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Search results

1000 results found for “Transforming Growth Factor”

Name

Description

Product #

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  • View Data Sheet

    Name :

    PEX19 Human

    Description:

    Peroxisomal Biogenesis Factor 19 Human Recombinant

    Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.

    Product # :

    PRO-925

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PEX19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 34.6 kDa.The PEX19 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PEX19 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEX19 is vital for peroxisome biogenesis in Saccharomyces cerevisiae. PEX19 is limited to the outer surface of peroxisomes in liver cells and is has a part in the early stage of peroxisome membrane assembly, prior to the import of matrix protein.

    • Synonyms

      Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.

    • 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 MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQC

    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.

    Pex19 Human
  • View Data Sheet

    Name :

    PRLR Human, Antagonist

    Description:

    Prolactin Receptor Antagonist Human Recombinant

    Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    Product # :

    CYT-1254

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    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
  • View Data Sheet

    Name :

    Midkine Rat

    Description:

    Midkine Rat Recombinant

    Midkine, MK, Mdk.

    Product # :

    CYT-747

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    Midkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a molecular mass of 13.2kDa.The Midkine Rat is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-100 ng/ml.

    More Info

    • Introduction

      Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
      Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
      The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
      Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
      Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
      Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

    • Synonyms

      Midkine, MK, Mdk.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      VAKKKDKVKK GSECSEWTWG PCTPSSKDCG MGFREGTCGA QTQRIHCKVP CNWKKEFGAD CKYKFESWGA CDGSTGTKAR QGTLKKARYN AQCQETIRVT KPCTSKTKSK AKAKKGKGKD.

    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.

    Midkine Rat
  • View Data Sheet

    Name :

    Leptin tA Human

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant

    Product # :

    CYT-352

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ta Human
  • View Data Sheet

    Name :

    C1QTNF2 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 2 Human Recombinant

    Complement C1q tumor necrosis factor-related protein 2, CTRP2, zacrp2.

    Product # :

    PRO-133

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • More Info

    Description

    C1QTNF2 Protein is a 29,640 Da protein containing 280 aa fused to a 10 aa N-Terminal His-tag.

    Source

    E. coli

    Formulation

    C1QTNF2 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 0.03M Acetate buffer, pH 4.

    More Info

    • Introduction

      C1QTNF2 can be found in many different organism parts such as the testis, cervix. C1QTNF2 is located in the extracellular space and has various roles such as activation of MAPK activity, positive regulation of fatty acid oxidation, positive regulation of glycogen biosynthetic process, and positive regulation of glucose import.

    • Synonyms

      Complement C1q tumor necrosis factor-related protein 2, CTRP2, zacrp2.

    • Stability

      Store lyophilized C1QTNF2 uman at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted C1QTNF2 an be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10?g/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS DPLLGAFARR DFRKGSPQLV CSLPGPQGPP GPPGAPGPSG MMGRMGFPGK DGQDGHDGDR GDSGEEGPPG DPLLGAFARR DFRKGSPQLV CSLPGPQGPP GPPGAPGPSG MMGRMGFPGK DGQDGHDGDR GDSGEEGPPG RTGNRGKPGP KGKAGAIGRA GPRGPKGVNG TPGKHGTPGK KGPKGKKGEP GLPGPCSCGS GHTKSAFSVA VTKSYPRERL PIKFDKILMN EGGHYNASSG KFVCGVPGIY YFTYDITLAN KHLAIGLVHN GQYRIRTFDA NTGNHDVASG STILALKQGD EVWLQIFYSE QNGLFYDPYW TDSLFTGFLI YADQDDPNEV.

    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.

    C1Qtnf2 Human
  • View Data Sheet

    Name :

    PEDF Human

    Description:

    Pigment Epithelium-Derived Factor Human Recombinant

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

    Product # :

    CYT-580

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    Description

    PEDF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 400 amino acids and having a molecular mass of 44.5 kDa. The Human PEDF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated (1mg/ml) protein solution was lyophilized with 20mM sodium phosphate buffer & 150mM NaCl pH-7.4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.

