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Search results

827 results found for “Biglycan”

Name

Description

Product #

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  • 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

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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.

    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 :

    UBE2D1 Human

    Description:

    Ubiquitin Conjugating Enzyme E2D1 Human Recombinant

    Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.

    Product # :

    ENZ-116

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    Description

    UBE2D1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-147 a.a.) and having a molecular mass of 19kDa.UBE2D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2D1 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2D1 is a member of the ubiquitin-conjugating enzyme family. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2D1 is strongly related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. In addition, UBE2D1 functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      UBE2D1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMALKRIQ KELSDLQRDP PAHCSAGPVG DDLFHWQATI MGPPDSAYQG GVFFLTVHFP TDYPFKPPKI AFTTKIYHPN INSNGSICLD ILRSQWSPAL TVSKVLLSIC SLLCDPNPDD PLVPDIAQIY KSDKEKYNRH AREWTQKYAM.

    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.

    Ube2D1 Human
  • View Data Sheet

    Name :

    UBE2D4 Human

    Description:

    Ubiquitin Conjugating Enzyme E2D4 Human Recombinant

    Ubiquitin-conjugating enzyme E2D 4 (putative), UBCH5D, HBUCE1, Ubiquitin carrier protein D4, Ubiquitin-protein ligase D4, EC 6.3.2.19.

    Product # :

    ENZ-179

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    Description

    UBE2D4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147) and having a molecular mass of 18.8 kDa.UBE2D4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      UBE2D4 is a member of the ubiquitin-conjugating enzyme family. Ubiquitin-conjugating enzymes (E2 enzymes or ubiquitin-carrier enzymes) execute the second step in the ubiquitination reaction which marks a protein for degradation using the proteasome. UBE2D4 receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro UBE2D4 can promote polyubiquitination using all 7 ubiquitin Lys residues, but usually selects 'Lys-11' and 'Lys-48'-linked polyubiquitination.

    • Synonyms

      Ubiquitin-conjugating enzyme E2D 4 (putative), UBCH5D, HBUCE1, Ubiquitin carrier protein D4, Ubiquitin-protein ligase D4, EC 6.3.2.19.

    • 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 MALKRIQKEL TDLQRDPPAQ CSAGPVGDDL FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV PEIAHTYKAD REKYNRLARE WTQKYAM

    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.

    Ube2D4 Human
  • View Data Sheet

    Name :

    UNC119B Human

    Description:

    UNC-119 Homolog B Human Recombinant

    Unc-119 homolog B (C. elegans), POC7B, POC7 centriolar protein homolog B, MGC5139.

    Product # :

    PRO-1034

    Price :

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    Description

    UNC119B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-251) and having a molecular mass of 30.3kDa.UNC119B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The UNC119B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      UCN119B is a member of the PDE6D/unc-119 family. UCN119B has a large number of photoreceptors of the retina. Additionaly, UCN119B has a strong homology with the C. elegans unc119 and is able to functionally complement the C. elegans unc119 mutation gene.

    • Synonyms

      Unc-119 homolog B (C. elegans), POC7B, POC7 centriolar protein homolog B, MGC5139.

    • 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 MSGSNPKAAA AASAAGPGGL VAGKEEKKKA GGGVLNRLKA RRQAPHHAAD DGVGAAVTEQ ELLALDTIRP EHVLRLSRVT ENYLCKPEDN IYSIDFTRFK IRDLETGTVL FEIAKPCVSD QEEDEEEGGG DVDISAGRFV RYQFTPAFLR LRTVGATVEF TVGDKPVSNF RMIERHYFRE HLLKNFDFDF GFCIPSSRNT CEHIYEFPQL SEDVIRLMIE NPYETRSDSF YFVDNKLIMH NKADYAYNGG Q

    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.

    Unc119B Human
  • View Data Sheet

    Name :

    CNN2 Human

    Description:

    Calponin 2 Human Recombinant

    Calponin 2, Calponin H2, Smooth Muscle, Neutral Calponin, calponin-2.

    Product # :

    PRO-1882

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    Description

    CNN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-131 a.a) and having a molecular mass of 16.9kDa.CNN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calponin 2 also known as CNN2 protein is capable of binding actin, calmodulin, troponin C, and tropomyosin, and also function in the structural organization of actin filaments. Furthermore, the interaction of CNN2 with actin inhibits the actomyosin Mg-ATPase activity. CNN2 takes part in smooth muscle contraction and cell adhesion. Two transcript variants encoding different isoforms have been found for this gene.

    • Synonyms

      Calponin 2, Calponin H2, Smooth Muscle, Neutral Calponin, calponin-2.

