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Search results

1000 results found for “vegf receptors”

Name

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  • View Data Sheet

    Name :

    PTX3 Human

    Description:

    Pentraxin-3 Human Recombinant

    TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

    Product # :

    PRO-694

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    Description

    Recombinant Human PTX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (18-381 a.a) and having a molecular mass of 44.4 kDa. PTX3 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTX3 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.

    • Synonyms

      TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMENS DDYDLMYVNL DNEIDNGLHP TEDPTPCDCG QEHSEWDKLF IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA RPCAPGAPAE ARLTSALDEL LQATRDAGRR LARMEGAEAQ RPEEAGRALA AVLEELRQTR ADLHAVQGWA ARSWLPAGCE TAILFPMRSK KIFGSVHPVR PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL SYQSIVFVVG GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE TGGAESCHIR GNIVGWGVTE IQPHGGAQYV S.

    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.

    Ptx3 Human
  • View Data Sheet

    Name :

    CCL5 Rat

    Description:

    Rantes Rat Recombinant (CCL5)

    Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.

    Product # :

    CHM-352

    Price :

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    Description

    Rantes Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 68 amino acids and having a molecular mass of 7876 Dalton. The Rat Rantes is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a solution in 2×PBS, pH7.4.

    Purity

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

    Biological Activity

    The activity is determined by the ability to chemoattract total human lymphocytes population at a concentration between 1-10ng/ml.

    Citations

    More Info

    • Introduction

      Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

    • Synonyms

      Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Rat Rantes although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat CCL5 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 Rantes in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPYGSDTTPC CFAYLSLALP RAHVKEYFYT SSKCSNLAVV FVTRRNRQVC ANPEKKWVQE YINYLEMS.

    • Background

      What is the molecular weight/Mw of CCL5 RAT Protein?
      CCL5 RAT Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CCL5 RAT Protein?
      Escherichia Coli.

      What is the Purity of CCL5 RAT Protein?
      CCL5 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL5 RAT Protein?
      The activity is determined by the ability to chemoattract total human lymphocytes population at a concentration between 1-10ng/ml.

      What is the amino acid sequence of CCL5 RAT Protein?
      SPYGSDTTPC CFAYLSLALP RAHVKEYFYT SSKCSNLAVV FVTRRNRQVC ANPEKKWVQE YINYLEMS.

      What applications can CCL5 RAT Protein be used in?
      CCL5 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL5 RAT Protein?
      The endotoxin level is minimal, CCL5 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL5 RAT 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 CCL5 RAT?
      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.

    Rantes Rat
  • View Data Sheet

    Name :

    YWHAG Human

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant

    14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    Product # :

    PKA-238

    Price :

    Quantity :

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    • description
    • source
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    Description

    YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 247 amino acids (1-247) and having a molecular mass of 28 kDa. YWHAG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAG solution containing 20mM Tris 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

    • Synonyms

      14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    • 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

      MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN.

    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.

    Ywhag Human
  • View Data Sheet

    Name :

    Leptin Mouse (D23L)

    Description:

    Leptin D23L Mutant Mouse Recombinant

    Product # :

    CYT-1249

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
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    • More Info
    • Citations

    Description

    Leptin Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin having a molecular mass of 16 kDa and was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Mouse is able to induce proliferation of BA/F3 cells stably transfected with the long form of human leptin receptor but its affinity toward this receptor was ~ 25-fold higher compared to non-mutated mouse leptin.

    Citations

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization Mouse Leptin can be stored at 4°C for 2-3 months. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Mouse in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids is Ala-Val-Pro-Ile-Gln

    • Background

      Leptin’s main part is to regulate long-term energy balance. Leptin produced mainly by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of different cells in the human body. The leptin receptor is found on various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value was calculated by DNA man program.

    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 Mouse Mutant
  • View Data Sheet

    Name :

    AREG Human

    Description:

    Amphiregulin Human Recombinant

    Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.

