Search results

1000 results found for “pigment epithelium-derived factor”

Name

Description

Product #

Price

Quantity

Shipping Method

  • View Data Sheet

    Description:

    Penta-EF-Hand Domain Containing 1 Human Recombinant

    Peflin, PEF protein with a long N-terminal hydrophobic domain, Penta-EF hand domain-containing protein 1, PEF1, ABP32, PEF1A.

    Product # :

    PRO-099

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PEF1 Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 320 amino acids (1-284 a.a.) and having a molecular mass of 34.5kDa. The PEF1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PEF1 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.2M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Penta-EF-hand domain containing 1 (PEF1) is a member of the penta-EF-hand protein family, which shares similarities to the apoptosis linked gene ALG-2. PEF1 forms heterodimers with PDCD6/ALG2 and dissociates from PDCD6/ALG2 in the presence of Ca (2+). Furthermore, PEF1 proteins bind calcium and participate in a various calcium-dependent processes in vertebrates.

    • Synonyms

      Peflin, PEF protein with a long N-terminal hydrophobic domain, Penta-EF hand domain-containing protein 1, PEF1, ABP32, PEF1A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASY PYRQGCPGAA GQAPGAPPGS
      YYPGPPNSGG QYGSGLPPGG GYGGPAPGGP YGPPAGGGPY GHPNPGMFPS GTPGGPYGGA
      APGGPYGQPP PSSYGAQQPG LYGQGGAPPN VDPEAYSWFQ SVDSDHSGYI SMKELKQALV
      NCNWSSFNDE TCLMMINMFD KTKSGRIDVY GFSALWKFIQ QWKNLFQQYD RDRSGSISYT
      ELQQALSQMG YNLSPQFTQL LVSRYCPRSA NPAMQLDRFI QVCTQLQVLT EAFREKDTAV
      QGNIRLSFED FVTMTASRML.

    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.

    Pef1 Human
  • View Data Sheet

    Description:

    Multiple Coagulation Factor Deficiency 2 Human Recombinant

    SDNSF, LMAN1IP, Multiple coagulation factor deficiency protein 2, Neural stem cell-derived neuronal survival protein, MCFD2, F5F8D, DKFZp686G21263.

    Product # :

    PRO-769

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    MCFD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (27-146 a.a.) and having a molecular wieght of 15.1kDa. The MCFD2 is is fused to 16 a.a. T7-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MCFD2 protein solution contains 20mM Tris-HCl, pH-7.5, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The MCFD2-LMAN1 complex forms an explicit cargo receptor for the ER-to-Golgi transport of selected proteins. MCFD2 is involved in the secretion of coagulation factors. MCFD2 is expressed by neural stem/progenitor cells of the hippocampus, and localized to region where neurogenesis persists throughout life. MCFD2 prevents NSC cell death and maintains stem cell characteristics. MCFD2 forms a complex with LAMN1 that facilitates the transport of coagulation factors V and VIII from the endoplasmic reticulum to the Golgi apparatus through an endoplasmic reticulum Golgi intermediate compartment. Mutations in the MCFD2 cause Factor V and Factor VIII combined deficiency.

    • Synonyms

      SDNSF, LMAN1IP, Multiple coagulation factor deficiency protein 2, Neural stem cell-derived neuronal survival protein, MCFD2, F5F8D, DKFZp686G21263.

    • 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

      MASMTGGQQM GRGSHMEEPA ASFSQPGSMG LDKNTVHDQE HIMEHLEGVI NKPEAEMSPQ ELQLHYFKMH DYDGNNLLDG LELSTAITHV HKEEGSEQAP LMSEDELINI IDGVLRDDDK NNDGYIDYAE FAKSLQ.

    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.

    Mcfd2 Human
  • View Data Sheet

    Description:

    Bone Morphogenetic Protein-4 Human Recombinant

    BMP4, ZYME, BMP2B, BMP2B1.

    Product # :

    CYT-361

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.

