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Search results

1000 results found for “lactoferrin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CGREF1 Human

    Description:

    Cell Growth Regulator With EF-Hand Domain 1 Human Recombinant

    Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.

    Product # :

    PRO-2154

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CGREF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (20-301 a.a) and having a molecular mass of 32.3kDa. CGREF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CGREF1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4).

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cell Growth Regulator with EF-Hand Domain 1, also known as CGREF1 is a secreted calcium ion binding protein. CGREF1 includes two EF-hand domains & both EF-hands are essential for function. CGREF1 is most likely digested extracellularly by an unfamiliar serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is capable to inhibit growth in more than a few cell lines.

    • Synonyms

      Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSAPKDGVT RPDSEVQHQL LPNPFQPGQE QLGLLQSYLK GLGRTEVQLE HLSREQVLLY LFALHDYDQS GQLDGLELLS MLTAALAPGA ANSPTTNPVI LIVDKVLETQ DLNGDGLMTP AELINFPGVA LRHVEPGEPL APSPQEPQAV GRQSLLAKSP LRQETQEAPG PREEAKGQVE ARRESLDPVQ EPGGQAEADG DVPGPRGEAE GQAEAKGDAP GPRGEAGGQA EAEGDAPGPR GEAGGQAEAR ENGEEAKELP GETLESKNTQ NDFEVHIVQV ENDEI.

    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.

    Cgref1 Human
  • View Data Sheet

    Name :

    VEGF (121a.a.) Human, HEK

    Description:

    Vascular Endothelial Growth Factor (121) Human Recombinant, HEK

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-116

    Price :

    Quantity :

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    • More Info

    Description

    Recombinant Human VEGF 121 amino acids, produced in HEK cells is a glycosylated 37kDa homodimer and 50kDa homotrimer.The VEGF is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    VEGF was lyophilized from a 0.2µm filtered solution containing 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of HUVEC cells (Human Umbilical Vein Endothelial Cells), the ED50 is 3ng/ml.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF 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 VEGF in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    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.

    Vegf121 Human Hek
  • View Data Sheet

    Name :

    WIBG Human

    Description:

    within BCGN Homolog Human Recombinant

    PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.

    Product # :

    PRO-864

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    WIBG Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-204 a.a.) and having a molecular mass of 23.7 kDa. The WIBG is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    WIBG Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WIBG is a cooperateing partner of Mago-Y14. The Mago-Y14 heterodimer is a key protein of the EJC(exon junction complex) that is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. WIBG is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. WIBG relates directly with Mago-Y14 by means of its N-terminal domain.

    • Synonyms

      PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.

    • 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

      MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS KEQLEKLARR RALEEELEDL ELGLLEHHHH 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.

    Wibg Human
  • View Data Sheet

    Name :

    VEGF Equine

    Description:

    Vascular Endothelial Growth Factor Equine Recombinant

    VEGF-A, VPF, glioma-derived endothelial cell mitogen.

    Product # :

    CYT-1200

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    VEGF Equine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 2 x 165 amino acids and having a total molecular mass of 38.6 kDa.The VEGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 10 mM Sodium Phosphate, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by HUVEC Proliferation is ≤ 10 ng/mL, corresponding to a specific activity of ≥ 1.0 x 10^5 units/mg.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      VEGF-A, VPF, glioma-derived endothelial cell mitogen.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MAPMAEGEHK THEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TAEFNITMQI MRIKPHQSQH IGEMSFLQHS KCECRPKKDK ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR

    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.

    Vegf Equine
  • View Data Sheet

    Name :

    OmpA

    Description:

    Outer Membrane Protein-A Bacterial Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-571

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
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    • More Info

    Description

    The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.

    More Info

    • Introduction

      The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.

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    Outer Membrane Protein A
  • View Data Sheet

    Name :

    Darbepoetin

    Description:

    Darbepoetin-Alpha Human Recombinant

    Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    Product # :

    CYT-1263

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    Description

    Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells(CHO).

