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1000 results found for “tgfbr”

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  • View Data Sheet

    Description:

    Platelet-Derived Growth Factor B Human Recombinant

    Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

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    CYT-492

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    Description

    PDGF-B Human Recombinant mature chain produced in E.Coli is a non-glycosylated, polypeptide chain containing 109 amino acids fragment (82-190) and having a molecular mass of 16.75 kDa. The PDGF-B is fused with an amino-terminal hexahistidine tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Platelet-Derived Growth Factor-B is supplied in 25mM Na-Acetate pH 4.8, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      The term ‘PDGF’ refers to a family of disulphide bond-linked dimeric isoforms that act as autocrine and paracrine growth factors and are produced by a variety of cell types other than platelets.
      They act as potent mitogens for almost all mesenchymally-derived cells. Aberrant expression is involved in certain cancers, fibroproliferative disorders and atherosclerosis. The protein also contributes to wound healing and neural regeneration. There are four members of the PDGF family – PDGF A, PDGF B, PDGF C and PDGF D. Two distinct types of PDGF-A exist – a short form that is soluble and a long form that is retained by the extracellular matrix.

    • Synonyms

      Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

    • 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.

    Pdgf B Human
  • View Data Sheet

    Description:

    Vascular Endothelial Growth Factor Receptor-3 Fc Chimera Human Recombinant

    Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3.

    Product # :

    PKA-245

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    Description

    Soluble FLT4 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a monomeric, glycosylated, polypeptide containing 774 amino acids and having a molecular mass of 260 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.The FLT4 Fc Chimera is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT4 Fc Chimera was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.

    Purity

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

    Biological Activity

    Measured by its ability to bind recombinant rat VEGF-C in a functional solid phase binding assay. Immobilised recombinant human VEGFR-3/FLT-4 at 5 µg/ml can bind recombinant rat VEGF-C in a linear range of 8-500 ng/ml.

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    • Introduction

      All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

    • Synonyms

      Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT4 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 FLT4 Fc Chimera in sterile water 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.

    Flt4 Human Fc
  • View Data Sheet

    Description:

    TP53RK Binding Protein Human Recombinant

    TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.

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    PRO-1185

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    Description

    TPRKB Human Recombinant produced E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.2kDa.TPRKB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TPRKB solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      TPRKB is a member of the CGI121/TPRKB family. TPRKB is localized to nucleus and cytoplasm and is ubiquitously expressed. TPRKB is known to cooperate with TP53RK/PRPK.

    • Synonyms

      TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.

    • 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 MGSHMQLTHQ LDLFPECRVT LLLFKDVKNA GDLRRKAMEG TIDGSLINPT VIVDPFQILV AANKAVHLYK LGKMKTRTLS TEIIFNLSPN NNISEALKKF GISANDTSIL IVYIEEGEKQ INQEYLISQV EGHQVSLKNL PEIMNITEVK KIYKLSSQEE SIGTLLDAII CRMSTKDVL

    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.

    Tprkb Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-basic Human Recombinant, Thermostable

    HBGH-2, HBGF-2, FGF-2, FGF-b, HBGH2, HBGF2, FGF2, FGFb, FGF2 Thermostable, FGF-2 Thermostable.

    Product # :

    CYT-943

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    Description

    FGF2 Thermostable is a stabilized form of FGF2 growth factor which enables a novel method to produce FGF2-dependent cell cultures more efficiently, having less media changes. FGF2 Thermostable can maintain its biological activity even after five days at 37°C. The increase in the stability of FGF2 in cell-culture enables a more homogenous, undifferentiated stem cell culture, while saving scientists crucial time and money, as frequent supplementation of FGF-basic and the everyday medium change is not necessary. Thermostable FGF-2 is a hyperstable protein. The Thermal stability of the protein is increased by 15°C compared to the wild-type FGF-2. Thermostable FGF-2 is more than 5-times prolonged half-life in human cell culture incubated at 37°C. The FGF-2 Thermostable protein is engineered with fully retained biological function and has no harmful stabilizing additives.Thermostable FGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a total calculated molecular mass is 17.2kDa.

    Source

    Escherichia Coli.

    Formulation

    FGF Basic Thermostable was lyophilized from 20mM Tris-HCl, 150mM NaCl & 5% Trehalose, pH-7.6.

    Purity

    Purity is greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as calculated by the dose-dependent proliferation of murine balb/c 3T3 cells is less than 0.05ng/ml, corresponding to a specific activity of >20,000,000 units/mg

    More Info

    • Synonyms

      FGF2 Thermostable, FGF-basic Thermostable.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thermostable FGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF2 Thermostable 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 FGF2 thermostable protein in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AAGSITTLPA LPEDGGSGAF PPGHFKDPKL LYCKNGGFFL RIHPDGRVDG TRDKSDPFIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL YAIKNVTDEC FFFERLEENN YNTYRSRKYP SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS

    • Background

      Why Choose FGF2 Thermostable?
      FGF2 can lose much of its activity after 1-2 days at 37°C due to unfolding and degradation. Thermostable FGF2 is engineered with amino acid substitutions that increase structural stability without significantly altering receptor binding or biological function.