    Purity

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

    More Info

    • Introduction

      The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

    • Synonyms

      BMP4, ZYME, BMP2B, BMP2B1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

    • Background

      What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant

      As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.

      Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.

      Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!

      How Does Bone Morphogenetic Protein-4 (BMP-4) Work?

      Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.

      The Role of BMP-4

      This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.

      However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:

      • Embryonic development
      • Wound healing
      • Bone remodeling
      • Immune response modulation
      • Tissue repair
      • Cardiac development and function

      What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?

      To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.

      As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.

      More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:

      • Cancer therapy
      • Development of engineered tissues and organs
      • Bone regeneration for the treatment of osteoporosis and nonunion fractures
      • Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
      • Promotion of tissue repair and regeneration

      Final Thoughts BMP-4

      Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.

      However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.

      What is the molecular weight/Mw of BMP4 Protein?
      BMP4 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP4 Protein?
      Escherichia Coli.

      What is the Purity of BMP4 Protein?
      BMP4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP4 Protein?
      The biological functionality of BMP4 Protein will be determined in the future.

      What is the amino acid sequence of BMP4 Protein?
      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

      What applications can BMP4 Protein be used in?
      BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP4 Protein?
      The endotoxin level is minimal, BMP4 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.

    Bmp4 Human
  • View Data Sheet

    Description:

    Keratinocyte Growth Factor Human Recombinant

    HBGF-7, FGF7, FGF-7, KGF.

    Product # :

    CYT-219

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Keratinocyte Growth Factor-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 18995 Dalton.The FGF-7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 8.0, 1M NaCl.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The biological activity was determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing KGF receptors yielding an ED50 <10ng/ml, corresponding to a Specific Activity of 1.0×105 IU/mg.

    More Info

    • Introduction

      KGF is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.

    • Synonyms

      HBGF-7, FGF7, FGF-7, KGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Keratinocyte Growth Factor1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 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 Keratinocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MCNDMTPEQM ATNVNCSSPE RHTRSYDYME GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNNYNIMEI RTVAVGIVAI KGVESEFYLA MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHNG GEMFVALNQK GIPVRGKKTK KEQKTAHFLP MAIT.

    • Background

      FGF stands for fibroblast growth factor that have proteins encoded inside them. The FGF family possess broad mitogenetic activities and are involved in a lot of processes in the body. Some of the biological processes that they are included in are embryonic development, cell growth, tumor growth and tissue repair. FGF-7 is often also commonly referred to as keratinocyte growth factor or KGF and studies have focused on the link between the protein and certain tumor growth.

      Structure
      Studies have found that the crystal structure of FGF7 is comparatively similar to that of FGF10. For instance, FGF7 does interact with D2, linker as well as D3 of the receptor. Similar to other FGFs much of interaction to do with D2 is confined to conserved residues as well as the residue Arg 251 in the linker domain and the hydrophobic surface of D2. That said there are notable differences and some models predict that FGF7 actually interacts with three loops in D3.

      Mechanism
      A member of the FGF family, this factor acts completely exclusively through a subset of FGF receptor isoforms. These are mainly expressed by epithelial cells. Indeed, studies suggest that the factor specifically acts on epithelial cells. This in turn causes increased proliferation differentiation and migrations of the aforementioned cells.

      Interactions
      FGF7 and FGF10 can interact with one of the FGF receptors that is expressed by the epithelial cells. As such, it could be the case that this interaction could cause a protective factor for these epithelial tissues. The protein has also been shown to interact with Perlecan. Also referred to as basement membrane specific heparan sulfate proteoglycan core protein, this is encoded by the HSPG2 gene. A large multi domain this cross-links and binds to various extracellular matrix components as well as self surface molecules. Since FGF7 binds specifically with the perlecan protein, research suggests that i should be considered a novel biological ligand for FGF-7. This could mean that interaction has an influence on both tissue remodeling and cancer growth.

