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Search results

1000 results found for “Hemoglobin”

Name

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  • View Data Sheet

    Name :

    TREM2 Human

    Description:

    Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant

    Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    Product # :

    PRO-1794

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    • source
    • formulation
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    • More Info

    Description

    TREM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (19-161 a.a) and having a molecular mass of 20.4kDa.TREM2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TREM2 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

    • Synonyms

      Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    • 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 KDRWGSHMHN TTVFQGVAGQ SLQVSCPYDS MKHWGRRKAW CRQLGEKGPC QRVVSTHNLW LLSFLRRWNG STAITDDTLG GTLTITLRNL QPHDAGLYQC QSLHGSEADT LRKVLVEVLA DPLDHRDAGD LWFPGESESF EDAHVEHSIS 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.

    Trem2 Human
  • View Data Sheet

    Name :

    LGALS8 Human

    Description:

    Galectin-8 Human Recombinant

    Galectin-8, Gal-8, Po66 carbohydrate-binding protein, Po66-CBP, Prostate carcinoma tumor antigen 1, PCTA-1, LGALS8.

    Product # :

    CYT-017

    Price :

    Quantity :

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    • description
    • source
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    • biological activity
    • More Info

    Description

    Galectin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 317 amino acids and having a molecular mass of 35.8kDa.The LGALS8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LGALS8 was lyophilized from a concentrated (1mg/ml) solution in 20mM 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 of Galectin-8 as determined by its ability to agglutinate human red blood cells is 0.8~4 µg/ml.

    More Info

    • Introduction

      Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Galectin-8 is a tandem-repeat-type member of the galectin family, consisting of 2 CRDs attached by a linker peptide. Galectin-8 is greatly expressed in lung carcinomas, a number of forms of prostate carcinomas, in addition to other tumor cells. Galectin-8 attaches to a subset of cell surface integrins to modulate ECM-integrin interactions. Once immobilized, Galectin-8 promotes cell adhesion by ligation and clustering of cell surface integrin receptors. On the other hand, as a soluble ligand, Galectin-8 can inhibit cell adhesion.

    • Synonyms

      Galectin-8, Gal-8, Po66 carbohydrate-binding protein, Po66-CBP, Prostate carcinoma tumor antigen 1, PCTA-1, LGALS8.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LGALS8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-8 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 Galectin-8 in sterile 18M-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-Met-Leu-Ser-Leu.

    • Background

      What is the molecular weight/Mw of LGALS8 HUMAN Protein?
      LGALS8 HUMAN Protein has a total Mw of 35.8kDa.

      What is the source or expression system of LGALS8 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS8 HUMAN Protein?
      LGALS8 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS8 HUMAN Protein?
      The ED50 of Galectin-8 as determined by its ability to agglutinate human red blood cells is 0.8~4 µg/ml.

      What is the amino acid sequence of LGALS8 HUMAN Protein?
      LGALS8 HUMAN Protein is composed from 317 amino acids.

      What applications can LGALS8 HUMAN Protein be used in?
      LGALS8 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS8 HUMAN Protein?
      The endotoxin level is minimal, LGALS8 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.

    Lgals8 Human
  • View Data Sheet

    Name :

    His Tag Antibody

    Description:

    Polyhistidine Tag, Mouse Antibody

    Product # :

    ANT-753

    Price :

    Quantity :

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    • More Info

    Description

    Monoclonal antibodies are produced by immunizing mouse with synthesized polypeptide 6 x His. This antibody was purified via protein-A affinity chromatography.

    Formulation

    1mg/ml in PBS (pH 7.4) 0.02% Sodium Azide & 10% Glycerol

    More Info

    • Introduction

      His tag peptide also called polyhistidine-tag is chain of amino acids that are attached to proteins and consist of at least six histidine (6xHis, Hexa Histidine) residues, often at the N- or C-terminus of the protein. Polyhistidine-tags are used for affinity purification of genetically engineered proteins.

    • Physical Appearance

      Sterile Filtered solution.

    • Ig Subclass

      Kappa IgG1.

