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Search results

1000 results found for “pleiotrophin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Leptin qA Human

    Description:

    Leptin Antagonist Quadruple Mutant Human Recombinant

    Product # :

    CYT-353

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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

    Description

    Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.Leptin Antagonist Quadruple Mutant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.89 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Qa 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

    Price :

    Quantity :

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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 :

    EFNA3 Human

    Description:

    Ephrin A3 Human Recombinant

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

    Product # :

    PRO-1460

    Price :

    Quantity :

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    • More Info

    Description

    EFNA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (23-214 a.a) and having a molecular mass of 24kDa. EFNA3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    EFNA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% 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

      MGSSHHHHHH SSGLVPRGSH MGSHMQGPGG ALGNRHAVYW NSSNQHLRRE GYTVQVNVND YLDIYCPHYN SSGVGPGAGP GPGGGAEQYV LYMVSRNGYR TCNASQGFKR WECNRPHAPH SPIKFSEKFQ RYSAFSLGYE FHAGHEYYYI STPTHNLHWK CLRMKVFVCC ASTSHSGEKP VPTLPQFTMG PNVKINVLED FEGENPQVPK LEKSISG

    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.

    Efna3 Human
  • View Data Sheet

    Name :

    Leptin Chicken

    Description:

    Leptin Chicken Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-505

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity is however 5-10 fold lower as compared to mammalian leptins.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

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

      Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 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 calibrated solution of Leptin Chicken 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.

    Leptin Chicken
  • View Data Sheet

    Name :

    PDGFRB Human

    Description:

    Platelet-Derived Growth Factor Receptor, Beta Human Recombinant

    Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b AntigenNDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,Platelet-Derived Growth Factor Receptor Beta.

    Product # :

    CYT-1051

    Price :

    Quantity :

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    • description
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    Description

    PDGFRB produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 739 amino acids (33-532a.a.) and having a molecular mass of 83.3kDa (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).PDGFRB is expressed with an 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet-derived growth factor receptor beta (PDGFRB), belongs to the class III subfamily of receptor tyrosine kinases (RTK) which also consist of the receptors for Flt3-ligand, SCF and M-CSF. PDGFRB takes a vital part in blood vessel development by promoting growth, migration as well as recruitment of pericytes and smooth muscle cells to endothelial cells. PDGFRB helps in rearrangement of the actin cytoskeleton in addition the formation of membrane ruffles. PDGFRB phosphorylates, NCK1, PIK3R1, PTPN11, CBL, SHC1, RASA1/GAP and PLCG1.

    • Synonyms

      Platelet-derived growth factor receptor beta, PDGF-R-beta, PDGFR-beta, Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, Platelet-derived growth factor receptor 1, PDGFR-1, CD140b, PDGFRB, Beta Platelet-Derived Growth Factor Receptor, Activated Tyrosine Kinase PDGFRB, CD140b Antigen
      NDEL1-PDGFRB, EC 2.7.10, CD140B, IBGC4, JTK12, PENTT, IMF1, KOGS, Platelet Derived Growth Factor Receptor Beta, Platelet-Derived Growth Factor Receptor, Beta Polypeptide, Beta-Type Platelet-Derived Growth Factor Receptor, Platelet-Derived Growth Factor Receptor 1, CD140, Antigen-Like Family Member B, PDGF-R-Beta, EC 2.7.10.1, PDGFR-Beta, PDGFR-1, PDGFR1, PDGFR,
      Platelet-Derived Growth Factor Receptor Beta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      LVVTPPGPEL VLNVSSTFVL TCSGSAPVVW ERMSQEPPQE MAKAQDGTFS SVLTLTNLTG LDTGEYFCTH NDSRGLETDE RKRLYIFVPD PTVGFLPNDA EELFIFLTEI TEITIPCRVT DPQLVVTLHE KKGDVALPVP YDHQRGFSGI FEDRSYICKT TIGDREVDSD AYYVYRLQVS SINVSVNAVQ TVVRQGENIT LMCIVIGNEV VNFEWTYPRK ESGRLVEPVT DFLLDMPYHI RSILHIPSAE LEDSGTYTCN VTESVNDHQD EKAINITVVE SGYVRLLGEV GTLQFAELHR SRTLQVVFEA YPPPTVLWFK DNRTLGDSSA GEIALSTRNV SETRYVSELT LVRVKVAEAG HYTMRAFHED AEVQLSFQLQ INVPVRVLEL SESHPDSGEQ TVRCRGRGMP QPNIIWSACR DLKRCPRELP PTLLGNSSEE ESQLETNVTY WEEEQEFEVV STLRLQHVDR PLSVRCTLRN AVGQDTQEVI VVPHSLPFKV LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.