      Function
      Studies have shown that FGF-7 expression is completely unregulated during minor or even chronic injury. This has lead researchers to believe that the protein is used to heal or repair epithelial cells. Furthermore, FGF-1 also triggers the formation of apical ectodermal ridge throughout the development of limbs in the body.
      Recently, it has seemed to be the case that FGF-7 has been linked to skin injury repair, and has also been found to play some sort of role in breast cancer. As well as this, it is a vital regulator of HPC’s. It is vital because it can induce de novo activation of these HPCs.

      Further research has shown that FGF6 is a niche signal that is required for the stimulation of adult liver progenitor cells and this can support liver regeneration. This research has lead to the suggestion that FGF7 could be a possibility therapeutic target for those suffering from liver diseases.
      Studies like this are just one of the reasons why researchers continue to explore fgf-7, it’s functions and interactions.

    • Protein content

      Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.9 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of KGF as a Reference Standard.

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

    Kgf Human
  • View Data Sheet

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

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

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

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor as a Reference Standard.

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

    Bdnf Human
  • View Data Sheet

    Description:

    Pentraxin-2 Mouse Recombinant

    Serum amyloid P-component, SAP, Apcs, Sap, Ptx2.

    Product # :

    PRO-2598

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PTX2 Mouse Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 210 amino acids (21-224 a.a) and having a molecular mass of 24.6kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). PTX2 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293.

    Formulation

    PTX2 protein solution (0.25mg/ml) contains 10% glycerol in Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PTX-2 or Pentraxin-2 is a phylogenetically conserved protein, commonly moving with homopentameric blood protein or with a protein that recognizes receptors of the innate immune system. The protein’s specific binding abilities may show that PTX-2 is specially bound in sites where injury accrued, therefore helps to eliminate damaged tissue by ways that are not phlogistics.

    • Synonyms

      Serum amyloid P-component, SAP, Apcs, Sap, Ptx2.

    • 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

      QTDLKRKVFV FPRESETDHV KLIPHLEKPL QNFTLCFRTY SDLSRSQSLF SYSVKGRDNE LLIYKEKVGE YSLYIGQSKV TVRGMEEYLS PVHLCTTWES SSGIVEFWVN GKPWVKKSLQ REYTVKAPPS IVLGQEQDNY GGGFQRSQSF VGEFSDLYMW DYVLTPQDIL FVYRDSPVNP NILNWQALNY EINGYVVIRP RVWDHHHHHH.

    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.

    Ptx2 Mouse
  • View Data Sheet

    Description:

    Epidermal Growth Factor Receptor Clone PAT2H8AT, Mouse Anti Human

    ERBB, ERBB1, Epidermal growth factor receptor, HER1, PIG61, epidermal growth factor receptor, Urogastrone, Proto-oncogene c-ErbB-1, Oncogene ERBB, Cell proliferation inducing protein 61, Cell growth inhibiting protein 40, Avian erythroblastic leukemia viral (verbb) oncogene homolog.

    Product # :

    ANT-751

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      Epidermal growth factor receptor or EGFR or Erb-1 is a membranal protein that acts as a receptor for the extracellular EGF proteins family. This protein is a part of a family of receptors called ErbB family which are all tyrosine kinases receptors. Mutations in the gene of this receptors can cause cancer.

    • Synonyms

      ERBB, ERBB1, Epidermal growth factor receptor, HER1, PIG61, epidermal growth factor receptor, Urogastrone, Proto-oncogene c-ErbB-1, Oncogene ERBB, Cell proliferation inducing protein 61, Cell growth inhibiting protein 40, Avian erythroblastic leukemia viral (verbb) oncogene homolog.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human EGFR mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EGFR amino acids 424-605 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT2H8AT.

    • Applications

      EGFR antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      EGFR 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.

    Anti Egfr
  • View Data Sheet

    Description:

    Epidermal Growth Factor Human Recombinant

    Urogastrone, URG, EGF.

    Product # :

    CYT-217

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.

    More Info

    • Introduction

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

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.

    • Background

      About EGF:

      In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF).

      Description:

      Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses.

      Function:

      By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers.

      Mechanism:

      EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses.

      What is the molecular weight/Mw of EGF Protein?
      EGF Protein has a total Mw of 6.2kDa.