    • Background

      About PEDF Human

      Also known as “Pigment Epithelium-Derived Factor” or “SERPINF1,” PEDF is a
      multifunctional protein found in vertebrates. It has anti-tumorigenic, anti-angiogenic, and
      neurotrophic functions. Currently, it’s being researched as a candidate for treatment for
      several conditions, including heart disease and cancer.

      What’s the Function of PEDF Human Recombinant?

      PEDF is created/secreted in several tissues across the body. It has a unique anti-angiogenic
      action because of its induction of apoptosis in proliferating endothelial cells. Also, PEDF
      can inhibit many angiogenic factors, including VEGF and FGF-2. PEDF-R is currently the
      only known signaling receptor to be used by a serpin family member.


      What’s the Application of PEDF Human Recombinant?

      This version of PEDF is produced in E. Coli. It’s a single, non-glycosylated, polypeptide
      chain that contains 400 amino acids. It has a molecular mass of 44.5 kDa, and it’s purified
      by proprietary chromatographic techniques.

      The main purpose of PEDF human recombinant is for research. It has the potential to
      become a potential treatment for different angiogenesis-related diseases, including
      various cancers. Moreover, it can become crucial during the recovery from vasculature-
      related neurodegenerative illness.

      Such a discovery could be revolutionary for the world, which is why more research is
      needed to determine the effect of this non-inhibitory serpin on the body.

    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.

    Serpinf1 Human
  • View Data Sheet

    Name :

    IL 11 Human, Pichia

    Description:

    Interleukin-11 Human Recombinant, Pichia

    Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    Product # :

    CYT-013

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    Description

    IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    IL11 was Lyophilized from a 0.2 µm filtered concentrated solution of 20mM PB, pH7.2 and 2% Glycine buffer.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 Interleukin -11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly.

    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.

    Il 11 Human Pichia
  • View Data Sheet

    Name :

    PRDX2 Mouse

    Description:

    Eukaryotic Translation Initiation Factor 4E Mouse Recombinant

    PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.  

    Product # :

    ENZ-1061

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    Description

    PRDX2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-198 a.a) and having a molecular mass of 24.3kDa. PRDX2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PRDX2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% Glycerol 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 700 pmol/min/ug, Activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for minute. 

    More Info

    • Introduction

      PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
      If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer.

    • Synonyms

      PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.

    • 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 MGSHMASGNA QIGKSAPDFT ATAVVDGAFK EIKLSDYRGK YVVLFFYPLD FTFVCPTEII AFSDHAEDFR KLGCEVLGVS VDSQFTHLAW INTPRKEGGL GPLNIPLLAD VTKSLSQNYG VLKNDEGIAY RGLFIIDAKG VLRQITVNDL PVGRSVDEAL RLVQAFQYTD EHGEVCPAGW KPGSDTIKPN VDDSKEYFSK HN

    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.

    PRDX2 Mouse
  • View Data Sheet

    Name :

    ACVR2A Human

    Description:

    Actv Receptor Type 2A Human Recombinant

    ACVR2A, ACTRIIA, ACTR-IIA,

    Product # :

    CYT-976

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    • sds-page

    Description

    ACVR2A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 124 amino acids (20-135a.a.) and having a molecular mass of 14.4kDa (Molecular size on SDS-PAGE will appear at approximately 28kDa.ACVR2A is fused to 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACVR2A protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    sds-page

    ACVR2A Human sds-page - Product image 1

    More Info

    • Introduction

      ACVR2A takes part in various biological processes including mesoderm induction, neural cell differentiation, bone remodeling, hematopoiesis, carcinogenesis, and inflammation. ACVR2A which is a receptor for Actv A, Actv B and inhibin A mediates induction of adipogenesis by GDF6.

    • Synonyms

      ACVR2A, ACTRIIA, ACTR-IIA,

    • 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

      AILGRSETQE CLFFNANWEK DRTNQTGVEP CYGDKDKRRH CFATWKNISG SIEIVKQGCW LDDINCYDRT DCVEKKDSPE VYFCCCEGNM CNEKFSYFPE MEVTQPTSNP VTPKPPLEHH HHHH.

