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1000 results found for “EPH Receptor”

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  • View Data Sheet

    Description:

    Prolactin Receptor Antagonist Human Recombinant

    Mammotropin, Luteotropic hormone, Luteotropin, PRL.

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    CYT-1254

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    Description

    Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.

    Purity

    Greater than 97.0% as determined by:

    (a) Analysis by Gel Filtration.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).

    More Info

    • Synonyms

      Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr

    • Background

      Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

    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.

    Prolactin Receptor Antagonist
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    Description:

    sFas Receptor Human Recombinant, His Tag

    CD95, CD-95, Tumor necrosis factor receptor superfamily member 6, FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95 antigen, FAS, APT1, FAS1, TNFRSF6, APO-1, FASTM, ALPS1A.

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    PRO-594

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    Description

    Recombinant FAS antigen/ CD95 purified from E. coli is a single non-glycosilated polypeptide chain containing amino acids 157-335 of Fas antigen. The recombinant CD95 is fused to C-terminal 6-histidine amino acids. The FAS antigen is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    10mM Sodium Phosphate, pH 8.0.

    Purity

    Greater than 95% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      FAS / CD95 is a 36kDa transmembrane type I receptor, which belongs to the NF/NGF receptor super-family. It is a potent inducer of apoptosis in cells of the immune system upon interaction with its natural ligand, CD95L. Although the CD95/CD95L system could play a role in tumor regression, tumor cells seem to down-regulate CD95 expression as a mechanism of resistance to CD95L-induced killing by T lymphocytes and NK cells. The Fas antigen is expressed on the surface of various cell types, including activated T and B lymphocytes and T lymphoblastoid cell line. CD95 is also expressed in a broad panel of non-transformed cells outside the immune system.

    • Synonyms

      CD95, CD-95, Tumor necrosis factor receptor superfamily member 6, FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95 antigen, FAS, APT1, FAS1, TNFRSF6, APO-1, FASTM, ALPS1A.

    • Physical Appearance

      Sterile liquid formulation.

    • Stability

      CD95 although stable at 10°C for 5 days, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Background

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

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

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

      What is the amino acid sequence of FAS Protein?
      FAS Protein is composed from 179 amino acids.

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

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

    Cd95 Human His
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    Description:

    Pigment Epithelium-Derived Factor Human Recombinant, HEK

    Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    Product # :

    CYT-553

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    Description

    PEDF Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 410 amino acids, having a molecular mass of 45.6 kDa and fused to an 11 aa FLAG tag at C-Terminus.The Human PEDF is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    The filtered (0.4µm) concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
      Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
      Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
      PEDF & VEGF genes contribute to the development of diabetic retinopathy.
      PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
      PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
      SerpinF1 is a new promising approach for the treatment of osteosarcoma.
      Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
      VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
      Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
      PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.

    • Synonyms

      Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    • 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.

    • Solubility

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

    • Amino Acid Sequence

      QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGPAAADYKDDDDK.

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    Serpinf1 Human Hek
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    Description:

    Hepatitis A Virus Cellular Receptor 2 Mouse Recombinant

    Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell membrane protein 3, TIM-3, HAVCR2, TIM3, TIMD3, TIM3, KIM-3

    Product # :

    HAV-233

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    Description

    HAVCR2 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (20-193 a.a) containing 413 amino acids and having a molecular mass of 46.3kDa.HAVCR2 is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The HAVCR2 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hepatitis A Virus Cellular Receptor 2 (HAVCR2) is a member of the immunoglobulin superfamily. HACVR2 controls macrophage activation. HACVR2 inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and stimulates immunological tolerance.

    • Synonyms

      Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell membrane protein 3, TIM-3, HAVCR2, TIM3, TIMD3, TIM3, KIM-3

    • 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

      RSLENAYVFE VGKNAYLPCS YTLSTPGALV PMCWGKGFCP WSQCTNELLR TDERNVTYQK SSRYQLKGDL NKGDVSLIIK NVTLDDHGTY CCRIQFPGLM NDKKLELKLD IKAAKVTPAQ TAHGDSTTAS PRTLTTERNG SETQTLVTLH NNNGTKISTW ADEIKDSGET IRTALEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH

    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.

    Havcr2 Mouse
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    Description:

    Eukaryotic Translation Initiation Factor 4H Human Recombinant

    Eukaryotic translation initiation factor 4H, eIF-4H, Williams-Beuren syndrome chromosomal region 1 protein, EIF4H, KIAA0038, WBSCR1, WSCR1.

