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  • View Data Sheet

    Description:

    Vascular Endothelial Growth Factor Receptor-1 D3 Human Recombinant, His Tag

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-338

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    Description

    FLT1 D1-3 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 298 amino acids fragment (31-328) and having a molecular mass of 38.16kDa. The receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT1 His (0.96mg/ml) is supplied in 25mM Na-Acetate pH 4.8 and 50% glycerol.

    Purity

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

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    • Introduction

      Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    Flt1 D3 Human His
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    Description:

    Vascular Endothelial Growth Factor Receptor-1 D3 Human Recombinant

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-234

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    Description

    FLT1 D1-3 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 327 amino acids and having a molecular mass of 45 kDa. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT1 D1-3 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity of FLT1D1-3 was determined by its ability to inhibit the VEGF-165-induced proliferation of HUVE cells.

    More Info

    • Introduction

      Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 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 FLT1 D3 in sterile water not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSI TKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYI FISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDT LIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQT NTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRA SVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSV HIYDKAFITVKHRKQQVLETVAGKRSY.

    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.

    Flt1 D3 Human
  • View Data Sheet

    Description:

    Vascular Endothelial Growth Factor receptor-1 Human Recombinant, HEK Active

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-134

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    Description

    FLT1 Human Recombinant is a single, glycosylated polypeptide chain containing 535 amino acids (27-328a.a) and having a molecular mass of 60.3kDa (calculated). FLT1 is fused to a 233 amino acid hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293

    Formulation

    FLT1 protein solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 60ng/ml and is measured by its ability to inhibit proliferation using HUVEC human umbilical vein endothelial cells in the
    presence of Human VEGF165. 

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    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    • Physical Appearance

      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.Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      SKLKDPELSL KGTQHIMQAG QTLHLQCRGE AAHKWSLPEM VSKESERLSI TKSACGRNGK QFCSTLTLNT AQANHTGFYS CKYLAVPTSK KKETESAIYI FISDTGRPFV EMYSEIPEII HMTEGRELVI PCRVTSPNIT VTLKKFPLDT LIPDGKRIIW DSRKGFIISN ATYKEIGLLT CEATVNGHLY KTNYLTHRQT NTIIDVQIST PRPVKLLRGH TLVLNCTATT PLNTRVQMTW SYPDEKNKRA SVRRRIDQSN SHANIFYSVL TIDKMQNKDK GLYTCRVRSG PSFKSVNTSV HILEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGK.

    • Background

      VEGFR-1 (Vascular Endothelial Growth Factor Receptor-1), also known as Flt-1 (Fms-like tyrosine kinase 1), is a critical receptor involved in angiogenesis and vascular development. This research paper delves into the structure, function, and therapeutic implications of VEGFR-1, shedding light on its multifaceted role in various physiological and pathological processes.

      VEGFR-1 is a transmembrane receptor tyrosine kinase belonging to the VEGF receptor family. It is primarily expressed on endothelial cells and plays a pivotal role in mediating the cellular responses to VEGF ligands. Upon ligand binding, VEGFR-1 initiates intracellular signaling cascades that regulate endothelial cell proliferation, migration, and survival, ultimately contributing to the formation of new blood vessels.

      The structure of VEGFR-1 comprises distinct domains, including an extracellular ligand-binding domain, a transmembrane domain, and an intracellular tyrosine kinase domain. The extracellular domain facilitates the interaction between VEGF ligands and the receptor, while the intracellular domain transduces downstream signals by phosphorylating specific tyrosine residues.

      VEGFR-1 exhibits not only ligand-dependent but also ligand-independent functions. In addition to its role as a VEGF receptor, it can act as a decoy receptor, sequestering VEGF and modulating the bioavailability of VEGF ligands. This unique property allows VEGFR-1 to regulate VEGF signaling and influence angiogenic processes.

      The signaling pathways activated by VEGFR-1 are diverse and intricate, involving multiple downstream effectors, such as PI3K/AKT, MAPK/ERK, and STAT proteins. These pathways regulate endothelial cell behaviors, including proliferation, migration, and differentiation, which are crucial for angiogenesis. Perturbations in VEGFR-1 signaling have been implicated in various pathological conditions, including cancer, retinopathy, and inflammatory disorders.

