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Search results

1000 results found for “visfatin”

Name

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  • View Data Sheet

    Name :

    ARTN Human

    Description:

    Artemin Human Recombinant

    ART, ARTN , EVN, NBN.

    Product # :

    CYT-306

    Price :

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    • source
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    Description

    Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

    Citations

    More Info

    • Introduction

      The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.

    • Synonyms

      ART, ARTN , EVN, NBN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

    • Background

      Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications

      Abstract:

      Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.

      Introduction:

      Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.

      Artemin Signaling and Mechanisms:

      Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.

      Artemin in Neurological Disorders:

      Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.

      Therapeutic Potential of Artemin Human Recombinant:

      Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.

      Challenges and Future Directions:

      While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.

      Conclusion:

      Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.

      What is the molecular weight/Mw of ARTN Protein?
      ARTN Protein has a total Mw of 24.2kDa.

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

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

      What is the Biological Activity of ARTN Protein?
      The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

      What is the amino acid sequence of ARTN Protein?
      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

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

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

    Artemin Human
  • View Data Sheet

    Name :

    S100A8 Human

    Description:

    S100 Calcium Binding Protein A8 Human Recombinant

    Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    Product # :

    PRO-800

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
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    Description

    S100A8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (1-93 a.a.) and having a molecular mass of 10.8 kDa. The S100A8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A8 solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

    • Synonyms

      Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    • Physical Appearance

      Sterile Filtered clear 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

      MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.

    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.

    S100A8 Human
  • View Data Sheet

    Name :

    ANXA1 Human

    Description:

    Annexin A1 Human Recombinant

    ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

    Product # :

    PRO-679

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    ANXA1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 346 amino acids (1-346 a.a.) and having a molecular mass of 38.7 kDa.ANXA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.

    • Synonyms

      ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

    • 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

      MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK
      PLDETLKKAL TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL
      LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK VLDLELKGDI EKCLTAIVKCATSKPAFFAE KLHQAMKGVG TRHKALIRIM VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN.

    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.

    Anxa1 Human
  • View Data Sheet

    Name :

    IGF1 LR3 Human

    Description:

    LR3 Insulin Like Growth Factor-1 Human Recombinant

    R3 IGF1, R3 IGF-1, R3IGF1, R3IGF-1, LONG IGF1, LONG IGF-1, LONG R3 IGF1, LONG R3IGF1, LONG R3 IGF-1, LONG R3IGF-1.

    Product # :

    CYT-022

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    Description

    The LR3 is a long-term analog of human IGF-1, specifically designed and manufactured for mammalian cell culture to support large-scale manufacturing of recombinant biopharmaceuticals. Recombinant Human LR3 Insulin Like Growth Factor-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9.1kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.2.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the stimulation of protein synthesis in L6 myoblasts is less than 10ng/ml, corresponding to a specific activity of 100,000units/mg.

    sds-page

    LR3 IGF1 sds-page - Product image 1

    Citations

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    • Introduction

      IGF-1 (Insulin-like growth factor-1) is a major hormonal mediator of statural growth. Under regular circumstances, GH (growth hormone) binds to its receptor in the liver, and other tissues, and stimulates the synthesis/secretion of IGF-1. In target tissues, the Type 1 IGF receptor, that is homologous to the insulin receptor, is activated by IGF-1, leading to intracellular signaling which stimulates multiple processes leading to statural growth. IGF-1 metabolic actions are partly directed at stimulating the uptake of glucose, fatty acids, and amino acids so that metabolism supports growing tissues.

    • Synonyms

      R3 IGF1, R3 IGF-1, R3IGF1, R3IGF-1, LONG IGF1, LONG IGF-1, LONG R3 IGF1, LONG R3IGF1, LONG R3 IGF-1, LONG R3IGF-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LR3 IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution the LR3 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 LR3 IGF1 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIV DECCFRSCDLRRLEMYCAPLKPAKSA.