    Product # :

    PRO-1114

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    Description

    EIF4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a) and having a molecular mass of 29.9kDa.EIF4H is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EIF4H 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

      Eukaryotic translation initiation factor 4H (EIF4H) is a 248 amino acid protein which localizes to the perinuclear region of the cytoplasm and is expressed as 2 isoforms, termed short and long. EIF4H functions to stimulate the initiation of protein synthesis at the level of mRNA employment. EIF4H stimulates the RNA-dependent ATP hydrolysis catalyzed by EIF4A and EIF4B. EIF4H gene defects linked to Williams- Beuren syndrome (WBS), a rare developmental disorder characterized by cardiovascular and musculo-skeletal abnormalities and caused by the deletion of contiguous genes at 7q11.23.

    • Synonyms

      Eukaryotic translation initiation factor 4H, eIF-4H, Williams-Beuren syndrome chromosomal region 1 protein, EIF4H, KIAA0038, WBSCR1, WSCR1.

    • 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 MGSHMADFDT YDDRAYSSFG GGRGSRGSAG GHGSRSQKEL PTEPPYTAYV GNLPFNTVQG DIDAIFKDLS IRSVRLVRDK DTDKFKGFCY VEFDEVDSLK EALTYDGALL GDRSLRVDIA EGRKQDKGGF GFRKGGPDDR GMGSSRESRG GWDSRDDFNS
      GFRDDFLGGR GGSRPGDRRT GPPMGSRFRD GPPLRGSNMD FREPTEEERA QRPRLQLKPR TVATPLNQVA NPNSAIFGGA RPREEVVQKE QE.

    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.

    Eif4H Human
  • View Data Sheet

    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.

    More Info

    • Introduction

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

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      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:

    Egl Nine Homolog 3 Human Recombinant

    Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.

    Product # :

    PRO-1143

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    Description

    EGLN3 Human Recombinant produced in E. coli is a single polypeptide chain containing 263 amino acids (1-239) and having a molecular mass of 29.8 kDa.EGLN3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EGLN3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 300mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.

    • Synonyms

      Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.

    • 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 MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED

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    Egln3 Human
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    Description:

    CD30 Ligand Receptor Mouse Recombinant

    Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1

    Product # :

    CYT-1165

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    Description

    TNFRSF8 Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 479 amino acids (19-258 aa) and having a molecular mass of 52.2kDa.TNFRSF8 is fused to a 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF8 protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-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

      FPTDRPLKTT CAGDLSHYPG EAARNCCYQC PSGLSPTQPC PRGPAHCRKQ CAPDYYVNED GKCTACVTCL PGLVEKAPCS GNSPRICECQ PGMHCCTPAV NSCARCKLHC SGEEVVKSPG TAKKDTICEL PSSGSGPNCS NPGDRKTLTS HATPQAMPTL ESPANDSARS LLPMRVTNLV QEDATELVKV PESSSSKARE PSPDPGNAEK NMTLELPSPG TLPDISTSEN SKEPASTAST LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

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    Cd30 Mouse
  • View Data Sheet

    Name :

    EPO Rat

    Description:

    Erythropoietin Rat Recombinant

    Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142. 

    Product # :

    CYT-1187

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    • sds-page

    Description

    EPO Rat Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-192 a.a) containing 175 amino acids and having a molecular mass of 19.6 kDa. EPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    EPO protein (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

    sds-page

    More Info

    • Introduction

      Erythropoietin or EPO is a hormone (glycoprotein), part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.

    • Synonyms

      Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.

    • 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

      DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.

    • Background

      What is the molecular weight/Mw of EPO Protein?
      EPO Protein has a total Mw of 19.6kDa.

      What is the source or expression system of EPO Protein?
      HEK293 cells.

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

      What is the Biological Activity of EPO Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

      What is the amino acid sequence of EPO Protein?
      DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.

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

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

    Epo Rat
  • View Data Sheet

    Description:

    Killer Cell Lectin-Like Receptor Subfamily C, Member 3 Human Recombinant

    Killer Cell Lectin-Like Receptor Subfamily C Member 3, NK Cell Receptor E, NKG2-E Type II Integral Membrane Protein, NKG2-E-Activating NK Receptor, NKG2E.

    Product # :

    PRO-1230

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    Description

    KLRC3 Human Recombinant produced in E. coli is a single polypeptide chain containing 171 amino acids (94-240) and having a molecular mass of 19.0 kDa.KLRC3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The KLRC3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      KLRC3 belongs to the NKG2 group that can be found mostly in natural killer (NK) cells and encodes a family of transmembrane proteins known for their C-type lectin domain and their type II membrane orientation (extracellular C terminus). The NKG2 gene family is situated inside the NK complex, a region which has quite a few C-type lectin genes mostly expressed on NK cells.