    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.

    Pdgfrb Human
  • View Data Sheet

    Name :

    PGLYRP1 Human

    Description:

    Peptidoglycan Recognition Protein 1 Human Recombinant

    Peptidoglycan recognition protein 1, Peptidoglycan recognition protein short, PGRP-S, PGLYRP1, PGLYRP, PGRP, TNFSF3L, TAG7, PGRPS.

    Product # :

    PRO-1597

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    Description

    PGLYRP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-196) containing 185 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 20.68kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    PGLYRP1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidoglycan Recognition Protein 1 (PGLYRP1) is a member of the N-acetylmuramoyl-L-alanine amidase 2 family. PGLYRP1 binds to peptidoglycan of bacteria and affects the peptidoglycan biosynthesis. PGLYRP1 displays bactericidal activity towards Gram-positive bacteria and is bacteriostatic towards Gram-negative bacteria. PGLYRP1 has a role in innate immunity. PGLYRP1 is highly expressed in the bone marrow, and weakly expressed in the kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils.

    • Synonyms

      Peptidoglycan recognition protein 1, Peptidoglycan recognition protein short, PGRP-S, PGLYRP1, PGLYRP, PGRP, TNFSF3L, TAG7, PGRPS.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely at 37°C. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. PGLYRP1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASQETEDPACCS PIVPRNEWKA LASECAQHLS LPLRYVVVSH TAGSSCNTPA SCQQQARNVQ HYHMKTLGWC DVGYNFLIGE DGLVYEGRGW NFTGAHSGHL WNPMSIGISF MGNYMDRVPT PQAIRAAQGL LACGVAQGAL RSNYVLKGHR DVQRTLSPGN QLYHLIQNWP HYRSP.

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    Pglyrp1 Human
  • View Data Sheet

    Name :

    CNTF Human, His Active

    Description:

    Ciliary Neurotrophic Factor Human Recombinant, His Tag Active

    Ciliary neurotrophic factor, CNTF, HCNTF.

    Product # :

    CYT-909

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    Description

    CNTF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200 a.a) and having a molecular mass of 25kDa. CNTF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNTF protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.5), 1 mM DTT,30% Glycerol and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      Ciliary neurotrophic factor, CNTF, HCNTF.

    • 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 MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.

    • Background

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 25kDa.

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

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

      What is the Biological Activity of CNTF Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.

      What is the amino acid sequence of CNTF Protein?
      MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.

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

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

    Cntf Human His Active
  • View Data Sheet

    Name :

    IGF1 Gilthead Seabream

    Description:

    IGF1 Gilthead Seabream Recombinant

    Somatomedin C, IGF-I, IGFI.

    Product # :

    CYT-295

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    Description

    IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.IGF-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.

    More Info

    • Introduction

      The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.

    • Synonyms

      Somatomedin C, IGF-I, IGFI.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK

    • Protein content

      Somatomedin C quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.60 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IGF1 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.

    Igf 1 Denis
  • View Data Sheet

    Name :

    TEF Human

    Description:

    Thyrotrophic Embryonic Factor Human Recombinant

    Thyrotroph embryonic factor, TEF, Thyrotroph embryonic factor isoform 1.FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.