    • 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 MGSMSSTQFN KGPSYGLSAE VKNRLLSKYD PQKEAELRTW IEGLTGLSIG PDFQKGLKDG TILCTLMNKL QPGSVPKINR SMQNWHQLEN LSNFIKAMVS YGMNPVDLFE ANDLFESGNM TQVQVSLLAL AGKA

    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.

    Cnn2 Human
  • View Data Sheet

    Name :

    MANF Mouse

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Mouse Recombinant

    Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    Product # :

    CYT-827

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    • description
    • source
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    Description

    MANF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18.2kDa.

    Source

    Escherichia Coli.

    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 as determined by a cell proliferation assay using rat C6 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

    More Info

    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIEEELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDNQ IDLSTVDLKK LRVKELKKIL DDWGEMCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.

    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.

    Manf Mouse
  • View Data Sheet

    Name :

    HBQ1 Human

    Description:

    Hemoglobin Theta 1 Human Recombinant

    Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.

    Product # :

    PRO-1616

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    Description

    HBQ1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-142) and having a molecular mass of 17.9kDa.HBQ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HBQ1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      HBQ1 is a member of the Hemoglobin family. Hemoglobin is a 66.7 kDa protein attached to four iron-binding, methenelinked tetrapyrrole rings (heme). The globin part of Hemoglobin contains 2 alpha chains and 2 beta chains organized as couples creating a tetramer. Every one of the 4 globin chains covalently connects with a heme group. The bonds between alpha and beta chains are frailer than between parallel globin chains, thus creating a cleavage plane which is vital for oxygen binding and release. Relaxation of the alpha1-beta2 cleavage plane results in high affinity for oxygen.

    • Synonyms

      Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.

    • 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 MGSMALSAED RALVRALWKK LGSNVGVYTT EALERTFLAF PATKTYFSHL DLSPGSSQVR AHGQKVADAL SLAVERLDDL PHALSALSHL HACQLRVDPA SFQLLGHCLL VTLARHYPGD FSPALQASLD KFLSHVISAL VSEYR

    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.

    Hbq1 Human
  • View Data Sheet

    Name :

    RPS18 Human

    Description:

    Ribosomal Protein S18 Human Recombinant

    Ribosomal Protein S18, D6S218E, 40S Ribosomal Protein S18, HKE3, KE-3, KE3, S18, Rhabdomyosarcoma Antigen MU-RMS-40.21, Ke-3, Ke3.

    Product # :

    PRO-984

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    Description

    RPS18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (1-152 a.a) and having a molecular mass of 20.1kDa.RPS18 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RPS18 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      40S ribosomal protein S18 (RPS18) is a member of the ribosomal protein S13P family.RPS18 is located in the cytoplasm. Ribosomes, the organelles which catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit.Jointly these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPS18 encodes a ribosomal protein which is a component of the 40S subunit. RPS18 is a recognized binding partner of Cofilin and has been proposed to be a novel substrate for CaMKII. Among the diseases associated with RPS18 are bowen-conradi syndrome, and pasteurellosis.

    • Synonyms

      Ribosomal Protein S18, D6S218E, 40S Ribosomal Protein S18, HKE3, KE-3, KE3, S18, Rhabdomyosarcoma Antigen MU-RMS-40.21, Ke-3, Ke3.

    • 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 MGSMSLVIPE KFQHILRVLN TNIDGRRKIA FAITAIKGVG RRYAHVVLRK ADIDLTKRAG ELTEDEVERV ITIMQNPRQY KIPDWFLNRQ KDVKDGKYSQ VLANGLDNKL REDLERLKKI RAHRGLRHFW GLRVRGQHTK TTGRRGRTVG VSKKK

    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.

    Rps18 Human
  • View Data Sheet

    Name :

    YWHAQ Antibody

    Description:

    Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta, Mouse Anti Human

    14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.

    Product # :

    ANT-387

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    • More Info

    Formulation

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

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 tau, a subtype of the 14-3-3 family of proteins, was found in T Cells, brain and testes. This 14-3-3 tau is upregulated in patients with amyotrophic lateral sclerosis.

    • Synonyms

      14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.

    • Immunogen

      Anti-human YWHAQ mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human YWHAQ amino acids 1-245 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT1A1AT.

    • Applications

      YWHAQ 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

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

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

    Ywhaq Antibody
  • View Data Sheet

    Name :

    SPARCL1 Mouse

    Description:

    SPARC Like 1 Mouse Recombinant

    Sparcl1, Ecm2, hevin, mast9, Sc1, SPARC-like protein 1, Extracellular matrix protein 2, Matrix glycoprotein Sc1.

