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Search results

1000 results found for “Macrophage Migration Inhibitory Factor”

Name

Description

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  • View Data Sheet

    Name :

    TNFRSF25 Human

    Description:

    TNF Ligand Receptor Superfamily Member 25 Recombinant Human

    Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

    Product # :

    CYT-980

    Price :

    Quantity :

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    Shipped with Ice Packs

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    • source
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    • More Info

    Description

    TNFRSF25 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 417 amino acids (25-199) and having a molecular mass of 46.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF25 is fused to a 242 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF25 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

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

    Biological Activity

    Determined by the binding ability in a functional ELISA with Human VEGI (CAT# cyt-589). The ED50 range ≤ 5ug/ml.

    More Info

    • Introduction

      TNF Ligand Receptor Superfamily Member 25 (TNFRSF25) belongs to the TNF receptor superfamily that binds to the TNF-like protein TL1A. TNFRSF25 interacts directly with the adapter TRADD and regulates lymphocyte homeostasis. TNFRSF25 is also mediates activation of NF-kappa-B and induces apoptosis. TNFRSF25 signals are vital to exert T helper cell 2 effector activity in Th2-polarized CD4 cells and co-stimulate interleukin-13 production by glycosphingolipid-activated NKT cells.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

    • 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

      ADPQGGTRSP RCDCAGDFHK KIGLFCCRGC PAGHYLKAPC TEPCGNSTCL VCPQDTFLAW ENHHNSECAR CQACDEQASQ VALENCSAVA DTRCGCKPGW FVECQVSQCV SSSPFYCQPC LDCGALHRHT RLLCSRRDTD CGTCLPGFYE HGDGCVSCPT STLGSCPERC AAVCGWRQLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

    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.

    Tnfrsf25 Human
  • View Data Sheet

    Name :

    pro-IGF2 Human

    Description:

    Pro-Insulin Like Growth Factor-2 Human Recombinant

    Pro-Insulin Like Growth Factor-2, pro-IGF2.

    Product # :

    CYT-110

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • More Info

    Description

    Pro-IGF2 Human Recombinant produced in HEK cells is a glycosylated monomer, contains 157 a.a. (24-180) having a total molecular weight of 25kDa.The Pro-IGF2 contains a C-terminal propeptide (E peptide) Arg92 to Lys180 and is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The Pro-IGF2 was lyophilized in 50mM Sodium Acetate pH 4.5 and 350mM NaCl.

    Purity

    Greater than 90% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of MCF-7 cells (human breast cancer cell line) and is typically 2-8ng/ml.

    More Info

    • Introduction

      IGF-2 is a member of the insulin family of polypeptide growth factors that is involved in development and growth. It is an imprinted gene and is expressed only from the paternally inherited allele. It is a candidate gene for eating disorders. There is a read-through, INS-IGF2, which aligns to this gene at the 3' region and to the upstream INS gene at the 5' region. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Pro-Insulin Like Growth Factor-2, pro-IGF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pro-IGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pro-IGF2 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 Pro-IGF2 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    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.

    Pro Igf2 Human
  • View Data Sheet

    Name :

    VEGF (121 a.a.) Mouse

    Description:

    Vascular Endothelial Growth Factor (121 a.a.) Mouse Recombinant

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-574

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Vascular Endothelial Growth Factor-121 Mouse Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 28.4 kDa.Recombinant Mouse VEGF-121 is a truncated version of Murine VEGF-165.The VEGF-121 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

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

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized VEGF-121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 VEGF-121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKCDKRPR R.

    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.

    Vegf121 Mouse
  • View Data Sheet

    Name :

    G CSF Human, HEK

    Description:

    Granulocyte-Colony Stimulating Factor Human Recombinant, HEK

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    CYT-088

    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

    G-CSF Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 21-25kDa due to glycosylation.The G-CSF is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The G-CSF was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells (Mouse Myeloid Leukemia indicator cell line), the ED50 is <0.01ng/ml.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized G-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution G-CSF 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 G-CSF in sterile 1xPBS containing 0.1% endotoxin-free recombinant HSA.

    • Background

      What is the molecular weight/Mw of G CSF HUMAN, HEK Protein?
      G CSF HUMAN, HEK Protein has a total Mw of 23kDa.