    • Background

      A Comprehensive Examination of the Activin Receptor Type 2A Human Recombinant: Biological Functions and Therapeutic Possibilities

      1. Abstract

      This paper delves into the complex world of Activin Receptor Type 2A Human Recombinant (ACVR2A), a crucial element of the Transforming Growth Factor-beta (TGF-beta) signaling pathway. The structure, biological implications, and signaling pathway of ACVR2A are all extensively reviewed. The potential for ACVR2A as a therapeutic target in various pathological conditions is also explored.

      2. Introduction

      The ACVR2A, a receptor protein vital to the TGF-beta signaling pathway, plays a significant role in a multitude of biological processes, including embryogenesis, cell differentiation, and homeostasis. Understanding the intricate operations of ACVR2A could open the door to innovative therapeutic strategies.

      3. Structure and Signaling of ACVR2A

      As a transmembrane serine/threonine kinase receptor, ACVR2A is characterized by a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Upon binding of specific ligands like activin, ACVR2A interacts with type I receptors to trigger phosphorylation events, leading to the activation of downstream SMAD signaling pathways.

      4. Biological Functions of ACVR2A

      ACVR2A plays a substantial role in a wide range of biological processes. These include embryonic development, cell differentiation, bone growth, immune responses, and homeostasis. Furthermore, ACVR2A is instrumental in follicle-stimulating hormone (FSH) regulation, highlighting its importance in reproduction.

      5. ACVR2A in Disease Pathology

      Impairments in ACVR2A signaling have been linked to several diseases, including various cancers and reproductive disorders. Mutations in the ACVR2A gene have been implicated in tumor progression, underscoring the receptor's role in cell proliferation and differentiation.

      6. Therapeutic Potential of ACVR2A

      The centrality of ACVR2A in critical biological processes and disease pathology suggests its therapeutic potential. By modulating ACVR2A signaling, it may be possible to intervene in diseases characterized by aberrant TGF-beta signaling. Additionally, ACVR2A antagonists are being studied for their potential in cancer treatment.

      7. Conclusion and Future Perspectives

      Our comprehension of ACVR2A's functions has substantially increased in recent years, yet much remains to be discovered. Further research into ACVR2A's precise molecular mechanisms and involvement in disease will undoubtedly yield new therapeutic strategies.

      What is the molecular weight / Mw of ACVR2A Protein?
      ACVR2A Protein has a total Mw of 14.4kDa.
      What is the source or expression system of ACVR2A Protein?
      Sf9, Baculovirus cells.

      What is the Purity of ACVR2A Protein?
      ACVR2A Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of ACVR2A Protein?
      The biological functionality of ACVR2A Protein will be determined in the future.

      What is the amino acid sequence of ACVR2A Protein?
      AILGRSETQE CLFFNANWEK DRTNQTGVEP CYGDKDKRRH CFATWKNISG SIEIVKQGCW LDDINCYDRT DCVEKKDSPE VYFCCCEGNM CNEKFSYFPE MEVTQPTSNP VTPKPPLEHH HHHH.

      What applications can ACVR2A Protein be used in?
      ACVR2A Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ACVR2A Protein?
      The endotoxin level is minimal, ACVR2A 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.

    Acvr2A Human
  • View Data Sheet

    Name :

    EEF2 Human

    Description:

    Eukaryotic Translation Elongation Factor 2 Human Recombinant

    Elongation factor 2, EF-2, EEF2, EF2, Eukaryotic Translation Elongation Factor 2, EEF-2.

    Product # :

    PRO-2076

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    Description

    EEF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (574-858) and having a molecular mass of 34.3kDa.EEF2 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EEF2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Eukaryotic Translation Elongation Factor 2 (EEF2) which is necessary factor for protein synthesis is a part of the GTP-binding translation elongation factor family. EEF2 catalyzes the GTP-dependent ribosomal translocation step during translation elongation. EEF2 is also catalyzes the coordinated movement of the mRNA as well as the 2 tRNA molecules and conformational changes in the ribosome. EF-2 kinase phosporylation inactivates the EEF2 protein.

