonyms

      Eukaryotic Translation Initiation Factor 3, Subunit F, EIF3S5 , Eukaryotic Translation Initiation Factor 3, Subunit 5 (Epsilon, 47kD), EC 3.4.19.12, Deubiquitinating Enzyme EIF3f, eIF3f, eIF-3-epsilon, EIF3 P47, Eukaryotic Translation Initiation Factor 3 Subunit 5, eIF3-p47, Eukaryotic Translation Initiation Factor 3, Subunit 5 Epsilon, 47kDa.

    • 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 MGSMATPAVP VSAPPATPTP VPAAAPASVP APTPAPAAAP VPAAAPASSS DPAAAAAATA APGQTPASAQ APAQTPAPAL PGPALPGPFP GGRVVRLHPV ILASIVDSYE RRNEGAARVI GTLLGTVDKH SVEVTNCFSV PHNESEDEVA VDMEFAKNMY ELHKKVSPNE LILGWYATGH DITEHSVLIH EYYSREAPNP IHLTVDTSLQ NGRMSIKAYV STLMGVPGRT MGVMFTPLTV KYAYYDTERI GVDLIMKTCF SPNRVIGLSS DLQQVGGASA RIQDALSTVL QYAEDVLSGK VSADNTVGRF LMSLVNQVPK IVPDDFETML NSNINDLLMV TYLANLTQSQ IALNEKLVNL.

    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.

    Eif3F Human
  • View Data Sheet

    Name :

    RCHY1 Human

    Description:

    Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant

    ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    Product # :

    PRO-1536

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    Description

    RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RCHY1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.

    • Synonyms

      ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.

    • 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 MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.

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    Rchy1 Human
  • View Data Sheet

    Name :

    RAMP1 Human

    Description:

    Receptor Activity-Modifying Protein 1 Human Recombinant

    Receptor (G Protein-Coupled) Activity Modifying Protein 1, Receptor (Calcitonin) Activity Modifying Protein 1, Calcitonin-Receptor-Like Receptor Activity-Modifying Protein 1, CRLR Activity-Modifying Protein 1.

    Product # :

    PRO-1841

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    Description

    RAMP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (27-117) and having a molecular mass of 12.9 kDa. RAMP1 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The RAMP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAMP belongs to the type I transmembrane family of proteins called RAMP (receptor/calcitonin activity modifying proteins) which include an extracellular N terminus and a cytoplasmic C terminus. RAMPs are essential for CRLR transport to the plasma membrane. CRLR (calcitonin-receptor-like receptor) has seven transmembrane domains. Depending on which members of the RAMP family are expressed CRLR receptor functions as either an adrenomedullin receptor or a calcitonin-gene-related peptide (CGRP) receptor. In the presence of RAMP1, CRLR functions as a CGRP receptor. The RAMP1 protein takes part in the terminal glycosylation, maturation, and presentation of the CGRP receptor to the cell surface.

    • Synonyms

      Receptor (G Protein-Coupled) Activity Modifying Protein 1, Receptor (Calcitonin) Activity Modifying Protein 1, Calcitonin-Receptor-Like Receptor Activity-Modifying Protein 1, CRLR Activity-Modifying Protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSCQEANYG ALLRELCLTQ FQVDMEAVGE TLWCDWGRTI RSYRELADCT WHMAEKLGCF WPNAEVDRFF LAVHGRYFRS CPISGRAVRD PPGS

    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.

    Ramp1 Human
  • View Data Sheet

    Name :

    Epoetin Fc Human

    Description:

    Erythropoietin-Alpha Fc-Chimera Human Recombinant

    EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    Product # :

    CYT-325

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    Description

    Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.

    Source

    Chinese Hamster Ovary Cells(CHO).

    Formulation

    Each mg of lyophilized powder contains 1x PBS pH-7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.

    More Info

    • Introduction

      This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

    • Synonyms

      EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      What is the molecular weight/Mw of EPOETIN Protein?
      EPOETIN Protein has a total Mw of 140kDa.