    • Synonyms

      Killer Cell Lectin-Like Receptor Subfamily C Member 3, NK Cell Receptor E, NKG2-E Type II Integral Membrane Protein, NKG2-E-Activating NK Receptor, NKG2E.

    • 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 MGSMIPFLEQ NNSSPNTRTQ KARPCGHCPE EWITYSNSCY YIGKERRTWE ESLQACASKN SSSLLSIDNE EEMKFLASIL PSSWIGVFRN SSHHPWVTIN GLAFKHEIKD SDHAERNCAM LHVRGLISDQ CGSSRIIRRG FIMLTRLVLN S

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    Klrc3 Human
  • View Data Sheet

    Description:

    Killer Cell Lectin Like Receptor D1 Human Recombinant

    Killer Cell Lectin Like Receptor D1, Killer Cell Lectin-Like Receptor Subfamily D, Member 1,  NK Cell Receptor, CD94 Antigen, CD94, KP43, Killer Cell Lectin-Like Receptor Subfamily D Member 1, Natural Killer Cells Antigen CD94,  KLRD1.   

    Product # :

    PRO-2483

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    Description

    KLRD1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (32-179 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 157 amino acids and having a molecular mass of 18.2kDa.KLRD1 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLRD1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KLRD1, also known as Killer Cell Lectin Like Receptor D1, is expressed on the surface of natural killer cells in the innate immune system. KLRD1 functions as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. KLRD1 can create disulfide-bonded heterodimer with NKG2 family members. CD94 & NKG2 complex interacts with (HLA)-E, Human Leukocyte Antigen on target cells on the surface of natural killer cells.

    • Synonyms

      Killer Cell Lectin Like Receptor D1, Killer Cell Lectin-Like Receptor Subfamily D, Member 1, NK Cell Receptor, CD94 Antigen, CD94, KP43, Killer Cell Lectin-Like Receptor Subfamily D Member 1, Natural Killer Cells Antigen CD94, KLRD1.

    • 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

      ADPKNSFTKL SIEPAFTPGP NIELQKDSDC CSCQEKWVGY RCNCYFISSE QKTWNESRHL CASQKSSLLQ LQNTDELDFM SSSQQFYWIG LSYSEEHTAW LWENGSALSQ YLFPSFETFN TKNCIAYNPN GNALDESCED KNRYICKQQL IHHHHHH

    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.

    Klrd1 Human
  • View Data Sheet

    Description:

    Protein-c Receptor Human Recombinant, Sf9

    Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA.

    Product # :

    PRO-2438

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    Description

    PROCR Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 435 amino acids (18-210a.a.) and having a molecular mass of 49.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PROCR is expressed with a 242 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein-c Receptor (PROCR) is a receptor for activated protein C, a serine protease activated by and involved in the blood coagulation pathway. The PROCR protein is an N-glycosylated type I membrane protein which enhances the activation of protein C. PROCR gene mutations are linked with venous thromboembolism and myocardial infarction, as well as with late fetal loss during pregnancy. In addition, PROCR may have a role in malarial infection and has been linked with cancer.

    • Synonyms

      Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA.

    • 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

      ADPSQDASDG LQRLHMLQIS YFRDPYHVWY QGNASLGGHL THVLEGPDTN TTIIQLQPLQ EPESWARTQS GLQSYLLQFH GLVRLVHQER TLAFPLTIRC FLGCELPPEG SRAHVFFEVA VNGSSFVSFR PERALWQADT QVTSGVVTFT LQQLNAYNRT RYELREFLED TCVQYVQKHI SAENTKGSQT SRSYTSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    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.

    Procr Protein
  • View Data Sheet

    Description:

    Erythropoietin-alpha Human Recombinant, HEK

    Erythropoietin-Alpha, EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    Product # :

    CYT-083

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    Description

    EPO-a Human Recombinant produced in HEK cells is a glycosylated monomer, having a total molecular weight of 36kDa.The EPO-alpha is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The EPO-alpha was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) and is typically 0.5-2.5ng/ml, corresponding to a specific activity of 400,000-2,000,000 units/mg.

    More Info

    • Introduction

      This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

    • Synonyms

      Erythropoietin-Alpha, EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      What is the molecular weight/Mw of EPOETIN Protein?
      EPOETIN Protein has a total Mw of 36kDa.

      What is the source or expression system of EPOETIN Protein?
      HEK.

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

      What is the Biological Activity of EPOETIN Protein?
      The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) and is typically 0.5-2.5ng/ml, corresponding to a specific activity of 400,000-2,000,000 units/mg.

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

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

    Epo A Human Hek
  • View Data Sheet

    Description:

    Endothelin-3 Human Recombinant

    EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.