    Product # :

    CYT-041

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    Description

    Amphiregulin (AREG) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.3 KDa.The AREG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

    Citations

    More Info

    • Synonyms

      Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

    • Background

      Amphiregulin Human Recombinant: Exploring its Role in Cancer Biology and Therapeutic Applications

      Abstract:


      Amphiregulin, a member of the epidermal growth factor (EGF) family, has gained significant attention in cancer research. This research paper provides an overview of Amphiregulin human recombinant, highlighting its molecular characteristics, signaling pathways, and therapeutic potential. Understanding the multifaceted role of Amphiregulin opens avenues for targeted cancer therapies. This article provides a concise analysis of Amphiregulin, emphasizing its impact on cancer biology and its therapeutic applications.

      Introduction:


      Cancer continues to be a significant health challenge worldwide, necessitating novel therapeutic approaches. Amphiregulin, an EGF family member, has emerged as a promising target in cancer research. This paper provides an overview of Amphiregulin, shedding light on its structure, function, and therapeutic potential.

      Amphiregulin Signaling and Mechanisms:


      Amphiregulin exerts its effects through the binding and activation of the EGF receptor (EGFR). Upon activation, a cascade of intracellular signaling pathways is triggered, including the MAPK and PI3K/AKT pathways. These pathways regulate critical cellular processes such as cell proliferation, survival, migration, and angiogenesis.

      Amphiregulin in Cancer Biology:


      Amphiregulin has been implicated in various aspects of cancer biology, including tumor growth, metastasis, and resistance to therapy. Its overexpression is observed in several cancer types, and its role in promoting tumor growth and metastasis has been demonstrated in preclinical studies. Targeting Amphiregulin signaling shows promise in inhibiting cancer progression and overcoming therapy resistance.

      Therapeutic Potential of Amphiregulin Human Recombinant:


      Amphiregulin human recombinant holds significant therapeutic potential in cancer treatment. Strategies aimed at blocking Amphiregulin-EGFR interactions or inhibiting downstream signaling pathways are being explored as potential therapeutic interventions. Additionally, Amphiregulin could serve as a predictive biomarker to identify patients who are more likely to respond to targeted therapies.

      Challenges and Future Directions:


      While the therapeutic targeting of Amphiregulin shows promise, several challenges need to be addressed. Further research is required to fully understand the complex interplay between Amphiregulin and other molecular pathways in cancer biology. Additionally, the development of specific and potent inhibitors and the identification of patient selection criteria are important considerations for successful clinical translation.

      Conclusion:


      Amphiregulin human recombinant represents a promising avenue for targeted cancer therapy. Understanding the molecular mechanisms and functional implications of Amphiregulin in cancer biology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve patient outcomes and contribute to the advancement of personalized medicine.

      What is the molecular weight/Mw of AREG Protein?
      AREG Protein has a total Mw of 11.3kDa.

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

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

      What is the Biological Activity of AREG Protein?
      Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

      What is the amino acid sequence of AREG Protein?
      SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

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

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

    Areg Human
  • View Data Sheet

    Name :

    EGF Long Human

    Description:

    Epidermal Growth Factor Long Human Recombinant

    Urogastrone, URG, EGF.

    Product # :

    CYT-798

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    Description

    Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa. The EGF Long is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.

    Citations

    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. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR

    • Background

      What is the molecular weight/Mw of EGF Protein?
      EGF Protein has a total Mw of 12.3kDa.

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

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

      What is the Biological Activity of EGF Protein?
      The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.

      What is the amino acid sequence of EGF Protein?
      MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR

      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 Long Human
  • View Data Sheet

    Name :

    SYT11 Human

    Description:

    Synaptotagmin XI Human Recombinant

    Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.

    Product # :

    PRO-2301

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    Description

    SYT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (37-431 a.a) and having a molecular mass of 47kDa. SYT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SYT11 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 50% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synaptotagmin-11 (SYT11) protein may be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may function as Ca2+ sensors in the process of vesicular trafficking and exocytosis.

    • Synonyms

      Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.