      What are the advantages of FGF2 Protein?
      *Better maintenance of pluripotency markers
      *Higher colony quality
      *Faster expansion rates
      *Reduced spontaneous differentiation
      *Greater viability after passaging

      What is the source or expression system of FGF2 Protein?
      Escherichia Coli.

      What is the Purity of FGF2 Protein?
      FGF2 Protein is >95% pure as determined by SDS-PAGE.

      What is the molecular weight / Mw of FGF2 Protein?
      FGF2 Protein having a total Mw of 17.2kDa.

      What is the Biological Activity of FGF2 Protein?
      The ED50 as calculated by the dose-dependent proliferation of murine balb/c 3T3 cells is less than 0.05ng/ml, corresponding to a specific activity of >20,000,000 units/mg.

      What is the endotoxin level for FGF2 Protein?
      The endotoxin level is minimal, FGF2 Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of FGF2 Protein?
      AAGSITTLPA LPEDGGSGAF PPGHFKDPKL LYCKNGGFFL RIHPDGRVDG TRDKSDPFIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL YAIKNVTDEC FFFERLEENN YNTYRSRKYP SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS

      Is FGF2 Protein conjugated to a Tag?
      FGF2 Protein is not conjugated to a tag.

      What applications can FGF2 Protein be used in?
      FGF2 Protein can probably be used in western blot, ELISA and Lateral Flow.

    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.

    Fgf2 Human Thermostable
  • View Data Sheet

    Description:

    Trefoil Factor-2 Human Recombinant

    TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    Product # :

    CYT-612

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    Description

    TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 106 amino acids (24-129) and having a total molecular mass of 12 kDa. TFF2 Human Recombinant includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds and was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 1mg/mL containing 1x PBS pH-7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human MCF-7 cells using a concentration 1.0-10.0 ng/ml.

    More Info

    • Introduction

      Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.

    • Synonyms

      TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 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 TFF2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.

    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.

    Tff2 Human
  • View Data Sheet

    Description:

    Epidermal Growth Factor Mouse Recombinant, His Tag

    Urogastrone, URG, EGF.

    Product # :

    CYT-138

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    • SDS-PAGE

    Description

    EGF mouse Recombinant produced in E. coli is a single polypeptide chain containing 77 amino acids (977-1029) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EGF solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    SDS-PAGE

    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 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 MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

    • Background

      Unveiling Epidermal Growth Factor Mouse Recombinant: Harnessing His Tag for Enhanced Insights and Therapeutic Prospects

      Abstract:

      This research paper delves into the realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), focusing on the strategic integration of a Histidine (His) Tag. By employing sophisticated methodologies encompassing protein engineering, chromatographic techniques, and cellular assays, this study unveils the multifaceted molecular attributes of EGF-MR with His Tag. The findings not only enhance our understanding of EGF-MR's behavior but also illuminate potential avenues for therapeutic interventions.

      Introduction:

      Epidermal Growth Factor (EGF) governs vital cellular processes. This paper delves into Epidermal Growth Factor Mouse Recombinant (EGF-MR) with a specific emphasis on the incorporation of a Histidine (His) Tag, unraveling its molecular intricacies and therapeutic implications.

      Protein Engineering and His Tag Integration:

      The paper navigates the tailored engineering of EGF-MR to accommodate a His Tag, a peptide sequence that facilitates protein purification. The process involves strategic modification of the EGF-MR gene to ensure proper folding and presentation of the His Tag.

      Chromatographic Purification and His Tag Affinity:

      Chromatographic techniques, specifically immobilized metal ion affinity chromatography (IMAC), are employed to purify the His-tagged EGF-MR. The His Tag's high affinity for metal ions facilitates efficient purification, yielding a highly purified and bioactive protein product.

      Structural and Functional Insights:

      The presence of the His Tag is not just for purification; it serves as a molecular handle to investigate EGF-MR's structural dynamics. High-resolution structural analyses coupled with biophysical assays unravel how the His Tag affects EGF-MR's conformation and binding interactions.

      Cellular Assays and Bioactivity Assessment:

      In vitro cellular assays, including proliferation and migration studies, provide insights into the impact of His Tag on EGF-MR's bioactivity. Comparative analyses shed light on the functionality of His-tagged EGF-MR and its potential implications in cellular responses.

      Therapeutic Prospects and Targeted Delivery:

      The incorporation of a His Tag presents a unique avenue for tailored drug delivery. The His Tag can serve as a docking site for targeted therapies, enabling precise interactions with specific receptors on target cells.