      The therapeutic targeting of VEGFR-1 has gained considerable attention for its potential in managing angiogenesis-related diseases. Inhibitors specifically designed to block VEGFR-1 have been developed to suppress aberrant angiogenesis and impede tumor growth. Moreover, VEGFR-1-based therapies have been explored for ocular diseases like wet age-related macular degeneration (AMD) and diabetic retinopathy, aiming to alleviate pathological neovascularization.

      The availability of VEGFR-1 human recombinant proteins has facilitated in-depth research and the development of potential therapeutic interventions. Recombinant VEGFR-1 proteins serve as valuable tools for investigating VEGF-VEGFR-1 interactions, screening drug candidates, and elucidating the underlying molecular mechanisms of VEGFR-1-mediated signaling pathways.

    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.

    Flt1 Human Hek Active
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    Description:

    Staphylococcal Protein A Recombinant

    Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    Product # :

    PRO-356

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    Description

    Recombinant Staphylococcal Protein A produced in E.Coli is a non-glycosylated, Polypeptide chain having a molecular mass of 46.7 kDa.Recombinant Staphylococcal Protein A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains no additives.

    Purity

    Greater than 95.0% as determined by RP-HPLC.

    Biological Activity

    Greater than 95.0% binding activity to human IgG.

    More Info

    • Introduction

      Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).

    • Synonyms

      Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    • Physical Appearance

      Sterile Filtered clear colorless solution.

    • Stability

      SPA should be stored at -20°C.

    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.

    Protein A
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    Description:

    Protein A/G Cys Recombinant

    Product # :

    PRO-1928

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    • sds-page, HPLC

    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 2 of protein G (C1-C3) containing 430 amino acids in total and having a molecular mass of 47.8kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

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

    sds-page, HPLC

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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 Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEC.

    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.

    Protein A G Cys
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    Description:

    Epidermal Growth Factor Mouse Recombinant

    Urogastrone, URG, EGF.

    Product # :

    CYT-326

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    Description

    Epidermal Growth Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids including 3 intramolecular disulfide-bonds and having a molecular mass of 6 kDa.The EGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells and is typically less than 0.1ng/ml.

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    • 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

      NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR.

    • Background

      Exploring Novel Frontiers: Epidermal Growth Factor Mouse Recombinant and its Potential Therapeutic Implications

      Abstract:

      This research paper delves into the uncharted realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), unraveling its intricate molecular attributes, cellular signaling, and therapeutic prospects. Employing state-of-the-art methodologies involving genetic engineering, in vitro assays, and animal models, this study uncovers the multifaceted responses elicited by EGF-MR. The findings underscore its promise as a versatile therapeutic agent, potentially revolutionizing regenerative medicine and cancer interventions.

      Introduction:

      Epidermal Growth Factor (EGF) plays a pivotal role in cellular dynamics. This paper ventures into the nuanced landscape of Epidermal Growth Factor Mouse Recombinant (EGF-MR), delving into its unique molecular characteristics and exploring the therapeutic horizons it presents.

      Molecular Insights and Receptor Binding:

      EGF-MR's interaction with the epidermal growth factor receptor (EGFR) sets the stage for intricate intracellular events. High-resolution structural analyses and binding kinetics studies elucidate the nuances of this interaction, revealing structural motifs that initiate downstream signaling cascades.

      Cellular Signaling and Functional Responses:

      EGF-MR initiates canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K)/Akt pathways. Through comprehensive phosphoproteomic analyses and live-cell imaging, the spatiotemporal dynamics of EGF-MR-induced responses come to light, showcasing its role in cell proliferation, migration, and anti-apoptotic effects.

      Genetic Engineering and In Vitro Assays:

      Precise genetic manipulation ensures optimal EGF-MR expression. Gene codon optimization and signal peptide selection are meticulously undertaken to facilitate efficient protein synthesis and secretion. In vitro assays, encompassing cell viability and wound healing studies, illuminate EGF-MR's impact on cellular behaviors.

      In Vivo Implications and Therapeutic Prospects:

      In animal models, EGF-MR emerges as a transformative factor in tissue regeneration. Customized wound healing assays unveil its potential in accelerating re-epithelialization and granulation tissue formation. Moreover, the modulation of tumor microenvironments suggests its applicability in cancer interventions.

      Future Directions and Challenges:

      While promising, challenges lie ahead, including understanding intricate cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosing regimens to harness EGF-MR's full therapeutic potential.