    • 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 MGSWSCCHQQ AEKKQKNPPY KFIHMLKGIS IYPETLSNKK KIIKVRRDKD GPGREGGRRN LLVDAAEAGL LSRDKDPRGP SSGSCIDQLP IKMDYGEELR SPITSLTPGE SKTTSPSSPE EDVMLGSLTF SVDYNFPKKA LVVTIQEAHG LPVMDDQTQG SDPYIKMTIL PDKRHRVKTR VLRKTLDPVF DETFTFYGIP YSQLQDLVLH FLVLSFDRFS RDDVIGEVMV PLAGVDPSTG KVQLTRDIIK RNIQKCISRG ELQVSLSYQP VAQRMTVVVL KARHLPKMDI TGLSGNPYVK VNVYYGRKRI AKKKTHVKKC TLNPIFNESF IYDIPTDLLP DISIEFLVID FDRTTKNEVV GRLILGAHSV TASGAEHWRE VCESPRKPVA KWHSLSEY.

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    Syt11 Human
  • View Data Sheet

    Name :

    TNFSF8 Human, Sf9

    Description:

    CD30 Ligand Human Recombinant, Sf9

    Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.

    Product # :

    CYT-954

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    Description

    TNFSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 181 amino acids (63-234a.a.) and having a molecular mass of 20.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). TNFSF8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.

    • Synonyms

      Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.

    • 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

      ADPQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSDHHHHH H.

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

    Tnfsf8 Human Sf9
  • View Data Sheet

    Name :

    CXCL7 95 a.a Human

    Description:

    Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-277

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    Description

    NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      NAP 2 is supplied as a sterile filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

    • Background

      What is the molecular weight/Mw of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CXCL7 95 A.A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL7 95 A.A HUMAN Protein?
      CXCL7 95 A.A HUMAN Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL7 95 A.A HUMAN Protein?
      The biological functionality of CXCL7 95 A.A HUMAN Protein will be determined in the future.

      What is the amino acid sequence of CXCL7 95 A.A HUMAN Protein?
      MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD

      What applications can CXCL7 95 A.A HUMAN Protein be used in?
      CXCL7 95 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL7 95 A.A HUMAN Protein?
      The endotoxin level is minimal, CXCL7 95 A.A 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.

    Nap 2 95 Aa Human
  • View Data Sheet

    Name :

    NKIRAS1 Human

    Description:

    NFKB Inhibitor Interacting Ras-Like 1 Human Recombinant

    NF-kappa-B inhibitor-interacting Ras-like protein 1, I-kappa-B-interacting Ras-like protein 1, Kappa B-Ras protein 1, KappaB-Ras1, NKIRAS1, KBRAS1.

    Product # :

    PRO-1039

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    Description

    NKIRAS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a) and having a molecular mass of 23.8kDa (Molecular weight on SDS-PAGE will appear higher).NKIRAS1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NKIRAS1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NF-kappa-B inhibitor-interacting Ras-like protein 1 (NKIRAS1) is a member of the small GTPase superfamily. NKIRAS1 is an unusual Ras-like protein which acts as a potent regulator of NF-kappa-B activity by thwarting the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, describing why NFKBIB is more resistant to degradation. NKIRAS1 functions by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB.

    • Synonyms

      NF-kappa-B inhibitor-interacting Ras-like protein 1, I-kappa-B-interacting Ras-like protein 1, Kappa B-Ras protein 1, KappaB-Ras1, NKIRAS1, KBRAS1.

    • 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 MGKGCKVVVC GLLSVGKTAI LEQLLYGNHT IGMEDCETME DVYMASVETD RGVKEQLHLY DTRGLQEGVE LPKHYFSFAD GFVLVYSVNN LESFQRVELL KKEIDKFKDK KEVAIVVLGN KIDLSEQRQV DAEVAQQWAK SEKVRLWEVT VTDRKTLIEP FTLLASKLSQ PQSKSSFPLP GRKNKGNSNS EN.