      Future Directions and Challenges:

      While promising, challenges such as potential steric hindrance from the His Tag require consideration. Future research should focus on optimizing the positioning of the His Tag to maintain EGF-MR's full biological activity.

      Conclusion:

      In a harmonious synthesis of advanced methodologies and innovative insights, the integration of His Tag into Epidermal Growth Factor Mouse Recombinant emerges as a transformative paradigm. The His Tag not only facilitates purification but also offers a molecular window into EGF-MR's behavior, potentially redefining targeted therapies and precision medicine.

      What is the molecular weight/Mw of EGF MOUSE, HIS Protein?
      EGF MOUSE, HIS Protein has a total Mw of 8.6kDa.

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

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

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

      What is the amino acid sequence of EGF MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

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

      What is the endotoxin level for EGF MOUSE, HIS Protein?
      The endotoxin level is minimal, EGF MOUSE, 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.

    Egf Mouse His
  • View Data Sheet

    Description:

    BAFF (BLyS) Receptor Human Recombinant, HEK

    TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

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    CYT-1224

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    Description

    BAFFR Human Recombinant is a single, glycosylated, polypeptide chain (1-78 a.a) containing a total of 314 amino acids and having a molecular mass of 34.4 kDa. BAFFR is fused to 233 a.a hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The BAFFR solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

    More Info

    • Synonyms

      TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

    • 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

      DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.

    • Background

      B-cell Activating Factor (BAFF) and its corresponding receptor, BAFF-R, are integral components of the immune system, orchestrating crucial processes in B-cell survival, maturation, and differentiation. As we delve into the intricate world of immunology, the study of BAFF and its receptor has unveiled essential pathways that govern the immune responses in health and disease. This research investigates the multifaceted role of BAFF Receptor Protein, shedding light on its structural complexities, signaling mechanisms, and its pivotal contributions to immune regulation. By exploring the interactions between BAFF and its receptor, scientists aim to decipher the delicate balance that underlies immune homeostasis and explore potential therapeutic avenues.

      Structural Architecture of BAFF Receptor Protein:

      BAFF Receptor, a transmembrane protein predominantly expressed on B cells, belongs to the tumor necrosis factor receptor (TNFR) superfamily. Its intricate structure involves various domains, each playing a unique role in ligand binding, receptor activation, and downstream signaling. Understanding the structural intricacies of BAFF Receptor is paramount to unraveling the molecular events that govern B-cell fate decisions and immune responses.

      Physiological Significance in B-Cell Biology:

      BAFF Receptor, upon binding with its ligand BAFF, initiates a cascade of events critical for B-cell survival and function. This interaction promotes B-cell maturation, prevents premature apoptosis, and influences the formation of immune synapses. Additionally, BAFF Receptor signaling is tightly regulated to prevent excessive B-cell activation, ensuring immune tolerance and preventing autoimmune responses. Disruptions in these pathways can lead to autoimmune disorders, underscoring the crucial role of BAFF Receptor in maintaining immune equilibrium.

      Regulation of Immune Responses:

      BAFF Receptor signaling not only affects B-cell development but also has broader implications for immune responses. By modulating antibody production, B-cell activation, and immune memory, BAFF Receptor plays a vital role in shaping adaptive immunity. Its dysregulation has been implicated in various autoimmune conditions, making it an attractive target for therapeutic interventions aimed at restoring immune balance.

      BAFF Receptor as a Therapeutic Target:

      The intricate involvement of BAFF Receptor in autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, has positioned it as a promising therapeutic target. Researchers are exploring monoclonal antibodies and other targeted therapies that aim to modulate BAFF Receptor signaling, providing a new frontier in autoimmune disease management. Additionally, understanding the BAFF-BAFF Receptor axis offers potential insights into the development of vaccines and immunotherapies, fostering innovative approaches in the fight against infectious diseases and malignancies.

      BAFF Receptor Protein, as a key player in immune regulation, embodies the complexities of immunology. Its interactions with BAFF orchestrate fundamental processes in B-cell biology and adaptive immunity. As scientists unravel the intricate signaling pathways and structural nuances of BAFF Receptor, they pave the way for novel therapeutic strategies and innovative treatments for autoimmune disorders and beyond. This research not only deepens our understanding of immune regulation but also holds the promise of transformative advancements in immunotherapy, ultimately shaping the future of immune-related healthcare.

      What is the molecular weight/Mw of BAFF-R Protein?
      BAFF-R Protein has a total Mw of 34.4kDa.

      What is the source or expression system of BAFF-R Protein?
      HEK293 Cells.

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

      What is the Biological Activity of BAFF-R Protein?
      The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

      What is the amino acid sequence of BAFF-R Protein?
      DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.

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

      What is the endotoxin level for BAFF-R Protein?
      The endotoxin level is minimal, BAFF-R 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.