    Product # :

    PRO-1523

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    Description

    TEF Human Recombinant produced in E. coli is a single polypeptide chain containing 326 amino acids (1-303) and having a molecular mass of 35.6kDa.TEF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TEF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thyrotroph embryonic factor (TEF) is a nuclear transcription factor which is a part of the bZIP (basic region/leucine zipper) family and PAR subfamily. TEF binds DNA as either a homodimer or heterodimer, and is known to transactivate the TSH beta promoter. TEF accumulates according to a robust circadian rhythm and is also inhibits cell growth by down-regulating beta chain expression of cytokine receptors.

    • Synonyms

      Thyrotroph embryonic factor, TEF, Thyrotroph embryonic factor isoform 1.FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.

    • 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 MGSMSDAGGG KKPPVDPQAG PGPGPGRAAG ERGLSGSFPL VLKKLMENPP REARLDKEKG KEKLEEDEAA AASTMAVSAS LMPPIWDKTI PYDGESFHLE YMDLDEFLLE NGIPASPTHL AHNLLLPVAE LEGKESASSS TASPPSSSTA IFQPSETVSS
      TESSLEKERE TPSPIDPNCV EVDVNFNPDP ADLVLSSVPG GELFNPRKHK FAEEDLKPQP MIKKAKKVFV PDEQKDEKYW TRRKKNNVAA KRSRDARRLK ENQITIRAAF LEKENTALRT EVAELRKEVG KCKTIVSKYE TKYGPL.

    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.

    Tef Human
  • View Data Sheet

    Name :

    PPARG Human (1-477)

    Description:

    Peroxisome Proliferator Activated Receptor Gamma Human Recombinant, (1-477 a.a)

    Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.

    Product # :

    PKA-334

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    Description

    PPARG Human Recombinant encoding amino acids 1-477 expressed in E.coli, is fused to a GST tag and it is antibody reactive.The PPARG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPARG at 0.1mg/ml in 50mM Tris-HCl and 10mM L-glutathione (reduced).

    More Info

    • Introduction

      Peroxisome proliferators are non-genotoxic carcinogens which are purported to exert their effect on cells through their interaction with members of the nuclear hormone receptor family termed peroxisome proliferators activated receptors (PPARs). Nuclear hormone receptors are ligand-dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate ligand. Studies indicate that PPARs are activated by peroxisome proliferators such as clofibric acid, nafenopin, and WY-14,643, as well as by some fatty acids.

    • Synonyms

      Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Avoid multiple freeze-thaw cycles.

    • Applications

      ELISA.
      Inhibition Assays.
      Western Blotting.

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    Pparg Human 477 Aa
  • View Data Sheet

    Name :

    PEDF Human, His

    Description:

    Pigment Epithelium-Derived Factor Human Recombinant, His Tag

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

    Product # :

    CYT-552

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    Description

    PEDF Human Recombinant produced in E.Coli containing a natural variant M72T is a single, non-glycosylated, polypeptide chain containing 420 amino acids (20-418 a.a.) and having a total molecular mass of 46.7 kDa. PEDF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PEDF solution contains 20mM Tris-HCl buffer(pH 8.0), 0.1M NaCl , and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      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). Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

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

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    Serpinf1 Human His
  • View Data Sheet

    Name :

    PGLYRP1 Human, HEK

    Description:

    Peptidoglycan Recognition Protein 1 Human Recombinant, HEK

    PGLYRP, PGRP, PGRP-S, PGRPS, TAG7, TNFSF3L, Peptidoglycan recognition protein 1, peptidoglycan recognition protein short.

    Product # :

    PRO-2726

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    Description

    PGLYRP1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 184 amino acids (22-196 a.a) and having a molecular mass of 20.5 kDa.PGLYRP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The PGLYRP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Peptidoglycan. The ED50 range ≤ 30 ng/ml.