      What is the source or expression system of EPOETIN Protein?
      Chinese Hamster Ovary Cells(CHO).

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

      What is the Biological Activity of EPOETIN Protein?
      The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.

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

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

    Epo Alpha Human Fc
  • View Data Sheet

    Name :

    GHBP Ovine

    Description:

    Growth Hormone Binding Protein Ovine Recombinant

    GHR, GHBP, GH receptor, Somatotropin receptor.

    Product # :

    CYT-470

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    Description

    Growth Hormone Binding Protein Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 244 amino acids and having a molecular mass of 28 kDa. GHBP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GHBP 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

    fully biologically active as evidenced by its ability of forming 2:1 complex with Human GH.

    More Info

    • Introduction

      GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

    • Synonyms

      GHR, GHBP, GH receptor, Somatotropin receptor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth Hormone Binding Protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHBP 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 GHBP Ovine in DDW or sterile 0.4% NaHCO3 adjusted to pH 10, not less than 100µg/ml, which can then be further diluted to other aqueous solutions preferably in presence of carrier proteins such as BSA or HSA.

    • Amino Acid Sequence

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

    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.

    Ghbp Ovine
  • View Data Sheet

    Name :

    PNRC2 Human

    Description:

    Proline-Rich Nuclear Receptor Coactivator 2 Human Recombinant

    Proline-rich nuclear receptor coactivator 2, PNRC2.

    Product # :

    PRO-1534

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    Description

    PNRC2 Human Recombinant produced in E. coli is a single polypeptide chain containing 162 amino acids (1-139) and having a molecular mass of 18kDa. PNRC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PNRC2 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.

    More Info

    • Introduction

      Proline-Rich Nuclear Receptor Coactivator 2 (PNRC2) takes part in controlling the energy balance between energy storage and energy expenditure. PNRC2 is involved in nonsense-mediated mRNA decay (NMD) by operating as a bridge between the mRNA decapping complex and the NMD machinery. PNRC2 is needed for UPF1/RENT1 localization to the P-body and also plays a role as a nuclear receptor coactivator.

    • Synonyms

      Proline-rich nuclear receptor coactivator 2, PNRC2.

    • 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 MGSMGGGERY NIPAPQSRNV SKNQQQLNRQ KTKEQNSQMK IVHKKKERGH GYNSSAAAWQ AMQNGGKNKN FPNNQSWNSS LSGPRLLFKS QANQNYAGAK FSEPPSPSVL PKPPSHWVPV SFNPSDKEIM TFQLKTLLKV QV.

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    Pnrc2 Human
  • View Data Sheet

    Name :

    PRL R Rat

    Description:

    Prolactin Soluble Receptor Rat Recombinant

    PRL-R, Prolactin receptor, Lactogen receptor, Prlr.

    Product # :

    CYT-533

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    Description

    Prolactin Receptor Rat Extra Celleular Domain Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 206 amino acids and having a molecular mass of 24120 Dalton. The Prolactin Receptor is 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 97.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Activity is determined by the dose-dependant inhibition of Prolactin-stimuled proliferation of Nb2 cells and by high affinity binding of oPLR and other lactogenic hormones.

    More Info

    • Introduction

      Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

    • Synonyms

      PRL-R, Prolactin receptor, Lactogen receptor, Prlr.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by two independent methods 1. UV spectroscopy at 280 nm using the absorbency value of 2.48 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a standard solution of PRLr-ECD as a Reference Standard.

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

    Prlr Rat
  • View Data Sheet

    Name :

    CHRNA6 Human

    Description:

    Cholinergic Receptor Nicotinic, Alpha 6 Human Recombinant

    CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.

    Product # :

    PRO-1878

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    Description

    CHRNA6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (26-239 a.a) and having a molecular mass of 29.3kDa. CHRNA6 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHRNA6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cholinergic Receptor Nicotinic, Alpha 6 (CHRNA6) is a part of the nicotinic acetylcholine receptors (nAChRs) family. nAChRs are heteropentameric ligand-gated ion channels generating from the assembly of alpha and beta protein subunits. After binding acetylcholine, the AChRs respond by a major change in conformation which affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. CHRNA6 receptors have a rather selective localization to the nigrostriatal pathway.