    Baff Receptor Human
  • View Data Sheet

    Description:

    HB-EGF Human Recombinant

    HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    Product # :

    CYT-119

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    Description

    HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

    More Info

    • Introduction

      HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

    • Synonyms

      HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC

      KYVKELRAPS CICHPGYHGE RCHGLSL.

    • Background

      What is the molecular weight/Mw of HB-EGF Protein?
      HB-EGF Protein has a total Mw of 9.9kDa.

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

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

      What is the Biological Activity of HB-EGF Protein?
      The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

      What is the amino acid sequence of HB-EGF Protein?
      MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
      KYVKELRAPS CICHPGYHGE RCHGLSL.

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

      What is the endotoxin level for HB-EGF Protein?
      The endotoxin level is minimal, HB-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.

    Hb Egf Human
  • View Data Sheet

    Name :

    CTF1 Rat

    Description:

    Cardiotrophin-1 Rat Recombinant

    Cardiotrophin-1, CT-1, Ctf1.

    Product # :

    CYT-199

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    Description

    Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

    More Info

    • Introduction

      Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
      CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
      Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
      Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.

    • Synonyms

      Cardiotrophin-1, CT-1, Ctf1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.

    • Background

      What is the molecular weight/Mw of CTF1 Protein?
      CTF1 Protein has a total Mw of 21.4kDa.

      What is the source or expression system of CTF1 Protein?
      Escherichia Coli.

      What is the Purity of CTF1 Protein?
      CTF1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF1 Protein?
      The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

      What is the amino acid sequence of CTF1 Protein?
      MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.

      What applications can CTF1 Protein be used in?
      CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF1 Protein?
      The endotoxin level is minimal, CTF1 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.

    Ct 1 Rat
  • View Data Sheet

    Description:

    Transcription Factor-A Recombinant Human

    Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.

    Product # :

    PRO-095

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    Description

    TFAM produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (43-246.a.a) and having a molecular mass of 26.6kDa. TFAM is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFAM protein solution (0.25mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TFAM is a mitochondrial transcription factor which is a main activator of mitochondrial transcription and is also a participant in mitochondrial genome replication. TFAM is situated primarily in the nuclei of elongated spermatids and takes part in the regulation of gene expression of the haploid male genome. TFAM is linked to mitochondrial disorder in humans characterized by ocular myopathy, exercise intolerance and muscle wasting.

    • Synonyms

      Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSVLASCPK KPVSSYLRFS KEQLPIFKAQ NPDAKTTELI RRIAQRWREL PDSKKKIYQD AYRAEWQVYK EEISRFKEQL TPSQIMSLEK EIMDKHLKRK AMTKKKELTL LGKPKRPRSA YNVYVAERFQ EAKGDSPQEK LKTVKENWKN LSDSEKELYI QHAKEDETRY HNEMKSWEEQ MIEVGRKDLL RRTIKKQRKY GAEEC

    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.

    Tfam Human
  • View Data Sheet

    Description:

    TRAIL/APO 2 Ligand (114-281 a.a.) Human Recombinant, Active

    Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    Product # :

    CYT-1014

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    Description

    Soluble TNF-related apoptosis-inducing ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (114-281) and having a molecular mass of 19.6 kDa. The sTRAIL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TRAIL protein solution (1mg/ml) containing 20mM Tris-HCl pH-7.5, 300mM NaCl, 0.1mM DTT & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell cytotoxicity assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 1 ng/ml.

    More Info

    • Introduction

      TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
      In humans, the gene that encodes for TRAIL is located at chromosome 3q26.
      TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    • Physical Appearance

      Sterile Filtered colorless liquid.

    • 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

      MVRERGPQRV AAHITGTRGR SNTLSSPNSK NEKALGRKIN SWESSRSGHS FLSNLHLRNGELVIHEKGFY YIYSQTYFRF QEEIKENTKN DKQMVQYIYK YTSYPDPILL MKSARNSCWSKDAEYGLYSI YQGGIFELKE NDRIFVSVTN EHLIDMDHEA SFFGAFLVG.

    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.

    Trail Human 114 281 Aa Active
  • View Data Sheet

    Description:

    Platelet-Derived Growth Factor BB Human Recombinant

    Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide.

    Product # :

    CYT-501

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    Description

    Platelet-Derived Growth Factor BB Human Recombinant is a homodimeric, non-glycosylated, polypeptide chain containing 2x109 amino acids (218 amino acids in total) and having a molecular mass of 24.3 kDa. PDGF-BB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

    Purity

    Greater than 95.0% 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 Balb/c 3T3 cells.
    The expected ED50 for this effect is 1.0-3.0 ng/ml.

    More Info

    • Introduction

      PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.

    • Synonyms

      Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Platelet-derived Growth Factor BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Platelet-derived Growth Factor-BB in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SLGSLTIAEP AMIAECKTRT EVFEISRRLI DRTNANFLVW PPCVEVQRCS GCCNNRNVQC RPTQVQLRPV QVRKIEIVRK KPIFKKATVT LEDHLACKCE TVAAARPVT.