    More Info

    • Introduction

      Peptidoglycan Recognition Protein 1 (PGLYRP1) is a member of the N-acetylmuramoyl-L-alanine amidase 2 family. PGLYRP1 binds to peptidoglycan of bacteria and affects the peptidoglycan biosynthesis. PGLYRP1 displays bactericidal activity towards Gram-positive bacteria and is bacteriostatic towards Gram-negative bacteria. PGLYRP1 has a role in innate immunity. PGLYRP1 is highly expressed in the bone marrow, and weakly expressed in the kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils.

    • Synonyms

      PGLYRP, PGRP, PGRP-S, PGRPS, TAG7, TNFSF3L, Peptidoglycan recognition protein 1, peptidoglycan recognition protein short.

    • 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

      DGSQETEDPA CCSPIVPRNE WKALASECAQ HLSLPLRYVV VSHTAGSSCN TPASCQQQAR NVQHYHMKTL GWCDVGYNFL IGEDGLVYEG RGWNFTGAHS GHLWNPMSIG ISFMGNYMDR VPTPQAIRAA QGLLACGVAQ GALRSNYVLK GHRDVQRTLS PGNQLYHLIQ NWPHYRSPHH HHHH

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    Pglyrp1 Protein
  • View Data Sheet

    Name :

    PLAUR Human

    Description:

    PLAUR Human Recombinant

    PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.

    Product # :

    PRO-2340

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    • More Info

    Description

    PLAUR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (23-305 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57 kDa).PLAUR is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PLAUR is one of 2 activators which convert the extracellular zymogen plasminogen to plasmin, a serine protease involved in a various normal and pathological processes that require cell migration and/or tissue destruction. PLAUR protein is synthesized and released from cells as a single-chain proenzyme with narrow enzymatic activity and is converted to an active two-chain disulfide-linked active enzyme by plasmin and other specific proteinases.

    • Synonyms

      PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.

    • 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

      LRCMQCKTNG DCRVEECALG QDLCRTTIVR LWEEGEELEL VEKSCTHSEK TNRTLSYRTG LKITSLTEVV CGLDLCNQGN SGRAVTYSRS RYLECISCGS SDMSCERGRH QSLQCRSPEE QCLDVVTHWI QEGEEGRPKD DRHLRGCGYL PGCPGSNGFH NNDTFHFLKC CNTTKCNEGP ILELENLPQN GRQCYSCKGN STHGCSSEET FLIDCRGPMN QCLVATGTHE PKNQSYMVRG CATASMCQHA HLGDAFSMNH IDVSCCTKSG CNHPDLDVQY RSGLEHHHHH H.

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

    Plaur Human
  • View Data Sheet

    Name :

    Darbepoetin

    Description:

    Darbepoetin-Alpha Human Recombinant

    Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    Product # :

    CYT-1263

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    Description

    Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells(CHO).

    Formulation

    Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

    More Info

    • Introduction

      Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.

    • Synonyms

      NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.

    • Background

      What is the molecular weight/Mw of DARBEPOETIN Protein?
      DARBEPOETIN Protein has a total Mw of 38.5kDa.

      What is the source or expression system of DARBEPOETIN Protein?
      Chinese Hamster Ovary Cells(CHO).

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

      What is the Biological Activity of DARBEPOETIN Protein?
      The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

      What is the amino acid sequence of DARBEPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD

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

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

    Darbepoetin
  • View Data Sheet

    Name :

    TFF3 Human

    Description:

    Trefoil Factor-3 Human Recombinant

    TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.

    Product # :

    CYT-005

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    Description

    TFF-3 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 59 amino acid chains which includes a 40 amino acid trefoil motif containing 3 conserved interamolecular disulfide bonds and having a total molecular mass of 13.2kDa. TFF-3 Human Recombinant 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 97.0% as determined by RP-HPLC and SDS-PAGE analysis.

    Biological Activity

    The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of > 100IU/mg.

    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. TFF3 induces ciliogenesis and promotes airway epithelial ciliated cell differentiation, relatively through an epidermal growth factor receptor-dependent pathway. TFF3 overexpression is crucial for progression in mouse and human hepatocellular carcinogenesis. TFF-3 is normally expressed in hepatocellular carcinoma and its expression associates with tumor grade.