    • Synonyms

      Elongation factor 2, EF-2, EEF2, EF2, Eukaryotic Translation Elongation Factor 2, EEF-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

      MGSSHHHHHH SSGLVPRGSH MGSDPVVSYR ETVSEESNVL CLSKSPNKHN RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW CFGPDGTGPN ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV RFDVHDVTLH ADAIHRGGGQ IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK RKGLKEGIPA LDNFLDKL.

    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.

    Eef2 Human
  • View Data Sheet

    Name :

    Leptin tA Rat

    Description:

    Leptin Antagonist Triple Mutant Rat Recombinant

    Product # :

    CYT-355

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    Description

    Leptin Antagonist Triple Mutant Rat Recombinant is a singly non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin-Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP-tA mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted 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 was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ta Rat
  • View Data Sheet

    Name :

    NDUFAF2 Human

    Description:

    NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 2 Human Recombinant

    Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.

    Product # :

    ENZ-150

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    Description

    NDUFAF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a.) and having a molecular mass of 22kDa.NDUFAF2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NDUFAF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mimitin (NDUFAF2) is a member of the complex I NDUFA12 subunit family.NADH dehydrogenase is an enzyme located in the inner mitochondrial membrane, which catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). NDUFAF2 is the "entry enzyme" of oxidative phosphorylation in the mitochondria. Mimitin protein functions as a molecular chaperone for mitochondrial complex I assembly.

    • Synonyms

      Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.

    • 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 MGWSQDLFRA LWRSLSREVK EHVGTDQFGN KYYYIPQYKN WRGQTIREKR IVEAANKKEV DYEAGDIPTE WEAWIRRTRK TPPTMEEILK NEKHREEIKI KSQDFYEKEK LLSKETSEEL LPPPVQTQIK GHASAPYFGK EEPSVAPSST GKTFQPGSWM PRDGKSHNQ.

    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.

    Ndufaf2 Human
  • View Data Sheet

    Name :

    IL 3 Human

    Description:

    Interleukin-3 Human Recombinant

    MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    Product # :

    CYT-210

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    • More Info

    Description

    Interleukin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 0.3 mg/ml of NaHCO3.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000 IU/mg.

    More Info

    • Introduction

      IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.

    • Synonyms

      MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 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 Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Met-Thr-Gln.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.84 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-3 as a Reference Standard.

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

    Il 3 Human
  • View Data Sheet

    Name :

    HHEX Human

    Description:

    Hematopoietically Expressed Homeobox Human Recombinant

    Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.

    Product # :

    PRO-1624

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    Description

    HHEX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-270) and having a molecular mass of 32.4kDa. HHEX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HHEX solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      The homeobox protein family of transcription factors has many members that take part in developmental processes such as HHEX. HHEX is known to interact with Promyelocytic leukemia protein and expression in specific hematopoietic lines indicates that this protein is involved in hematopoietic differentiation.

    • Synonyms

      Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.

    • 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 MGSMQYPHPG PAAGAVGVPL YAPTPLLQPA HPTPFYIEDI LGRGPAAPTP APTLPSPNSS FTSLVSPYRT PVYEPTPIHP AFSHHSAAAL AAAYGPGGFG GPLYPFPRTV NDYTHALLRH DPLGKPLLWS PFLQRPLHKR KGGQVRFSND QTIELEKKFE TQKYLSPPER KRLAKMLQLS ERQVKTWFQN RRAKWRRLKQ ENPQSNKKEE LESLDSSCDQ RQDLPSEQNK GASLDSSQCS PSPASQEDLE SEISEDSDQE VDIEGDKSYF NAG

    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.

    Hhex Human
  • View Data Sheet

    Name :

    MTHSFD Human

    Description:

    Methenyltetrahydrofolate Synthetase Domain Containing Human Recombinant

    Methenyltetrahydrofolate synthase domain-containing protein, Methenyltetrahydrofolate synthase domaincontaining protein, Methenyltetrahydrofolate synthase

    Product # :

    PRO-2646

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    Description

    MTHSFD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-383 a.a.) and having a molecular mass of 44.5kDa. MTHSFD is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MTHSFD solution (0.25mg/ml) contains 30% glycerol, 1mM DTT and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MTHSFD, also known as Methenyltetrahydrofolate Synthetase Domain Containing protein, is linked to Pancreas, Annular and Gastrointestinal Defects. It has also been associated with Immunodeficiency Syndrome. Some of the Gene Ontology annotations that are related to the MTHSFD gene are nucleic acid binding and nucleotide binding.