      What is the source or expression system of G CSF HUMAN, HEK Protein?
      HEK.

      What is the Purity of G CSF HUMAN, HEK Protein?
      G CSF HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of G CSF HUMAN, HEK Protein?
      The specific activity was determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells (Mouse Myeloid Leukemia indicator cell line), the ED50 is <0.01ng/ml.

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

      What is the endotoxin level for G CSF HUMAN, HEK Protein?
      The endotoxin level is minimal, G CSF HUMAN, HEK 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.

    G Csf Human Hek
  • View Data Sheet

    Name :

    4 1BBL Human, His

    Description:

    4-1BB Ligand Human Recombinant, His Tag

    CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.

    Product # :

    CYT-649

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    • sds-page

    Description

    TNFSF9 Human Recombinant fused to 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (71-254 a.a.) and having a molecular mass of 23.8 kDa. The TNFSF9 37 aa His tag fusion protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Recombinant 4-1BBL solution (1mg/ml) contains 20mM Tris-HCl buffer pH-8, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE

    sds-page

    4-1BBL-His-sds-page - Product image 1

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    • Introduction

      4-1BBL is a transmembrane cytokine that is part of the tumor necrosis factor (TNF) ligand family. 4-1BBL is a bidirectional signal transducer that performs as a ligand for TNFRSF9, which is a costimulatory receptor molecule in T lymphocytes. TNFSF9 and its TNFRSF9 take part in the antigen presentation development and in the generation of cytotoxic T cells. 4-1BBR is absent from resting T lymphocytes but rapidly expressed upon antigenic stimulation. TNFSF9 reactivates anergic T lymphocytes as well as promoting T lymphocyte proliferation. 4-1BB Ligand is needed for the optimal CD8 responses in CD8 T cells. 4-1BBL is expressed in carcinoma cell lines, and is thought to be involved in T cell-tumor cell interaction. 4-1BBL is expressed by activated B cells, macrophages, dendritic cells, activated T cells, neurons and astrocytes. The interaction of 4-1BB with TNFRSF9 strongly regulates immunity and has been proposed to preferentially control T cell responses based on studies in various murin

    • Synonyms

      CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.

    • 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 KDRWGSHMRE GPELSPDDPA GLLDLRQGMF AQLVAQNVLL IDGPLSWYSD PGLAGVSLTGGLSYKEDTKE LVVAKAGVYY VFFQLELRRV VAGEGSGSVS LALHLQPLRS AAGAAALALT VDLPPASSEA RNSAFGFQGR LLHLSAGQRL GVHLHTEARA RHAWQLTQGA TVLGLFRVTP EIPAGLPSPR SE.

    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.

    4-1Bbl Protein
  • View Data Sheet

    Name :

    C1QTNF8 Human

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 8 Human Recombinant

    CTRP8, UNQ5829, C1q/TNF-related protein 8, Complement C1q tumor necrosis factor-related protein 8.

    Product # :

    PRO-134

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    Description

    C1QTNF8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 255 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 28.4kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    C1QTNF8 filtered (0.4 µm) solution in 0.03M Acetate buffer pH-4.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CTRP8, UNQ5829, C1q/TNF-related protein 8, Complement C1q tumor necrosis factor-related protein 8.

    • Physical Appearance

      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

      MKHHHHHHAS WPGLPRRPCV HCCRPAWPPG PYARVSDRDL WRGDLWRGLP RVRPTIDIEI LKGEKGEAGV RGRAGRSGKE GPPGARGLQG RRGQKGQVGP PGAACRRAYA AFSVGRRAYA AFSVGRREGL HSSDHFQAVP FDTELVNLDG AFDLAAGRFL CTVPGVYFLS LNVHTWNYKE TYLHIMLNRR PAAVLYAQPS ERSVMQAQSL MLLLAAGDAV WVRMFQRDRD NAIYGEHGDL YITFSGHLVK PAAEL.

    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.

    C1Qtnf8 Human
  • View Data Sheet

    Name :

    IL 4 Mouse

    Description:

    Interleukin-4 Mouse Recombinant

    BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

    Product # :

    CYT-282

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    Description

    Interleukin-4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13500 Dalton. The IL-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    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 the dose-dependant induction of HT-2 cell proliferation is less than 2 ng/ml corresponding to a Specific Activity of 500,000IU/mg.