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

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

      What is the Biological Activity of EGF Protein?
      The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.

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

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

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

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

    Egf Human
  • View Data Sheet

    Description:

    Phenazine Biosynthesis-Like Protein Domain Containing Human Recombinant

    Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.

    Product # :

    PRO-010

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PBLD Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 308 amino acids (1-288 a.a.) and having a molecular mass of 33.9kDa. The PBLD is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PBLD is member of the phenazine biosynthesis-like protein (PhzF) family. PBLD which is expressed in most tissues is the only representative of the PhzF family in the human genome. PBLD participates in the MAPK signaling pathway. PBLD is involved in multiple basic cellular functions, its expression is elevated in several disease processes, including folate deficiency and hypotension.

    • Synonyms

      Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.

    • 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 MKLPIFIADA FTARAFRGNP AAVCLLENEL DEDMHQKIAR EMNLSETAFI RKLHPTDNFA QSSCFGLRWF TPASEVPLCG HATLASAAVL FHKIKNMNST LTFVTLSGEL RARRAEDGIV LDLPLYPAHP QDFHEVEDLI KTAIGNTLVQ DICYSPDTQK LLVRLSDVYN RSFLENLKVN TENLLQVENT GKVKGLILTL KGEPGGQTQA FDFYSRYFAP WVGVAEDPVT GSAHAVLSSY WSQHLGKKEM HAFQCSHRGG ELGISLRPDG RVDIRGGAAV VLEGTLTA.

    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.

    Pbld Human
  • View Data Sheet

    Description:

    Nuclear Apoptosis Inducing Factor 1 Human Recombinant

    bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    Product # :

    PRO-1978

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.

    • Synonyms

      bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.

    • 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 MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.

    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.

    Naif1 Human
  • View Data Sheet

    Description:

    Eukaryotic Translation Initiation Factor 4E Recombinant Mouse

    eIF-4E, eIF4E, mRNA cap-binding protein, eIF-4F 25 kDa subunit, Eif4e.

    Product # :

    PRO-2411

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    EIF4E Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 241 amino acids (1-217 a.a) and having a molecular mass of 27.6kDa. EIF4E is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EIF4E protein solution (1mg/ml) 20mM Tris-HCl Buffer (pH8.0), 10% glycerol, 1mM DTT, 0.1M NaCl and 0.1mM PMSF.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      eIF-4E, eIF4E, mRNA cap-binding protein, eIF-4F 25 kDa subunit, Eif4e.

    • 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 MGSHMATVEP ETTPTTNPPP AEEEKTESNQ EVANPEHYIK HPLQNRWALW FFKNDKSKTW QANLRLISKF DTVEDFWALY NHIQLSSNLM PGCDYSLFKD GIEPMWEDEK NKRGGRWLIT LNKQQRRSDL DRFWLETLLC LIGESFDDYS DDVCGAVVNV RAKGDKIAIW TTECENRDAV THIGRVYKER LGLPPKIVIG YQSHADTATK SGSTTKNRFV V

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

    Eif4E Mouse
  • View Data Sheet

    Description:

    Hepatoma-Derived Growth Factor Human Recombinant

    High-mobility group protein 1-like 2, HMG1L2, HMG-1L2, Hepatoma-derived growth factor, HDGF, FLJ96580, DKFZp686J1764.

    Product # :