    • Background

      What is the molecular weight/Mw of IGF1 LR3 HUMAN Protein?
      IGF1 LR3 HUMAN Protein has a total Mw of 9.1kDa.

      What is the source or expression system of IGF1 LR3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IGF1 LR3 HUMAN Protein?
      IGF1 LR3 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGF1 LR3 HUMAN Protein?
      The ED50 as determined by the stimulation of protein synthesis in L6 myoblasts is less than 10ng/ml, corresponding to a specific activity of 100,000units/mg.

      What is the amino acid sequence of IGF1 LR3 HUMAN Protein?
      MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIV DECCFRSCDLRRLEMYCAPLKPAKSA.

      What applications can IGF1 LR3 HUMAN Protein be used in?
      IGF1 LR3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGF1 LR3 HUMAN Protein?
      The endotoxin level is minimal, IGF1 LR3 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.

    Long R3 Igf1 Human
  • View Data Sheet

    Name :

    Streptavidin Antibody

    Description:

    Streptavidin, Mouse Antibody

    Product # :

    ANT-345

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    Formulation

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

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    • 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 Filtered clear solution.

    • Immunogen

      Anti Streptavidin mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant Streptavidin amino acids 25-183 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      P1C2AT.

    • Applications

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

    • Type

      Mouse Antibody 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

      Streptavidin antibody was purified from mouse ascitic fluids by protein-G 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.

    Streptavidin Antibody
  • View Data Sheet

    Name :

    Exendin 4

    Description:

    Exendin-4 Recombinant

    Product # :

    HOR-269

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    Description

    Exendin-4 Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 39 amino acids and having a molecular mass of approximately 4.2kDa. Exendin-4 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 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    1. Regulates Glucose levels rapidly
    2. Reduces Insulin resistance 
    3. Reduces Glucagon

    4. Stimulates beta cell growth production.

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    • Introduction

      Exedin-4 Recombinant is a like peptide-1 receptor agonist. The native hormone is produced in the gut of Gila monster Heloderma suspectrum (a type of reptile found in the desert) that stimulates production without causing threateningly low blood sugar, which can occur after using some anti-diabetes products. Recently, researchers used extracted saliva from gila monsters to create an unprecedented breakthrough in Diabetes Type 2 treatment. Unlike other products taken for type 2 diabetes, Exedin-4 has not been linked with weight gain and actually resulted in weight loss, according to the researchers. Exedin-4 enhances glucose-dependant secretion, suppresses inappropriately elevated secretion and slows gastric emptying in vivo. It also promotes B-cell proliferation and neogenesis in vitro and in animal models. Exedin-4 stimulates an increase in acinar cAMP, without stimulating the release of amylase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HGEGTFTSDL SKQMEEEAVR LFIEWLKNGG PSSGAPPPS.

    • Background

      What is the molecular weight/Mw of EXENDIN 4 Protein?
      EXENDIN 4 Protein has a total Mw of 4.2kDa.

      What is the source or expression system of EXENDIN 4 Protein?
      Escherichia Coli.

      What is the Purity of EXENDIN 4 Protein?
      EXENDIN 4 Protein is > 96% pure as determined by SDS-PAGE.

      What is the Biological Activity of EXENDIN 4 Protein?
      1. Regulates Glucose levels rapidly
      2. Reduces Insulin resistance
      3. Reduces Glucagon
      4. Stimulates beta cell growth production.

      What is the amino acid sequence of EXENDIN 4 Protein?
      HGEGTFTSDL SKQMEEEAVR LFIEWLKNGG PSSGAPPPS

      What applications can EXENDIN 4 Protein be used in?
      EXENDIN 4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EXENDIN 4 Protein?
      The endotoxin level is minimal, EXENDIN 4 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant EXENDIN 4 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of EXENDIN 4?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Exendin 4
  • View Data Sheet

    Name :

    Myostatin Human, His

    Description:

    Myostatin Human Recombinant, His Tag

    GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.