    More Info

    • Introduction

      Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.

    • Synonyms

      BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 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 4 in sterile 10mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHIHGCDKNH LREIIGILNE VTGEGTPCTE MDVPNVLTAT KNTTESELVC RASKVLRIFY LKHGKTPCLK KNSSVLMELQ RLFRAFRCLD SSISCTMNES KSTSLKDFLE SLKSIMQMDY 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.

    Il 4 Mouse
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    Name :

    TGFB1 Mouse

    Description:

    Transforming Growth Factor-Beta 1 Mouse Recombinant

    Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.

    Product # :

    CYT-858

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    Description

    TGFB1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (279-390 a.a) and having a molecular mass of 15.2kDa. TGFB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TGFB1 protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions which occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins which are very similar in that each is cleaved to yield a 112 amino acid polypeptide which remains associated with the latent portion of the molecule.

    • Synonyms

      Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.

    • 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 MGSALDTNYC FSSTEKNCCV RQLYIDFRKD LGWKWIHEPK GYHANFCLGP CPYIWSLDTQ YSKVLALYNQ HNPGASASPC CVPQALEPLP IVYYVGRKPK VEQLSNMIVR SCKCS.

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    Tgfb1 Mouse
  • View Data Sheet

    Name :

    FGF4 Human

    Description:

    Fibroblast Growth Factor-4 Human Recombinant

    HBGF4, FGF-4, FGF4, KFGF, HSTF1.

    Product # :

    CYT-312

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    Description

    FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa. The FGF4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF4 protein was lyophilized with 20mM sodium phosphate and 500mM NaCl pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.

    More Info

    • Introduction

      FGF4 holds s comprehensive mitogenic and cell survival activities and takes part in a range of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF4 possess oncogenic transforming activity. FGF4 and FGF3, oncogenic growth factors are localized on chromosome 11. Co-amplification of both factors was found in several kinds of human tumors. FGF4 functions in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway.

    • Synonyms

      HBGF4, FGF-4, FGF4, KFGF, HSTF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-4 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 FGF4 Human Recombinant sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.

    • Background

      What is the molecular weight/Mw of FGF4 HUMAN Protein?
      FGF4 HUMAN Protein has a total Mw of 19.8kDa.

      What is the source or expression system of FGF4 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FGF4 HUMAN Protein?
      FGF4 HUMAN Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF4 HUMAN Protein?
      The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.

      What is the amino acid sequence of FGF4 HUMAN Protein?
      MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.

      What applications can FGF4 HUMAN Protein be used in?
      FGF4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF4 HUMAN Protein?
      The endotoxin level is minimal, FGF4 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.

    Fgf4 Human
  • View Data Sheet

    Name :

    FGF 18 Human

    Description:

    Fibroblast Growth Factor-18 Human Recombinant

    Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

    Product # :

    CYT-120

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    Description

    FGF-18 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 21.1kDa. The FGF-18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-18 protein was lyophilized from a 0.2µm filtered concentrated solution in 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 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

    More Info

    • Introduction

      Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.

    • Synonyms

      Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AEENVDFRIH VENQTRARDD VSRKQLRLYQ LYSRTSGKHI QVLGRRISAR GEDGDKYAQL LVETDTFGSQ VRIKGKETEF YLCMNRKGKL VGKPDGTSKE CVFIEKVLEN NYTALMSAKY SGWYVGFTKK GRPRKGPKTR ENQQDVHFMK RYPKGQPELQ KPFKYTTVTK RSRRIRPTHP A.

    • Background

      What is the molecular weight/Mw of FGF18 Protein?
      FGF18 Protein has a total Mw of 21.1kDa.

      What is the source or expression system of FGF18 Protein?
      Escherichia Coli.

      What is the Purity of FGF18 Protein?
      FGF18 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF18 Protein?
      The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

      What is the amino acid sequence of FGF18 Protein?
      AEENVDFRIH VENQTRARDD VSRKQLRLYQ LYSRTSGKHI QVLGRRISAR GEDGDKYAQL LVETDTFGSQ VRIKGKETEF YLCMNRKGKL VGKPDGTSKE CVFIEKVLEN NYTALMSAKY SGWYVGFTKK GRPRKGPKTR ENQQDVHFMK RYPKGQPELQ KPFKYTTVTK RSRRIRPTHP A.