      Conclusion:

      In a convergence of advanced methodologies and visionary therapeutic possibilities, Epidermal Growth Factor Mouse Recombinant takes center stage. Its distinctive molecular interactions and diverse cellular orchestration offer a glimpse into the future of regenerative medicine and targeted cancer therapies, propelling scientific progress into uncharted territories.

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

      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 activity is determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells and is typically less than 0.1ng/ml.

      What is the amino acid sequence of EGF Protein?
      NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW 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 Mouse Recombinant
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    Description:

    Bone Morphogenetic Protein-4 Human Recombinant

    BMP4, ZYME, BMP2B, BMP2B1.

    Product # :

    CYT-361

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    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:

    Protein A/G Recombinant

    Product # :

    PRO-646

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    Description

    The recombinant Protein A/G consists of 5 IgG-binding regions of protein A and 2 of protein G, which corresponds to the Protein A and G domains that are included in the recombinant sequence. Cell wall binding region, cell membrane binding region and albumin binding region have been removed from the recombinant Protein A/G to ensure the maximum specific IgG binding. The Protein A portion is from Staphylococcus aureus segments E, D, A, B and C. The Protein G portion is from Streptococcus segments C1 and C3. The fusion protein has a predicted molecular mass of 47.7kDa and containing 429 amino acids.

    Source

    Escherichia coli.

    Formulation

    Lyophilized white Powder containing no additives.

    Purity

    >97% as determined by SDS-PAGE and RP-HPLC.

    More Info

    • Introduction

      Recombinant Protein A/G fusion protein joins IgG binding domains of both Protein A and Protein G.
      Protein A/G includes four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50.4 kDa. The binding dependency to pH of Protein A/G lower than Protein A, but has the additive properties of Protein A and G together. Protein A/G binds to all subclasses of human IgG, making it helpful for purifying polyclonal or monoclonal IgG antibodies whose subclasses have not been identifieed. Protein A/G binds to IgA, IgE, IgM and IgD. Protein A/G binds to all subclasses of mouse IgG excluding mouse IgA, IgM or serum albumin. This permits Protein A/G to be used in purification and detection of mouse monoclonal IgG antibodies, with no interference from IgA, IgM and serum albumin. Mouse monoclonal antibodies normally have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G. Protein A/G also has been used for purification of macaque IgG.

    • Stability

      After reconstitution, aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTE.

    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.

    Protein A G
  • View Data Sheet

    Description:

    Von Hippel-Lindau Binding Protein 1 Human Recombinant

    Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.

    Product # :

    PRO-1325

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    Description

    VBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a) and having a molecular mass of 25kDa.VBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    VBP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prefoldin subunit 3 (VBP1) is a member of the prefoldin subunit alpha family. VBP1 interacts with the Von Hippel-Lindau protein in order to create an intracellular complex. Since VBP1 serves as a chaperone protein, it is assumed to have a role in the transport of the Von Hippel-Lindau protein from the perinuclear granules to the nucleus or cytoplasm. VBP1 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. VBP1 also binds to nascent polypeptide chain and stimulates folding in an environment in which there are numerous competing pathways for nonnative proteins.

    • Synonyms

      Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.

    • 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 MGSMAAVKDS CGKGEMATGN GRRLHLGIPE AVFVEDVDSF MKQPGNETAD TVLKKLDEQY QKYKFMELNL AQKKRRLKGQ IPEIKQTLEI LKYMQKKKES TNSMETRFLL ADNLYCKASV PPTDKVCLWL GANVMLEYDI DEAQALLEKN LSTATKNLDS LEEDLDFLRD QFTTTEVNMA RVYNWDVKRR NKDDSTKNKA.

    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.

    Vbp1 Human
  • View Data Sheet

    Description:

    Vesicular Overexpressed in Cancer, Prosurvival Protein 1 Human Recombinant

    Vesicular overexpressed in cancer prosurvival protein 1, EGFR-coamplified and overexpressed protein, ECop, Glioblastoma-amplified secreted protein, Putative NF-kappa-B-activating protein 055N, VOPP1, ECOP, GASP, FLJ20532, DKFZp564K0822.