    • Clone

      PAT1D6AT.

    • Applications

      ELISA and W.B. The researcher should titrate to obtain optimal results.

    • Type

      Mouse Antibody Monoclonal.

    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.

    His Tag Antibody
  • View Data Sheet

    Name :

    HPRT PAT1D9AT Antibody

    Description:

    Hypoxanthine-Guanine Phosphoribosyltransferase Clone PAT1D9AT, Mouse Anti Human

    Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.

    Product # :

    ANT-727

    Price :

    Quantity :

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    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.

    • Synonyms

      Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human HPRT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HPRT amino acids 1-218 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT1D9AT.

    • Applications

      HPRT antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

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

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

    Hprt1 Antibody
  • View Data Sheet

    Name :

    MIF Human His N

    Description:

    Macrophage Migration Inhibitory Factor Human, Recombinant His Tag N-Terminus

    Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    Product # :

    CYT-431

    Price :

    Quantity :

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    • description
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    Description

    MIF human Recombinant, fused to 40 a.a. His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques. Macrophage Inducing Factor Human Recombinant ( 1-115 a.a. ) is a single, non-glycosylated, polypeptide chain having a total amino acids of 155 and molecular mass of 17kDa.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml solution containing PBS pH-7.4.

    Purity

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

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Liquid MIF although stable 4°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.

    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.

    Mif Human His N
  • View Data Sheet

    Name :

    CCL13 Human

    Description:

    Monocyte Chemotactic Protein-4 Human Recombinant (CCL13)

    Small inducible cytokine A13, CCL13, Monocyte chemotactic protein 4, MCP-4, Monocyte chemoattractant protein 4, CK-beta-10, NCC-1, chemokine (C-C motif) ligand 13, NCC1, CKb10, SCYL1, SCYA13, MGC17134.

    Product # :

    CHM-319

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    Description

    Monocyte Chemotactic Protein-4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 75 amino acids and having a molecular mass of 8.6 kDa. The MCP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution in 20mM PB, pH 7.4, 130mM NaCl.

    Purity

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

    Biological Activity

    The specific activity as determined by the ability of MCP-4 to chemoattaract human monocytes at 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 13 (CCL13 / MCP-4) is a small cytokine belonging to the CC chemokine family. The MCP-4 gene is located on human chromosome 17 within a large cluster of other CC chemokines. MCP-4 induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. Activity of the MCP-4 chemokine has been implicated in allergic reactions such as asthma. MCP-4 can be induced by the inflammatory cytokines interleukin-1 and TNF-a.

    • Synonyms

      Small inducible cytokine A13, CCL13, Monocyte chemotactic protein 4, MCP-4, Monocyte chemoattractant protein 4, CK-beta-10, NCC-1, chemokine (C-C motif) ligand 13, NCC1, CKb10, SCYL1, SCYA13, MGC17134.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QPDALNVPSTCCFTFSSKKISLQRLKSYVITTSRCPQKAV
      IFRTKLGKEICADPKEKWVQNYMKHLGRKAHTLKT.

    • Background

      What is the molecular weight/Mw of CCL13 HUMAN Protein?
      CCL13 HUMAN Protein has a total Mw of 8.6kDa.

      What is the source or expression system of CCL13 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL13 HUMAN Protein?
      CCL13 HUMAN Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL13 HUMAN Protein?
      The specific activity as determined by the ability of MCP-4 to chemoattaract human monocytes at 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.

      What is the amino acid sequence of CCL13 HUMAN Protein?
      QPDALNVPSTCCFTFSSKKISLQRLKSYVITTSRCPQKAV
      IFRTKLGKEICADPKEKWVQNYMKHLGRKAHTLKT.

      What applications can CCL13 HUMAN Protein be used in?
      CCL13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL13 HUMAN Protein?
      The endotoxin level is minimal, CCL13 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.