    Product # :

    PRO-2617

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    Description

    SPARCL1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 642 amino acids (17-650 a.a) and having a molecular mass of 71.7kDa.SPARCL1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SPARCL1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SPARC-like protein 1 or SPARC1 is an anti-adhesive protein with a similarity to the SPARC protein’s structure. SPARC1 is highly expressed in several tissues such as brain, lungs, kidney, heart, although it is not found in the liver tissue. The protein inhibits spreading or adhesion of many substrates and is considered to lead to antiadhesive signaling that stops neuronal migration, that occurs during development or as a trauma response, consistent with production by glial and neuronal cells.

    • Synonyms

      Sparcl1, Ecm2, hevin, mast9, Sc1, SPARC-like protein 1, Extracellular matrix protein 2, Matrix glycoprotein Sc1.

    • 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

      IPTSTRFLSD HSNPTTATLV TPEDATVPIA GVEATADIEN HPSDKAEKPS ALNSEEETHE
      QSTEQDKTYS FEVDLKDEED GDGDLSVDPT EGTLTLDLQE GTSEPQQKSL PENGDFPATV
      STSYVDPNQR ANITKGKESQ EQPVSDSHQQ PNESSKQTQD LKAEESQTQD PDIPNEEEEE
      EEDEEEEEEE EPEDIGAPSD NQEEGKEPLE EQPTSKWEGN REQSDDTLEE SSQPTQISKT
      EKHQSEQGNQ GQESDSEAEG EDKAAGSKEH IPHTEQQDQE GKAGLEAIGN QKDTDEKAVS
      TEPTDAAVVP RSHGGAGDNG GGDDSKHGAG DDYFIPSQEF LEAERMHSLS YYLKYGGGEE
      TTTGESENRR EAADNQEAKK AESSPNAEPS DEGNSREHSA GSCTNFQCKR GHICKTDPQG
      KPHCVCQDPE TCPPAKILDQ ACGTDNQTYA SSCHLFATKC RLEGTKKGHQ LQLDYFGACK
      SIPACTDFEV AQFPLRMRDW LKNILMQLYE PNPKHGGYLN EKQRSKVKKI YLDEKRLLAG
      HPIELLLRD FKKNYHMYVY PVHWQFNELD QHPADRILTH SELAPLRASL VPMEHCITRF
      FEECDPNKDK HITLKEWGHC FGIKEEDIDE NLLFLEHHHH HH

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

    Sparcl1 Mouse
  • View Data Sheet

    Name :

    CoV-2 S1 (16-685), Biotin

    Description:

    Coronavirus 2019 Spike Glycoprotein-S1 (16-685 a.a.), Biotinylated Recombinant

    Product # :

    SARS-028

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    Description

    The HEK293 derived Biotinylated recombinant protein contains the Coronavirus 2019 CoV-2 Spike Glycoprotein S1, Wuhan-Hu-1 strain, amino acids 16-685 fused to His tag & Avi-tag at C-terminal.

    Source

    HEK293 Cells.

    Formulation

    CoV-2 S1 protein is supplied in 1x PBS pH-7.4 & 5% trehalose.

    Purity

    Protein is >90% pure as determined SDS-PAGE.

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cov-2 Spike S1 Glycoprotein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Spike protein 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.

    • Purification Method

      Purified by Metal-Afinity chromatographic technique.

    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.

    product_image.jpg
  • View Data Sheet

    Name :

    DKK1 Mouse

    Description:

    Dickkopf-Related Protein 1 Mouse Recombinant

    Dkk-1, mDkk-1, Dkk1, Dickkopf-related protein 1, Dickkopf-1.

    Product # :

    PRO-2756

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    Description

    DKK1 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (32-272a.a) containing 247 amino acids and having a molecular mass of 26.9kDa.DKK1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The DKK1 solution (0.25mg/ml) contains 50mM MES buffer (pH 6.5) and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dickkopf-related protein 1 (DKK1) antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by creating a ternary complex with the transmembrane protein KREMEN which promotes internalization of LRP5/6. DKKs have a significant role in vertebrate development, where they locally inhibit Wnt controlled processes for instance antero-posterior axial patterning, limb development, somitogenesis and eye formation. Furthermore, Dkks are involved in bone formation and bone disease, cancer and Alzheimer disease in Adults.

    • Synonyms

      Dkk-1, mDkk-1, Dkk1, Dickkopf-related protein 1, Dickkopf-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

      TLNSVLINSN AIKNLPPPLG GAGGQPGSAV SVAPGVLYEG GNKYQTLDNY QPYPCAEDEE CGSDEYCSSP SRGAAGVGGV QICLACRKRR KRCMRHAMCC PGNYCKNGIC MPSDHSHFPR GEIEESIIEN LGNDHNAAAG DGYPRRTTLT SKIYHTKGQE GSVCLRSSDC AAGLCCARHF WSKICKPVLK EGQVCTKHKR KGSHGLEIFQ RCYCGEGLAC RIQKDHHQAS NSSRLHTCQR
      HHHHHHH

    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.