    Product # :

    PRO-200

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    Description

    VOPP1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 112 amino acids (82-172 a.a.) and having a molecular mass of 12kDa. The VOPP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VOPP1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.2M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vesicular overexpressed in cancer prosurvival protein 1 (VOPP1) has been previously shown to be over-expressed in human glioblastoma multiform and squamous cell carcinoma. VOPP1 is a crucial regulator of NF-kappaB signaling, and this high-level, amplification-mediated VOPP1 expression, such as that occurring in tumors with amplified EGFR, might impact the resistance to apoptosis.

    • Synonyms

      Vesicular overexpressed in cancer prosurvival protein 1, EGFR-coamplified and overexpressed protein, ECop, Glioblastoma-amplified secreted protein, Putative NF-kappa-B-activating protein 055N, VOPP1, ECOP, GASP, FLJ20532, DKFZp564K0822.

    • 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 MRRRMYPPPL IEEPAFNVSY TRQPPNPGPG AQQPGPPYYT DPGGPGMNPV GNSMAMAFQV PPNSPQGSVA CPPPPAYCNT PPPPYEQVVK AK.

    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.

    Vopp1 Human
  • View Data Sheet

    Description:

    Von Hippel-Lindau Protein Human Recombinant

    Von Hippel-Lindau disease tumor suppressor, pVHL, Protein G7, VHL, RCA1, VHL1, HRCA1.

    Product # :

    PRO-440

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    Description

    Recombinant Human Von Hippel-Lindau Protein b-domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154) & having a molecular mass of 19.2 kDa. The Von Hippel-Lindau antigen is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Von Hippel-Lindau Protein contains 1x PBS pH-7.4, 2mM EDTA, and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Von Hippel-Lindau disease is a dominant inherited syndrome characterized by the predisposition to develop various kinds of benign and malignant tumors, including clear cell renal carcinomas, pheochromocytomas and hemangioblastomas of the central nervous system and retina. VHL syndrome is caused by germline mutation in the VHL tumor suppressor, and VHL tumors are associated with loss or mutation of the remaining wild-type allele. VHL has two domains: a roughly 100-residue NH2-terminal domain rich in b sheet (b-domain) and a smaller a-helical domain (a-domain), held together by two linkers and a polar interface. VHL protein is also involved in the degradation of hypoxia-inducible factor (HIF).

    • Synonyms

      Von Hippel-Lindau disease tumor suppressor, pVHL, Protein G7, VHL, RCA1, VHL1, HRCA1.

    • 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 MPRRAENWDE AEVGAEEAGV EEYGPEEDGG EESGAEESGPEESGPEELGA EEEMEAGRPR PVLRSVNSRE PSQVIFCNRS PRVVLPVWLN FDGEPQPYPT LPPGTGRRIH SYRGHLWLFR DAGTHDGLLV NQTELFVPSL NVDGQPIFAN ITLP.

    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.

    Vhl Human
  • View Data Sheet

    Description:

    Epidermal Growth Factor Rat

    Urogastrone, URG, EGF.

    Product # :

    CYT-556

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    Description

    Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.

    Source

    Adult Male Rat Submandibular Glands.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

    Purity

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

    • Background

      Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential

      Abstract:

      This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.

      Introduction:

      Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.

      Protein Expression and Purification:

      The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.

      Receptor Binding Assays and Ligand Interaction:

      Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.

      Cellular Signaling Pathways and Responses:

      In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.

      Bioinformatics Insights and Structural Modeling:

      Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.

      Therapeutic Implications and Future Prospects:

      EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.

      Challenges and Future Directions:

      Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.

      Conclusion:

      A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.

      What is the molecular weight/Mw of EGF RAT Protein?
      EGF RAT Protein has a total Mw of 6.15kDa.

      What is the source or expression system of EGF RAT Protein?
      Adult Male Rat Submandibular Glands.

      What is the Purity of EGF RAT Protein?
      EGF RAT Protein is >99% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of EGF RAT Protein?
      EGF RAT Protein is composed from 53 amino acids.

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

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

    Description:

    Platelet Factor-4 Human (CXCL4)

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-234

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    Description

    Human PF-4 a 7.8 kDa protein consisting of 70 amino acid residues.

    Source

    Human Platelets.

    Formulation

    The CXCL4 protein was lyophilized in PBS buffer pH-7.4.

    Purity

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

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL4 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 four N-terminal amino acids was determined and was found to be Glu-Ala-Glu-Glu.

    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.