    Formulation

    Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

    More Info

    • Introduction

      Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.

    • Synonyms

      NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.

    • Background

      What is the molecular weight/Mw of DARBEPOETIN Protein?
      DARBEPOETIN Protein has a total Mw of 38.5kDa.

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

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

      What is the Biological Activity of DARBEPOETIN Protein?
      The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

      What is the amino acid sequence of DARBEPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD

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

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

    Darbepoetin
  • View Data Sheet

    Name :

    S100A3 Mouse

    Description:

    S100 Calcium Binding Protein A3 Mouse Recombinant

    Protein S100-A3, Protein S-100E, S100 calcium-binding protein A3, S100a3, S100E.

    Product # :

    PRO-1166

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    Description

    S100A3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-101 a.a) and having a molecular mass of 14.3kDa.S100A3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 2mM DTT and 150mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.

    • Synonyms

      Protein S100-A3, Protein S-100E, S100 calcium-binding protein A3, S100a3, S100E.

    • Physical Appearance

      S100A3 is supplied as a sterile filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMTRPLE QAVAAIVCTF QEYAGRCGDK YKICQSELKE LLQKELPTWT PSEFRECDYN KFMSVLDTNK DCEVDFGEYV RSLASLCLYC HEYFKECPPE PPCPQ.

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    S100A3 Mouse
  • View Data Sheet

    Name :

    MIP 1a Mouse

    Description:

    Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3)

    Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.

    Product # :

    CHM-320

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    Description

    Macrophage Inflammatory Protein-1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 1mg/ml solution containing no additives.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

    • Synonyms

      Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 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 Macrophage Inflammatory Protein-1a 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, Ala-Pro-Tyr-Gly-Ala.

    • Background

      What is the molecular weight/Mw of MIP 1A MOUSE Protein?
      MIP 1A MOUSE Protein has a total Mw of 7.82kDa.

      What is the source or expression system of MIP 1A MOUSE Protein?
      Escherichia Coli.

      What is the Purity of MIP 1A MOUSE Protein?
      MIP 1A MOUSE Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1A MOUSE Protein?
      The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of MIP 1A MOUSE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.

      What applications can MIP 1A MOUSE Protein be used in?
      MIP 1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for MIP 1A MOUSE Protein?
      The endotoxin level is minimal, MIP 1A MOUSE Protein was purified using conventional chromatography techniques.



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    Mip 1A Mouse
  • View Data Sheet

    Name :

    SERPING1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant

    C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    Product # :

    PRO-1401

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    Description

    SERPING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 499 amino acids (23-500a.a) and having a molecular mass of 55.1kDa. SERPING1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SERPING1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

    • Synonyms

      C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    • 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 MNPNATSSSS QDPESLQDRG EGKVATTVIS KMLFVEPILE VSSLPTTNST TNSATKITAN TTDEPTTQPT TEPTTQPTIQ PTQPTTQLPT DSPTQPTTGS FCPGPVTLCS DLESHSTEAV LGDALVDFSL KLYHAFSAMK KVETNMAFSP FSIASLLTQV LLGAGENTKT NLESILSYPK DFTCVHQALK GFTTKGVTSV SQIFHSPDLA IRDTFVNASR TLYSSSPRVL SNNSDANLEL INTWVAKNTN NKISRLLDSL PSDTRLVLLN AIYLSAKWKT TFDPKKTRME PFHFKNSVIK VPMMNSKKYP VAHFIDQTLK AKVGQLQLSH NLSLVILVPQ NLKHRLEDME QALSPSVFKA IMEKLEMSKF QPTLLTLPRI KVTTSQDMLS IMEKLEFFDF SYDLNLCGLT EDPDLQVSAM QHQTVLELTE TGVEAAAASA ISVARTLLVF EVQQPFLFVL WDQQHKFPVF MGRVYDPRA.