    Product # :

    CYT-445

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    Description

    Total 152AA. M.W. 16.7kDa (calculated). N-terminal His-tag and spacer (43AA – highlighted). The AA sequence of the human myostatin part of the fusion protein is corresponding to the UniProtKB/Swiss-Prot entry O14793.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M acetate buffer, pH 4.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Myostatin (GDF-8) is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 113 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor ? superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology.

    • Synonyms

      GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.

    • 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

      Add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDPSSRSAVR SRRDFGLDCD EHSTESRCCR YPLTVDFEAFGWDWIIAPKR YKANYCSGEC EFVFLQKYPH THLVHQANPR GSAGPCCTPT KMSPINMLYF NGKEQIIYGKIPAMVVDRCG CS.

    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.

    Myostatin Human Fc
  • View Data Sheet

    Name :

    Tri a 14.0101

    Description:

    Non-Specific Lipid-Transfer Protein Tri a 14 Recombinant

    Non-specific lipid-transfer protein, ltp142.

    Product # :

    ALR-025

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    Description

    Recombinant Non-Specific Lipid-Transfer Protein Tri a 14 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 13kDa. Tri a 14.0101 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Tri a 14.0101 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Tri a 14.0101 is a non-specific lipid transfer protein and a major wheat allergen. Those who are sensitive to this allergen may have baker’s asthma, a frequent occupational allergic disease caused mainly by inhalation of cereal flour, especially wheat flour. Tri a 14.0101 consists of 4 helical fragments and irregular C-terminal regions which are highly stable to heat treatment and proteolytic attack.

    • Synonyms

      Non-specific lipid-transfer protein, ltp142.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE-type human antibodies.2. Immunodot test with positive/negative samples.

    • Applications

      Tested by LAL (Limulus Amoebocyte Lysate) chromogenic endotoxin assay.

    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.

    Tri A 140101
  • View Data Sheet

    Name :

    ADFP Human

    Description:

    Adipose Differentiation-Related Protein Human Recombinant

    Adipophilin, Adipose differentiation-related protein, ADRP, ADFP, MGC10598.

    Product # :

    PRO-405

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    Description

    ADFP Human Recombinant produced in E.Coli is a signle, non-glycosylated, Polypeptide chain containing 444 amino acids and having a molecular mass of 49 kDa. The protein contains an extra 8 amino acid His tag at N-terminus. The ADFP amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q99541 amino acids 4–437.The ADFP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human ADFP was lyophilized from 0.5mg/ml solution containing 20mM Tris pH-7.5, and 20mM NaCl.

    Purity

    Greater than 95% as determined by SDS PAGE.

    Citations

    More Info

    • Introduction

      ADFP is related with the globule surface membrane material. ADFP is a major constituent of the globule surface. Rise in mRNA levels is one of the initial indications of adipocyte differentiation. Mycobacterium leprae regulates ADFP expression to facilitate the accumulation of lipids within infected macrophages for intracellular survival. ADFP is expressed in lipid droplets of vitamin A-storing hepatic stellate cells and additionally in lipid droplets of steatotic hepatocytes. ADFP expression has a role in clear cell renal carcinoma differentiation. ADFP is a component of the lipid droplets in THP-1 cells.

    • Synonyms

      Adipophilin, Adipose differentiation-related protein, ADRP, ADFP, MGC10598.

    • 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

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

    • Amino Acid Sequence

      MKHHHHHHAS VAVDPQPSVV TRVVNLPLVS STYDLMSSAY LSTKDQYPYL KSVCEMAENG VKTITSVAMT SALPIIQKLE PQIAVANTYA CKGLDRIEER LPILNQPSTQ IVANAKGAVT GAKDAVTTTV TGAKDSVAST ITGVMDKTKG AVTGSVEKTK SVVSGSINTV LGSRMMQLVS SGVENALTKS ELLVEQYLPL TEEELEKEAK KVEGFDLVQK PSYYVRLGSL STKLHSRAYQ QALSRVKEAK QKSQQTISQL HSTVHLIEFA RKNVYSANQK IQDAQDKLYL SWVEWKRSIG YDDTDESHCA EHIESRTLAI ARNLTQQLQT TCHTLLSNIQ GVPQNIQDQA KHMGVMAGDI YSVFRNAASF KEVSDSLLTS SKGQLQKMKE SLDDVMDYLV NNTPLNWLVG PFYPQLTESQ NAQDQGAEMD KSSQETQRSEHKTH.