    Product # :

    HOR-017

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    Description

    EDN3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (26-238 a.a) and having a molecular mass of 25.2kDa.EDN3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EDN3 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by RP-HPLC.

    SDS-PAGE

    More Info

    • Introduction

      EDN3 interacts with endothelin receptor B, on the surface of cells. Throughout embryonic development, EDN3 takes part in neural crest cells that migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. EDN3 and EDN3R are necessary for the formation of nerves in the large intestine (enteric nerves) and melanocytes (produce melanin). Mutations in the EDN3 gene is linked with Waardenburg syndrome, type IV that is characterized by changes in skin, hair, and eye coloring. Mutations in the EDN3 gene is linked with Hirschsprung disease that causes severe constipation or intestinal blockage

    • Synonyms

      EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.

    • 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 MGSGDAGRRG VSQAPTAARS EGDCEETVAG PGEETVAGPG EGTVAPTALQ GPSPGSPGQE QAAEGAPEHH RSRRCTCFTY KDKECVYYCH LDIIWINTPE QTVPYGLSNY RGSFRGKRSA GPLPGNLQLS HRPHLRCACV GRYDKACLHF CTQTLDVSSN SRTAEKTDKE EEGKVEVKDQ QSKQALDLHH PKLMPGSGLA LAPSTCPRCL FQEGAP.

    • Background

      What is the molecular weight/Mw of EDN3 HUMAN Protein?
      EDN3 HUMAN Protein has a total Mw of 25.2kDa.

      What is the source or expression system of EDN3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of EDN3 HUMAN Protein?
      EDN3 HUMAN Protein is > 85% pure as determined by SDS-PAGE.

      What is the Biological Activity of EDN3 HUMAN Protein?
      The biological functionality of EDN3 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of EDN3 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSGDAGRRG VSQAPTAARS EGDCEETVAG PGEETVAGPG EGTVAPTALQ GPSPGSPGQE QAAEGAPEHH RSRRCTCFTY KDKECVYYCH LDIIWINTPE QTVPYGLSNY RGSFRGKRSA GPLPGNLQLS HRPHLRCACV GRYDKACLHF CTQTLDVSSN SRTAEKTDKE EEGKVEVKDQ QSKQALDLHH PKLMPGSGLA LAPSTCPRCL FQEGAP.

      What applications can EDN3 HUMAN Protein be used in?
      EDN3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EDN3 HUMAN Protein?
      The endotoxin level is minimal, EDN3 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant EDN3 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of EDN3 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Edn3 Human Recombinant
  • View Data Sheet

    Description:

    Fc-Epsilon RI-Alpha Human Recombinant, HEK

    FCERIA, FCERA, Fc epsilon receptor Ia, Fcepsilon RI-alpha, Fc epsilon RI alpha chain, FcERI, High affinity immunoglobulin epsilon receptor subunit alpha isoform1, IgE Fc receptor subunit alpha, FCER1A, FCE1A.

    Product # :

    PRO-2779

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    Description

    FCER1A Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 186 amino acids (26-205aa) and having a molecular mass of 21.8kDa. FCER1A is fused to a 6 His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293.

    Formulation

    FCER1A protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 0.01 ug/ml and is measured by its binding ability in a functional ELISA with Human IgE.

    More Info

    • Synonyms

      FCERIA, FCERA, Fc epsilon receptor Ia, Fcepsilon RI-alpha, Fc epsilon RI alpha chain, FcERI, High affinity immunoglobulin epsilon receptor subunit alpha isoform1, IgE Fc receptor subunit alpha, FCER1A, FCE1A.

    • 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

      VPQKPKVSLN PPWNRIFKGE NVTLTCNGNN FFEVSSTKWF HNGSLSEETN SSLNIVNAKF EDSGEYKCQH QQVNESEPVY LEVFSDWLLL QASAEVVMEG QPLFLRCHGW RNWDVYKVIY YKDGEALKYW YENHNISITN ATVEDSGTYY CTGKVWQLDY ESEPLNITVI KAPREKYWLQ HHHHHH

    • Background

      The FCER1A gene encodes the alpha subunit of the high-affinity immunoglobulin E (IgE) receptor, known as FCER1A. This receptor is primarily expressed on mast cells and basophils, and its activation plays a pivotal role in allergic and inflammatory responses. This research aims to explore the significance of FCER1A and its potential implications in allergic disorders and immune-mediated diseases. By investigating the functions and regulation of FCER1A, we can gain insights into its role in immune responses and identify potential therapeutic targets.