    • Synonyms

      TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF3 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 TFF3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EEYVGLSANQ CAVPAKDRVD CGYPHVTPKE CNNRGCCFDS RIPGVPWCFK PLQEAECTF.

    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.

    Tff3 Human
  • View Data Sheet

    Name :

    FGF23 Human

    Description:

    Fibroblast Growth Factor-23 Human Recombinant

    Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    Product # :

    CYT-020

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    Description

    Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 22.5kDa. The FGF-23 is and purified by chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF-23 protein (0.5mg/ml) was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

    More Info

    • Introduction

      FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. The FGF-23 gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF-23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. FGF-23 mutations have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.

    • Synonyms

      Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized FGF-23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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-23 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.

    • Background

      Before it was discovered in 2000, there was a hypothesis that a similar type of protein existed that performed many of the functions we see in FGF23. This was originally referred to as phosphatonin. Various effects were described and noted by researchers including inhibition of production and inhibition of secretion of parathyroid hormone. Derived from the bone Fibroblast Growth Factor 23 is a phosphaturic hormone. It increases phosphate excretion when acting on the kidney and also suppresses the biosynthesis of 1,25(OH)2D3.

      Mechanism
      Despite various research studies into the topic, many of the mechanisms for the regulations of FGF23 production remain a mystery to the scientific community. While we know that mutations in PHEX, ENPP1 and DMP1 result in the increased expression of FGF23, it is unclear why this occurs. This also means that currently, it is not possible to regulate the production of FGF23 either. We also do not know how signals from FGF23 regulate vitamin D metabolism. However, understanding these types of mechanisms could offer information needed to provide better treatment for deranged bone and mineral metabolism.

      Interactions
      Molecular interactions involving FGF-23, vitamin D and klotho do provide the solution needed to regulate phosphate levels within the body. Furthermore, an interaction between Vitamin D and FGF3 can have an impact on renal phosphate balance. As well as this, when in the presence of klotho, FGF3 does actually increase bioactivity and begins to change systemic phosphate homeostasis.

      Function
      Based on research it seems that the main function for FGF23 is the regulation of phosphate concentration in plasma. It seems to be secreted from the osteocytes due to elevated levels . When acting upon the kidneys, the hormone reduces the expression of NPT2. This is a sodium-phosphate cotransporter found in the proximal tube.
      As such, it appears as though FGF23 is able to reduce the reabsorption, all the while maxing the excretion of phosphate. It has also been suggested that the hormone is able to suppress 1-alpha-hydroxylase. If this is the case, it can limit its potential to activate vitamin D and thus impair the ability for calcium absorption.

      Structure
      FGF243 is located on the chromosome 12. It is composed of three exons. The crystal structure of FGF23 is completely different from the common conformation typically adopted by paracrine-acting FGFs. Instead, there is a conformation of the HPR region between beta strands 10 and 12. As well as this, there is a cleft between the other HPR-binding region, the beta1-beta12 loop and this one. This comes before a direct interaction between HPR sulfate and FGF23s backbone atoms. Due to this, endocrine function is benefitted and HPR-binding affinity is reduced for the lipangs.
      Certain mutations that cause the protein to be completely resistant to proteolytic cleavage does trigger a surge in activity of the protein and the renal phosphate loss typically found in certain human diseases including hypophosphatemic rickets.
      Studies have also revealed that FGF23 is overproduced in certain tumors including phosphaturic mesenchymal tumors. Furthermore a reduced level of activity for this protein is believed to lead to higher phosphate levels and familial tumor calcinosis clinical syndrome.

      What is the molecular weight/Mw of FGF23 HUMAN Protein?
      FGF23 HUMAN Protein has a total Mw of 22.5kDa.