    • Synonyms

      CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSKGCV GCATEERLFH KLFSHYNQFI RPVENVSDPV TVHFEVAITQ LANVDEVNQI METNLWLRHI WNDYKLRWDP MEYDGIETLR VPADKIWKPD IVLYNNAVGD FQVEGKTKAL LKYNGMITWT PPAIFKSSCP MDITFFPFDH QNCSLKFGSW TYDKAEIDLL IIGSKVDMND FWENSEWEII DASGYKHDIK YNCCEEIYTD ITYSFYIRRL.

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    Chrna6 Human
  • View Data Sheet

    Name :

    TLR2 Mouse

    Description:

    Toll Like Receptor 2 Mouse Recombinant

    Toll-like receptor 2, CD282.

    Product # :

    PRO-2430

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    Description

    TLR2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 805 amino acids (25-587a.a.) and having a molecular mass of 90.7kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).TLR2 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TLR2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TLR2 belongs to the Toll-like receptor (TLR) family that plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) which are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. TLR2 is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria and yeast via stimulation of NF-kappaB.

    • Synonyms

      Toll-like receptor 2, CD282.

    • 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

      ADLQESLSCD ASGVCDGRSR SFTSIPSGLT AAMKSLDLSF NKITYIGHGD LRACANLQVL MLKSSRINTI EGDAFYSLGS LEHLDLSDNH LSSLSSSWFG PLSSLKYLNL MGNPYQTLGV TSLFPNLTNL QTLRIGNVET FSEIRRIDFA GLTSLNELEI KALSLRNYQS QSLKSIRDIH HLTLHLSESA FLLEIFADIL SSVRYLELRD TNLARFQFSP LPVDEVSSPM KKLAFRGSVL TDESFNELLK LLRYILELSE VEFDDCTLNG LGDFNPSESD VVSELGKVET VTIRRLHIPQ FYLFYDLSTV YSLLEKVKRI TVENSKVFLV PCSFSQHLKS LEFLDLSENL MVEEYLKNSA CKGAWPSLQT LVLSQNHLRS MQKTGEILLT LKNLTSLDIS RNTFHPMPDS CQWPEKMRFL NLSSTGIRVV KTCIPQTLEV LDVSNNNLDS FSLFLPRLQE LYISRNKLKT LPDASLFPVL LVMKIRENAV STFSKDQLGS FPKLETLEAG DNHFVCSCEL LSFTMETPAL AQILVDWPDS YLCDSPPRLH GHRLQDARPS VLECHQLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    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.

    Tlr2 Mouse
  • View Data Sheet

    Name :

    EGF Mouse, Biotin

    Description:

    Epidermal Growth Factor Mouse Recombinant, Biotin

    Urogastrone, URG, EGF.

    Product # :

    CYT-841

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    Quantity :

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    • description
    • source
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    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.

    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
  • View Data Sheet

    Name :

    EMCN Human

    Description:

    Endomucin Human Recombinant

    Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.

    Product # :

    PRO-1156

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    EMCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (19-190 a.a) and having a molecular mass of 20.5kDa.EMCN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EMCN protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Endothelial sialomucin (Endomucin) interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix. Endomucin is expressed in the heart, kidney and lung.

    • Synonyms

      Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.

    • 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 MGSHMNSTGV LEAANNSLVV TTTKPSITTP NTESLQKNVV TPTTGTTPKG TITNELLKMS LMSTATFLTS KDEGLKATTT DVRKNDSIIS NVTVTSVTLP NAVSTLQSSK PKTETQSSIK TTEIPGSVLQ PDASPSKTGT LTSIPVTIPE NTSQSQVIGT EGGKNASTSA TSRSYSS.

    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.

    Emcn Human
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