    Mcp 4 Human
  • View Data Sheet

    Name :

    NME3 Human

    Description:

    Non-Metastatic Cells 3 Human Recombinant

    Protein expressed in non-metastatic cells 3, DR-nm23, Nucleoside diphosphate kinase C, NDPKC,  NDK 3, NDP kinase 3, EC 2.7.4.6, NM23H3, KIAA0516, NDPK-C, NM23-H3, c371H6.2, NDP kinase C, nucleoside diphosphate kinase 3, nm23-H3.

    Product # :

    PRO-082

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    Description

    NME3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (22-169.a.a) and having a molecular mass of 19.1kDa. NME3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NME3 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      NME3-a potential suppressor of metastasis, is expressed significantly less in highly metastatic cells than in cells with lower metastatic potential. NME3-a is vital for the synthesis of nucleoside triphosphates and has a part in apoptosis induction and hematopoiesis and is mainly expressed during early stages of myeloid differentiation of highly purified CD34+ cells.

    • Synonyms

      Protein expressed in non-metastatic cells 3, DR-nm23, Nucleoside diphosphate kinase C, NDPKC, NDK 3, NDP kinase 3, EC 2.7.4.6, NM23H3, KIAA0516, NDPK-C, NM23-H3, c371H6.2, NDP kinase C, nucleoside diphosphate kinase 3, nm23-H3.

    • 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 MERTFLAVKP DGVQRRLVGE IVRRFERKGF KLVALKLVQA SEELLREHYA ELRERPFYGR LVKYMASGPV VAMVWQGLDV VRTSRALIGA TNPADAPPGT IRGDFCIEVG KNLIHGSDSV ESARREIALW FRADELLCWE DSAGHWLYE.

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    Nme3 Human
  • View Data Sheet

    Name :

    EFNA3 Human, Sf9

    Description:

    Ephrin A3 Human Recombinant, Sf9

    Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.

    Product # :

    PRO-2614

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    Description

    EFNA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (23-214aa) and having a molecular mass of 48.7kDaEFNA3 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.

    • Synonyms

      Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPQGPGGAL GNRHAVYWNS SNQHLRREGY TVQVNVNDYL DIYCPHYNSS GVGPGAGPGP
      GGGAEQYVLY MVSRNGYRTC NASQGFKRWE CNRPHAPHSP IKFSEKFQRY SAFSLGYEFH
      AGHEYYYIST PTHNLHWKCL RMKVFVCCAS TSHSGEKPVP TLPQFTMGPN VKINVLEDFE
      GENPQVPKLE KSISGLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV
      TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY
      KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV
      EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH
      HHHH

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    Efna3 Protein
  • View Data Sheet

    Name :

    BOLA1 Human

    Description:

    BolA Homolog 1 Human Recombinant

    BolA-like protein 1, hBolA, BOLA1, CGI-143.

    Product # :

    PRO-302

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    Description

    BOLA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (21-137 a.a) and having a molecular mass of 14kDa.BOLA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BOLA1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BolA Homolog 1(BOLA1) is a member of the bolA/yrbA family. BolA proteins, which include the: hBolA1, hBolA2, and hBolA3, are novel non-classical secreted proteins detected with bioinformatics and molecular biology experiments. The 3 BolA fusion proteins with c-Myc tag can be secreted into the culture medium of the transfected Cos-7 cells, even though they could not be colocalized with Golgi apparatus. Also, the secretion of 3 BolA proteins could not be inhibited after BFA treatment.

    • Synonyms

      BolA-like protein 1, hBolA, BOLA1, CGI-143.

    • 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 MGSQGSAGSG AIGPVEAAIR TKLEEALSPE VLELRNESGG HAVPPGSETH FRVAVVSSRF EGLSPLQRHR LVHAALAEEL GGPVHALAIQ ARTPAQWREN SQLDTSPPCL GGNKKTLGTP.

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    Bola1 Human
  • View Data Sheet

    Name :

    PCNP Human

    Description:

    PEST proteolytic Signal Containing Nuclear Protein Human Recombinant

    PEST proteolytic signal-containing nuclear protein, PCNP, PEST-containing nuclear protein.