    • Synonyms

      Methenyltetrahydrofolate synthase domain-containing protein, Methenyltetrahydrofolate synthase domaincontaining protein, Methenyltetrahydrofolate synthase

    • 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 MGSMEPRAVG VSKQDIREQI WGYMESQNLA DFPRPVHHRI PNFKGASHAA EQLPRLQAFK TARTIKVNPD APQKSARFFV LESKKTLLVP TPRLRTGLFN KITPPPGATK DILRKCATSQ GVRNYSVPIG LDSRVLVDLV VVGSVAVSEK GWRIGKGEGY ADLEYAMMVS MGAVSKETPV VTIVHDCQVV DIPEELVEEH DITVDYILTP TRVIATGCKR PKPMGITWFK ISLEMMEKIP ILRSLRAREQ QAGKDVTLQG EHQHLPEPGC QQTVPLSVGR RPPDTPGPET NSMEAAPGSP PGEGAPLAAD VYVGNLPGDA RVSDLKRALR ELGSVPLRLT WQGPRRRAFL HYPDSAAAQQ AVSCLQGLRL GTDTLRVALA RQQRDK

    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.

    Mthsfd Human
  • View Data Sheet

    Name :

    BMP4 Human, Active

    Description:

    Bone Morphogenetic protein-4 Active Active, Human Recombinant

    BMP4, ZYME, BMP2B, BMP2B1.

    Product # :

    CYT-1293

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    Description

    Bone Morphogenetic protein-4 Active Human Recombinant produced in E.coli is a homodimer , non-glycosylated, polypeptide chain containing 2x116 amino acids (ser293-arg408) and having a total molecular mass of 26.2kDa. BMP4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a sterile (0.2µm) filtered solution containing 4mM HCL.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as calculated by Alkaline phosphatase activity induced in ATDC-5 cells is 157.2ng/ml corresponding to a specific activity which is 6361 units/mg.

    More Info

    • Synonyms

      BMP4, ZYME, BMP2B, BMP2B1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized BMP4 in sterile 4mM HCl at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions

    • Amino Acid Sequence

      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAI VQT LVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

    • Background

      The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily.

      The superfamily includes large families of growth and differentiation factors.

      Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.

      This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva.

      What is the molecular weight/Mw of BMP4 Protein?
      BMP4 Protein has a total Mw of 26.2kDa.

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

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

      What is the Biological Activity of BMP4 Protein?

      The ED50, as calculated by Alkaline phosphatase activity induced in ATDC-5 cells is 157.2ng/ml corresponding to a specific activity which is 6361 units/mg.

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

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

      What is the endotoxin level for BMP4 Protein?
      The endotoxin level is minimal, BMP4 Protein was purified using conventional chromatography techniques.

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

    Bmp4 Human Active
  • View Data Sheet

    Name :

    IL 6 Human

    Description:

    Interleukin-6 Human Recombinant

    B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2,Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    Product # :

    CYT-213

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    Description

    Interleukin-6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 21000 Dalton. The IL6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2um filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine 7TD1 cells is less than 0.1 ng/ml, corresponding to the specific activity of 1.0 x 10,000,000 Units per mg.

    More Info

    • Introduction

      Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.

    • Synonyms

      B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2,Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 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 Interleukin-6 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Val-Pro-Pro.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.47 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-6 as a Reference Standard.

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

    Il 6 Human
  • View Data Sheet

    Name :

    FASLG Human, HEK

    Description:

    FAS Ligand Human Recombinant, HEK

    Fas ligand (TNF superfamily, member 6), APT1LG1, FASL, TNFSF6, CD178, tumor necrosis factor (ligand) superfamily member 6, Apoptosis antigen ligand, Fas antigen ligand, APTL, CD95-L.

    Product # :

    CYT-051

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    Description

    Recombinant Human FAS Ligand produced in HEK293 cells is a polypeptide chain containing 147 amino acids (134-281a.a).FASLG is fused to a 6 amino acid His-tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The FASLG solution (0.6mg/ml) contains 1xPBS.