    CYT-681

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • SDS-PAGE

    Description

    The HDGF Human recombinant protein is a single, non-glycosylated polypeptide chain produced in E. coli, having a molecular weight of 11.5kDa and containing 100 amino acids.The HDGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HDGF protein solution (1mg/ml) is formulated in 20mM Tris-HCl pH-7.5, 1mM DTT, 10% glycerol and 1mM EDTA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      HDGF is a member of the hepatoma-derived growth factor family. HDGF plays a role as a secreted mitogen from the human hepatoma cell line Huh-7. HDGF is a nuclear targeted vascular smooth muscle cell mitogen as well as a heparin-binding protein that is greatly expressed in tumor cells where it stimulates proliferation. HDGF takes part in organ development and lung remodeling after injury by promoting proliferation of lung epithelial cells. HDGF plays a role in the carcinogenesis of gastric epithelial cells through promotion of cell proliferation by Erk1/2 activation. HDGF is linked with tumorigenesis and the growth of cancer. HDGF is a self-regulating factor connected with the prognosis of liver cancer, non-small cell lung cancer and pancreatic cancer. HDGF has proliferative, angiogenic, and neurotrophic activity. HDGF is a distinctive nuclear targeting growth factor that is vastly expressed in HCC cells and is a prognostic factor for HCC.

    • Synonyms

      High-mobility group protein 1-like 2, HMG1L2, HMG-1L2, Hepatoma-derived growth factor, HDGF, FLJ96580, DKFZp686J1764.

    • 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

      MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF GTHETAFLGP KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY.

    • Background

      What is the molecular weight/Mw of HDGF HUMAN Protein?
      HDGF HUMAN Protein has a total Mw of 11.5kDa.

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

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

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

      What is the amino acid sequence of HDGF HUMAN Protein?
      MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF GTHETAFLGP KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY.

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

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

    Hdgf Human
  • View Data Sheet

    Description:

    Prolactin-Induced Protein Human Recombinant

    Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.

    Product # :

    CYT-793

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (29-146 a.a.) and having a molecular mass of 15.9kDa.PIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PIP protein 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

      Prolactin-inducible protein (PIP) is a main protein component of benign breast gross cysts. PIP is a famous indicator of breast cancer, since it is found in around 50% of all breast cancer specimens. PIP is expressed in exocrine glands, in pathologic conditions, in breast cysts and breast cancers exhibiting apocrine features. PIP and prostate specific antigen are co-expressed in androgen receptor-positive breast tumours.

    • Synonyms

      Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.

    • 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 MGSQDNTRKI IIKNFDIPKS VRPNDEVTAV LAVQTELKEC MVVKTYLISS IPLQGAFNYK YTACLCDDNP KTFYWDFYTN RTVQIAAVVD VIRELGICPD DAAVIPIKNN RFYTIEILKV E.

    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.

    Human Pip
  • View Data Sheet

    Description:

    Hepatocyte Growth Factor Human Recombinant, CHO

    Scatter Factor (SF), Hepatopoietin (HPTA), HGF.

    Product # :

    CYT-251

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Hepatocyte Growth Factor Human Recombinant produced in CHO is a heterodimer, non-glycosylated, polypeptide chain consisting an a-chain of 463 amino acids and b-chain of 234 having a total molecular mass of approximately 75kDa. The HGF is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovarian Cells.

    Formulation

    The protein was lyophilized from a concentrated (1.4mg/ml) solution containing Phosphate-Buffered Saline with 0.02% Tween 80, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

    More Info

    • Introduction

      Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.

    • Synonyms

      Scatter Factor (SF), Hepatopoietin (HPTA), HGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Agrees with the sequence of native human HGF.

    • Background

      What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein has a total Mw of 75kDa.

      What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      Chinese Hamster Ovarian Cells.

      What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      The ED50, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

      What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      Agrees with the sequence of native human HGF.

      What applications can HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein be used in?
      HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
      The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN, CHO 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.

    Hgf Human Cho
  • View Data Sheet

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Pichia

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

    Product # :

    CYT-324

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in Yeast is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 26-32 kDa. rhGMCSF differs from the natural human GM-CSF by a substitution of leucine at position 23 (R to L), and the carbohydrate moiety may be different from the native protein. GM-CSF is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM phosphate buffer pH 7.0, 40 mg mannitol and 10 mg sucrose.

    Purity

    Greater than 97.0% as determined by1. Analysis by RP-HPLC.
    2. Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor 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-Ala-Arg-Ser.

    • Background

      What is the molecular weight/Mw of GM-CSF HUMAN, PICHIA Protein?
      GM-CSF HUMAN, PICHIA Protein has a total Mw of 29kDa.