    Product # :

    PRO-906

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    Description

    PCNP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-178 a.a.) and having a molecular mass of 21.5kDa.PCNP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEST proteolytic signal containing nuclear protein (PCNP) is a nuclear protein involved in cell cycle regulation and tumorigenesis. The PCNP protein is ubiquitinated post-translationally by NIRF (an ubiquitin ligase). The PCNP exists as 3 isoforms produced by alternative splicing events.

    • Synonyms

      PEST proteolytic signal-containing nuclear protein, PCNP, PEST-containing nuclear protein.

    • 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 MGSHMADGKA GDEKPEKSQR AGAAGGPEEE AEKPVKTKTV SSSNGGESSS RSAEKRSAEE EAADLPTKPT KISKFGFAIG SQTTKKASAI SIKLGSSKPK ETVPTLAPKT LSVAAAFNED EDSEPEEMPP EAKMRMKNIG RDTPTSAGPN SFNKGKHGFS DNQKLWERNI KSHLGNVHDQ DN.

    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.

    Pcnp Human
  • View Data Sheet

    Name :

    TGIF2LX Human

    Description:

    TGFB-Induced Factor Homeobox 2-Like, X-Linked Human Recombinant

    Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked.

    Product # :

    PRO-1902

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    Description

    TGIF2LX Human Recombinant produced in E. coli is. a single polypeptide chain containing 264 amino acids (1-241) and having a molecular mass of 29.1kDa.TGIF2LX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TGIF2LX solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TGFB-Induced Factor Homeobox 2-Like, X-Linked (TGIF2LX) belongs to the TALE/TGIF homeobox family of transcription factors and takes part in spermatogenesis. A homolog of TGIF2LX is located in the male specific region of chromosome Y, in a block of sequence which is the outcome of a large X-to-Y transposition.

    • Synonyms

      Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein,
      TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked.

    • 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 MGSMEAAADG PAETQSPVEK DSPAKTQSPA QDTSIMSRNN ADTGRVLALP EHKKKRKGNL PAESVKILRD WMYKHRFKAY PSEEEKQMLS EKTNLSLLQI SNWFINARRR ILPDMLQQRR NDPIIGHKTG KDAHATHLQS TEASVPAKSG PSGPDNVQSL PLWPLPKGQM SREKQPDPES APSQKLTGIA QPKKKVKVSV TSPSSPELVS PEEHADFSSF LLLVDAAVQR AAELELEKKQ EPNP.

    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.

    Tgif2Lx Human
  • View Data Sheet

    Name :

    GNLY Human

    Description:

    Granulysin Human Recombinant

    LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    Product # :

    PRO-852

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    Description

    GNLY Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and fused to a double His Tag (N+C terminus) and having a total molecular mass of 18.1 kDa.The GNLY is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

    • Synonyms

      LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHHSSGLVPRGSHMMEGLVFSRLSPEYYD
      LARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYR
      TCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWR
      DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPS
      TGPLGSHHHHHH.

    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.

    Gnly Human
  • View Data Sheet

    Name :

    UQCRC1 Human

    Description:

    Ubiquinol-Cytochrome C Reductase Core Protein I Human Recombinant

    D3S3191, QCR1, UQCR1, Cytochrome b-c1 complex subunit 1, mitochondrial, Complex III subunit 1, Core protein I, Ubiquinol-cytochrome-c reductase complex core protein 1.

    Product # :

    PRO-1894

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    Description

    UQCRC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 471 amino acids (35-480 a.a) and having a molecular mass of 51.8kDa.UQCRC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UQCRC1protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquinol-Cytochrome C Reductase Core Protein I (UQCRC1) is a member of the peptidase M16 family,UQCRC1/QCR1 subfamily. UQCRC1 is a part of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is component of the mitochondrial respiratory chain. UQCRC1 can mediate formation of the complex between cytochromes c and c1.