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    Serping1 Human
  • View Data Sheet

    Name :

    EEF2 Human

    Description:

    Eukaryotic Translation Elongation Factor 2 Human Recombinant

    Elongation factor 2, EF-2, EEF2, EF2, Eukaryotic Translation Elongation Factor 2, EEF-2.

    Product # :

    PRO-2076

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    Description

    EEF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (574-858) and having a molecular mass of 34.3kDa.EEF2 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EEF2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic Translation Elongation Factor 2 (EEF2) which is necessary factor for protein synthesis is a part of the GTP-binding translation elongation factor family. EEF2 catalyzes the GTP-dependent ribosomal translocation step during translation elongation. EEF2 is also catalyzes the coordinated movement of the mRNA as well as the 2 tRNA molecules and conformational changes in the ribosome. EF-2 kinase phosporylation inactivates the EEF2 protein.

    • Synonyms

      Elongation factor 2, EF-2, EEF2, EF2, Eukaryotic Translation Elongation Factor 2, EEF-2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSDPVVSYR ETVSEESNVL CLSKSPNKHN RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW CFGPDGTGPN ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV RFDVHDVTLH ADAIHRGGGQ IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK RKGLKEGIPA LDNFLDKL.

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    Eef2 Human
  • View Data Sheet

    Name :

    NOV Human

    Description:

    Nephroblastoma Overexpressed Human Recombinant

    Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    Product # :

    CYT-805

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    Description

    Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.

    Purity

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

    Biological Activity

    Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

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    • Introduction

      Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

    • Synonyms

      Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M.

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    Nov Human
  • View Data Sheet

    Name :

    SOSTDC1 Human

    Description:

    Sclerostin Domain Containing 1 Human Recombinant

    Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    Product # :

    PRO-426

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    Description

    SOSTDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (24-206 a.a) and having a molecular mass of 23kDa.SOSTDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SOSTDC1 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

      Sclerostin Domain Containing 1 (SOSTDC1) belongs to the sclerostin family and an N-glycosylated, secreted protein with a C-terminal cystine knot-like domain. The SOSTDC1 protein acts as a bone morphogenetic protein (BMP) antagonist. Specifically, SOSTDC1 directly associates with BMPs, prohibiting them from binding their receptors, thus regulating BMP signaling throughout cellular proliferation, differentiation, and programmed cell death. SOSTDC1 may also be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and hinders TGF-beta signaling. In addition, SOSTDC1 directly antagonizes the activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner.

    • Synonyms

      Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.

    • 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 MGSFKNDATE ILYSHVVKPV PAHPSSNSTL NQARNGGRHF SNTGLDRNTR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLPVL PNWIGGGYGT KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE SMSPAKPVQH HRERKRASKS SKHSMS.

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    Sostdc1 Human
  • View Data Sheet

    Name :

    NTAL Human

    Description:

    Non-T-cell Activation Linker Human Recombinant

    LAT2, Linker for Activation of T CellsFamily Member 2, HSPC046, LAB, WBSCR15, WBSCR5, WSCR5, Non-T-cell activation linker, Linker for activation of B-cells, Membrane-associated adapter molecule, Williams-Beuren syndrome chromosomal region 5 protein, Williams-Beuren syndrome chromosomal region 15 protein.

    Product # :

    PRO-827

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    Description

    NTAL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (27-243 a.a.) and having a molecular mass of 26.2 kDa. NTAL protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    NTAL Human solution containing 20mM Trsi HCL pH-8, & 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

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    • Introduction

      NTAL participates in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. NTAL takes part in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2.

    • Synonyms

      LAT2, Linker for Activation of T CellsFamily Member 2, HSPC046, LAB, WBSCR15, WBSCR5, WSCR5, Non-T-cell activation linker, Linker for activation of B-cells, Membrane-associated adapter molecule, Williams-Beuren syndrome chromosomal region 5 protein, Williams-Beuren syndrome chromosomal region 15 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

      MGSSHHHHHH SSGLVPRGSH MRCSRPGAKR SEKIYQQRSL REDQQSFTGS RTYSLVGQAW PGPLADMAPT RKDKLLQFYP SLEDPASSRY QNFSKGSRHG SEEAYIDPIA MEYYNWGRFS KPPEDDDANS YENVLICKQK TTETGAQQEG IGGLCRGDLS LSLALKTGPT SGLCPSASPE EDEESEDYQN SASIHQWRES RKVMGQLQRE ASPGPVGSPD EEDGEPDYVN GEVAATEA.