    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.

    Adfp Human
  • View Data Sheet

    Name :

    OLR1 Human, Sf9

    Description:

    Oxidized Low Density Lipoprotein Receptor 1 Human Recombinant, Sf9

    Oxidized Low Density Lipoprotein Receptor 1, C-Type Lectin Domain Family 8 Member A, Lectin-Type Oxidized LDL Receptor 1, CLEC8A, HLOX-1, LOX1, Oxidised Low Density Lipoprotein (Lectin-Like) Receptor 1, Oxidized Low Density Lipoprotein (Lectin-Like) Receptor 1, Oxidized Low-Density Lipoprotein Receptor 1, Soluble Form, Oxidized Low-Density Lipoprotein Receptor 1, Scavenger Receptor Class E, Member 1, Lectin-Like Oxidized LDL Receptor 1, Lectin-Like OxLDL Receptor 1, Ox LDL Receptor 1, Ox-LDL Receptor 1, SCARE1, LOXIN, SLOX1, LOX-1, Oxidized low-density lipoprotein receptor 1, Ox-LDL receptor 1, C-type lectin domain family 8 member A, LOX-1, Lectin-like oxLDL receptor 1, hLOX-1, Lectin-type oxidized LDL receptor 1.

    Product # :

    PRO-2373

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    Description

    OLR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 225 amino acids (58-273a.a) and having a molecular mass of 25.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). OLR1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    OLR1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

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    • Introduction

      OLR1 is a type II membrane protein which belongs to the C-type lectin family and performs as a cell-surface receptor for Ox-LDL. Ox-LDL has a part in early ather-osclerosis, which includes the transformation of monocyte-derived macro-phages to foam cells in atherosclerotic lesions. In addition, OLR1 protein triggers the activation of the NF?B signal transduction pathway.

    • Synonyms

      Oxidized Low Density Lipoprotein Receptor 1, C-Type Lectin Domain Family 8 Member A, Lectin-Type Oxidized LDL Receptor 1, CLEC8A, HLOX-1, LOX1, Oxidised Low Density Lipoprotein (Lectin-Like) Receptor 1, Oxidized Low Density Lipoprotein (Lectin-Like) Receptor 1, Oxidized Low-Density Lipoprotein Receptor 1, Soluble Form, Oxidized Low-Density Lipoprotein Receptor 1, Scavenger Receptor Class E, Member 1, Lectin-Like Oxidized LDL Receptor 1, Lectin-Like OxLDL Receptor 1, Ox LDL Receptor 1, Ox-LDL Receptor 1, SCARE1, LOXIN, SLOX1, LOX-1, Oxidized low-density lipoprotein receptor 1, Ox-LDL receptor 1, C-type lectin domain family 8 member A, LOX-1, Lectin-like oxLDL receptor 1, hLOX-1, Lectin-type oxidized LDL receptor 1.

    • 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

      ADPMQLSQVS DLLTQEQANL THQKKKLEGQ ISARQQAEEA SQESENELKE MIETLARKLN EKSKEQMELH HQNLNLQETL KRVANCSAPC PQDWIWHGEN CYLFSSGSFN WEKSQEKCLS LDAKLLKINS TADLDFIQQA ISYSSFPFWM GLSRRNPSYP WLWEDGSPLM PHLFRVRGAV SQTYPSGTCA YIQRGAVYAE NCILAAFSIC QKKANLRAQH HHHHH.

    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.

    Olr1 Human Sf9
  • View Data Sheet

    Name :

    C19ORF80 Rat

    Description:

    Chromosome 19 Open Reading Frame 80 Rat Recombinant

    Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.