      What applications can FGF18 Protein be used in?
      FGF18 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF18 Protein?
      The endotoxin level is minimal, FGF18 Protein was purified using conventional chromatography tech

    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 18 Human
  • View Data Sheet

    Name :

    EIF5A2 Human

    Description:

    Eukaryotic Translation Initiation Factor 5A2 Human Recombinant

    eIF-5A-2, EIF-5A2, eIF5AII, Eukaryotic translation initiation factor 5A-2, Eukaryotic initiation factor 5A isoform 2, EIF5A2.

    Product # :

    PRO-846

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    Description

    EIF5A2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-153 a.a.) and having a molecular mass of 18.9 kDa. The EIF5A2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EIF5A2 Human solution containing 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EIF5A2 is part of the eukaryotic initiation factor 5A subfamily, is an vital protein strongly linked to cellular polyamine homeostasis. EIF5A2 promotes the formation of the first peptide bond during the initial stage of protein synthesis. EIF5A2 is the single eukaryotic protein to have a hypusine residue, which is a post-translational modification of a lysine by the addition of a butylamino group.

    • Synonyms

      eIF-5A-2, EIF-5A2, eIF5AII, Eukaryotic translation initiation factor 5A-2, Eukaryotic initiation factor 5A isoform 2, EIF5A2.

    • 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 MADEIDFTTG DAGASSTYPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG IDIFTGKKYE DICPSTHNMD VPNIKRNDYQ LICIQDGYLS LLTETGEVRE DLKLPEGELG KEIEGKYNAG EDVQVSVMCA MSEEYAVAIK PCK.

    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.

    Eif5A2 Human
  • View Data Sheet

    Name :

    TGFA Human

    Description:

    Transforming Growth Factor-Alpha Human Recombinant

    Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.

    Product # :

    CYT-871

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    Description

    TGFA Human Recombinant (40-89) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.6kDa. The TGFA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 0.1% TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a proliferation assay using mouse BALB/c 3T3 cells, is 0.395ng/ml.

    More Info

    • Introduction

      Transforming Growth Factor-Alpha (TGF-alpha) belongs to the EGF family of cytokines. TGFA soluble form is discharged from the membrane by proteolytic cleavage. Membrane-bound proTGF-alpha is biologically active and has a role in cell-cell adhesion or in the stimulation of adjacent cells. TGFA expression is common in transformed cells. Additionally, TGFA is expressed in normal tissues during embryogenesis and in adult cells/tissues, including the pituitary, keratinocytes, and macrophages.

    • Synonyms

      Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VVSHFNDCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA.

    • Background

      Title: Transforming Growth Factor-Alpha Human Recombinant, Yeast: A Versatile Biopharmaceutical for Therapeutic Applications

      Abstract:


      Transforming Growth Factor-Alpha (TGF-α) is a potent growth factor involved in numerous physiological processes, including cell proliferation, differentiation, and tissue repair. The development of TGF-α human recombinant using yeast expression systems has provided a valuable biopharmaceutical tool for therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic applications of TGF-α human recombinant derived from yeast, highlighting its versatility and clinical significance.

      Introduction:


      TGF-α is a crucial growth factor that regulates cellular functions and plays a vital role in tissue development and repair. Harnessing the therapeutic potential of TGF-α has been limited by challenges in its production and stability. However, the development of TGF-α human recombinant using yeast expression systems has overcome these limitations, making it an attractive biopharmaceutical for therapeutic interventions.

      Production Process and Characteristics:


      TGF-α human recombinant derived from yeast is produced through recombinant DNA technology, utilizing yeast cells as expression hosts. Yeast expression systems offer several advantages, including high expression yields, cost-effectiveness, and the ability to produce correctly folded and biologically active TGF-α. The resulting TGF-α human recombinant closely resembles native TGF-α in terms of structure and function, allowing for effective therapeutic intervention.

      Therapeutic Applications:


      TGF-α human recombinant derived from yeast has shown promise in various therapeutic applications. It has been investigated for its wound-healing properties, where it promotes tissue regeneration and accelerates the healing process. Additionally, TGF-α has been explored in tissue engineering and regenerative medicine, playing a crucial role in stimulating cell proliferation and tissue development. Furthermore, TGF-α has been studied in the context of cancer research, as it is involved in tumor growth and angiogenesis, making it a potential target for anticancer therapies.