    • Synonyms

      D3S3191, QCR1, UQCR1, Cytochrome b-c1 complex subunit 1, mitochondrial, Complex III subunit 1, Core protein I, Ubiquinol-cytochrome-c reductase complex core protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFTATFA QALQFVPETQ VSLLDNGLRV ASEQSSQPTC TVGVWIDVGS RFETEKNNGA GYFLEHLAFK GTKNRPGSAL EKEVESMGAH LNAYSTREHT AYYIKALSKD LPKAVELLGD IVQNCSLEDS QIEKERDVIL REMQENDASM RDVVFNYLHA TAFQGTPLAQ AVEGPSENVR KLSRADLTEY LSTHYKAPRM VLAAAGGVEH QQLLDLAQKH LGGIPWTYAE DAVPTLTPCR FTGSEIRHRD DALPFAHVAI AVEGPGWASP DNVALQVANA IIGHYDCTYG GGVHLSSPLA SGAVANKLCQ SFQTFSICYA ETGLLGAHFV CDRMKIDDMM FVLQGQWMRL CTSATESEVA RGKNILRNAL VSHLDGTTPV CEDIGRSLLT YGRRIPLAEW ESRIAEVDAS VVREICSKYI YDQCPAVAGY GPIEQLPDYN RIRSGMFWLR F.

    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.

    Uqcrc1 Human
  • View Data Sheet

    Name :

    GTSF1 Human

    Description:

    Gametocyte Specific Factor 1 Human Recombinant

    Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.

    Product # :

    PRO-561

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    Description

    GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.

    • Synonyms

      Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.

    • 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 MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.

    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.

    Gtsf1 Human
  • View Data Sheet

    Name :

    VEGI Human, His

    Description:

    Vascular Endothelial Growth InhibitorHuman Recombinant, His Tag

    Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.

    Product # :

    CYT-589

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    Description

    VEGI Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids(72-251a.a.) and having a molecular mass of 22.7kDa. The VEGI is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VEGI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50% glycerol, 1mM DTT and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.

    • 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 MLKGQEFAPS HQQVYAPLRA DGDKPRAHLT VVRQTPTQHF KNQFPALHWE HELGLAFTKN RMNYTNKFLL IPESGDYFIY SQVTFRGMTS ECSEIRQAGR PNKPDSITVV ITKVTDSYPE PTQLLMGTKS VCEVGSNWFQ PIYLGAMFSL QEGDKLMVNV SDISLVDYTK EDKTFFGAFL L

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    Vegi Human His
  • View Data Sheet

    Name :

    WWC1 Human

    Description:

    WW And C2 Domain Containing 1 Human Recombinant

    WW and C2 domain containing 1, HBEBP3, HBEBP36, KIBRA, Protein KIBRA, HBeAg-binding protein 3, Kidney and brain protein, WW domain-containing protein 1, WWC1, KIAA0869.

    Product # :

    PRO-1863

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    Description

    WWC1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 152 amino acids (655-783) and having a molecular mass of 17kDa. WWC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The WWC1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      WW and C2 Domain Containing 1 (WWC1) is a cytoplasmic phosphoprotein which interacts with PRKC-zeta and dynein light chain-1. WWC1 takes part in cognition and memory performance. In some individuals, alleles of WWC1 have enhanced memory.

    • Synonyms

      WW and C2 domain containing 1, HBEBP3, HBEBP36, KIBRA, Protein KIBRA, HBeAg-binding protein 3, Kidney and brain protein, WW domain-containing protein 1, WWC1, KIAA0869.

    • 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 MGSEAVGATR IQIALKYDEK NKQFAILIIQ LSNLSALLQQ QDQKVNIRVA VLPCSESTTC LFRTRPLDAS DTLVFNEVFW VSMSYPALHQ KTLRVDVCTT DRSHLEECLG GAQISLAEVC RSGERSTRWY NL.

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    Wwc1 Human
  • View Data Sheet

    Name :

    BMP3 Human

    Description:

    Bone Morphogenetic protein-3 Human Recombinant

    Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    Product # :

    CYT-937

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    Description

    BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

    More Info

    • Introduction

      Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.

    • Synonyms

      Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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 BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

    • Background

      Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration

      Abstract:

      Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.

      Introduction:

      Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.

      Production of BMP-3 Human Recombinant:

      Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.

      Potential Therapeutic Applications:

      BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.