      The FCER1A receptor is responsible for the binding of IgE antibodies, initiating a cascade of signaling events upon allergen exposure. Crosslinking of IgE-bound FCER1A leads to the release of various inflammatory mediators, such as histamine, cytokines, and leukotrienes, which contribute to the clinical manifestations of allergic reactions. Understanding the molecular mechanisms underlying FCER1A activation and downstream signaling is crucial for comprehending allergic diseases.

      In addition to its role in allergies, FCER1A has been implicated in immune-mediated inflammatory diseases, including asthma, atopic dermatitis, and autoimmune conditions. Dysregulation of FCER1A expression and signaling pathways can lead to exaggerated immune responses and chronic inflammation. Investigating the genetic and epigenetic factors influencing FCER1A expression and the interplay between FCER1A and other immune molecules can provide valuable insights into disease pathogenesis.

      This research will delve into the molecular mechanisms governing FCER1A expression, activation, and downstream signaling pathways. The paper will explore the regulatory effects of FCER1A on mast cell and basophil activation, the release of inflammatory mediators, and the recruitment of other immune cells. Additionally, it will examine the impact of FCER1A dysregulation in allergic and immune-mediated diseases and discuss the potential of FCER1A as a therapeutic target for intervention.

      The study will also investigate the diagnostic and prognostic value of FCER1A in various allergic and immune disorders. Understanding the expression patterns and alterations of FCER1A in different diseases and patient populations may aid in disease stratification, treatment selection, and monitoring of treatment response.

      By unraveling the molecular mechanisms underlying FCER1A's functions in allergic and inflammatory responses, this research aims to contribute to our understanding of immune-mediated diseases. Furthermore, it highlights the potential of FCER1A as a target for therapeutic interventions and emphasizes the need for further investigations to develop novel treatments and improve patient outcomes.

    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.

    Fcer1A Protein
  • View Data Sheet

    Description:

    Signal Sequence Receptor Beta, Mouse Anti Human

    HSD25, TLAP, TRAP-BETA, TRAPB, Translocon-associated protein subunit beta, Signal sequence receptor subunit beta, SSR-beta.

    Product # :

    ANT-501

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    • More Info

    Formulation

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

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    • Introduction

      The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum membrane receptor related with protein translocation across the ER membrane. The SSR consists of 2 subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD glycoprotein (beta-SSR or SSR2). The human beta-signal sequence receptor gene (SSR2) maps to chromosome bands 1q21-q23. Diseases correlated with SSR2 include calcaneonavicular coalition, and osteosarcoma, and among its related super-pathways are Viral mRNA Translation and Generic Transcription Pathway.

    • Synonyms

      HSD25, TLAP, TRAP-BETA, TRAPB, Translocon-associated protein subunit beta, Signal sequence receptor subunit beta, SSR-beta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human SSR2 mAb, clone PAT31G6AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human SSR2 protein 18-149 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT31G6AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:500.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      SSR2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Ssr2 Antibody
  • View Data Sheet

    Description:

    Fc-Epsilon RI-Alpha Human Recombinant

    Fc Fragment Of IgE, High Affinity I, Receptor For; Alpha Polypeptide, FCE1A, IgE Fc Receptor Subunit Alpha, FcERI, Fc-Epsilon RI-Alpha, Fc Epsilon RI Alpha-Chain, Fc IgE Receptor, Alpha Polypeptide, High Affinity Immunoglobulin Epsilon Receptor Alpha-Subunit, High Affinity Immunoglobulin Epsilon Receptor Subunit Alpha, Immunoglobulin E Receptor, High-Affinity, Of Mast Cells, Alpha Polypeptide.

    Product # :

    PRO-1741

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    Description

    FCER1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (26-205aa) and having a molecular mass of 23.4kDa.FCER1A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FCER1A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide (FCER1A) binds to the Fc region of immunoglobulins epsilon. FCER1A is a high affinity receptor. In addition FCER1A is responsible for starting the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators such as histamine which is responsible for the manifestations of allergy. This receptor is contains of an alpha subunit, a beta subunit, and two gamma subunits. FCER1A stands for the alpha subunit. Among the diseases associated with FCER1A are mast-cell leukemia, and allergic asthma.

    • Synonyms

      Fc Fragment Of IgE, High Affinity I, Receptor For; Alpha Polypeptide, FCE1A, IgE Fc Receptor Subunit Alpha, FcERI, Fc-Epsilon RI-Alpha, Fc Epsilon RI Alpha-Chain, Fc IgE Receptor, Alpha Polypeptide, High Affinity Immunoglobulin Epsilon Receptor Alpha-Subunit, High Affinity Immunoglobulin Epsilon Receptor Subunit Alpha, Immunoglobulin E Receptor, High-Affinity, Of Mast Cells, Alpha Polypeptide.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSVPQKPKV SLNPPWNRIF KGENVTLTCN GNNFFEVSST KWFHNGSLSE ETNSSLNIVN AKFEDSGEYK CQHQQVNESE PVYLEVFSDW LLLQASAEVV MEGQPLFLRC HGWRNWDVYK VIYYKDGEAL KYWYENHNIS ITNATVEDSG TYYCTGKVWQ LDYESEPLNI TVIKAPREKY WLQ

    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.