    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.

    Ntal Human
  • View Data Sheet

    Name :

    CALB2 Human

    Description:

    Calbindin-2 Human Recombinant

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

    Product # :

    PRO-401

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Calb2 Human
  • View Data Sheet

    Name :

    CALM2 Human

    Description:

    Calmodulin-2 Human Recombinant

    PHKD, CAMII, PHKD2, Calmodulin-2, CALM2, CALM1 protein, Phosphorylase kinase delta.

    Product # :

    PRO-618

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    Description

    Recombinant CALM2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 16 kDa. CALM2 is purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The CALM2 solution (1mg/ml) contains 20mM Tris-HCl, pH-7.5.

    Purity

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

    More Info

    • Introduction

      Calmodulin-2 acts as an intracellular calcium sensor protein. When the intracellular Ca2+ concentration increases, calmodulin can bind up to four Ca2+, changing its conformation and regulating cellular functions such as activation or inhibition of a large number of enzymes, ion channels, and receptors. P53 protein stimulates CALM2 gene expression in 041 cells. CALM-2 is involved in the processes of Ca(2+)-induced neuronal cell death and the blockage of calmodulin attenuates brain injury after cerebral ischemia. Calmodulin-2 mediates the control of a large number of enzymes and other proteins by ca(2+). among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases.

    • Synonyms

      PHKD, CAMII, PHKD2, Calmodulin-2, CALM2, CALM1 protein, Phosphorylase kinase delta.

    • 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

      MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK.

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    Calm2 Human
  • View Data Sheet

    Name :

    CALML3 Human

    Description:

    Calmodulin Like 3 Human Recombinant

    Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.

    Product # :

    PRO-1323

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    Description

    CALML3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-149 a.a.) and having a molecular mass of 19kDa.CALML3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CALML3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calmodulin Like 3 (CALML3) is a member of the calmodulin family and contains 4 EF-hand domains. The CALML3 protein may be similar to that of genuine calmodulin and may in fact compete with calmodulin by binding, with different affinities, to cellular substrates. CALML3 protein is expressed in normal mammary, prostate, cervical, and epidermal tissues.

    • Synonyms

      Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.

    • 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 MGSHMADQLT EEQVTEFKEA FSLFDKDGDG CITTRELGTV MRSLGQNPTE AELRDMMSEI DRDGNGTVDF PEFLGMMARK MKDTDNEEEI REAFRVFDKD GNGFVSAAEL RHVMTRLGEK LSDEEVDEMI RAADTDGDGQ VNYEEFVRVL VSK.

    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.

    Calml3 Human
  • View Data Sheet

    Name :

    LAP3 Human

    Description:

    Leucine Aminopeptidase 3 Human Recombinant

    Leucine Aminopeptidase 3, Peptidase S, PEPS, Proline Aminopeptidase, Leucyl Aminopeptidase, Prolyl Aminopeptidase, EC 3.4.11.1, LAP-3, LAPEP, Epididymis Secretory Protein Li 106, Cytosol Aminopeptidase, EC 3.4.11.5, HEL-S-106, EC 3.4.11, LAP, Cytosol aminopeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Proline aminopeptidase, Prolyl aminopeptidase.