      What is the source or expression system of GM-CSF HUMAN, PICHIA Protein?
      Pichia Pastoris.
      What is the Purity of GM-CSF HUMAN, PICHIA Protein?
      GM-CSF HUMAN, PICHIA Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF HUMAN, PICHIA Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.

      What is the amino acid sequence of GM-CSF HUMAN, PICHIA Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

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

      What is the endotoxin level for GM-CSF HUMAN, PICHIA Protein?
      The endotoxin level is minimal, GM-CSF HUMAN, PICHIA Protein was purified using conventional chromatography techniques.


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

    Gm Csf Human Pichia
  • View Data Sheet

    Description:

    Vascular Endothelial Growth Factor Mouse Recombinant, His Tag

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, Vegf120, Vegf164, Vegf188, Vegfa.

    Product # :

    CYT-680

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (205-324 a.a.) and having a total molecular mass of 16.3kDa. Mouse VEGF is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Mouse VEGF contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using NIH-3T3 mouse embryonic fibroblast. The ED50 for this effect is 0.5-1.5ng/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, Vegf120, Vegf164, Vegf188, Vegfa.

    • 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 MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKPR R.

    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 Mouse His
  • View Data Sheet

    Description:

    Transforming Growth Factor-Beta 2 Human Recombinant, HEK

    Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    Product # :

    CYT-112

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    TGF-b 2 Human Recombinant produced in HEK cells is a non-glycosylated homodimer, having a total molecular weight of 25kDa.The TGF-b 2 is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    TGF-b 2 was lyophilized from a 0.2µm filtered solution containing 50mM sodium acetate pH 4.5.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2), the ED50 is 0.16ng/ml.

    More Info

    • Introduction

      TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-beta (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.

    • Synonyms

      Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGF-b 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 2 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 TGF-b 2 in sterile solution containing 20% ethanol, 50mM sodium acetate and 75mM acetic acid.

    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.

    Tgf B 2 Human Hek
  • View Data Sheet

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant, His Tag

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim

    Product # :

    CYT-1160

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    GMCSF Poricne Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (18-144a.a.) and having a molecular mass of 16.6kDa.GMCSF is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

    More Info

    • Introduction

      The hematopoietic growth factor GM-CSF or granulocyte macrophage colony-stimulating factor, stimulates the development of neutrophils & macrophages, enhance proliferation and development of early erythroid megakaryocytic & eosinophilic progenitor cells. GM-CSF is secreted from the fibroblasts, monocytes, T-lymphocytes & endothelial cells. This protein blocks the migration of neutrophils & induces the biological activity of mature end-cells.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim

    • 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 MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK

    • Background

      What is the molecular weight/Mw of GM-CSF PORCINE, HIS Protein?
      GM-CSF PORCINE, HIS Protein has a total Mw of 16.6kDa.

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

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

      What is the Biological Activity of GM-CSF PORCINE, HIS Protein?
      The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

      What is the amino acid sequence of GM-CSF PORCINE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK

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

      What is the endotoxin level for GM-CSF PORCINE, HIS Protein?
      The endotoxin level is minimal, GM-CSF PORCINE, HIS Protein was purified using conventional chromatography techniques.


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

    Porcine Gm Csf
  • View Data Sheet

    Description:

    Leptin-A Tilapia Recombinant

    Product # :

    CYT-1109

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Leptin-A Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 16,491 Dalton. The Leptin-A Tilapia is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.

    Purity

    Greater than 95.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.

    More Info

    • Introduction

      Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin-A Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.33 for 1 mg/ml Leptin-A Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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

    Leptin A
  • View Data Sheet

    Description:

    Epigen Human Recombinant

    EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

    Product # :

    CYT-601

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Epigen Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9 kDa. Epigen is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EPGN was lyophilized from 20mM PBS buffer pH-7.4 .

    Purity

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

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.

    More Info

    • Introduction

      EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.

    • Synonyms

      EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA

    • Background

      What is the molecular weight/Mw of EPIGEN Protein?
      EPIGEN Protein has a total Mw of 7.9kDa.