    Fcer1A Human
  • View Data Sheet

    Description:

    Epithelial Cell Adhesion Molecule, Mouse Anti Human

    Epithelial cell adhesion molecule, Ep-CAM, Adenocarcinoma-associated antigen, Cell surface glycoprotein Trop-1, Epithelial cell surface antigen, Epithelial glycoprotein, EGP, Epithelial glycoprotein 314, EGP314, hEGP314, KS 1/4 antigen, KSA, Major gastrointestinal tumor-associated protein GA733-2, Tumor-associated calcium signal transducer 1, CD326, EPCAM, GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1, ESA, MK-1, DIAR5, EGP-2, EGP40, KS1/4, HNPCC8.

    Product # :

    ANT-525

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    • More Info

    Formulation

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

    More Info

    • Introduction

      EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.

    • Synonyms

      Epithelial cell adhesion molecule, Ep-CAM, Adenocarcinoma-associated antigen, Cell surface glycoprotein Trop-1, Epithelial cell surface antigen, Epithelial glycoprotein, EGP, Epithelial glycoprotein 314, EGP314, hEGP314, KS 1/4 antigen, KSA, Major gastrointestinal tumor-associated protein GA733-2, Tumor-associated calcium signal transducer 1, CD326, EPCAM, GA733-2, M1S2, M4S1, MIC18, TACSTD1, TROP1, ESA, MK-1, DIAR5, EGP-2, EGP40, KS1/4, HNPCC8.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human EPCAM mAb, clone PAT37F9AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human EPCAM protein 24-265 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT36F10AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:500.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      EPCAM antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Epcam Antibody
  • View Data Sheet

    Description:

    Eukaryotic Translation Initiation Factor 3K Human Recombinant

    Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.

    Product # :

    PRO-179

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    Description

    EIF3K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218a.a.) and having a molecular mass of 27.2 kDa. EIF3K is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EIF3K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF3K is a member of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a number of other subunits of eIF3 and the 40S ribosomal subunit. EIF3K is conserved among high eukaryotes, including mammals, insects, and plants, and it is universally expressed in human tissues. EIF3K is distributed both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4 (Cdk4).

    • Synonyms

      Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.

    • 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 MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS ADESGQIFIC SQEESIKPKN IVEKIDFDSV SSIMASSQ

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    Eif3K Human
  • View Data Sheet

    Description:

    Eukaryotic Translation Initiation Factor 4E-Binding Protein 3 Human Recombinant

    Eukaryotic translation initiation factor 4E-binding protein 3, 4E-BP3, eIF4E-binding protein 3, EIF4EBP3, 4EBP3.

    Product # :

    PRO-2054

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    Description

    EIF4EBP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 123 amino acids (1-100) and having a molecular mass of 13.3 kDa.EIF4EBP3 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EIF4EBP3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic Translation Initiation Factor 4E-Binding Protein 3 (EIF4EBP3) belongs to the EIF4EBP family whose proteins bind to eukaryotic initiation factor 4E and regulate its assembly into EIF4F, the multi-subunit translation initiation factor that identifies the mRNA cap structure.

    • Synonyms

      Eukaryotic translation initiation factor 4E-binding protein 3, 4E-BP3, eIF4E-binding protein 3, EIF4EBP3, 4EBP3.

    • 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 MGSMSTSTSC PIPGGRDQLP DCYSTTPGGT LYATTPGGTR IIYDRKFLLE CKNSPIARTP PCCLPQIPGV TTPPTAPLSK LEELKEQETE EEIPDDAQFE MDI.

    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.

    Eif4Ebp3 Human
  • View Data Sheet

    Description:

    Folate Receptor 1 Human Recombinant

    Folate Receptor 1 (Adult), Ovarian Tumor-Associated Antigen MOv18, Adult Folate-Binding Protein, Folate Receptor Adult , KB Cells FBP, FR-Alpha, FOLR, FBP, Folate Binding Protein, Folate Receptor Alpha, Folate Receptor 1.