    Purity

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

    Biological Activity

    Fas ligand is biologically active as determined by its ability to induce cytotoxicity in Jurkat cells in the absence of any cross-linking. The expected ED50< 10 ng/ml, corresponding to a specific activity of 1x105 units/mg.

    More Info

    • Introduction

      The type II transmembrane protein FASLG is a member of the tumor necrosis factor (TNF) superfamily. A fas ligand/receptor interaction has a significant part in the regulation of the immune system and the advancement of cancer. FASLG is expressed on the activated T cell surface as a nondisulfidelinked homotrimer. FASLG binding to Fas/CD95/TNFRSF6 on a nearby cell prompts apoptosis in the Fas expressing cell. FASLG is released from the cell surface by metalloproteinases as a soluble molecule that stays trimeric and is able to bind with Fas, but its capability to activate apoptosis is radically reduced. In addition, FASLG binds to DcR3 - a soluble trap receptor with no signal transduction capabilities. Flawed Fas-mediated apoptosis causes oncogenesis in addition to drug resistance in existing tumors. Constitutive expression of FASLG in a variety of tumors enables their immune evasion. Both mouse and human FASLG are active on mouse and human cells.

    • Synonyms

      Fas ligand (TNF superfamily, member 6), APT1LG1, FASL, TNFSF6, CD178, tumor necrosis factor (ligand) superfamily member 6, Apoptosis antigen ligand, Fas antigen ligand, APTL, CD95-L.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      FASLG Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Background

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

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

      What is the Biological Activity of FASL Protein?
      Fas ligand is biologically active as determined by its ability to induce cytotoxicity in Jurkat cells in the absence of any cross-linking. The expected ED50< 10 ng/ml, corresponding to a specific activity of 1x105 units/mg.

      What is the amino acid sequence of FASL Protein?
      FASL Protein is composed from 147 amino acids.

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

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

    Faslg Human Hek
  • View Data Sheet

    Name :

    TSLP Human

    Description:

    Thymic Stromal Lymphopoietin Human Recombinant

    Thymic Stromal Lymphopoietin, TSLP.

    Product # :

    CYT-572

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    Description

    TSLP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 15 kDa.The TSLP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated solution (1mg/ml) contains 130mM NaCl, and 20mM sodium phosphate, pH 7.4.

    Purity

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

    Biological Activity

    The ED50 is determined by the ability to induce proliferation of human Interleukin-7 receptor alpha & human TSLP Receptor co-transfected with mouse BaF3 cells which was found to be less than 0.3ng/ml.

    More Info

    • Introduction

      TSLP protein is a hemopoietic cytokine which signals throughout a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor & the Interleukin-7 receptor alpha chain. TSLP impacts myeloid cells thus induces the discharge of T cell-attracting chemokines from monocytes & increases the growth of CD11c(+) dendritic cells. TSLP is mainly expressed in the heart, liver and prostate. TSLP is related in its biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the Interleukin-7 receptor alpha chain & the TSLPR. Similar to IL-7, TSLP enhances phosphorylation of STAT3 and STAT5, though uses kinases excluding JAKs for its activation. TSLP induces the release of T cell-attracting chemokines such asTARC & MDC from monocytes & triggers CD11c(+) dendritic cells. TSLP activated dendritic cells primes naive T cells to manufacture pro-allergic cytokines such as Iinterleukin-4, Interleukin-5, Interleukin-13 and TNF-alpha whereas down-regulating Interleukin-10 and IFN-gamma play a role in the initiation of allergic inflammation.

    • Synonyms

      Thymic Stromal Lymphopoietin, TSLP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MYDFTNCDFE KIKAAYLSTI SKDLITYMSG TKSTEFNNTV SCSNRPHCLT EIQSLTFNPT AGCASLAKEM FAMKTKAALA IWCPGYSETQ INATQAMKKR RKRKVTTNKC LEQVSQLQGL WRRFNRPLLK QQ.

    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.