      Advantages and Challenges:


      The use of yeast expression systems for producing TGF-α human recombinant offers several advantages, including scalability, cost-effectiveness, and the ability to produce bioactive protein. However, challenges remain, such as optimizing production processes, purification methods, and ensuring product consistency and stability. Further research is needed to address these challenges and maximize the clinical potential of TGF-α human recombinant derived from yeast.

      Conclusion:


      TGF-α human recombinant derived from yeast represents a versatile biopharmaceutical tool with significant therapeutic potential. Its production using yeast expression systems offers advantages in terms of scalability, cost-effectiveness, and bioactivity. The therapeutic applications of TGF-α human recombinant extend to wound healing, tissue engineering, and cancer research. Continued research and development efforts are crucial to optimizing production processes, overcoming challenges, and fully exploiting the clinical benefits of TGF-α human recombinant as a therapeutic agent.

    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.

    Tgfa Human
  • 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 :

    IL 1 beta Human, HEK

    Description:

    Interleukin-1 beta Human Recombinant, HEK

    Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    Product # :

    CYT-094

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    Description

    Interleukin-1 beta Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 18-25kDa due to glycosylation.The IL-1 beta is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The IL-1 beta was lyophilized from 1mg/ml in 1xPBS.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells and is typically 0.02-0.08ng/ml.

    More Info

    • Introduction

      Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.

    • Synonyms

      Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-1 beta although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 beta 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 IL-1b in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

    • Amino Acid Sequence

      APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIP
      VALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFES
      AQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS.

    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 1 Beta Human Hek
  • View Data Sheet

    Name :

    CXCL2 Rat

    Description:

    GRO-beta/MIP-2 Rat Recombinant (CXCL2)

    Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta, CINC-3.

    Product # :

    CHM-372

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    Description

    GRO-Beta Rat Recombinant also called Rat MIP-2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7923 Dalton. The GRO-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 99.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.

    • Synonyms

      Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta, CINC-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Rat in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.

    • Background

      What is the molecular weight/Mw of CXCL2 RAT Protein?
      CXCL2 RAT Protein has a total Mw of 7.92kDa.

      What is the source or expression system of CXCL2 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL2 RAT Protein?
      CXCL2 RAT Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL2 RAT Protein?
      The biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

      What is the amino acid sequence of CXCL2 RAT Protein?
      VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.

      What applications can CXCL2 RAT Protein be used in?
      CXCL2 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL2 RAT Protein?
      The endotoxin level is minimal, CXCL2 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.

    Gro B Rat
  • View Data Sheet

    Name :

    IL 7 Mouse

    Description:

    Interleukin-7 Mouse Recombinant

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-372

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    Description

    Interleukin-7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4 and 2% trehalose.

    Purity

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

    Biological Activity

    The ED50was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2 ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.

    More Info

    • Introduction

      Interleukin-7 is a potent lymphoid cell growth factor produced primarily by stromal cells. IL-7 has been shown to support the proliferation and differentiation of pre B- and early T cells as well as displaying a biological effect on cells of NK and myeloid lineages.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ECHIKDKEGK AYESVLMISI DELDKMTGTD SNCPNNEPNF FRKHVCDDTK EAAFLNRAAR KLKQFLKMNI SEEFNVHLLT VSQGTQTLVN CTSKEEKNVK EQKKNDACFL KRLLREIKTC WNKILKGSI.

    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 7 Mouse
  • View Data Sheet

    Name :

    ARHGEF39 Human

    Description:

    Rho Guanine Nucleotide Exchange Factor 39 Human Recombinant

    Rho guanine nucleotide exchange factor 39, ARHGEF39, C9orf100, RP11-331F9.7.

    Product # :

    PRO-2101

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    Description

    ARHGEF39 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-335 a.a) and having a molecular mass of 40.7kDa.ARHGEF39 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARHGEF39 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Rho Guanine Nucleotide Exchange Factor 39, also known as ARHGEF39, is a protein coding gene which owns one DH (DBL-homology) domain and one PH domain. ARHGEF39 encourages cell proliferation.

    • Synonyms

      Rho guanine nucleotide exchange factor 39, ARHGEF39, C9orf100, RP11-331F9.7.