    Pf 4 Human
  • View Data Sheet

    Description:

    Platelet Derived Growth Factor-CC Human Recombinant

    Platelet Derived Growth Factor C, Spinal Cord-Derived Growth Factor, FALLOTEIN, PDGF-C, VEGF-E, SCDGF, Secretory Growth Factor-Like Protein, Platelet-Derived Growth Factor C, PDGFC.

    Product # :

    CYT-872

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    Description

    PDGF-CC Human Recombinant (235-345) produced in E.Coli is a disulfide-linked homodimer containing 2x118 amino acids and having a total molecular mass of 26.8kDa.The PDGF-CC is fused to a 7 amino acid His tag [M-HHHHHH] at N-terminal and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 350ng/ml.

    More Info

    • Introduction

      Platelet Derived Growth Factor-CC (PDGF-CC) belongs to the PGDF family of growth factors. PDGF-CC binds with high-affinity to PDGF R-a and activates PDGF R-ab heterodimers. During development, PDGF-CC is involved in ductal morphogenesis, cardiovascular smooth muscle cell proliferation; also PDGF-CC is an angiogenic factor. Furthermore, PDGF-CC is expressed in numerous tumors and tumor cell lines, and may be linked with tumorigenesis.

    • Synonyms

      Platelet Derived Growth Factor C, Spinal Cord-Derived Growth Factor, FALLOTEIN, PDGF-C, VEGF-E, SCDGF, Secretory Growth Factor-Like Protein, Platelet-Derived Growth Factor C, PDGFC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MHHHHHHVVD LNLLTEEVRL YSCTPRNFSV SIREELKRTD TIFWPGCLLV KRCGGNCACC LHNCNECQCV PSKVTKKYHE VLQLRPKTGV RGLHKSLTDV ALEHHEECDC VCRGSTGG.

    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 Cc Human
  • View Data Sheet

    Description:

    Carcinoembryonic Antigen Human

    CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    Product # :

    PRO-2801

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    Description

    CEA produced from patient source colon carcinoma liver metastatic tissue can be used as general marker in screening and monitoring malignant disease states.

    Source

    Liver tissue.

    Formulation

    CEA protein solution contains 0.1M PBS, pH 7.4, 0.09 % NaN3 and 2 % methyl-mannoside.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    • 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.

    • Applications

      Blood samples from tissue donors were tested and found to be negative for HBsAg, HIV-1 and HIV-2 antibodies and HCV.

    • Background

      Carcinoembryonic Antigen, commonly known as CEA, is a glycoprotein that was initially identified as a tumor marker. Over the years, research into CEA has unveiled its intricate involvement in various physiological processes, not only in cancer but also in the context of normal development and inflammatory conditions. This research aims to delve into the multifaceted roles of CEA, exploring its structural intricacies, regulatory mechanisms, and its implications in health, disease, and beyond.

      Structural Complexity of CEA:

      CEA, belonging to the immunoglobulin superfamily, is a complex glycoprotein featuring multiple structural domains. Its diverse forms and glycosylation patterns contribute to its functional versatility. CEA is primarily expressed in fetal tissues, but its presence is often detected in adults under pathological conditions, especially in various types of cancer.

      CEA in Cancer Biology:

      CEA was first recognized as a biomarker for colorectal cancer, but its overexpression is not limited to this context. Elevated CEA levels have been associated with several other malignancies, including breast, lung, and pancreatic cancers. CEA’s involvement in cancer biology ranges from promoting angiogenesis and metastasis to inhibiting immune responses, making it a critical player in tumor progression and evasion.

      Beyond Cancer: CEA in Development and Inflammation:

      While CEA’s role in cancer is prominent, recent studies have uncovered its participation in normal physiological processes. During embryonic development, CEA is involved in cell adhesion, contributing to tissue organization and morphogenesis. Additionally, CEA expression can be induced in inflammatory conditions, suggesting its involvement in immune responses and tissue repair mechanisms.

      CEA as a Diagnostic and Therapeutic Target:

      The diverse expression patterns of CEA in various diseases make it a valuable diagnostic tool. CEA assays are widely used for cancer screening, monitoring disease progression, and assessing treatment efficacy. Moreover, CEA’s presence on the surface of cancer cells has made it a target for immunotherapy, enabling the development of targeted therapies aimed at specifically eradicating CEA-positive tumor cells.