    Dkk1 Mouse
  • View Data Sheet

    Name :

    IFNA2C Human

    Description:

    Interferon-alpha 2c Human Recombinant

    Interferon alpha-2, IFN-alpha-2, Interferon alpha-A, LeIF A, IFNA2, IFNA2A, IFNA2B, IFNA2C.

    Product # :

    CYT-1117

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    • More Info

    Description

    Interferon-alpha 2c Recombinant Human produced in yeast is a single, glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 19.3kDa. The IFNA2C is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4 and 0.02 % Tween-20.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by the cytopathic effect inhibition assay. 

    More Info

    • Introduction

      IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

    • Synonyms

      Interferon alpha-2, IFN-alpha-2, Interferon alpha-A, LeIF A, IFNA2, IFNA2A, IFNA2B, IFNA2C.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFNA2C although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interferon-alpha 2c 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 Interferon-alpha 2c in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.

    • Background

      What is the molecular weight/Mw of IFNA2C HUMAN Protein?
      IFNA2C HUMAN Protein has a total Mw of 19.3kDa.

      What is the source or expression system of IFNA2C HUMAN Protein?
      Saccharomyces cerevisiae.

      What is the Purity of IFNA2C HUMAN Protein?
      IFNA2C HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNA2C HUMAN Protein?
      The activity is determined by the cytopathic effect inhibition assay.

      What is the amino acid sequence of IFNA2C HUMAN Protein?
      CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.

      What applications can IFNA2C HUMAN Protein be used in?
      IFNA2C HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNA2C HUMAN Protein?
      The endotoxin level is minimal, IFNA2C 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.

    Ifna2C Human
  • View Data Sheet

    Name :

    RABL5 Human

    Description:

    RAB, Member RAS Oncogene Family-Like 5 Human Recombinant

    Rab-like protein 5 isoform a, Rab-like protein 5, RABL5, RAB, Member RAS Oncogene Family-Like 5.

    Product # :

    PRO-1472

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    Description

    RABL5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-185) and having a molecular mass of 23.2 kDa. RABL5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RABL5 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAB, Member RAS Oncogene Family-Like 5 (RABL5) belongs to the Ras superfamily of small GTP-binding proteins. The Ras-related superfamily of guanine nucleotide binding proteins includes the R-Ras, Rap, Ral/Rec and Rho/Rab subfamilies. Rab proteins have an essential role in endocytosis or in biosynthetic protein transport. The transporting process of newly synthesized proteins from the endoplasmic reticulum to various stacks of the Golgi complex and to secretory vesicles includes the movement of carrier vesicles and requires Rab protein function.

    • Synonyms

      Rab-like protein 5 isoform a, Rab-like protein 5, RABL5, RAB, Member RAS Oncogene Family-Like 5.

    • 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 MGSMLKAKIL FVGPCESGKT VLANFLTESS DITEYSPTQG VRILEFENPH VTSNNKGTGC EFELWDCGGD AKFESCWPAL MKDAHGVVIV FNADIPSHRK EMEMWYSCFV QQPSLQDTQC MLIAHHKPGS GDDKGSLSLS PPLNKLKLVH SNLEDDPEEI RMEFIKYLKS IINSMSESRD REEMSIMT.

    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.

    Rabl5 Human
  • View Data Sheet

    Name :

    il 18 Human

    Description:

    Interleukin-18 Human Recombinant

    IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.

    Product # :

    CYT-269

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    • More Info

    Description

    Interleukin-18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 18.2 kDa. The IL-18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.

    • Synonyms

      IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin 18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL18 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 18 in sterile PBS at 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED

    • Background

      Also known as IFN-gamma inducing factor, Interleukin-18 or IL18 is a protein. In humans this protein is encoded by the IL18 gene. The protein is a proinflammatory cytokine.

      Mechanism
      The levels of IL-18 in the human body are increased at sites of inflammation. This includes cases of rheumatoid arthritis as well as other similar conditions. Osteoblastic cells express the protein and it is capable of inhibiting osteoclast formation. It is able to do this through a variety of mechanisms.
      For instance, it is able to stimulate GM-CSF. This is created by T cells and is a response to treatment using IL-18. As well as this, the cytokine does stimulate INF-y production through vivo in bone. Furthermore, the impact on bone resorption and osteoclastogenesis is increased when used in conjunction with IL-12 treatment. Studies have shown that IL-18 provides an indirect stimulus on osteoclastogenesis due to the effect it has on T lymphocytes.
      Furthermore, evidence has shown that IL-18 does increase the production of OPG. This was studied in research on transgenic mice that overexpressed IL-18. In these cases osteoclasts decreased as did bone mass. This suggested that IL-18 also has an impact on bone growth.