    • Background

      PDGF BB HUMAN: Overview of Its Production, Properties, and Clinical Significance

      PDGF BB HUMAN, standing for Platelet-Derived Growth Factor BB, is a powerful protein in the field of medical research, particularly in cell growth and healing. This growth factor plays a crucial role in the development and repair of tissues by stimulating cells primarily of mesenchymal origin.

      Characteristics and Production

      PDGF is produced as a recombinant protein in E. coli. It presents as a homodimer consisting of two identical polypeptide chains, each containing 109 amino acids, culminating in a total molecular mass of 24.3 kDa. The production process ensures a high-purity product, which is essential for reliable scientific results.

      Physical Properties and Formulation

      This growth factor appears as a white, sterile, lyophilized powder. It is formulated in a buffered solution (PBS, pH 7.4) and then filtered to ensure sterility and purity, essential for laboratory use. The formulation process is designed to maintain the stability and activity of the protein under various research conditions.

      Solubility and Storage Instructions

      PDGF BB is recommended to be reconstituted in sterile water to achieve a concentration of no less than 100µg/ml. This solution can then be diluted further to meet experimental needs.

      Once reconstituted, the protein should be stored at 4°C for short-term use (2-7 days) and below -18°C for long-term storage. Avoiding freeze-thaw cycles is crucial to preserve its biological activities.

      Stability and Purity

      The lyophilized form of PDGF BB remains stable at room temperature for up to three weeks but requires desiccation for longer storage.

      Moreover, the purity of this growth factor exceeds 95%, as confirmed by rigorous testing, including RP-HPLC and SDS-PAGE, ensuring that researchers receive a highly effective product.

      Research Applications

      PDGF BB HUMAN is widely used in laboratory research to explore various biological processes, including wound healing, angiogenesis, and the development of certain types of cancers. It is also instrumental in studying the cellular mechanisms underlying tissue repair and regeneration.

      Biological Activity

      The effectiveness of PDGF BB is measured by its ability to stimulate the proliferation of Balb/c 3T3 cells, with an effective dose (ED50) ranging from 1.0 to 3.0 ng/ml. This high level of activity underscores its utility in promoting cell growth, making it an invaluable tool in tissue engineering and regenerative medicine.

      Usage Guidelines

      It is important to note that PDGF BB HUMAN is intended solely for laboratory research and is not suitable for drug, food, or cosmetic applications. Researchers must handle this growth factor under controlled conditions to ensure safety and efficacy.

      Essentially, PDGF BB is a pivotal component in the toolkit of biomedical researchers, offering profound insights into cellular processes and potential therapeutic approaches. Also, its well-defined properties and controlled production make it a staple in studies focused on cell growth and tissue repair.



    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.

    Pdgf Bb Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-8 Mouse Recombinant, 194 a.a.

    FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

    Product # :

    CYT-840

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    Description

    FGF 8 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 5mM Na3PO4 and 50 mM NaCl, pH 7.5.

    Purity

    Greater than 97.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

    More Info

    • Introduction

      FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

    • Synonyms

      FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF 8 although stable at room temperature for 3 weeks, should be stored desiccated below -18?C. Upon reconstitution FGF 8 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 FGF 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR

    • Background

      What is the molecular weight/Mw of FGF8 Protein?
      FGF8 Protein has a total Mw of 22.5kDa.

      What is the source or expression system of FGF8 Protein?
      Escherichia Coli.

      What is the Purity of FGF8 Protein?
      FGF8 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF8 Protein?
      The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

      What is the amino acid sequence of FGF8 Protein?
      MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR

      What applications can FGF8 Protein be used in?
      FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF8 Protein?
      The endotoxin level is minimal, FGF8 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.

    Fgf 8 Mouse 194 Aa
  • View Data Sheet

    Description:

    MYDGF Mouse Recombinant, His Tag

    D17Wsu104e, Il25, Ly6elg, MYDGF, Interleukin-25, IL-25, Stromal cell-derived growth factor SF20.

    Product # :

    CYT-1040

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    • sds-page

    Description

    MYDGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (25-166 a.a) and having a molecular mass of 18.1kDa. MYDGF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYDGF protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      Myeloid-derived growth factor (Mydgf) is a paracrine-acting protein and a bone marrow-derived monocyte which stimulates cardiac myocyte survival and adaptive angiogenesis for cardiac protection and repair after myocardial infarction. Mydgf induces endothelial cell proliferation through a MAPK1/3-, STAT3- and CCND1-mediated signaling lane. When comparing wild-type mice to mice with a Mydgf-deficiency, the later develop larger infarct scars and more acute contractile dysfunction.

    • Synonyms

      D17Wsu104e, Il25, Ly6elg, MYDGF, Interleukin-25, IL-25, Stromal cell-derived growth factor SF20.