    Product # :

    PRO-2024

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    Description

    C19ORF80 Rat Recombinant produced in E. coli is a polypeptide chain containing 193 amino acids and having a total molecular mass of 22.0 kDa. C19ORF80 has a N-Terminal His-tag (10 AA residue).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from a 0.5mg/ml solution containing 0.03M Acetate buffer pH 4.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.

    • Synonyms

      Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.

    • 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. 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. C19ORF80 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS VRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYKA TEARLTEAGR NLGLFDQALE FLGREVNQGR DATRELRTSL SEIQAEEDTL HLRAEATARS LREVARAQHA LRNSVRRLQV QLRGAWLGQA HQEFENLKDR ADKQNHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHMAA LPA

    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.

    C19Orf80 Rat
  • View Data Sheet

    Name :

    FGF12 Human

    Description:

    Fibroblast Growth Factor 12 Human Recombinant

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

    Product # :

    CYT-1113

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    Citations

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    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 12 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Fibroblast Growth Factor 12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

      What is the endotoxin level for FGF12 Protein?
      The endotoxin level is minimal, FGF12 Protein was purified using conventional chromatography techniques.

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

    Fgf 12 Protein
  • View Data Sheet

    Name :

    FGF8 Human, HEK

    Description:

    Fibroblast Growth Factor-8 Human Recombinant, HEK

    FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

    Product # :

    CYT-087

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    Description

    FGF-8 Human Recombinant is a single, glycosylated, polypeptide chain (23-215 a.a) containing a total of 204 amino acids and having a molecular mass of 23.7 kDa. FGF-8 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK.

    Formulation

    The FGF-8 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as obsereved by SDS-PAGE.

    Biological Activity

    The ED50 is ≤5 µg/ml, measured  in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.

    Citations

    More Info

    • Introduction

      FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

    • Synonyms

      FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

    • 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

      DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.

    • Background

      What is the molecular weight/Mw of FGF8 Protein?
      FGF8 Protein has a total Mw of 23.7kDa.

      What is the source or expression system of FGF8 Protein?
      HEK.

      What is the Purity of FGF8 Protein?
      FGF8 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF8 Protein?
      The ED50 is ≤5 µg/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.

      What is the amino acid sequence of FGF8 Protein?
      DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.

      What applications can FGF8 Protein be used in?
      FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF8 Protein?
      The endotoxin level is minimal, FGF8 Protein was purified using conventional chromatography techniques.

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

    Fgf 8 Human Hek
  • View Data Sheet

    Name :

    PI3 Human, Sf9

    Description:

    Peptidase Inhibitor 3 Human Recombinant, Sf9

    Elafin, ESI, SKALP, WAP3, WFDC14.

    Product # :

    PRO-2653

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    Description

    PI3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 101 amino acids (23-117a.a) and having a molecular mass of 10.7kDa.PI3 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The PI3 solution (0.2mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Peptidase Inhibitor 3, also referred to PI3, is neutrophil and pancreatic elastase-specific inhibitor of skin. The protein may prevent elastase mediated tissue proteolysis. PI3 has shown inhibition of alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor, a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation channel subfamily V member 1.

    • Synonyms

      Elafin, ESI, SKALP, WAP3, WFDC14.

    • 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

      AVTGVPVKGQ DTVKGRVPFN GQDPVKGQVS VKGQDKVKAQ EPVKGPVSTK PGSCPIILIR CAMLNPPNRC LKDTDCPGIK KCCEGSCGMA CFVPQHHHHH 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.

    Elafin Human
  • View Data Sheet

    Name :

    Lymphotactin Human, His

    Description:

    Lymphotactin Human Recombinant (XCL1), His Tag

    XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

    Product # :

    CHM-357

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    Description

    XCL1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 114 amino acids (22-114 a.a.) and having a molecular mass of 12.5 kDa. The XCL1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Recombinant XCL1 contains 20mM Tris buffer pH-8, 200mM NaCl, 2mM DTT and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      XCL1 is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is located in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to another chemokine called XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.