      Interactions
      Research has also explored the different interactions of IL-18 on other proteins. This includes the interaction between IL-18 and IL-18R. This has been shown to decrease the power of protective immunity and increase pathogenic responses during an infection involving intracellular bacteria. This interaction suggests that the presence or absence of IL-18R signal does impact the pathogenic compared to protective immunity.
      Another interaction between interleukin 19 and Astrocyte has shown that it can improve neuropathic pain processing following nerve injury. It is proposed this is due to the fact that the nociceptive signals in the spinal cord are augmented due to this reaction.

      Function
      Belonging to the IL-1 superfamily, this cytokine is produced by macrophages as well as various other cells. It operates after binding with the interleukin-18 receptor. Working with IL-12, the protein is then able to induce-cell mediated immunity after an infection from lipopolysaccharide and other microbial products.
      Once stimulated by IL-18 other cells including natural killer and T cells then release IFN-y. This type II IFN plays a crucial part in activating the macrophages of various other cells.
      Together IL12 and IL-18 are able to successfully inhibit IgE and IG1 production that is dependent on IL-4. As well as this, the protein is also able to increase IgG2a production through B cells. IL-18 will interact specifically with this type of cytokine and has a negative impact on regulation of biological activity.

      Structure
      Many researchers have suggested that the structure of IL-18 is a key way to understand it’s receptor activation mechanism. The structure of IL-18 closely resembles of IL-1 and has various similarities. It is folded into a beta-trefoil structure and three sites have been shown to be important for receptor activation. These were revealed through extensive mutagenesis. Two of the sites provide binding sites for the IL-18 receptor and are located in positions similar to IL-1. The third structure seems to be used for IL-18 receptor beta binding.

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

    Il 18 Human
  • View Data Sheet

    Name :

    LYVE1 Human 25-235 a.a.

    Description:

    Lymphatic Vessel Endothelial Hyaluronic Acid Receptor 1 (25-235 a.a) Human Recombinant

    HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing protein.

    Product # :

    PKA-349

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    Description

    LYVE1 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 229 amino acids and having a molecular mass of 24.8 kDa. As a result of glycosylation, the LYVE1 migrates on SDS-PAGE at approximately 50 kDa. LYVE1 is expressed with 15 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    High Five insect cells.

    Formulation

    The LYVE1 protein solution contains 20mM Tris buffer pH-7.5 and 10% Glycerol.

    Purity

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

    More Info

    • Introduction

      LYVE1 is a selective marker of the lymphatic endothelium & a surface endocytic receptor for both soluble and immobilized hyaluronan, LYVE1 is an extracellular glycosaminoglycan that plays a role in cell adhesion and migration. LYVE1 functions in lympathic hyaluronan transport and is involved in tumor metastasis. Recombinant human LYVE1 was expressed in and purified by conventional chromatography techniques. The normal adult human choroid is endowed with a significant number of LYVE-1 positive macrophages. LYVE-1 is expressed in a reticulum cell neoplasm in an axillary lymph node. This reticulum cell sarcoma is a lymphatic sinus lining cell sarcoma which might represent another subtype of reticulum cell sarcomas.
      LYVE-1 immunohistochemistry is a functional method for detecting lymphatics invaded by cancer cells, and detailed examination of the submucosa around the tumor is important for predicting LN metastasis.

    • Synonyms

      HAR, XLKD1, LYVE-1, CRSBP-1, LYVE1, Lymphatic vessel endothelial hyaluronic acid receptor 1 precursor, Cell surface retention sequence-binding protein 1, Hyaluronic acid receptor, Extracellular link domain-containing protein.

    • 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

      DPLRAEELS IQVSCRIMGI TLVSKKANQQ LNFTEAKEAC RLLGLSLAGK DQVETALKAS FETCSYGWVG DGFVVISRIS PNPKCGKNGV GVLIRKVPVS RQFAAYCYNS SDTWTNSCIP EIITTKDPIF NTQTATQTTE FIVSDSTYSV ASPYSTIPAP TTTPPAPAST SIPRRKKLIC VTEVFMETST MSTETEPFVE NKAAFKNEAA GFGGSGRLVP RGSHHHHHH.

    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.

    Lyve1 Human 25 235 Aa
  • View Data Sheet

    Name :

    L1CAM Human

    Description:

    L1 Cell Adhesion Molecule Human Recombinant

    L1 Cell Adhesion Molecule, Antigen Identified By Monoclonal Antibody R1, N-CAM-L1, NCAM-L1, CAML1, MIC5, Neural Cell Adhesion Molecule L1, CD171 Antigen, N-CAML1, CD171, HSAS1, MASA, HSAS, SPG1, S10.