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    Cea Human
  • View Data Sheet

    Description:

    Vascular Endothelial Growth Factor receptor-1 Mouse Recombinant

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-139

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    Description

    FLT1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (23-759 a.a) containing a total of 970 amino acids, having a molecular mass of 108.9kDa. FLT1 is fused to a 233 amino acid hIgG-his tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    FLT1 protein solution (1mg/ml) containing 10% glycerol and PBS.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 50ng/ml and is measured by its ability to inhibit proliferation using HUVEC human umbilical vein endothelial cells in the presence of Human VEGF165.

    More Info

    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-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

      YGSGSKLKVP ELSLKGTQHV MQAGQTLFLK CRGEAAHSWS LPTTVSQEDK RLSITPPSAC GRDNRQFCST LTLDTAQANH TGLYTCRYLP TSTSKKKKAE SSIYIFVSDA GSPFIEMHTD IPKLVHMTEG RQLIIPCRVT SPNVTVTLKK FPFDTLTPDG QRITWDSRRG FIIANATYKE IGLLNCEATV NGHLYQTNYL THRQTNTILD VQIRPPSPVR LLHGQTLVLN CTATTELNTR VQMSWNYPGK ATKRASIRQR IDRSHSHNNV FHSVLKINNV ESRDKGLYTC RVKSGSSFQS FNTSVHVYEK GFISVKHRKQ PVQETTAGRR SYRLSMKVKA FPSPEIVWLK DGSPATLKSA RYLVHGYSLI IKDVTTEDAG DYTILLGIKQ SRLFKNLTAT LIVNVKPQIY EKSVSSLPSP PLYPLGSRQV LTCTVYGIPR PTITWLWHPC HHNHSKERYD FCTENEESFI LDPSSNLGNR IESISQRMTV IEGTNKTVST LVVADSQTPG IYSCRAFNKI GTVERNIKFY VTDVPNGFHV SLEKMPAEGE DLKLSCVVNK FLYRDITWIL LRTVNNRTMH HSISKQKMAT TQDYSITLNL VIKNVSLEDS GTYACRARNI YTGEDILRKT EVLVRDSEAP HLLQNLSDYE VSISGSTTLD CQARGVPAPQ ITWFKNNHKI QQEPGIILGP GNSTLFIERV TEEDEGVYRC RATNQKGAVE

    • Background

      Endothelial cells express 3 different vascular endothelial growth factor receptors: VEGFR-1 (Flt1), VEGFR-2 (KDR/Flk1), VEGFR-3 (Flt4) which are a part of the receptor tyrosine kinases family. Those receptors express mostly in endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. Flt1 contains 7 immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Flt-1, when compared to VEGFR-2 receptor has a higher affinity for VEGF but a weaker signalling activity. VEGFR-1 also mediates signals for differentiation.

    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.

    Flt1 Mouse
  • View Data Sheet

    Description:

    Coagulation Factor-VIII Human Recombinant

    Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.

    Product # :

    PRO-318

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    Description

    Antihemophilic Facor Human Recombinant produced in CHO is a glycosylated polypeptide chain having 2332 amino acids. The Factor-VIII is purified by proprietary chromatographic techniques.

    Source

    CHO cells (Chinese Hamster Ovarian Cells).

    Formulation

    Each 250IU vial was lyophilized from a solution containing 8mg Tween-80, 112mM NaCl, 40mg Mannitol, 10mg Trehalose, 1ng VWF and 4.2mM CaCl2.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 7,058 IU/mg.

    More Info

    • Introduction

      Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.

    • Synonyms

      Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Factor-VIII although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Factor-VIII 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 250IU lyophilized Factor-VIII in 5ml sterile 18M-cm H2O, 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.

    Factor Viii Human Recombinant
  • View Data Sheet

    Description:

    Von Willebrand Factor A Domain Containing 2 Human Recombinant

    A domain-containing protein similar to matrilin and collagen, AMACO, Colon cancer secreted protein 2, CCSP-2.

    Product # :

    PRO-2752

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    Description

    VWA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (341-517 a.a) and having a molecular mass of 19.3kDa.The VWA2 is expressed with an amino-terminal hexahistidine tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VWA2 protein solution contains 20mM Tris-HCl, pH 8.0, 0.8M Urea & 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      Von Willebrand Factor A Domain Containing 2 (VWA2) is an extracellular matrix protein containing vWA-like domains. VWA2 contains a signal peptide sequence, an N-terminal VWA domain connected to 2 additional tandem vWA domains by a cysteine-rich sequence and an EGF-like domain. Also, another EGF-like domain is located at the C-terminus. Expression of VWA2 is induced in stage II, III and IV colon cancers and colon adenomas and is considered a novel serum marker for the diagnosis of early-stage colon cancer.