    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.

    Nkiras1 Human
  • View Data Sheet

    Name :

    EGLN3 Human

    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.

    Citations

    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
  • View Data Sheet

    Name :

    C7ORF49 Human

    Description:

    Chromosome 7 Open Reading Frame 49 Human Recombinant

    MRI, Modulator of retrovirus infection homolog, C7orf49.

    Product # :

    PRO-1415

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    Description

    C7ORF49 Human Recombinant produced in E. coli is a single polypeptide chain containing 180 amino acids (1-157) and having a molecular mass of 19.2kDa. C7ORF49 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The C7ORF49 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Chromosome 7 Open Reading Frame 49 (C7ORF49) is affiliated with the lncRNA class. C7ORF49 characterizes the hamster ortholog and suggests that it may modulate the ability of the proteasome to degrade retroviral cores upon cellular infection.

    • Synonyms

      MRI, Modulator of retrovirus infection homolog, C7orf49.

    • 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 MGSMETLQSE TKTRVLPSWL TAQVATKNVA PMKAPKRMRM AAVPVAAARL PATRTVYCMN EAEIVDVALG ILIESRKQEK ACEQPALAGA DNPEHSPPCS VSPHTSSGSS SEEEDSGKQA LAPGLSPSQR PGGSSSACSR SPEEEEEEDV LKYVREIFFS.

    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.

    C7Orf49 Human
  • View Data Sheet

    Name :

    PLGF2 Human, HEK

    Description:

    Placental Growth Factor-2, HEK Human Recombinant

    PIGF, PGF, PlGF-2, PLGF-2.

    Product # :

    CYT-1228

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    Description

    PLGF2 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-170) containing 158 amino acids and having a molecular mass of 18.1kDa. PLGF2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    PLGF2 protein (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human VEGFR1/Flt-1.

    Citations

    More Info

    • Synonyms

      PIGF, PGF, PlGF-2, PLGF-2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RRHHHHHH.

    • Background

      PLGF2, a homodimeric glycoprotein, exhibits a unique structural configuration essential for its interactions with VEGF receptors and other signaling molecules. The human recombinant form provides a controlled platform for studying the three-dimensional structure of PLGF2, elucidating its binding affinities and conformational dynamics. Understanding its structure is fundamental for deciphering how PLGF2 mediates angiogenic signaling and vascular remodeling.

    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.

    Pigf2 Human
  • View Data Sheet

    Name :

    NOV Human, HEK

    Description:

    Nephroblastoma Overexpressed Human Recombinant, HEK

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

    Product # :

    CYT-1032

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    Description

    NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 33-357) containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    NOV filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEVSDS SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH H.

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

    Nov Protein
  • View Data Sheet

    Name :

    EIF3K Human

    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.

    Citations

    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

    Name :

    SRP54 Human

    Description:

    Signal Recognition Particle 54kDa Human Recombinant

    Signal Recognition Particle 54 kDa protein

    Product # :

    PRO-113

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    Description

    SRP54 is a full-length cDNA coding for the human SRP54 protein having a molecular mass of 62kDa (pH 8.9). SRP54 protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    SRP54 is supplied in 16mM HEPES buffer pH-8.0, 320mM NaCl, 5mM DTT, 1mM EDTA, 0.16mM GDP and 20% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SRP54 is a 54-kDa subunit of the signal recognition particle (SRP), a cytoplasmic ribonucleoprotein complex which leads the translocation of newly synthesized secretory proteins from the polysome to the endoplasmic reticulum. SRP is composed of six polypeptides and a tRNA-like molecule known as 7SL RNA. SRP54 is a GTP-binding protein that directly binds the signal sequences of nascent secretory and membrane proteins. Anti-SRP autoantibodies take place in patients with an autoimmune chronic muscle inflammation called polymyositis. These auto-antibodies predominantly recognize the SRP54 subunit and in addition are able to immunoprecipitate several of the SRP subunits and the RNA component. Nearly 5% of myositis patients are positive for anti-SRP autoantibodies, increasing to 18% in the subgroup of Jo-1 autoantibody-negative patients. The classic 'anti-SRP syndrome' is a severe form of polymyositis in which the myositic inflammation is acute and aggressive onset, with common myalgias and cardiac involvement. Normally there is a poor reaction to therapy with a 5-year survival rate of about 25%.