      Conclusion:

      BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.

      What is the molecular weight/Mw of BMP3 Protein?
      BMP3 Protein has a total Mw of 24.8kDa.

      What is the source or expression system of BMP3 Protein?
      Escherichia Coli.

      What is the Purity of BMP3 Protein?
      BMP3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP3 Protein?
      The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

      What is the amino acid sequence of BMP3 Protein?
      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

      What applications can BMP3 Protein be used in?
      BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP3 Protein?
      The endotoxin level is minimal, BMP3 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.

    Bmp3 Human
  • View Data Sheet

    Name :

    FLRT2 Human

    Description:

    Fibronectin Leucine Rich Transmembrane Protein 2 Human Recombinant

    Leucine-rich repeat transmembrane protein FLRT2, Fibronectin-like domain-containing leucine-rich transmembrane protein 2, KIAA0405, UNQ232/PRO265.

    Product # :

    PRO-2635

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    Description

    FLRT2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 514 amino acids (36-541 a.a) and having a molecular mass of 57.5kDa.FLRT2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The FLRT2 solution (0.25mg/1ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fibronectin Leucine Rich Transmembrane Protein 2 or FLRT2 is a glycoprotein, part of the 3 FLRT glycoproteins (fibronectin, leucine rich repeat, transmembrane). This protein can be found in apparent areas of the brain and additional tissues. The genes of FLRT1 & FLRT3 extracellular domain has about 47% similarity to FLRT2. A domain of fibronectin in FLRT1, FLRT3 & FLRT2 can be bound to epidermal growth factor receptors.

    • Synonyms

      Leucine-rich repeat transmembrane protein FLRT2, Fibronectin-like domain-containing leucine-rich transmembrane protein 2, KIAA0405, UNQ232/PRO265.

    • 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

      CPSVCRCDRN FVYCNERSLT SVPLGIPEGV TVLYLHNNQI NNAGFPAELH NVQSVHTVYL YGNQLDEFPM NLPKNVRVLH LQENNIQTIS RAALAQLLKL EELHLDDNSI STVGVEDGAF REAISLKLLF LSKNHLSSVP VGLPVDLQEL RVDENRIAVI SDMAFQNLTS LERLIVDGNL LTNKGIAEGT FSHLTKLKEF SIVRNSLSHP PPDLPGTHLI RLYLQDNQIN HIPLTAFSNL RKLERLDISN NQLRMLTQGV FDNLSNLKQL TARNNPWFCD CSIKWVTEWL KYIPSSLNVR GFMCQGPEQV RGMAVRELNM NLLSCPTTTP GLPLFTPAPS TASPTTQPPT LSIPNPSRSY TPPTPTTSKL PTIPDWDGRE RVTPPISERI QLSIHFVNDT SIQVSWLSLF TVMAYKLTWV KMGHSLVGGI VQERIVSGEK QHLSLVNLEP RSTYRICLVP LDAFNYRAVE DTICSEATTH ASYLNNGSNT ASSHEQTTSH SMGSPFLEHH HHHH

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    Flrt2 Human
  • View Data Sheet

    Name :

    GLP-1 Human (31 a.a.)

    Description:

    Glucagon Like Peptide-1 (31 a.a.) Human Recombinant

    GLP1, GLP2, GRPP.

    Product # :

    HOR-236

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    Description

    Glucagon Like Peptide-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 31 amino acids and having a molecular mass of 3.3 kDa. The GLP-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Recombinant GLP-1 concentrated solution (1mg/ml) was lyophilized after extensive dialyses against 0.1mg sodium phosphate monobasic & 1.6mg sodium phosphate dibasic.

    Purity

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

    More Info

    • Introduction

      Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
      GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
      GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety.

    • Synonyms

      GLP1, GLP2, GRPP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HAEGTFTSDV SSYLEGQAAK EFIAWLVKGR G.