      What is the source or expression system of FGF23 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of FGF23 HUMAN Protein?
      FGF23 HUMAN Protein is >95X% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF23 HUMAN Protein?
      The biological activity of FGF-23 was measured in a cell proliferation assay using NIH/3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.05-0.5µg/ml in the presence of 5µg/ml of Recombinant Mouse Klotho and 10 µg/ml of HPR.

      What is the amino acid sequence of FGF23 HUMAN Protein?
      MYPNASPLLG SSWGGLIHLY TATARNSYHL QIHKNGHVDG APHQTIYSAL MIRSEDAGFV VITGVMSRRY LCMDFRGNIF GSHYFDPENC RFQHQTLENG YDVYHSPQYH FLVSLGRAKR AFLPGMNPPP YSQFLSRRNE IPLIHFNTPI PRRHTRSAED DSERDPLNVL KPRARMTPAP ASCSQELPSA EDNSPMASDP LGVVRGGRVN THAGGTGPEG CRPFAKFI.

      What applications can FGF23 HUMAN Protein be used in?
      FGF23 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF23 HUMAN Protein?
      The endotoxin level is minimal, FGF23 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.

    Fgf23 Human
  • View Data Sheet

    Name :

    PEDF Human

    Description:

    Pigment Epithelium-Derived Factor Human Recombinant

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

    Product # :

    CYT-580

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Background

      About PEDF Human

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

      What’s the Function of PEDF Human Recombinant?

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


      What’s the Application of PEDF Human Recombinant?

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

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

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

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

    Serpinf1 Human
  • View Data Sheet

    Name :

    PFN4 Human

    Description:

    Profilin-4 Human Recombinant

    PFN-4, Profilin-IV, Profilin4.

    Product # :

    PRO-818

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    Description

    PFN4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 149 amino acids (1-129 a.a.) and having a molecular mass of 16.4 kDa. PFN4 protein is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN4 Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PFN4 is a small actin-binding protein that participates in the dynamic turnover and restructuring of the actin cytoskeleton. PFN4 is localized in all eukaryotic organisms in the majority of cells. PFN4 is crucial for spatially and temporally controlled growth of actin microfilaments, which is a necessary process in cellular locomotion and cell shape changes.

    • Synonyms

      PFN-4, Profilin-IV, Profilin4.

    • 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 MSHLQSLLLD TLLGTKHVDS AALIKIQERS LCVASPGFNV TPSDVRTLVN GFAKNPLQAR REGLYFKGKD YRCVRADEYS LYAKNENTGV VVVKTHLYLL VATYTEGMYP SICVEATESL GDYLRKKGS.

    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.

    Pfn4 Human
  • View Data Sheet

    Name :

    Terlipressin

    Description:

    Terlipressin

    Product # :

    HOR-287

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    Description

    Terlipressin contains 12 amino acids Gly-Gly-Gly-c[Cys-Tyr-Phe-Gln-Asn-Cys]-Pro-Lys-Gly-NH2 and having a molecular weight of 1227.37 Dalton.

    Formulation

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

    Purity

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

    More Info

    • Introduction

      Terlipressin is similar to a naturally occurring hormone present in the body, known as antidiuretic hormone (ADH) or vasopressin. ADH has two main effects in the body. Firstly, it causes narrowing of blood vessels (vasoconstriction), thereby limiting blood flow to a particular area of the body. It also acts on receptors in the kidney to retain water in the body, which helps to prevent excessive loss of water in the urine. Terlipressin is commonly used to stop bleeding of varices in the food pipe (oesophagus). Varices are fragile distended veins that can occur in various parts of the body such as the oesophagus. This is caused by an increase in blood pressure in certain diseases such as severe liver disease. These fragile varices can rupture and lead to life threatening bleeding. Terlipressin is therefore given to narrow blood vessels, and so restricting blood flow to the varices and stopping the bleeding.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Terlipressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Terlipressin 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 Terlipressin18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Terlipressin
  • View Data Sheet

    Name :

    pGH 22kDa Human

    Description:

    Growth Hormone Placental 22kDa Human Recombinant

    GHL, GHV, GH-V, hGH-V, PGH.