    • Synonyms

      Signal Recognition Particle 54 kDa protein

    • 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.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.

    • coating concentration

      0.5-0.9 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with myositis sera or monoclonal anti-hexa-His-tag antibody.

    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.

    Srp54 Human
  • View Data Sheet

    Name :

    TNFA Rat, His Active

    Description:

    Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active

    Tumor Necrosis Factor-alpha, TNF a His,  Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

    Product # :

    CYT-1057

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    Description

    TNFA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235 a.a) and having a molecular mass of 19.9kDa.TNFA Rat is expressed with an 25 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFA Rat protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D.
    The ED50 for this effect is ≤ to 0.2 ng/ml.

    Citations

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.

    • Physical Appearance

      Sterile Filtered colorless liquid.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.

    • Background

      Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active: An In-Depth Analysis

      Abstract:


      Tumor Necrosis Factor-alpha (TNF-α) is a cytokine that plays a significant role in various physiological and pathological processes. This human research paper provides an in-depth analysis of TNF-α Rat Recombinant with a His Tag, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the potential applications of TNF-α Rat Recombinant in human research.

      Introduction:


      TNF-α is a key mediator of inflammation and immune responses in humans. This research paper aims to provide a comprehensive analysis of TNF-α Rat Recombinant with a His Tag, highlighting its significance in human physiology and its potential applications in human research.

      Structure and Function of TNF-α:


      TNF-α is a homotrimeric protein that binds to two distinct receptors, TNFR1 and TNFR2, initiating downstream signaling cascades. It regulates immune cell activation, cytokine production, and cellular responses, influencing diverse biological processes.

      Signaling Pathways:


      Upon binding to its receptors, TNF-α activates various signaling pathways, including the NF-κB pathway, MAPK pathway, and cell death pathways. These pathways regulate gene expression and mediate cellular responses, impacting inflammation, apoptosis, and tissue homeostasis.

      Functions of TNF-α:


      TNF-α plays a crucial role in immune responses, inflammation, and tissue homeostasis. It regulates the activation and migration of immune cells, promotes cytokine production, and modulates cell survival and death. Dysregulation of TNF-α is implicated in the pathogenesis of various human diseases, making it an attractive target for research and therapeutic interventions.

      Applications in Human Research:


      TNF-α Rat Recombinant with a His Tag has diverse applications in human research. It can be used to investigate TNF-α signaling pathways, study its effects on immune cell functions, and explore its role in disease pathogenesis. Additionally, this recombinant protein can be utilized for in vitro and in vivo studies aimed at developing novel therapeutic strategies.

      Future Directions:


      Further research is necessary to unravel the intricate mechanisms of TNF-α signaling and its contributions to human diseases. Continued investigations will enable the development of targeted therapies and personalized medicine approaches. Future studies should also focus on optimizing the use of TNF-α Rat Recombinant in preclinical and clinical research settings.

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    Tnfa Rat 2
  • View Data Sheet

    Name :

    VAT1 Human

    Description:

    Vesicle Amine Transport Protein 1 Homolog Human Recombinant

    Synaptic vesicle membrane protein VAT-1 homolog, VAT1, VATI.

    Product # :

    PRO-1011

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    Description

    VAT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-393 a.a.) and having a molecular mass of 44.1kDa. VAT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    VAT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synaptic vesicle membrane protein VAT-1 homolog (VAT1) is a member of the quinone oxidoreductase subfamily of zinc-containing alcohol dehydrogenase proteins. Synaptic vesicles are in charge of regulating the storage and release of neurotransmitters in the nerve terminal. VAT1 has an increased calcium ion-dependent expression in glioblastomas and on wounding, in basal keratinocytes. VAT1 is an abundant integral membrane protein of cholinergic synaptic vesicles and is believed to be involved in vesicular transport.