    Tslp Human
  • View Data Sheet

    Name :

    WIF1 Mouse

    Description:

    WNT Inhibitory Factor 1 Mouse Recombinant

    Wnt inhibitory factor 1, WIF-1, Wif1.

    Product # :

    PRO-2248

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    Description

    WIF1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 359 amino acids (29-379a.a.) and having a molecular mass of 39.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).WIF1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    WIF1 protein solution (1mg/ml) contains 20mM MES (pH5.5), 1mM DTT, 1mM PMSF and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.

    • Synonyms

      Wnt inhibitory factor 1, WIF-1, Wif1.

    • 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

      GQPPEESLYL WIDAHQARVL IGFEEDILIV SEGKMAPFTH DFRKAQQRMP AIPVNIHSMN FTWQAAGQAE YFYEFLSLRS LDKGIMADPT VNVPLLGTVP HKASVVQVGF PCLGKQDGVA AFEVNVIVMN SEGNTILRTP QNAIFFKTCQ QAECPGGCRN GGFCNERRVC ECPDGFYGPH
      CEKALCIPRC MNGGLCVTPG FCICPPGFYG VNCDKANCST TCFNGGTCFY PGKCICPPGL EGEQCELSKC PQPCRNGGKC IGKSKCKCPK GYQGDLCSKP VCEPGCGAHG TCHEPNKCQC REGWHGRHCN KRYGASLMHA PRPAGAGLER HTPSLKKAED RRDPPESNYI WVEHHHHHH.

    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.

    Wif1 Mouse
  • View Data Sheet

    Name :

    Erythropoietin Human, Active

    Description:

    Erythropoietin Receptor Human Recombinant, Active

    EPO-R, EPOR, Erythropoietin Receptor.

    Product # :

    CYT-997

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    Description

    EPOR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (25-250a.a.) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPOR is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.

    More Info

    • Introduction

      Erythropoietin receptor, also known as EPOR arbitrates erythropoietin-induced erythroblast proliferation as well as differentiation. During EPO binding, EPOR activates Jak2 tyrosine kinase which activates various intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. Furthermore, stimulated EPOR has a function in erythroid cell survival. Mutations in EPOR may possibly produce erythroleukemia and familial erythrocytosis. In addition, dysregulation of EPOR can affect on the growth of selected tumors.

    • Synonyms

      EPO-R, EPOR, Erythropoietin Receptor.

    • 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

      APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.

    • Background

      What is the molecular weight/Mw of ERYTHROPOIETIN Protein?
      ERYTHROPOIETIN Protein has a total Mw of 25.6kDa.

      What is the source or expression system of ERYTHROPOIETIN Protein?
      Sf9, Baculovirus cells.

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

      What is the Biological Activity of ERYTHROPOIETIN Protein?
      Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.

      What is the amino acid sequence of ERYTHROPOIETIN Protein?
      APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.

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

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

    Epor Human Sf9
  • View Data Sheet

    Name :

    Epoetin Human, His

    Description:

    Erythropoietin-alpha Human Recombinant, His Tag

    800x600 Erythropoietin, EP, INN=Epoetin, EPO a, Erythropoietin-alpha, EPO. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    CYT-791

    Price :

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    • description
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    • More Info
    • sds-page

    Description

    800x600 EPO a Human Recombinant produced in Baculovirus is a single, glycosylated polypeptide chain containing 174 amino acids (28-193a.a.) and having a molecular mass of 19.5kDa.EPO a is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤0.5ng/ml and measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

    sds-page

    Epoetin-sds-page - Product image 1

    More Info

    • Introduction

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

    • Synonyms

      Erythropoietin, EP, INN=Epoetin, EPO a, Erythropoietin-alpha, EPO.

    • 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

      APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

    • Background

      What is the molecular weight/Mw of EPOETIN Protein?
      EPOETIN Protein has a total Mw of 19.5kDa.

      What is the source or expression system of EPOETIN Protein?
      Sf9, Baculovirus cells.

      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 ED50 range is ≤0.5ng/ml and measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

      What is the amino acid sequence of EPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.

      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 His Human
  • View Data Sheet

    Name :

    GADD45G Human

    Description:

    Growth Arrest and DNA-Damage-Inducible Gamma Human Recombinant

    DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.