    Product # :

    CYT-235

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    Description

    Placental HGH 22kDa Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 22367 Dalton. Predicted pI=7.80. Placental Growth Hormone has dimished lactogenic (prolactin receptor mediated) activity characteristic to pituitary GHs. GH Placental Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3 previously adjusted pH 8-9.

    Purity

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

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GHL, GHV, GH-V, hGH-V, PGH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH placental although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization HGH placental can be stored at 4°C for up to 4 weeks. For long term storage and more diluted solutions 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 Placental HGH in 0.4% NaHCO3or water adjusted to pH 9, not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.18 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 GH-22K-placental 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.

    Placental Gh 22K Human
  • View Data Sheet

    Name :

    TANK Human

    Description:

    TRAF Family Member-Associated NFKB Activator Human Recombinant

    TRAF, TRAF2, TRAF-interacting protein, ITRAF.

    Product # :

    PRO-1348

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    Description

    TANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 448 amino acids (1-425a.a) and having a molecular mass of 50.2kDa. TANK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TANK protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      TRAF Family Member-Associated NFKB Activator (TANK) is located in the cytoplasm and binds Either TRAF1, TRAF2 or TRAF3. TANK is an inhibitor of TRAF function which regulates TRAF protein activity via sequestering TRAFs in a dormant position in the cytoplasm. Overexpression of TANK, inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and also inhibits LMP1-mediated NFkappa-B activation by blocking the connection of TRAF2 with LMP1.

    • Synonyms

      TRAF, TRAF2, TRAF-interacting protein, ITRAF.

    • 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 MGSMDKNIGE QLNKAYEAFR QACMDRDSAV KELQQKTENY EQRIREQQEQ LSLQQTIIDK LKSQLLLVNS TQDNNYGCVP LLEDSETRKN NLTLDQPQDK VISGIAREKL PKVRRQEVSS PRKETSARSL GSPLLHERGN IEKTFWDLKE EFHKICMLAK AQKDHLSKLN IPDTATETQC SVPIQCTDKT DKQEALFKPQ AKDDINRGAP SITSVTPRGL CRDEEDTSFE SLSKFNVKFP PMDNDSTFLH STPERPGILS PATSEAVCQE KFNMEFRDNP GNFVKTEETL FEIQGIDPIA SAIQNLKTTD KTKPSNLVNT CIRTTLDRAA CLPPGDHNAL YVNSFPLLDP SDAPFPSLDS PGKAIRGPQQ PIWKPFPNQD SDSVVLSGTD SELHIPRVCE FCQAVFPPSI TSRGDFLRHL NSHFNGET.

    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.

    Tank Human
  • View Data Sheet

    Name :

    Leptin tA Mouse, PEG

    Description:

    Leptin Antagonist Triple Mutant Pegylated Mouse Recombinant

    Product # :

    CYT-566

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    Description

    Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Mouse Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    Leptin Antagonist Triple Mutant Mouse Recombinant half-life in circulation after SC injection was over 20 hours.
    Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Mouse Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ta Mouse Peg
  • View Data Sheet

    Name :

    MANF Human

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant

    Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    Product # :

    CYT-141

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    Description

    MANF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids and having a molecular mass of 18.1 kDa. The MANF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 was determined by its ability to stimulate the proliferation of rat C6 cells is typically 15-25 µg/ml.

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    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIENELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDKQ IDLSTVDLKK LRVKELKKIL DDWGETCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.

    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.

    Manf Human Recombinant
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    Name :

    EG VEGF Human

    Description:

    Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant

    PK1, PRK1, Prokineticin 1, EG-VEGF.

    Product # :

    CYT-338

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

      PK1, PRK1, Prokineticin 1, EG-VEGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.

    • Background

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

      Abstract:


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

      Introduction:


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

      Production and Characterization:


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

      Role in Endocrine Disorders:


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

      Therapeutic Implications:


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

      Conclusion:


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

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

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

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

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

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

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

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

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

    Eg Vegf Human
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