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    Glucagon Like Peptide 1 Human
  • View Data Sheet

    Name :

    PON1 Human, HEK

    Description:

    Paraoxonase-1 Human Recombinant, HEK

    Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5

    Product # :

    ENZ-1154

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    Description

    PON1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (16-355 a.a) containing a total of 346 amino acids, having a molecular mass of 39.0kDa. PON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The PON1 solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500 pmol/min/ug. Defined by the amount of enzyme that  hydrolyzes 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37˚C.

    More Info

    • Introduction

      Paraoxonase-1 or PON1 is part of the paraoxonase group of proteins. PON1 is an enzyme, responsible to the toxic metabolites of a different of organophosphorus insecticides hydrolyzation. Furthermore, PON1 is a dominant anti-atherosclerotic part of HDL. The enzyme needs PPAR-gamma for activation, leading to synthesis and release of paraoxonase 1 from the liver tissue, resulting in atherosclerosis reduction. PON1 has many qualities for atheroprotective through inflammatory lipid peroxides metabolism. This enzyme can hydrolyze a large number of substrates, for example cyclic carbonates, lactones, nerve gases etc.

    • Synonyms

      Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5

    • 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

      LFRNHQSSYQ TRLNALREVQ PVELPNCNLV KGIETGSEDL EILPNGLAFI SSGLKYPGIK SFNPNSPGKI LLMDLNEEDP TVLELGITGS KFDVSSFNPH GISTFTDEDN AMYLLVVNHP DAKSTVELFK FQEEEKSLLH LKTIRHKLLP NLNDIVAVGP EHFYGTNDHY FLDPYLQSWE MYLGLAWSYV VYYSPSEVRV VAEGFDFANG INISPDGKYV YIAELLAHKI HVYEKHANWT LTPLKSLDFN TLVDNISVDP ETGDLWVGCH PNGMKIFFYD SENPPASEVL RIQNILTEEP KVTQVYAENG TVLQGSTVAS VYKGKLLIGT VFHKALYCEL HHHHHH

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    Pon1 Enzyme
  • View Data Sheet

    Name :

    Streptavidin-NC

    Description:

    Streptavidin-NC Recombinant

    Product # :

    PRO-338

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    Description

    Recombinant Streptavidin-NC produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 24kDa. Streptavidin-NC is engineered to bind to nitrocellulose.

    Source

    Escherichia Coli.

    Formulation

    The sterile solution contains 10mM K2HPO4-KH2PO4, pH 7.3.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Liquid formulation.

    • Stability

      Streptavidin-NC although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.

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    Streptavidin Nc
  • View Data Sheet

    Name :

    Aprotinin Protein

    Description:

    Aprotinin

    Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.

    Product # :

    PRO-285

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    Description

    Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.

    Source

    Bovine Lung.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    More Info

    • Introduction

      Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).

    • Synonyms

      Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Specific Activity

      5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/mg.

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    Bpti
  • View Data Sheet

    Name :

    VEGF Human

    Description:

    Vascular Endothelial Growth Factor Human Recombinant

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

    Product # :

    CYT-241

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    Description

    Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38.2kDa.The VEGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 3.7-5.6 ng/ml, corresponding to a Specific Activity of 178,570-270,270IU/mg.

    More Info

    • Introduction

      Vascular endothelial growth factor (VEGF) is an important signaling protein involved in vessel formation 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 vasculogenesis and endothelial cell production, 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. VEGF is located in normal cartilage though only osteoarthritic cartilage expresses the VEGF receptors, NP1, VEGFR1 and VEGFR2. The VEGF level in the culture media from OA chondrocytes was more than 3 folds higher than in media from normal chondrocytes

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

    • Amino Acid Sequence

      APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENPCGPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR

    • Protein content

      VEGF protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.2875 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 calibrated solution of VEGF as a Reference Standard.

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    Vegf Human
  • View Data Sheet

    Name :

    Protein-A/G Cys

    Description:

    Protein A/G Cys Recombinant

    Product # :

    PRO-1928

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    • sds-page, HPLC

    Description

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

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

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

    sds-page, HPLC

    protein a/g cys hplc - Product image 1
    protein a/g cys sds-page - Product image 2

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

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

    Protein A G Cys
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