    • Synonyms

      XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

    • 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 MVGSEVSDKR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG.

    • Background

      What is the molecular weight/Mw of LYMPHOTACTIN HUMAN, HIS Protein?
      LYMPHOTACTIN HUMAN, HIS Protein has a total Mw of 12.5kDa.

      What is the source or expression system of LYMPHOTACTIN HUMAN, HIS Protein?
      Escherichia Coli.

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

      What is the Biological Activity of LYMPHOTACTIN HUMAN, HIS Protein?
      The biological functionality of LYMPHOTACTIN HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of LYMPHOTACTIN HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MVGSEVSDKR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG.

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

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

      Who supplies recombinant LYMPHOTACTIN HUMAN, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of LYMPHOTACTIN HUMAN, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Lymphotactin Human His
  • View Data Sheet

    Name :

    AAMDC Human

    Description:

    Adipogenesis Associated, Mth938 Domain Containing Human Recombinant

    Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.

    Product # :

    PRO-2116

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    Description

    AAMDC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-122 a.a) and having a molecular mass of 15.7 kDa.AAMDC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AAMDC protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adipogenesis Associated, Mth938 Domain Containing, also known as AAMDC is a member of the AAMDC family and takes part in preadipocyte differentiation andadipogenesis.

    • Synonyms

      Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.

    • 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 MGSMTSPEIA SLSWGQMKVK GSNTTYKDCK VWPGGSRTWD WRETGTEHSP GVQPADVKEV VEKGVQTLVI GRGMSEALKV PSSTVEYLKK HGIDVRVLQT EQAVKEYNAL VAQGVRVGGV FHSTC.

    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.

    Aamdc Human
  • View Data Sheet

    Name :

    MIF Human His C

    Description:

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

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

    Product # :

    CYT-521

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    Description

    MIF human Recombinant, fused to His-tag at C-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 is a single, non-glycosylated, polypeptide chaincontaining 123 amino acidsand having a molecular mass of 13.5 kDa.

    Source

    Escherichia Coli.

    Formulation

    Human MIF was lyophilized from a 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.

    Biological Activity

    Measured by its ability to bind rhCD74 in a functional ELISA.

    Citations

    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 lyophilized powder.

    • Stability

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

    • Amino Acid Sequence

      MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPC
      ALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTF
      ALEHHHHHH.

    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 C
  • View Data Sheet

    Name :

    HIF1AN Human

    Description:

    Hypoxia-Inducible Factor-1 Alpha Inhibitor Human Recombinant

    FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.

    Product # :

    PRO-662

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    Description

    HIF1AN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-349) and having a molecular mass of 40.2kDa. The HIF1AN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Overexpression of the HIF1AN is linked with tumor aggressiveness in pancreatic endocrine tumors. HIF1AN hydroxylates Notch ICD at two residues that are crucial for the function of Notch ICD as a transactivator within cells and during neurogenesis and myogenesis. HIF1AN is commonly expressed in invasive breast carcinoma. The hypoxic response and survival recommends that tumour regulation of HIF1AN is an additional important mechanism for HIF pathway activation. HIF1AN is an asparaginyl hydroxylase enzyme that controls the transcriptional activity of hypoxia-inducible factor. FIH1 is a part of the Fe2+ and 2-oxoglutarate-dependent dioxygenase superfamily, FIH1 is protein that hydoxylates a specific asparagine residue (Asn-803) within the HIF1A C-terminal transactivation domain. In normoxia, the HIF1AN-mediated hydroxylation of the HIF1? transactivation domain which results in blockage of the HIF1A-p300/CBP interaction and represses transcriptional activity of HIF1A targeted genes.

    • Synonyms

      FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.

    • 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

      MAATAAEAVA SGSGEPREEA GALGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMAN FQNFKPRSNR EEMKFHEFVE KLQDIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGYKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE RFPNFQNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN.