    • 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 MGSVSEPTTV PFDVRPGGVV HSFSQDVGPG NKFTCTFTYA SQGGTNEQWQ MSLGTSEDSQ HFTCTIWRPQ GKSYLYFTQF KAELRGAEIE YAMAYSKAAF ERESDVPLKS EEFEVTKTAV SHRPGAFKAE LSKLVIVAKA ARSEL.

    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.

    Mydgf Mouse
  • View Data Sheet

    Description:

    Insulin Like Growth Factor Binding Protein-6 (28-240 a.a.) Human Recombinant

    Insulin-like growth factor-binding protein 6, IBP-6, IGF-binding protein 6, IGFBP-6, IGFBP6, IBP6.

    Product # :

    CYT-786

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    Description

    IGFBP6 Human Recombinant produced in E. coli is a single polypeptide chain containing 236 amino acids (28-240) and having a molecular mass of 25.0kDa (Molecular size on SDS-PAGE will appear higher).IGFBP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IGFBP6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      IGFBP6 plays a role in lipoprotein assembly and dietary cholesterol absorption. in addition to its acyltransferase activity, it may act as a ligase. may provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.

    • Synonyms

      Insulin-like growth factor-binding protein 6, IBP-6, IGF-binding protein 6, IGFBP-6, IGFBP6, IBP6.

    • 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 MGSRCPGCGQ GVQAGCPGGC VEEEDGGSPA EGCAEAEGCL RREGQECGVY TPNCAPGLQC HPPKDDEAPL RALLLGRGRC LPARAPAVAE ENPKESKPQA GTARPQDVNR RDQQRNPGTS TTPSQPNSAG VQDTEMGPCR RHLDSVLQQL QTEVYRGAQT LYVPNCDHRG FYRKRQCRSS QGQRRGPCWC VDRMGKSLPG SPDGNGSSSC PTGSSG.

    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.

    Igfbp6 28 240 Human
  • View Data Sheet

    Description:

    Insulin Like Growth Factor Binding Protein-7Human Recombinant, His Tag

    Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.

    Product # :

    CYT-809

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    Description

    IGFBP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (27-282 a.a.) and having a molecular mass of 28.8kDa.IGFBP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IGFBP7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 1mM EDTA.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Insulin-like Growth Factor-Binding Protein 7 (IGFBP7) is a member of the IGFBP family. IGFBP family members are all cysteine rich proteins with conserved cysteine and have an IGFBP domain, a Kazal-like domain and an Ig-like C2-type domain. IGFBP7 is expressed in a broad range of normal human tissues and it mostly shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. IGFBP7 has a role in skeletal myogenesis by binding to IGF in a manner which inhibits IGF induced differentiation of skeletal myoblasts, without disturbing IGF induced proliferation. Moreover, IGFBP7 suppresses growth and colony formation of prostate and breast cancer cell lines via an IGF independent mechanism, which triggers a delay in the G1 phase of the cell cycle, and increased apoptosis.

    • Synonyms

      Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.

    • 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 MGSSSSDTCG PCEPASCPPL PPLGCLLGET RDACGCCPMC ARGEGEPCGG GGAGRGYCAP GMECVKSRKR RKGKAGAAAG GPGVSGVCVC KSRYPVCGSD GTTYPSGCQL RAASQRAESR GEKAITQVSK GTCEQGPSIV TPPKDIWNVT GAQVYLSCEV IGIPTPVLIW NKVKRGHYGV QRTELLPGDR DNLAIQTRGG PEKHEVTGWV LVSPLSKEDA GEYECHASNS QGQASASAKI TVVDALHEIP VKKGEGAEL.

    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.

    Igfbp7 Human His
  • View Data Sheet

    Description:

    IGF-Like Family Receptor 1 Human Recombinant

    TMEM149, U2AF1L4, IGF-like family receptor 1, Transmembrane protein 149, U2 small nuclear RNA auxiliary factor 1-like 4, IGFLR1. 

    Product # :

    PRO-1432

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    Description

    IGFLR1 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (23-163) and having a molecular mass of 17.5kDa. IGFLR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IGFLR1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GF-like family receptor 1 (IGFLR1) is encoded by a gene mapping to human chromosome 19. IGFLR1 which is cell membrane receptor for the IGF-like family proteins binds IGFL1 and IGFL3 with a higher affinity and may as well bind IGFL2.

    • Synonyms

      TMEM149, U2AF1L4, IGF-like family receptor 1, Transmembrane protein 149, U2 small nuclear RNA auxiliary factor 1-like 4, IGFLR1.

    • 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 MGSSQYCGRL EYWNPDNKCC SSCLQRFGPP PCPDYEFREN CGLNDHGDFV TPPFRKCSSG QCNPDGAELC SPCGGGAVTP TPAAGGGRTP WRCRERPVPA KGHCPLTPGN PGAPSSQERS SPASSIAWRT PEPVPQQAWP NFLP.