    • Synonyms

      Synaptic vesicle membrane protein VAT-1 homolog, VAT1, VATI.

    • 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 MSDEREVAEA ATGEDASSPP PKTEAASDPQ HPAASEGAAA AAASPPLLRC LVLTGFGGYD KVKLQSRPAA PPAPGPGQLT LRLRACGLNF ADLMARQGLY DRLPPLPVTP GMEGAGVVIA VGEGVSDRKA GDRVMVLNRS GMWQEEVTVP SVQTFLIPEA MTFEEAAALL VNYITAYMVL FDFGNLQPGH SVLVHMAAGG VGMAAVQLCR TVENVTVFGT ASASKHEALK ENGVTHPIDY HTTDYVDEIK KISPKGVDIV MDPLGGSDTA KGYNLLKPMG KVVTYGMANL LTGPKRNLMA LARTWWNQFS VTALQLLQAN RAVCGFHLGY LDGEVELVSG VVARLLALYN QGHIKPHIDS VWPFEKVADA MKQMQEKKNV GKVLLVPGPE KEN.

    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.

    Vat1 Human
  • View Data Sheet

    Name :

    VTN Human

    Description:

    Vitronectin Human Recombinant

    Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.

    Product # :

    PRO-2008

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    Description

    VTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 482 amino acids (20-478 a.a) and having a molecular mass of 54.7kDa. VTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.

    • Synonyms

      Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSDQESCKG RCTEGFNVDK KCQCDELCSY YQSCCTDYTA ECKPQVTRGD VFTMPEDEYT VYDDGEEKNN ATVHEQVGGP SLTSDLQAQS KGNPEQTPVL KPEEEAPAPE VGASKPEGID SRPETLHPGR PQPPAEEELC SGKPFDAFTD LKNGSLFAFR GQYCYELDEK AVRPGYPKLI RDVWGIEGPI DAAFTRINCQ GKTYLFKGSQ YWRFEDGVLD PDYPRNISDG FDGIPDNVDA ALALPAHSYS GRERVYFFKG KQYWEYQFQH QPSQEECEGS SLSAVFEHFA MMQRDSWEDI FELLFWGRTS AGTRQPQFIS RDWHGVPGQV DAAMAGRIYI SGMAPRPSLA KKQRFRHRNR KGYRSQRGHS RGRNQNSRRP SRATWLSLFS SEESNLGANN YDDYRMDWLV PATCEPIQSV FFFSGDKYYR VNLRTRRVDT VDPPYPRSIA QYWLGCPAPG HL.

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    Vtn Human
  • View Data Sheet

    Name :

    FGF 21 Rat

    Description:

    Fibroblast Growth Factor-21 Rat Recombinant

    Fibroblast growth factor 21, FGF-21.

    Product # :

    CYT-130

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    Description

    FGF 21 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The FGF 21 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 determined by a cell proliferation assay using murine NIH/3T3 cells is less than 700 ng/ml, corresponding to a specific activity of > 1.4 × 1000 IU/mg in the presence of 5µg/ml of rMuKlotho-beta.

    Citations

    More Info

    • Introduction

      The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
      FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
      FGF-19, has been shown to cause resistance to diet-induced obesity and desensitization and to improve glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
      FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.

    • Synonyms

      Fibroblast growth factor 21, FGF-21.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF 21 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF 21 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FGF 21 Rat Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AYPISDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGTAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GTLYGSPHFD PEACSFRELL LKDGYNVYQS EAHGLPLRLP QKDSQDPATR GPVRFLPMPG LPHEPQEQPG VLPPEPPDVG SSDPLSMVEP LQGRSPSYAS

    • Background

      What is the molecular weight/Mw of FGF21-RAT Protein?
      FGF21-RAT Protein has a total Mw of 19.7kDa.