    • 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 MGSMELSCPG SRCPVQEQRA RWERKRACTA RELLETERRY QEQLGLVATY FLGILKAKGT LRPPERQALF GSWELIYGAS QELLPYLEGG CWGQGLEGFC RHLELYNQFA ANSERSQTTL QEQLKKNKGF RRFVRLQEGR PEFGGLQLQD LLPLPLQRLQ QYENLVVALA ENTGPNSPDH QQLTRAARLI SETAQRVHTI GQKQKNDQHL RRVQALLSGR QAKGLTSGRW FLRQGWLLVV PPHGEPRPRM FFLFTDVLLM AKPRPPLHLL RSGTFACKAL YPMAQCHLSR VFGHSGGPCG GLLSLSFPHE KLLLMSTDQE ELSRWYHSLT WAISSQKN.

    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.

    Arhgef39 Human
  • View Data Sheet

    Name :

    Ecotin E.Coli

    Description:

    Ecotin E.Coli Recombinant

    E. coli serine protease inhibitor.

    Product # :

    ENZ-058

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    Description

    Ecotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (21-162a.a.) and having a molecular mass of 18.3kDa.Ecotin is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Ecotin protein solution (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ecotin inhibits pancreatic serine proteases. Ecotin protein inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The power of inhibition is not linked to a specific protease specificity.

    • Synonyms

      E. coli serine protease inhibitor.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAESVQPLEK IAPYPQAEKG MKRQVIQLTP QEDESTLKVE LLIGQTLEVD CNLHRLGGKL ENKTLEGWGY DYYVFDKVSS PVSTMMACPD GKKEKKFVTA YLGDAGMLRY NSKLPIVVYT PDNVDVKYRV WKAEEKIDNA VVR

    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.

    Ecotin Ecoli
  • View Data Sheet

    Name :

    ASF1B Human

    Description:

    ASF1 Anti-Silencing Function 1 Homolog B Human Recombinant

    Histone chaperone ASF1B, Anti-silencing function protein 1 homolog B, hAsf1, hAsf1b, CCG1-interacting factor A-II, CIA-II, hCIA-II, ASF1B.

    Product # :

    PRO-1163

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    Description

    ASF1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-202 a.a) and having a molecular mass of 23.4kDa.ASF1B is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ASF1B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASF1 Anti-Silencing Function 1 Homolog B (ASF1B) belongs to the H3/H4 family of histone chaperone proteins and is similar to the anti-silencing function-1 protein in yeast. ASF1B is the substrate of the tousled-like kinase family of cell cycle-regulated kinases, and may have a crucial role in modulating the nucleosome structure of chromatin by guaranteeing a regular supply of histones at sites of nucleosome assembly. ASF1B cooperates with CAF-1 (chromatin assembly factor 1) to stimulate replication-dependent chromatin assembly. ASF1B is highly expressed in the testis and at lower levels in colon, small intestine and thymus. ASF1B is necessary for spermatogenesis.

    • Synonyms

      Histone chaperone ASF1B, Anti-silencing function protein 1 homolog B, hAsf1, hAsf1b, CCG1-interacting factor A-II, CIA-II, hCIA-II, ASF1B.

    • 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

      MAKVSVLNVA VLENPSPFHS PFRFEISFEC SEALADDLEW KIIYVGSAES EEFDQILDSV LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT YHGQEFIRVG YYVNNEYLNP ELRENPPMKP DFSQLQRNIL ASNPRVTRFH INWDNNMDRL EAIETQDPSL GCGLPLNCTP
      IKGLGLPGCI PGLLPENSMD CILEHHHHHH.

    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.

    Asf1B Human
  • View Data Sheet

    Name :

    BD 1 Rat

    Description:

    Beta Defensin -1 Rat Recombinant

    Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.

    Product # :

    CYT-062

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    Description

    BD-1 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4.1kDa.The BD-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BD-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

    More Info

    • Introduction

      The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
      Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
      Beta Defensin is highly expressed by epithelial cells.
      Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.

    • Synonyms

      Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BD-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 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 BD-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.

    • Background

      What is the molecular weight/Mw of BD1 Protein?
      BD1 Protein has a total Mw of 4.1kDa.

      What is the source or expression system of BD1 Protein?
      Escherichia Coli.