    Product # :

    ENZ-889

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    Description

    LAP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 539 amino acids (1-519 a.a) and having a molecular mass of 58.3kDa. LAP3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LAP3 protein solution (0.5mg/ml) containing 20mM Tris-HCl(pH8.5), 50% glycerol, 5mM DTT and 1mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leucine Aminopeptidase 3 also known as LAP3 is a member of the peptidase M17 family. LAP3 is implicated in the processing as well as regular turnover of intracellular proteins. LAP3 catalyzes the removal of unsubstituted N-terminal amino acids from different peptides. LAP3 is responsible of releasing an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but could be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are as well readily hydrolyzed; however rates on arylamides are exceedingly low.

    • Synonyms

      Leucine Aminopeptidase 3, Peptidase S, PEPS, Proline Aminopeptidase, Leucyl Aminopeptidase, Prolyl Aminopeptidase, EC 3.4.11.1, LAP-3, LAPEP, Epididymis Secretory Protein Li 106, Cytosol Aminopeptidase, EC 3.4.11.5, HEL-S-106, EC 3.4.11, LAP, Cytosol aminopeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Proline aminopeptidase, Prolyl aminopeptidase.

    • 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 MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA.

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    Lap3 Human
  • View Data Sheet

    Name :

    GLRX1 Human

    Description:

    Glutaredoxin 1 Human Recombinant

    Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin-1, Thioltransferase-1, TTase-1, GLRX, MGC117407.

    Product # :

    ENZ-391

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    Description

    Glutaredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 106 amino acids having a molecular mass of 11.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    Glutaredoxin solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

    • Synonyms

      Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin-1, Thioltransferase-1, TTase-1, GLRX, MGC117407.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ.

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    Glrx1 Human
  • View Data Sheet

    Name :

    VEGF Human, Yeast

    Description:

    Vascular Endothelial Growth Factor Human Recombinant, Yeast

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-577

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    Description

    Vascular Endothelial Growth Factor Human Recombinant produced in Yeast is a double, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 42 kDa.

    Source

    Pichia Pastoris.

    Formulation

    The protein contains 20mM Phosphate- Buffered Saline, pH 7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its ability to stimulate 3H-Thymidine incorporation in human umbilical vein endothelial cells, the ED50 for this effect was found to be 2-6ng/ml.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      Vascular Endothelial Growth Factor Human although stable at 15°C for 2 weeks, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    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.

    Vegf Human Yeast
  • View Data Sheet

    Name :

    MBL2 Human

    Description:

    Mannose-Binding Lectin 2 Human Recombinant

    COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.

    Product # :

    PRO-1285

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    Description

    MBL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (108-248) and having a molecular mass of 18 kDa. MBL2 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MBL2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 20% glycerol and 0.2M Nacl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mannose-binding protein C (MBL2),belongs to the collectin family of patternrecognition molecules and is an important component in the innate immune system. MBL2 is a secreted glycoprotein which recognizes mannose and N-acetylglucosamine on various microorganisms, and is capable of activating the classical complement pathway. Lacking MBL2 has been associated with susceptibility to autoimmune and infectious diseases.

    • Synonyms

      COLEC1, HSMBPC, MBL, MBL2D, MBP, MBP-C, MBP1, Mannose-binding protein C, Collectin-1, Mannan-binding protein, Mannose-binding lectin.

    • 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 MGSAASERKA LQTEMARIKK WLTFSLGKQV GNKFFLTNGE IMTFEKVKAL CVKFQASVAT PRNAAENGAI QNLIKEEAFL GITDEKTEGQ FVDLTGNRLT YTNWNEGEPN NAGSDEDCVL LLKNGQWNDV PCSTSHLAVC EFPI.

    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.

    Mbl2 Human
  • View Data Sheet

    Name :

    TNFRSF10A Human

    Description:

    TRAIL Receptor-1 Human Recombinant

    TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.          

    Product # :

    CYT-1043

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    Description

    TNFRSF10A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 224 amino acids (24-239a.a.) and having a molecular mass of 23.9kDa. TNFRSF10A is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF10A protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.

    • Synonyms

      TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.