    • Synonyms

      A domain-containing protein similar to matrilin and collagen, AMACO, Colon cancer secreted protein 2, CCSP-2.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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.

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    Vwa2 Human
  • View Data Sheet

    Description:

    Hepatoma-Derived Growth Factor-2 Human Recombinant

    Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.

    Product # :

    CYT-132

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    • SDS-PAGE

    Description

    HDGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a.) and having a molecular mass of 25.1kDa (Molecular weight on SDS-PAGE will appear higher). HDGF2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HDGF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      Hepatoma-derived growth factor, related protein 3 (HDGFRP3/HDGF2) is the original member of a family of polypeptides labeled HDGF related proteins (HRPs). The HDGF2 protein augments DNA synthesis and may play a part in cell proliferation. HDGF2 is expressed primarily in the testis and the brain, to an intermediate extent in the heart, and to a slight extent in the ovaries, kidneys, spleen, and liver in humans.

    • Synonyms

      Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.

    • 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 MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
      KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.

    • Background

      What is the molecular weight/Mw of HDGF2 HUMAN Protein?
      HDGF2 HUMAN Protein has a total Mw of 25.1kDa.

      What is the source or expression system of HDGF2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of HDGF2 HUMAN Protein?
      HDGF2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of HDGF2 HUMAN Protein?
      The biological functionality of HDGF2 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of HDGF2 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
      KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.

      What applications can HDGF2 HUMAN Protein be used in?
      HDGF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HDGF2 HUMAN Protein?
      The endotoxin level is minimal, HDGF2 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.

    Hdgf2 Human
  • View Data Sheet

    Description:

    Protein A/G/L Recombinant

    Product # :

    PRO-1936

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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 805 amino acids in total and having a molecular mass of 89.2kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein- A/G/L was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG.

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    Protein A G L
  • View Data Sheet

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

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    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 in sterile water or 0.4% NaHCO3 pH-8-9, 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-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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).

    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 Human
  • View Data Sheet

    Description:

    Vascular Endothelial Growth Factor Receptor-1 D1-7 Mouse Recombinant

    FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    Product # :

    PKA-312

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    Description

    Soluble FLT1 Mouse Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric , polypeptide containing 965 amino acids. The monomers have a molecular mass of 130 kDa. The soluble receptor protein contains all 7 extracellular domains (Tyr23-Asn757), which contain all the information necessary for high affinity ligand binding.

    Source

    Insect Cells.

    Formulation

    FLT1 D1-7 was lyophilized from a concentrated (1 mg/ml) sterile solution containing PBS Buffer.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity of sVEGFR-1/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells.

    More Info

    • Introduction

      Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

    • Synonyms

      FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution FLT1 should be stored at 4C between 2-7 days and for future use below -18C. 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 FLT1 Fc/Chimera in PBS not less than 50µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      YGSGSKLKVP ELSLKGTQHV MQAGQTLFLK CRGEAAHSWS LPTTVSQEDK RLSITPPSAC GRDNRQFCST LTLDTAQANH TGLYTCRYLP TSTSKKKKAE SSIYIFVSDA GSPFIEMHTD IPKLVHMTEG RQLIIPCRVT SPNVTVTLKK FPFDTLTPDG QRITWDSRRG FIIANATYKE IGLLNCEATV NGHLYQTNYL THRQTNTILD VQIRPPSPVR LLHGQTLVLN CTATTELNTR VQMSWNYPGK ATKRASIRQR IDRSHSHNNV FHSVLKINNV ESRDKGLYTC RVKSGSSFQS FNTSVHVYEK GFISVKHRKQ PVQETTAGRR SYRLSMKVKA FPSPEIVWLK DGSPATLKSA RYLVHGYSLI IKDVTTEDAG DYTILLGIKQ SRLFKNLTAT LIVNVKPQIY EKSVSSLPSP PLYPLGSRQV LTCTVYGIPR PTITWLWHPC HHNHSKERYD FCTENEESFI LDPSSNLGNR IESISQRMTV IEGTNKTVST LVVADSQTPG IYSCRAFNKI GTVERNIKFY VTDVPNGFHV SLEKMPAEGE DLKLSCVVNK FLYRDITWIL LRTVNNRTMH HSISKQKMAT TQDYSITLNL VIKNVSLEDS GTYACRARNI YTGEDILRKT EVLVRDSEAP HLLQNLSDYE VSISGSTTLD CQARGVPAPQ ITWFKNNHKI QQEPGIILGP GNSTLFIERV TEEDEGVYRC RATNQKGAVE SAAYLTVQGT SDKSNAASDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSREEMTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPMLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGK

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    Flt1 D7 Mouse
  • View Data Sheet

    Description:

    Vacuolar Protein Sorting 24 Human Recombinant

    Charged multivesicular body protein 3, Chromatin-modifying protein 3, Neuroendocrine differentiation factor, Vacuolar protein sorting-associated protein 24, hVps24, CHMP3, CGI149, NEDF, VPS24, CGI-149.

    Product # :

    PRO-872

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    Description

    VPS24 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-222 a.a) and having a molecular mass of 27.2kDa (Molecular weight on SDS-PAGE will appear higher).VPS24 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    VPS24 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Charged multivesicular body protein 3 (VPS24/CHMP3) is a member of the vacuolar sorting protein family and function as chromatin modifying proteins. VPS24 links directly with CHMP2 and CHMP4 for the disassembly of ESCRT-III complex in an ATP-dependent manner. During HIV-1 infection, the virus uses the ESCRT-III complex to mediate budding and exocytosis of viral proteins. VPS24 overexpression strongly hinders HIV-1 release.

    • Synonyms

      Charged multivesicular body protein 3, Chromatin-modifying protein 3, Neuroendocrine differentiation factor, Vacuolar protein sorting-associated protein 24, hVps24, CHMP3, CGI149, NEDF, VPS24, CGI-149.

    • 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 MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKDVC IVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEE AEMEIDRILF EITAGALGKA PSKVTDALPE PEPPGAMAAS EDEEEEEEAL EAMQSRLATL RS.

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    Vps24 Human
  • View Data Sheet

    Description:

    Vascular cell adhesion molecule 1 Mouse Recombinant

    V-CAM 1, VCAM-1, CD106, Vcam1, Vcam-1, Vascular cell adhesion protein 1.

    Product # :

    PRO-2257

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    Description

    VCAM1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 682 amino acids (25-698 a.a) and having a molecular mass of 75.4kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). VCAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    VCAM1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).

    • Synonyms

      V-CAM 1, VCAM-1, CD106, Vcam1, Vcam-1, Vascular cell adhesion 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

      FKIEISPEYK TIAQIGDSMA LTCSTTGCES PLFSWRTQID SPLNAKVRTE GSKSVLTMEP VSFENEHSYL CTATCGSGKL ERSIHVDIYS FPKDPEIQFS GPLEVGKPVT VKCLAPDIYP VYRLEIDLFK GDQLMNRQEF SSEEMTKSLE TKSLEVTFTP VIEDIGKALV CRAKLHIDQI DSTLKERETV KELQVYISPR NTTISVHPST RLQEGGAVTM TCSSEGLPAP EIFWGRKLDN EVLQLLSGNA TLTLIAMRME DSGVYVCEGV NLIGRDKAEV ELVVQEKPFI VDISPGSQVA AQVGDSVVLT CAAIGCDSPS FSWRTQTDSP LNGVVRNEGA KSTLVLSSVG FEDEHSYLCA VTCLQRTLEK RTQVEVYSFP EDPVIKMSGP LVHGRPVTVN CTVPNVYPFD HLEIELLKGE TTLMKKYFLE EMGIKSLETK ILETTFIPTI EDTGKSLVCL ARLHSGEMES EPKQRQSVQP LYVNVAPKET TIWVSPSPIL EEGSPVNLTC SSDGIPAPKI LWSRQLNNGE LQPLSENTTL TFMSTKRDDS GIYVCEGINE AGISRKSVEL IIQVSPKDIQ LTVFPSKSVK EGDTVIISCT CGNVPETWII LKKKAKTGDM VLKSVDGSYT IRQAQLQDAG IYECESKTEV GSQLRSLTLD VKGKEHNKNY FSPELEHHHH HH.

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

    Vcam1 Mouse