    Product # :

    PRO-2162

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    Description

    FOLR1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (25-234 a.a) and having a molecular mass of 27kDa. FOLR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FOLR1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Folate Receptor 1, also known as FOLR1, is a part of the folate receptor family whose members bind folic acid. FOLR1 binds to folate and reduced folic acid derivatives and facilitates transfer of 5-methyltetrahydrofolate and folate analogs into the cells. FOLR1 is either attaches to membranes through a glycosyl-phosphatidylinositol linkage or exists in a soluble form. FOLR1 is also needed for embryonic development and normal cell proliferation.

    • Synonyms

      Folate Receptor 1 (Adult), Ovarian Tumor-Associated Antigen MOv18, Adult Folate-Binding Protein, Folate Receptor Adult , KB Cells FBP, FR-Alpha, FOLR, FBP, Folate Binding Protein, Folate Receptor Alpha, Folate Receptor 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSRIAWART ELLNVCMNAK HHKEKPGPED KLHEQCRPWR KNACCSTNTS QEAHKDVSYL YRFNWNHCGE MAPACKRHFI QDTCLYECSP NLGPWIQQVD QSWRKERVLN VPLCKEDCEQ WWEDCRTSYT CKSNWHKGWN WTSGFNKCAV GAACQPFHFY FPTPTVLCNE IWTHSYKVSN YSRGSGRCIQ MWFDPAQGNP NEEVARFYAA AMS.

    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.

    Folr1 Human
  • View Data Sheet

    Description:

    Endothelin-2 Human Recombinant

    ET2, PPET2, Endothelin-2, ET-2, Preproendothelin-2, EDN2.

    Product # :

    HOR-006

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    • SDS-PAGE

    Description

    EDN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (25-178 a.a.) and having a molecular mass of 19.9kDa. EDN2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    EDN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      Endothelin-2 is a Hypoxia-induced Autocrine Survival Factor for Breast Tumor Cells. The synthesis of EDN2 by human kidney carcinoma cells is decreased by EGF. EDN2 is a chemoattractant for macrophages and THP-1 monocytic cells. Chemotaxis towards EDN2 is via the MAPK pathway: p44 and p42 are phosphorylated when THP-1 cells are stimulated with EDN2. Migration to EDN2 is inhibited by hypoxia and by pertussis toxin. EDN2 leads to activation of macrophages. EDN2 shares a similar peptide sequence with chemokines and may signal via a similar receptor and MAPK-mediated pathway. Furthermore, EDN2 expression by tumors may modulate the behavior of macrophages such that activated cells accumulate in areas of hypoxia.

    • Synonyms

      ET2, PPET2, Endothelin-2, ET-2, Preproendothelin-2, EDN2.

    • 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 MGSQAAATLE QPASSSHAQG THLRLRRCSC SSWLDKECVY FCHLDIIWVN TPEQTAPYGL GNPPRRRRRS LPRRCQCSSA RDPACATFCL RRPWTEAGAV PSRKSPADVF QTGKTGATTG ELLQRLRDIS TVKSLFAKRQ QEAMREPRST HSRWRKR.

    • Background

      What is the molecular weight/Mw of EDN2 HUMAN Protein?
      EDN2 HUMAN Protein has a total Mw of 19.9kDa.

      What is the source or expression system of EDN2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of EDN2 HUMAN Protein?
      EDN2 HUMAN Protein is > 85% pure as determined by SDS-PAGE.

      What is the Biological Activity of EDN2 HUMAN Protein?
      The biological functionality of EDN2 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of EDN2 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSQAAATLE QPASSSHAQG THLRLRRCSC SSWLDKECVY FCHLDIIWVN TPEQTAPYGL GNPPRRRRRS LPRRCQCSSA RDPACATFCL RRPWTEAGAV PSRKSPADVF QTGKTGATTG ELLQRLRDIS TVKSLFAKRQ QEAMREPRST HSRWRKR.

      What applications can EDN2 HUMAN Protein be used in?
      EDN2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EDN2 HUMAN Protein?
      The endotoxin level is minimal, EDN2 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant EDN2 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of EDN2 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Edn2 Human His
  • View Data Sheet

    Description:

    TEK Tyrosine Kinase Endothelial Mouse Recombinant

    Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.

    Product # :

    PKA-083

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    Description

    TEK produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 730 amino acids (23-746 a.a.) and having a molecular mass of 81.6kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). TEK is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.

    • Synonyms

      Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.