    Product # :

    PRO-2446

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    Description

    L1CAM Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1104 amino acids (20-1115a.a.) and having a molecular mass of 123.6kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa). L1CAM is expressed with a 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    L1CAM protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    More to 30% measured by the ability of the immobilized protein to support the adhesion of Neuro-2a mouse neuroblastoma cells. When cells are added to human L1CAM coated plates 1 ug/ml.

    More Info

    • Introduction

      L1 Cell Adhesion Molecule (L1CAM) which is a cell adhesion receptor of the immunoglobulin superfamily takes part in nerve cell function. L1CAM is a neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. L1CAM takes part in cell migration, neurite outgrowth and myelination. Furthermore, L1CAM plays an important role in the dynamics of neuronal structure and function in the mature brain.

    • Synonyms

      L1 Cell Adhesion Molecule, Antigen Identified By Monoclonal Antibody R1, N-CAM-L1, NCAM-L1, CAML1, MIC5, Neural Cell Adhesion Molecule L1, CD171 Antigen, N-CAML1, CD171, HSAS1, MASA, HSAS, SPG1, S10.

    • 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

      IQIPEELMEP PVITEQSPRR LVVFPTDDIS LKCEASGKPE VQFRWTRDGV HFKPKEELGV TVYQSPHSGS FTITGNNSNF AQRFQGIYRC FASNKLGTAM SHEIRLMAEG APKWPKETVK PVEVEEGESV VLPCNPPPSA EPLRIYWMNS KILHIKQDER VTMGQNGNLY FANVLTSDNH SDYICHAHFP GTRTIIQKEP IDLRVKATNS MIDRKPRLLF PTNSSSHLVA LQGQPLVLEC IAEGFPTPTI KWLRPSGPMP ADRVTYQNHN KTLQLLKVGE EDDGEYRCLA ENSLGSARHA YYVTVEAAPY WLHKPQSHLY GPGETARLDC QVQGRPQPEV TWRINGIPVE ELAKDQKYRI QRGALILSNV QPSDTMVTQC EARNRHGLLL ANAYIYVVQL PAKILTADNQ TYMAVQGSTA YLLCKAFGAP VPSVQWLDED GTTVLQDERF FPYANGTLGI RDLQANDTGR YFCLAANDQN NVTIMANLKV KDATQITQGP RSTIEKKGSR VTFTCQASFD PSLQPSITWR GDGRDLQELG DSDKYFIEDG RLVIHSLDYS DQGNYSCVAS TELDVVESRA QLLVVGSPGP VPRLVLSDLH LLTQSQVRVS WSPAEDHNAP IEKYDIEFED KEMAPEKWYS LGKVPGNQTS TTLKLSPYVH YTFRVTAINK YGPGEPSPVS ETVVTPEAAP EKNPVDVKGE GNETTNMVIT WKPLRWMDWN APQVQYRVQW RPQGTRGPWQ EQIVSDPFLV VSNTSTFVPY EIKVQAVNSQ GKGPEPQVTI GYSGEDYPQA IPELEGIEIL NSSAVLVKWR PVDLAQVKGH LRGYNVTYWR EGSQRKHSKR HIHKDHVVVP ANTTSVILSG LRPYSSYHLE VQAFNGRGSG PASEFTFSTP EGVPGHPEAL HLECQSNTSL LLRWQPPLSH NGVLTGYVLS YHPLDEGGKG QLSFNLRDPE LRTHNLTDLS PHLRYRFQLQ ATTKEGPGEA IVREGGTMAL SGISDFGNIS ATAGENYSVV SWVPKEGQCN FRFHILFKAL GEEKGGASLS PQYVSYNQSS YTQWDLQPDT DYEIHLFKER MFRHQMAVKT NGTGRVRLPP AGFATELEHH HHHH.

    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.

    L1Cam Human
  • View Data Sheet

    Name :

    CD44 Anti-Human, Biotin

    Description:

    CD44, Mouse Anti-Human Biotin

    MDU2, MDU3, MIC4, CDW44, CSPG8, HCELL, HUTCH-I, Phagocytic glycoprotein I, PGP-1, Extracellular matrix receptor-III, ECMR-III, Hermes antigen, Hyaluronate receptor, Heparan sulfate proteoglycan, Epican) CDw44.

    Product # :

    ANT-243

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    • More Info

    Formulation

    1mg/ml in PBS (after reconstitution).

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    • Introduction

      CD44 is a cell-surface glycoprotein that plays a role in cell-cell interactions, cell adhesion and migration. CD44 is a receptor for hyaluronic acid and also interacts with other ligands, such as osteopontin, collagens, and matrix metalloproteinases. CD44 participates in a wide variety of cellular functions such as lymphocyte activation, recirculation and homing, hematopoiesis, and tumor metastasis. CD44 and CD49d are putative activity markers and CD44 a potential novel therapeutic target in multiple sclerosis. Increased CD44 antigen is associated with relapses in non-small cell lung cancers.