      What is the source or expression system of FGF21-RAT Protein?
      Escherichia Coli.

      What is the Purity of FGF21-RAT Protein?
      FGF21-RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF21-RAT Protein?
      The ED50 determined by a cell proliferation assay using murine NIH/3T3 cells is less than 700 ng/ml, corresponding to a specific activity of > 1.4 × 1000 IU/mg in the presence of 5µg/ml of rMuKlotho-beta.

      What is the amino acid sequence of FGF21-RAT Protein?
      AYPISDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGTAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GTLYGSPHFD PEACSFRELL LKDGYNVYQS EAHGLPLRLP QKDSQDPATR GPVRFLPMPG LPHEPQEQPG VLPPEPPDVG SSDPLSMVEP LQGRSPSYAS

      What applications can FGF21-RAT Protein be used in?

      FGF21-RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF21-RAT Protein?
      The endotoxin level is minimal, FGF21-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.

    Fgf 21 Rat
  • View Data Sheet

    Name :

    TNFSF14 Mouse

    Description:

    LIGHT Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.

    Product # :

    CYT-826

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    Description

    TNFSF14 Mouse Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids and having a molecular mass of 18.4kDa.

    Source

    Escherichia Coli.

    Formulation

    TNFSF14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by a cytotoxicity assay using human HT-29 cells is less than 2µg/ml, corresponding to a specific activity of > 500 IU/mg in the presence of murine anti-polyHistidine monoclonal antibody and rHuIFN-g.

    Citations

    More Info

    • Introduction

      TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFSF14 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 TNFSF14 in sterile 100mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DGGKGSWEKL IQDQRSHQAN PAAHLTGANA SLIGIGGPLL WETRLGLAFL RGLTYHDGAL VTMEPGYYYV YSKVQLSGVG CPQGLANGLP ITHGLYKRTS RYPKELELLV SRRSPCGRAN SSRVWWDSSF LGGVVHLEAG EEVVVRVPGN RLVRPRDGTR SYFGAFMV.

    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.

    Tnfsf14 Mouse
  • View Data Sheet

    Name :

    MERTK Mouse

    Description:

    MER Proto-Oncogene Tyrosine Kinase Mouse Recombinant

    Tyrosine-protein kinase Mer, Proto-oncogene c-Mer, Receptor tyrosine kinase MerTK, Mertk, Mer.

    Product # :

    PKA-119

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    Description

    MERTK Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 718 amino acids (19-497 aa) and having a molecular mass of 79.2kDa.MERTK is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Proto-oncogene tyrosine-protein kinase MER is a protein, this enzyme is coded from the MERTK gene. This gene is a part of the TYRO3/AXL/MER receptor kinase group and encodes a transmembrane protein with two fibronectin type-III domains, two Ig-like C2-type (immunoglobulin-like) sites, and one tyrosine kinase site. Mutations in this gene have been correlated with interruption of the retinal pigment epithelium phagocytosis process and commencement of autosomal recessive retinitis pigmentosa.

    • Synonyms

      Tyrosine-protein kinase Mer, Proto-oncogene c-Mer, Receptor tyrosine kinase MerTK, Mertk, Mer.

    • 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

      GGTAEKWEET ELDQLFSGPL PGRLPVNHRP FSAPHSSRDQ LPPPQTGRSH PAHTAAPQVT
      STASKLLPPV AFNHTIGHIV LSEHKNVKFN CSINIPNTYQ ETAGISWWKD GKELLGAHHS
      ITQFYPDEEG VSIIALFSIA SVQRSDNGSY FCKMKVNNRE IVSDPIYVEV QGLPYFIKQP
      ESVNVTRNTA FNLTCQAVGP PEPVNIFWVQ NSSRVNEKPE RSPSVLTVPG LTETAVFSCE
      AHNDKGLTVS KGVHINIKVI PSPPTEVHIL NSTAHSILVS WVPGFDGYSP LQNCSIQVKE
      ADRLSNGSVM VFNTSASPHL YEIQQLQALA NYSIAVSCRN EIGWSAVSPW ILASTTEGAP
      SVAPLNITVF LNESNNILDI RWTKPPIKRQ DGELVGYRIS HVWESAGTYK ELSEEVSQNG
      SWAQIPVQIH NATCTVRIAA ITKGGIGPFS EPVNIIIPEH SKVDYAPSST PAPGNTDSM
      LEPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF
      NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT
      ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP
      PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH

    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.