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    Igflr1 Human
  • View Data Sheet

    Description:

    Glucagon Receptor Human Recombinant

    GL-R, GLR, Glucagon Receptor.

    Product # :

    HOR-020

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    Description

    GCGR Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain (a.a 29-142) containing 125 amino acids including an 8 a.a C-terminal His tag. The total molecular mass is 19.9kDa (calculated).

    Source

    E. coli

    Formulation

    GCGR filtered (0.4 µm) and lyophilized from solution in acetonitrile/0,1%TFA and 1% (w/v) trehalose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glucagon receptor is part of the glucagon receptor family which also contains GLP-1, GLP-2, GHRH and GIP receptors. GCGR regulates blood glucose levels and is mainly expressed in the pancreas, liver and kidneys. Mutations in GCGR are a cause of non-insulin-dependent diabetes mellitus.

    • Synonyms

      GL-R, GLR, Glucagon Receptor.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MQVMDFLFEK WKLYGDQCHH NLSLLPPPTE LVCNRTFDKY SCWPDTPANT TANISCPWYL PWHHKVQHRF VFKRCGPDGQ WVRGPRGQPW RDASQCQMDG EEIEVQKEVA KMYSSFQLEH HHHHH.

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    Gcgr Human
  • View Data Sheet

    Description:

    Beta Nerve Growth Factor Mouse Recombinant

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-581

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    Description

    Recombinant Mouse b-NGF produced in E.Coli is a noncovalently disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 identical chains of 120 amino acids each and having a molecular mass of 13,471 Dalton each.The Recombinant Mouse-beta-NGF is purified by advanced biology purification technology.

    Source

    Escherichia Coli.

    Formulation

    The Recombinant Mouse b-NGF was lyophilized without additives.

    Purity

    Greater than 98% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE .

    Biological Activity

    The Mouse b-NGF activity was measured in a cell proliferation assay using a factor-dependent human erythroleukemic cell line, TF-1, the ED50 for this effect is 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 units/mg.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis. Nerve Growth Factor was the 1st protein found from the family of neurotrophic factors that influence the growth and differentiation of sympathetic and sensory neurons. NGF consists of 3 different subunits: alpha, beta, and gamma. The beta subunit is accountable for its growth stimulating activity. The synthesis of NGF in astrocytes is enhanced by a range of cytokines such as IL1, TNF-a, PDGF & TGF-b.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse Beta-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Murine NGF-Beta should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Murine NGF-beta in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSSTHPVFHM GEFSVCDSVS VWVGDKTTAT DIKGKEVTVL AEVNINNSVF RQYFFETKCR ASNPVESGCR GIDSKHWNSY CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR G.

    • Background

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

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

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

      What is the Biological Activity of B NGF Protein?
      The Mouse b-NGF activity was measured in a cell proliferation assay using a factor-dependent human erythroleukemic cell line, TF-1, the ED50 for this effect is 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 units/mg.


      What is the amino acid sequence of B NGF Protein?
      MSSTHPVFHM GEFSVCDSVS VWVGDKTTAT DIKGKEVTVL AEVNINNSVF RQYFFETKCR ASNPVESGCR GIDSKHWNSY CTTTHTFVKA LTTDEKQAAW RFIRIDTACV CVLSRKATRR G.

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

    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.

    Beta Ngf Mouse Recombinant
  • View Data Sheet

    Description:

    Platelet Derived Growth Factor-BB Human Recombinant, Yeast

    Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

    Product # :

    CYT-242

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    Description

    Platelet-Derived Growth Factor BB Human Recombinant is a glycosylated homodimer produced in Saccharomyces cerevisiae, containing 2x109 amino acids and having a molecular mass of 32kDa. PDGF-BB is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae.

    Formulation

    The PDGF-BB was lyophilized from 0.2 µm filtered solution in 20mM sodium phosphate in absence of any carrier protein.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to stimulate proliferation of mouse 3T3 fibroblasts is typically 1 ng/ml, corresponding to a Specific Activity of 1,000,000IU/mg.

    More Info

    • Introduction

      PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.

    • Synonyms

      Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Platelet-derived Growth Factor BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Platelet-derived Growth Factor-BB in sterile 18M-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 Ser-Leu-Gly-Ser-Leu.

    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.

    Pdgf Bb Human Yeast
  • View Data Sheet

    Description:

    Tubby Like Protein 1 Human Recombinant

    Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.