    Product # :

    PRO-570

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    Description

    GADD45G Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids and having a molecular mass of 17.1 kDa.

    Source

    Escherichia Coli.

    Formulation

    The GADD45G protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GADD45G is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45G reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45G acts as a new-age tumor suppressor however is being frequently inactivated epigenetically in multiple tumors. GADD45G mRNA expression is down-regulated in hepatocellular carcinoma. GADD45G causes cell cycle arrest at G2/M transition when transfected into Hep-G2 cells. GADD45 Gamma induction by androgens involves new protein synthesis. Overexpression of GADD45 Gamma inhibits cell growth and causes morphological modifications in prostate cell lines thus GADD45 gamma takes part in differentiation induction by androgens.

    • Synonyms

      DDIT2, GADD45gamma, GADD45G, Growth arrest and DNA-damage-inducible protein GADD45 gamma, Cytokine-responsive protein CR6, DNA-damage-inducible transcript 2, DDIT-2, CR6, GRP17.

    • 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

      MTLEEVRGQD TVPESTARMQ GAGKALHELL LSAQRQGCLT AGVYESAKVL NVDPDNVTFC VLAAGEEDEG DIALQIHFTL IQAFCCENDIDIVRVGDVQR LAAIVGAGEE AGAPGDLHCI LISNPNEDAW KDPALEKLSL FCEESRSVND WVPSITLPE.

    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.

    Gadd45G Human
  • View Data Sheet

    Name :

    GRAP2 Human

    Description:

    GRB2-Related Adaptor Protein 2 Human Recombinant

    GRB2-related adaptor protein 2, GADS, GRBLG, GRID, GRBX, Grf40, Mona, Adapter protein GRID, Growth factor receptor-binding protein, Hematopoietic cell-associated adapter protein GRPL, GRB2L, P38, GRB-2-like protein, SH3-SH2-SH3 adapter Mona, GRAP-2, GRB2-related protein with insert domain, Growth Factor Receptor-bound protein 2-related adaptor protein 2, SH3-SH2-SH3 adaptor molecule, Protein GADS.

    Product # :

    PRO-081

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    Description

    GRAP2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-330.a.a) and having a molecular mass of 40.0kDa. GRAP2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GRAP2 protein solution (0.5mg/ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GRAP2 belongs to the GRB2/Sem5/Drk family. GRAP2 is an adaptor-like protein has a part in leukocyte-specific protein-tyrosine kinase signaling. Similar to related family member, GRB2-related adaptor protein contains an SH2 domain flanked by two SH3 domains and it interacts with other proteins, for example GRB2-associated binding protein 1 (GAB1) and the SLP-76 leukocyte protein (LCP2), through its SH3 domains.

    • Synonyms

      GRB2-related adaptor protein 2, GADS, GRBLG, GRID, GRBX, Grf40, Mona, Adapter protein GRID, Growth factor receptor-binding protein, Hematopoietic cell-associated adapter protein GRPL, GRB2L, P38, GRB-2-like protein, SH3-SH2-SH3 adapter Mona, GRAP-2, GRB2-related protein with insert domain, Growth Factor Receptor-bound protein 2-related adaptor protein 2, SH3-SH2-SH3 adaptor molecule, Protein GADS.

    • 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 MEAVAKFDFT ASGEDELSFH TGDVLKILSN QEEWFKAELG SQEGYVPKNF IDIQFPKWFH EGLSRHQAEN LLMGKEVGFF IIRASQSSPG DFSISVRHED DVQHFKVMRD NKGNYFLWTE KFPSLNKLVD YYRTNSISRQ KQIFLRDRTR EDQGHRGNSL DRRSQGGPHL SGAVGEEIRP SMNRKLSDHP PTLPLQQHQH QPQPPQYAPA PQQLQQPPQQ RYLQHHHFHQ ERRGGSLDIN DGHCGTGLGS EMNAALMHRR HTDPVQLQAA GRVRWARALY DFEALEDDEL GFHSGEVVEV LDSSNPSWWT GRLHNKLGLF PANYVAPMTR.

    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.

    Grap2 Human
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