      What is the Purity of BD1 Protein?
      BD1 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD1 Protein?
      Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

      What is the amino acid sequence of BD1 Protein?
      DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.

      What applications can BD1 Protein be used in?
      BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD1 Protein?
      The endotoxin level is minimal, BD1 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.

    Bd 1 Rat
  • View Data Sheet

    Name :

    FGF12 Human

    Description:

    Fibroblast Growth Factor 12 Human Recombinant

    FGF-12, FGF12, FGF12B, FHF1, Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1, FHF-1, Myocyte-activating factor.

    Product # :

    CYT-1113

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    Description

    Fibroblast Growth Factor 12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.5kDa. The FGF12 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 1mM DTT.

    Purity

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

    Biological Activity

    Determined by FGF12 binding ability in a functional ELISA. Immobilized FGFR4/Fc Chimera at 5 µg/mL (100 µL/well) can bind FGF12 with a linear range of 1.6100 ng/mL.

    More Info

    • Introduction

      FGF12 is part of the Fibroblast Growth Factor (FGF) family which has a vast mitogenic and cell survival functions, and play a role in a range of biological activities, among them are embryonic development, cell growth, morphogenesis, tissue repair, tumor growth, and invasion. FGF-12 doesn’t obtain the N-terminal signal sequence present in the majority of the FGF family members, but it contains clusters of basic residues that act as a nuclear localization signal. When transfected into mammalian cells, FGF12 accumulated in the nucleus, but was not secreted. FGF12 is involved in nervous system development and function. FGF12 binds to IB2 (islet brain-2), a cellular kinase scaffold, and voltage gated sodium channels and is also involved in intracellular signalling and ion exchange.

    • Synonyms

      FGF-12, FGF12, FGF12B, FHF1, Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1, FHF-1, Myocyte-activating factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 12 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 Fibroblast Growth Factor 12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T.

    • Background

      What is the molecular weight/Mw of FGF12 Protein?
      FGF12 Protein has a total Mw of 20.5kDa.

      What is the source or expression system of FGF12 Protein?
      Escherichia Coli.

      What is the Purity of FGF12 Protein?
      FGF12 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF12 Protein?
      Determined by FGF12 binding ability in a functional ELISA. Immobilized FGFR4/Fc Chimera at 5 µg/mL (100 µL/well) can bind FGF12 with a linear range of 1.6100 ng/mL.

      What is the amino acid sequence of FGF12 Protein?
      MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T.

      What applications can FGF12 Protein be used in?
      FGF12 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF12 Protein?
      The endotoxin level is minimal, FGF12 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 12 Protein
  • View Data Sheet

    Name :

    IL 1 Alpha Porcine

    Description:

    Interleukin-1 Alpha Porcine Recombinant

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

    Product # :

    CYT-396

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    Description

    Interleukin-1A Porice Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 158 amino acids and having a molecular mass of 18076 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    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 the dose-dependant stimulation of D10S cells is < 0.03 ng/ml.

    More Info

    • Introduction

      Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.

    • Synonyms

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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-1 alpha 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 Ser-Ala-Thr-Tyr-Ser.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.669 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-1 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 1 Alpha Porcine
  • View Data Sheet

    Name :

    TFF2 Human, His

    Description:

    Trefoil Factor-2 Human Recombinant, His Tag

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

    Product # :

    CYT-611

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids (24-129) which includes a 10 amino acid His Tag fused at N-terminus and having a total molecular mass of 13.2 kDa. TFF2 Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5, and 20mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHAS EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.

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

    Tff2 Human His
  • View Data Sheet

    Name :

    IL 9 Mouse

    Description:

    Interleukin-9 Mouse Recombinant

    P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.

    Product # :

    CYT-373

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Interleukin-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa. The IL-9 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution 10mM Na2PO4, pH 7.5.

    Purity

    Greater than 96.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of human MO7e cells is < 0.5 ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.

    More Info

    • Introduction

      Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.

    • Synonyms

      P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 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 9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQRCSTTWGI RDTNYLIENL KDDPPSKCSC SGNVTSCLCL SVPTDDCTTP CYREGLLQLT NATQKSRLLP VFHRVKRIVE VLKNITCPSF SCEKPCNQTM AGNTMSFLKS LLGTFQKTEM QRQKSRP.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.6 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-9 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.

    Il9 Mouse
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