    • Synonyms

      MDU2, MDU3, MIC4, CDW44, CSPG8, HCELL, HUTCH-I, Phagocytic glycoprotein I, PGP-1, Extracellular matrix receptor-III, ECMR-III, Hermes antigen, Hyaluronate receptor, Heparan sulfate proteoglycan, Epican) CDw44.

    • Solubility

      Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Purified human T-Cells.

    • Ig Subclass

      Mouse IgG2a.

    • Clone

      hCD44.

    • Applications

      Staining antibody. For staining, use 5-10µl/1,000,000 cells.

    • Available Conjugates

      This antibody is also available conjugated to biotin and FITC. For staining with biotin or FITC-conjugated antibody use 5-10µl/106 cells.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.

    • Purification Method

      Protein-A.

    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.

    Cd44 Antibody Biotin
  • View Data Sheet

    Name :

    ARTN Human

    Description:

    Artemin Human Recombinant

    ART, ARTN , EVN, NBN.

    Product # :

    CYT-306

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    Description

    Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

    More Info

    • Introduction

      The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.

    • Synonyms

      ART, ARTN , EVN, NBN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

    • Background

      Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications

      Abstract:

      Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.

      Introduction:

      Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.

      Artemin Signaling and Mechanisms:

      Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.

      Artemin in Neurological Disorders:

      Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.

      Therapeutic Potential of Artemin Human Recombinant:

      Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.

      Challenges and Future Directions:

      While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.

      Conclusion:

      Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.

      What is the molecular weight/Mw of ARTN Protein?
      ARTN Protein has a total Mw of 24.2kDa.

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

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

      What is the Biological Activity of ARTN Protein?
      The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

      What is the amino acid sequence of ARTN Protein?
      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

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

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

    Artemin Human
  • View Data Sheet

    Name :

    CYTL1 Human

    Description:

    Cytokine-Like 1 Human Recombinant

    Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.

    Product # :

    CYT-775

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    Description

    CYTL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 23-136) containing 124 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 14.6kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    CYTL1 was filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokine-like protein 1 (CYTL1) is a secreted protein. CYTL1 is expressed in CD34+ cell populations of bone marrow and cord blood which function as hematopoietic stem/progenitor cells. However, CYTL1 is not expressed in CD34- cells. Experiments with knock-out mice (Cytl1-/-) propose that CYTL1 is essential for the maintenance of cartilage homeostasis rather than cartilage and bone development, and loss of CYTL1 function is linked with experimental osteoarthritic cartilage destruction in mice.

    • Synonyms

      Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. CYTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.

    • Background

      Title: Cytokine-Like 1 Human Recombinant: Exploring its Role in Immune Regulation and Therapeutic Potential

      Abstract:


      Cytokine-like 1 (CYTL1) is an emerging cytokine that exhibits pleiotropic effects on immune regulation and tissue homeostasis. This research paper provides a comprehensive analysis of human recombinant CYTL1, focusing on its production, characterization, and potential applications in immune modulation. The paper highlights the significance of CYTL1 in immune cell function, inflammation, and tissue repair. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYTL1 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYTL1 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Cytokine-like 1 (CYTL1) is a recently discovered cytokine with diverse biological functions, including immune regulation and tissue repair. Human recombinant CYTL1, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological activities and explore its therapeutic potential.

      Production and Characterization:


      Recombinant CYTL1 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYTL1.

      Role in Immune Regulation:


      CYTL1 has been shown to modulate immune cell function and inflammation. It can influence the differentiation and activation of various immune cell subsets, including T cells and macrophages. Recombinant CYTL1 serves as a valuable tool for investigating the mechanisms underlying immune regulation and exploring its potential as an immunomodulatory agent.

      Therapeutic Implications:


      The dysregulation of immune responses is associated with numerous pathological conditions, including autoimmune diseases and chronic inflammation. Recombinant CYTL1 holds promise as a potential immunotherapeutic agent due to its ability to modulate immune cell function and regulate inflammatory processes. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYTL1 in various diseases, including autoimmune disorders and tissue regeneration.

      Conclusion:


      Human recombinant CYTL1 is a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune regulation contribute to our understanding of immune responses and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYTL1 offer promising avenues for improving outcomes in autoimmune diseases, chronic inflammation, and tissue repair.

      What is the molecular weight/Mw of CYTL1 Protein?
      CYTL1 Protein has a total Mw of 14.6kDa.

      What is the source or expression system of CYTL1 Protein?
      Escherichia Coli.

      What is the Purity of CYTL1 Protein?
      CYTL1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CYTL1 Protein?
      The biological functionality of CYTL1 Protein will be determined in the future.

      What is the amino acid sequence of CYTL1 Protein?
      MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.