    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.

    Hif1An Human
  • View Data Sheet

    Name :

    CXCL12 Rat beta

    Description:

    Stromal Cell-Derived Factor-1 beta Rat Recombinant (CXCL12)

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    Product # :

    CHM-248

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    Description

    SDF-1 beta Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8.4 kDa. The Rat SDF-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Rat SDF1B protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phsophate buffer pH-7.4 and 0.15M NaCl.

    Purity

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

    Biological Activity

    The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 100-150ng/ml corresponding to a Specific Activity of 6,667-10,000IU/mg.

    Citations

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
      The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 SDF-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNKRL KM.

    • Background

      What is the molecular weight/Mw of CXCL12 RAT BETA Protein?
      CXCL12 RAT BETA Protein has a total Mw of 8.4kDa.

      What is the source or expression system of CXCL12 RAT BETA Protein?
      Escherichia Coli.

      What is the Purity of CXCL12 RAT BETA Protein?
      CXCL12 RAT BETA Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL12 RAT BETA Protein?
      The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 100-150ng/ml corresponding to a Specific Activity of 6,667-10,000IU/mg.

      What is the amino acid sequence of CXCL12 RAT BETA Protein?
      KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNKRL KM.

      What applications can CXCL12 RAT BETA Protein be used in?
      CXCL12 RAT BETA Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL12 RAT BETA Protein?
      The endotoxin level is minimal, CXCL12 RAT BETA Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL12 RAT BETA that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL12 RAT BETA?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Sdf 1B Rat
  • View Data Sheet

    Name :

    CIAPIN1 Human

    Description:

    Cytokine Induced Apoptosis Inhibitor 1 Human Recombinant

    DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.

    Product # :

    PRO-024

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    Description

    CIAPIN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312 a.a.) and having a molecular mass of 36kDa.CIAPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CIAPIN1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Anamorsin, ( CIAPIN) is a member of anamorsin family. CIAPIN mainly expressed in the cytoplasm of liver, pancreas and heart tissue cells and does not show any homology to known apoptosis regulatory molecules of the Bcl-2 or CASP families, or to signal transduction molecules. CIAPIN1 Expression is reliant on growth factor stimulation. It is a ubiquitously expressed protein, and when it is overexpressed, it grants apoptotic resistance.

    • Synonyms

      DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.

    • 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 MGSMADFGIS AGQFVAVVWD KSSPVEALKG LVDKLQALTG NEGRVSVENI KQLLQSAHKE SSFDIILSGL VPGSTTLHSA EILAEIARIL RPGGCLFLKE PVETAVDNNS KVKTASKLCS ALTLSGLVEV KELQREPLTP EEVQSVREHL GHESDNLLFV QITGKKPNFE VGSSRQLKLS ITKKSSPSVK PAVDPAAAKL WTLSANDMED DSMDLIDSDE LLDPEDLKKP DPASLRAASC GEGKKRKACK NCTCGLAEEL EKEKSREQMS SQPKSACGNC YLGDAFRCAS CPYLGMPAFK PGEKVLLSDS NLHDA.

    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.

    Ciapin1 Human
  • View Data Sheet

    Name :

    GTF2F2 Human

    Description:

    General Transcription Factor IIF, Polypeptide 2 Human Recombinant

    General transcription factor IIF subunit 2, ATP-dependent helicase GTF2F2, General transcription factor IIF 30 kDa subunit, Transcription initiation factor IIF subunit beta, TFIIF-beta, Transcription initiation factor RAP30, GTF2F2, RAP30, BTF4, TF2F2, TFIIF.

    Product # :

    PRO-1093

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    Description

    GTF2F2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-249 a.a) and having a molecular mass of 30.5kDa (Molecular weight on SDS-PAGE will appear higher).GTF2F2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GTF2F2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.2M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      General Transcription Factor IIF Polypeptide 2 (GTF2F2) is a general transcription initiation factor which binds to RNA polymerase II and helps engage it in the initiation complex in collaboration with TFIIB. GTF2F2 promotes transcription elongation. GTF2F2 shows ATP-dependent DNA-helicase activity.