    • 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

      ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSEHPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSRGCPR GMVKVKDCTP WSDIECVHKE SGNGHNLEHH HHHH

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    TNFRSF10A Human
  • View Data Sheet

    Name :

    ATF1 Human

    Description:

    Activating Transcription Factor-1 Human Recombinant

    Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-1.

    Product # :

    PKA-019

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    Description

    ATF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 295 amino acids (1-271 and having a molecular mass of 31.8kDa.ATF1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ATF1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ATF1, a cyclic-AMP dependent transcription factor, is expressed in a large selection of cell types and can dimerize with CREB. MSK1 and MSK2 protein kinases are essential for the stress-induced phosphorylation of transcription factors CREB and ATF1 in primary embryonic fibroblasts. Epidermal growth factor induction of c-jun expression needs ATF1 and MEF2 sites in the c-jun promoter.

    • Synonyms

      Activating transcription factor 1, cyclic AMP-dependent transcription factor ATF-1, Protein TREB36, EWS-ATF1, FUS/ATF-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMEDSHK STTSETAPQP GSAVQGAHIS HIAQQVSSLS ESEESQDSSD SIGSSQKAHG ILARRPSYRK ILKDLSSEDT RGRKGDGENS GVSAAVTSMS VPTPIYQTSS GQYIAIAPNG ALQLASPGTD GVQGLQTLTM TNSGSTQQGT TILQYAQTSD GQQILVPSNQ VVVQTASGDM QTYQIRTTPS ATSLPQTVVM TSPVTLTSQT TKTDDPQLKR EIRLMKNREA ARECRRKKKE YVKCLENRVA VLENQNKTLI EELKTLKDLY SNKSV

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    Atf1 Human
  • View Data Sheet

    Name :

    IFNA7 Human

    Description:

    IFN-alpha 7 Human Recombinant

    IFN alpha-7, IFN-alpha-7, IFN alpha-J, LeIF J, IFN alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.

    Product # :

    CYT-196

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    • SDS-PAGE

    Description

    IFNA7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (24-189 a.a) and having a molecular mass of 22.3kDa.IFNA7 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IFNA7 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    SDS-PAGE

    IFNA7 Human - Product image 1

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    • Introduction

      IFN alpha 7 (IFNA7) is a member of the alpha/beta IFN family. IFNA7 is generated by macrophages. IFN-alpha has antiviral functions. IFN promotes the production of 2 enzymes: a protein kinase and an oligoadenylate synthetase.

    • Synonyms

      IFN alpha-7, IFN-alpha-7, IFN alpha-J, LeIF J, IFN alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.

    • 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 MGSHMCDLPQ THSLRNRRAL ILLAQMGRIS PFSCLKDRHE FRFPEEEFDG HQFQKTQAIS VLHEMIQQTF NLFSTEDSSA AWEQSLLEKF STELYQQLND LEACVIQEVG VEETPLMNED FILAVRKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSFSFS TNLKKGLRRK D.

    • Background

      What is the molecular weight/Mw of IFNA7 HUMAN Protein?
      IFNA7 HUMAN Protein has a total Mw of 22.3kDa.

      What is the source or expression system of IFNA7 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IFNA7 HUMAN Protein?
      IFNA7 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNA7 HUMAN Protein?
      The biological functionality of IFNA7 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IFNA7 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMCDLPQ THSLRNRRAL ILLAQMGRIS PFSCLKDRHE FRFPEEEFDG HQFQKTQAIS VLHEMIQQTF NLFSTEDSSA AWEQSLLEKF STELYQQLND LEACVIQEVG VEETPLMNED FILAVRKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSFSFS TNLKKGLRRK D.
      What applications can IFNA7 HUMAN Protein be used in?
      IFNA7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNA7 HUMAN Protein?
      The endotoxin level is minimal, IFNA7 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.

    Ifna7 Human
  • View Data Sheet

    Name :

    IL 12 p35 Human

    Description:

    Interleukin-12 p35 Human Recombinant

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

    Product # :

    CYT-487

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

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

    Il 12 P35 Human His
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