      What applications can CYTL1 Protein be used in?
      CYTL1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CYTL1 Protein?
      The endotoxin level is minimal, CYTL1 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.

    Cytl1 Human
  • View Data Sheet

    Name :

    UBE2K Human

    Description:

    Ubiquitin-Conjugating Enzyme E2K Human Recombinant

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

    Product # :

    ENZ-339

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Ube2K Human
  • View Data Sheet

    Name :

    Resistin Rat

    Description:

    Resistin Rat Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-1129

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.

    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.

    Rat Resistin Protein
  • View Data Sheet

    Name :

    IGJ Human

    Description:

    Immunoglobulin J Human Recombinant

    IGCJ, JCH, Immunoglobulin J chain, IGJ.

    Product # :

    PRO-1420

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    Description

    IGJ Human Recombinant produced in E. coli is a single polypeptide chain containing 160 amino acids (23-159) and having a molecular mass of 18kDa. IGJ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Immunoglobulin J chain (IGJ) helps to link 2 monomer units of either IgM or IgA and also also helps to bind these immunoglobulins to secretory component. When it comes to IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer and in the case of IgA it induces larger polymers.

    • Synonyms

      IGCJ, JCH, Immunoglobulin J chain, IGJ.

    • 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 MGSQEDERIV LVDNKCKCAR ITSRIIRSSE DPNEDIVERN IRIIVPLNNR ENISDPTSPL RTRFVYHLSD LCKKCDPTEV ELDNQIVTAT QSNICDEDSA TETCYTYDRN KCYTAVVPLV YGGETKMVET ALTPDACYPD.

    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.

    Igj Human
  • View Data Sheet

    Name :

    BMP 5 Human

    Description:

    Bone Morphogenetic protein-5 Human Recombinant

    Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    Product # :

    CYT-660

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    • sds-page

    Description

    BMP-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (317-454 a.a.) and having a total molecular mass of 15.7 kDa.BMP-5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BMP-5 solution contains 10mM Sodium Citrate buffer (pH3.5) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    BMP5-sds-page - Product image 1

    More Info

    • Introduction

      BMP5 belongs to the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. This superfamily is comprised of large families of growth and differentiation factors. Bone morphogenetic proteins were initially identified by their ability of demineralizing bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
      BMP5 is an essential signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. It was shown that BMP-5 increases the levels of osteopontin, BMP-2, alkaline phosphatase and core binding factor alpha 1 mRNAs in human periodontal (HPL) ligament cells. The BMP5 protein is expressed in normal synovial tissue and reduced in osteoarthritis and rheumatoid arthritis. BMP5 may have a role in certain cancers given that it is differentially regulated during the formation of different tumors.

    • Synonyms

      Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    • 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

      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

    • Background

      Bone Morphogenetic Protein-5 Human Recombinant: Unleashing the Potential for Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-5 (BMP-5) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, repair, and regeneration. This research paper provides an in-depth analysis of BMP-5, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-5 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine hold great promise for addressing the challenges of tissue repair and regeneration. BMP-5, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the unique features of BMP-5 and presents novel approaches for the production and optimization of BMP-5 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-5 is a secreted growth factor that belongs to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intracellular signaling cascades. BMP-5 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, thereby influencing tissue development and repair.

      Production of BMP-5 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-5 human recombinant. Recombinant protein expression systems, including mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-5. Optimization strategies, such as codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-5 recombinant protein.

      Potential Therapeutic Applications:

      BMP-5 human recombinant holds tremendous potential in the field of tissue engineering and regenerative medicine. It plays a crucial role in bone formation, cartilage regeneration, and wound healing, making it a promising candidate for the treatment of skeletal disorders, osteochondral defects, and tissue injuries. Furthermore, the ability of BMP-5 to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-5 human recombinant emerges as a key regulator in tissue engineering and regenerative medicine, with significant implications for tissue repair and regeneration. Optimizing production methodologies and further elucidating its signaling mechanisms will enhance its therapeutic applications. With its involvement in bone and cartilage formation, as well as wound healing, BMP-5 human recombinant represents a promising tool for promoting tissue regeneration and addressing the challenges of tissue repair in various clinical contexts.

      What is the molecular weight/Mw of BMP5 Protein?
      BMP5 Protein has a total Mw of 15.7kDa.

      What is the source or expression system of BMP5 Protein?
      Escherichia Coli.

      What is the Purity of BMP5 Protein?
      BMP5 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP5 Protein?
      The biological functionality of BMP5 Protein will be determined in the future.

      What is the amino acid sequence of BMP5 Protein?
      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

      What applications can BMP5 Protein be used in?
      BMP5 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP5 Protein?
      The endotoxin level is minimal, BMP5 Protein was purified using conventional chromatography techniques.

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

    Bmp 5 Human
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