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

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

      What is the Biological Activity of EPIGEN Protein?
      Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.

      What is the amino acid sequence of EPIGEN Protein?
      AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA

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

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

    Epgn Human
  • View Data Sheet

    Description:

    Peptidase Inhibitor 3 Human Recombinant, Sf9

    Elafin, ESI, SKALP, WAP3, WFDC14.

    Product # :

    PRO-2653

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PI3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 101 amino acids (23-117a.a) and having a molecular mass of 10.7kDa.PI3 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The PI3 solution (0.2mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidase Inhibitor 3, also referred to PI3, is neutrophil and pancreatic elastase-specific inhibitor of skin. The protein may prevent elastase mediated tissue proteolysis. PI3 has shown inhibition of alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor, a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation channel subfamily V member 1.

    • Synonyms

      Elafin, ESI, SKALP, WAP3, WFDC14.

    • 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

      AVTGVPVKGQ DTVKGRVPFN GQDPVKGQVS VKGQDKVKAQ EPVKGPVSTK PGSCPIILIR CAMLNPPNRC LKDTDCPGIK KCCEGSCGMA CFVPQHHHHH H

    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.

    Elafin Human
  • View Data Sheet

    Description:

    Macrophage Colony Stimulating Factor Rat Recombinant HEK

    CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-046

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    MCSF Rat Recombinant produced in HEK-293 cells is a secreted protein (amino acids Glu33-Arg254). M-CSF is disulfide-linked homodimer containing 2 x 222 a.a chains.

    Source

    HEK293

    Formulation

    The recombinant MCSF was lyophilized after extensive dialysis against PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of mouse M-NFS-60 cells.

    More Info

    • Introduction

      Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    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.

    M Csf Rat
  • View Data Sheet

    Description:

    Profilin-1 Human Recombinant

    Profilin-1, Profilin I, PFN1.

    Product # :

    PRO-528

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PFN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids (1-140 a.a.) and having a molecular mass of 15kDa.The PFN1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PFN1 protein solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Profilin1 (PFN1) is a ubiquitous actin monomer-binding protein which is a member of the profilin family. PFN1 significantly boosts skin wound healing in-vitro and in-vivo which may be mediated by purinergic receptors. PFN1 is also active in endothelial cell migration and vessel sprouting. PFN1 is thought to control actin polymerization in response to extracellular signals. PFN1 binds to actin and affects the formation of the cytoskeleton. In addition, PFN1 has an important role in the regulation of epithelial cell-cell adhesion. At high concentrations, profilin averts the polymerization of actin, while at low concentrations it enhances the polymerization. PFN1 gene deletion is linked to Miller-Dieker syndrome.

    • Synonyms

      Profilin-1, Profilin I, PFN1.

    • 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

      MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV LVGKDRSSFY VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN VTVTKTDKTL VLLMGKEGVH GGLINKKCYE MASHLRRSQY.

    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.

    Pfn1 Human
  • View Data Sheet

    Description:

    Omentin 298 a.a. Human Recombinant

    Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    Product # :

    CYT-061

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Omentin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (17-313) and having a molecular mass of 33.2 kDa.The Omentin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Omentin protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.4M Urea and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

    • Synonyms

      Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    • 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

      MWSTDEANTY FKEWTCSSSP SLPRSCKEIK DECPSAFDGL YFLRTENGVI YQTFCDMTSG GGGWTLVASV HENDMRGKCT VGDRWSSQQG SKAVYPEGDG NWANYNTFGS AEAATSDDYK NPGYYDIQAK DLGIWHVPNK SPMQHWRNSS LLRYRTDTGF LQTLGHNLFG IYQKYPVKYG EGKCWTDNGP VIPVVYDFGD AQKTASYYSP YGQREFTAGF VQFRVFNNER AANALCAGMR VTGCNTEHHC IGGGGYFPEA SPQQCGDFSG FDWSGYGTHV GYSSSREITE AAVLLFYR

    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.

    Omentin 298 Aa Human