    MERTK Mouse
  • View Data Sheet

    Name :

    Mouse OX40L

    Description:

    OX40 Ligand Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l

    Product # :

    CYT-1191

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    Description

    OX40L Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 157 amino acids (51-198 aa) and having a molecular mass of 17.7kDa.OX40L is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its binding ability in a functional ELISA with Human TNFRSF4 (CAT# cyt-1039).

    Citations

    More Info

    • Introduction

      OX40 Ligandis a part of the tumor necrosis factor (TNF)receptor family. OX40L receptor is OX40 which is expressed predominantly on activated CD4+ T cells.OX40 Ligandis expressed on various antigen-presenting cells such asmacrophages, DC2sand activated Blymphocytes. Expression of OX40 is momentary following engagement of T cell receptors. The ligation of OX40-OX40L stimulates proliferation anddifferentiation of activated B cells,increases immunoglobulin secretion and is also a sourceof survival signal for T cells and enables the development of memory T cells.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l

    • 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

      ADPSSSPAKD PPIQRLRGAV TRCEDGQLFI SSYKNEYQTM EVQNNSVVIK CDGLYIIYLK GSFFQEVKID LHFREDHNPI SIPMLNDGRR IVFTVVASLA FKDKVYLTVN APDTLCEHLQ INDGELIVVQ LTPGYCAPEG SYHSTVNQVP LHHHHHH

    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.

    Ox40L Mouse
  • View Data Sheet

    Name :

    MECP2 Human

    Description:

    Methyl CpG Binding Protein 2 Human Recombinant

    Methyl CpG binding protein 2 (Rett syndrome), MeCp-2 protein, AUTSX3, MRX16, MRX79, MRXS13, MRXSL, PPMX, RTT, Mental retardation, X-linked 16, DKFZp686A24160.

    Product # :

    PRO-212

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    Description

    MECP2 Human Recombinant is expressed in 293 cells. The protein contains 486 amino acids (1-486a.a.) and fused to an N-terminal Flag tag, having an Mw of 53.56kDa.

    Source

    Mammalian system, 293 cells.

    Formulation

    The MECP2 solution (0.45mg/ml) contains 50mM Tris, 135mM NaCl, 20% Glycerol, pH 7.5 and 200µg/ml FLAG peptide.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MECP2 is the key modificator of eukaryotic genomes and has a crucial part in mammalian development.
      Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 form a family of nuclear proteins linked by the existence in each of a methyl-CpG binding domain (MBD). Each one of these proteins, with the exception of MBD3, can bind specifically to methylated DNA. In addition, MECP2, MBD1 and MBD2 can inhibit transcription from methylated gene promoters. Unlike other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is expendable in stem cells, but is vital for embryonic development. MECP2 gene mutations are the cause of most cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common reasons of mental retardation in females.

    • Synonyms

      Methyl CpG binding protein 2 (Rett syndrome), MeCp-2 protein, AUTSX3, MRX16, MRX79, MRXS13, MRXSL, PPMX, RTT, Mental retardation, X-linked 16, DKFZp686A24160.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      MECP2 although stable 4°C for 4 weeks, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MDYKDDDDKMVAGMLGLREEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSA
      EPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAG
      KYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGT
      GRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMV
      IKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIE
      VKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESPKAPVP
      LLPPLPPPPPEPESSEDPTSPPEPQDLSSSVCKEEKMPRGGSLESDGCPKEPAKTQPAVATAATAA
      EKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS.

    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.

    Mecp2 Human
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