    • Synonyms

      General transcription factor IIF subunit 2, ATP-dependent helicase GTF2F2, General transcription factor IIF 30 kDa subunit, Transcription initiation factor IIF subunit beta, TFIIF-beta, Transcription initiation factor RAP30, GTF2F2, RAP30, BTF4, TF2F2, TFIIF.

    • 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 MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVGG QTLTVFTESS SDKLSLEGIV VQRAECRPAA SENYMRLKRL QIEESSKPVR LSQQLDKVVT TNYKPVANHQ
      YNIEYERKKK EDGKRARADK QHVLDMLFSA FEKHQYYNLK DLVDITKQPV VYLKEILKEI GVQNVKGIHK NTWELKPEYR HYQGEEKSD.

    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.

    Gtf2F2 Human
  • View Data Sheet

    Name :

    Desmin Human

    Description:

    Desmin Human Recombinant

    Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    Product # :

    PRO-520

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    Description

    Desmin Human Recombinant having a calculated molecular mass of 53,539 Dalton, showing a 55kDa band on SDS-page, pI-5.16.

    Source

    Escherichia Coli.

    Formulation

    Desmin was lyophilized from a 1mg/ml solution containing 30mM Tris-HCl pH 8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Desmin is a muscle-specific class III intermediate filament. Homopolymers of this protein form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. Mutations in this gene are associated with desmin-related myopathy, a familial cardiac and skeletal myopathy (CSM), and with distal myopathies.

    • Synonyms

      Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.

    • Solubility

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

    • Reconstitution to filaments

      After Desmin is dissolved in 9.5M urea buffer (see formulation), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Tris-HCl, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

    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.

    Desmin Human
  • View Data Sheet

    Name :

    FGFR2 Human

    Description:

    Fibroblast Growth Factor Receptor 2 Fc Chimera Human Recombinant

    Keratinocyte growth factor receptor 2, CD332, FGFR2.

    Product # :

    PKA-231

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    Description

    Soluble FGFR-2a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain containing 602 amino acids and having a molecular mass of 170 kDa. The FGFR2 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    CD332 was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its ability to inhibit human FGF-2 dependent proliferation on HUVE cells. The ED50 for this effect is typically at 15 - 30ng/ml. 

    Citations

    More Info

    • Introduction

      Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.

    • Synonyms

      Keratinocyte growth factor receptor 2, CD332, FGFR2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGFR2A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFR2 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 FGFR-2 in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      RPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWT KDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVT DAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKF RCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNY TCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVY SDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVT FEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEDPRRASIE GRGDPEEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTC VVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDW LNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSL TCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW QQGNVFSCSVMHEALHNHYTQKSLSLSPGK

    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.

    Fgfr2 Human
  • View Data Sheet

    Name :

    CST11 Human

    Description:

    Cystatin 11 Human Recombinant

    CST8L, CTES2, dJ322G13.6, SC13.

    Product # :

    PRO-1475

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    Description

    CST11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (26-103 a.a.) and having a molecular mass of 11.8kDa.CST11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CST11 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cystatin 11 (CST11) is a member of the Cystatin family. The Cystatin superfamily is comprised of proteins with multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, other family members have lost or perhaps never developed this inhibitory activity. The Cystatin superfamily consists of three inhibitory families, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. The majority of the type 2 cystatin genes and pseudogenes are contained in the cystatin locus on chromosome 20. CST11 is located in the cystatin locus and encodes an epididymal-specific protein whose specific function has not been verified yet.

    • Synonyms

      CST8L, CTES2, dJ322G13.6, SC13.

    • 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 MGSARKKTFL SVHEVMAVEN YAKDSLQWIT DQYNKESDDK YHFRIFRVLK VQRQQVNCFF SVFAVPWFEQ YKILNKSCSS D.

    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.

    Cst11 Human
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