    • 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

      AMDLILINSL PLVSDAETSL TCIASGWHPH EPITIGRDFE ALMNQHQDPL EVTQDVTREW AKKVVWKREK ASKINGAYFC EGRVRGQAIR IRTMKMRQQA SFLPATLTMT VDRGDNVNIS FKKVLIKEED AVIYKNGSFI HSVPRHEVPD ILEVHLPHAQ PQDAGVYSAR YIGGNLFTSA FTRLIVRRCE AQKWGPDCSR PCTTCKNNGV CHEDTGECIC PPGFMGRTCE KACEPHTFGR TCKERCSGPE GCKSYVFCLP DPYGCSCATG WRGLQCNEAC PSGYYGPDCK LRCHCTNEEI CDRFQGCLCS QGWQGLQCEK EGRPRMTPQI EDLPDHIEVN SGKFNPICKA SGWPLPTSEE MTLVKPDGTV LQPNDFNYTD RFSVAIFTVN RVLPPDSGVW VCSVNTVAGM VEKPFNISVK VLPEPLHAPN VIDTGHNFAI INISSEPYFG DGPIKSKKLF YKPVNQAWKY IEVTNEIFTL NYLEPRTDYE LCVQLARPGE GGEGHPGPVR RFTTASIGLP PPRGLSLLPK SQTALNLTWQ PIFTNSEDEF YVEVERRSLQ TTSDQQNIKV PGNLTSVLLS NLVPREQYTV RARVNTKAQG EWSEELRAWT LSDILPPQPE NIKISNITDS TAMVSWTIVD GYSISSIIIR YKVQGKNEDQ HIDVKIKNAT VTQYQLKGLE PETTYHVDIF AENNIGSSNP AFSHELRTLP HSPASADLGG GKMLHHHHHH.

    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.

    Tek Mouse
  • View Data Sheet

    Description:

    Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant

    PK1, PRK1, Prokineticin 1, EG-VEGF.

    Product # :

    CYT-338

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    • More Info

    Description

    EG-VEGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa. The EG-VEGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.

    More Info

    • Introduction

      Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.

    • Synonyms

      PK1, PRK1, Prokineticin 1, EG-VEGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF 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 Endocrine Gland Vascular Endothelial 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

      AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.

    • Background

      Title: Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant: Insights into its Role in Endocrine Disorders and Therapeutic Applications

      Abstract:


      Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a unique angiogenic factor that plays a crucial role in the development and function of endocrine glands. This research paper provides a comprehensive analysis of human recombinant EG-VEGF, focusing on its production, characterization, and potential applications in endocrine disorders. The paper highlights the significance of EG-VEGF in endocrine gland angiogenesis and explores its role in the pathogenesis of endocrine-related diseases. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EG-VEGF in endocrine disorders and related conditions. The information presented in this paper aims to enhance our understanding of human recombinant EG-VEGF and its utility as a research tool and a potential therapeutic agent.

      Introduction:


      Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a growth factor specifically expressed in endocrine tissues. Human recombinant EG-VEGF, produced through genetic engineering techniques, offers a valuable tool for studying its angiogenic properties and exploring its potential therapeutic applications in endocrine disorders.

      Production and Characterization:


      Recombinant EG-VEGF is typically generated using mammalian cell expression systems. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EG-VEGF.

      Role in Endocrine Disorders:


      EG-VEGF is involved in the regulation of endocrine gland angiogenesis, which is critical for their development, hormone secretion, and overall function. Dysregulation of EG-VEGF signaling has been implicated in various endocrine disorders, including preeclampsia, gestational trophoblastic diseases, and adrenal disorders. Recombinant EG-VEGF serves as a valuable tool for investigating the mechanisms underlying EG-VEGF-mediated angiogenesis and its potential implications in endocrine-related diseases.

      Therapeutic Implications:


      Manipulation of angiogenesis holds promise as a therapeutic approach in various endocrine disorders. Recombinant EG-VEGF offers potential therapeutic applications in promoting neovascularization and restoring endocrine gland function. Ongoing research and clinical trials are investigating the therapeutic potential of recombinant EG-VEGF in conditions such as hypopituitarism, ovarian disorders, and other endocrine-related pathologies.

      Conclusion:


      Human recombinant EG-VEGF represents a valuable research tool and a potential therapeutic agent. Its production, characterization, and applications in endocrine disorders contribute to our understanding of endocrine gland angiogenesis and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EG-VEGF offer promising avenues for improving outcomes in endocrine disorders and related conditions.

      What is the molecular weight/Mw of EG-VEGF Protein?
      EG-VEGF Protein has a total Mw of 9.7kDa.

      What is the source or expression system of EG-VEGF Protein?
      Escherichia Coli.

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

      What is the Biological Activity of EG-VEGF Protein?
      The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.

      What is the amino acid sequence of EG-VEGF Protein?
      AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.

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

      What is the endotoxin level for EG-VEGF Protein?
      The endotoxin level is minimal, EG-VEGF 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.

    Eg Vegf Human