    Product # :

    PRO-1191

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    Description

    TULP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 276 amino acids (290-542) and having a molecular mass of 31.1 kDa.TULP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TULP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tubby-related protein 1 (TULP1) belongs to the TULP family of 4 proteins (TUB and TULP1, -2, and -3), categorized structurally by the highly conserved C-terminal half of the protein. Tubby-like gene family (TULPs) members are found in plants, vertebrates, and invertebrates and encode proteins of unknown function. TULP proteins share a conserved C-terminal region of roughly 200 amino acid residues. In the retina, TULP1 is observed exclusively in the photoreceptor cells, localizing predominantly in the inner segments and connecting cilium and to a lesser degree in the perinuclear cytoplasm and synaptic termini. TULP1 gene mutations are linked with retinitis pigmentosa.

    • Synonyms

      Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related 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 MGSEPREFVL RPAPQGRTVR CRLTRDKKGM DRGMYPSYFL HLDTEKKVFL LAGRKRKRSK TANYLISIDP TNLSRGGENF IGKLRSNLLG NRFTVFDNGQ NPQRGYSTNV ASLRQELAAV IYETNVLGFR GPRRMTVIIP GMSAENERVP IRPRNASDGL LVRWQNKTLE SLIELHNKPP VWNDDSGSYT LNFQGRVTQA SVKNFQIVHA DDPDYIVLQF GRVAEDAFTL DYRYPLCALQ AFAIALSSFD GKLACE

    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.

    Tulp1 Human
  • View Data Sheet

    Description:

    Complement Factor B (26-259 a.a.) Human Recombinant

    Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    Product # :

    PRO-1860

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    Description

    CFB (26-259) Human Recombinant produced in E. coli is. a single polypeptide chain containing 257 amino acids and having a molecular mass of 28.4kDa. CFB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

    • Synonyms

      Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    • 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 SSGLVPRGSQ SHMTPWSLAR PQGSCSLEGV EIKGGSFRLL QEGQALEYVC PSGFYPYPVQ TRTCRSTGSW STLKTQDQKT VRKAECRAIH CPRPHDFENG EYWPRSPYYN VSDEISFHCY DGYTLRGSAN RTCQVNGRWS GQTAICDNGA GYCSNPGIPI GTRKVGSQYR LEDSVTYHCS RGLTLRGSQR RTCQEGGSWS GTEPSCQDSF MYDTPQEVAE AFLSSLTETI EGVDAEDGHG PGEQQKR.

    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.

    Cfb 26 259 Human
  • View Data Sheet

    Description:

    Lipopolysaccharide-Induced TNF Factor Human Recombinant

    Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.

    Product # :

    PRO-1350

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    Description

    LITAF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 19.2 kDa. LITAF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Lipopolysaccharide-induced TNF-alpha factor (LITAF) is a small integral membrane protein of lysosome/late endosome. The expression of inflammatory cytokines such as TNF-alpha in Lipopolysaccharide-induced processes is mediated by LITAF. LITAF connects to STAT6B, which belongs to the STAT6 family forming a complex on the TNF-alpha promoter that modifies TNF activity. High levels of expression of LITAF mRNA are observed mostly in the placenta, peripheral blood leukocytes, lymph nodes and spleen.

    • Synonyms

      Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.

    • 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 MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L.

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    Litaf Human
  • View Data Sheet

    Description:

    Granzyme-B Human Recombinant

    Granzyme B, C11, CTLA-1, Cathepsin G-like 1, CTSGL1, Cytotoxic T-lymphocyte proteinase 2, Lymphocyte protease, Fragmentin-2, Granzyme-2, Human lymphocyte protein, HLP, SECT, T-cell serine protease 1-3E, CGL1, CSPB, CTLA1, GRB, GZMB, CCPI, CGL-1, CSP-B.

    Product # :

    ENZ-855

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    Description

    GZMB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (21-247 a.a.) and having a molecular mass of 27.8kDa.GZMB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GZMB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Granzyme-B (GZMB) is essential for target cell lysis in cell-mediated immune responses. GZMB is related to an activation cascade of caspases responsible for apoptosis execution. GZMB cuts caspase-3, -7, -9 and 10 to activate enzymes mediating apoptosis.

    • Synonyms

      Granzyme B, C11, CTLA-1, Cathepsin G-like 1, CTSGL1, Cytotoxic T-lymphocyte proteinase 2, Lymphocyte protease, Fragmentin-2, Granzyme-2, Human lymphocyte protein, HLP, SECT, T-cell serine protease 1-3E, CGL1, CSPB, CTLA1, GRB, GZMB, CCPI, CGL-1, CSP-B.

    • 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 MIIGGHEAKP HSRPYMAYLM IWDQKSLKRC GGFLIQDDFV LTAAHCWGSS INVTLGAHNI KEQEPTQQFI PVKRPIPHPA YNPKNFSNDI MLLQLERKAK RTRAVQPLRL PSNKAQVKPG QTCSVAGWGQ TAPLGKHSHT LQEVKMTVQE DRKCESDLRH YYDSTIELCV GDPEIKKTSF KGDSGGPLVC NKVAQGIVSY GRNNGMPPRA CTKVSSFVHW IKKTMKRY.

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    Gzmb Human