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Search results

390 results found for “bartonella h.”

Name

Description

Product #

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  • View Data Sheet

    Name :

    IL 1 beta Human, His

    Description:

    Interleukin-1 beta Human Recombinant, His Tag

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

    Product # :

    CYT-480

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
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    Description

    Interleukin-1 beta His-Tag Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 153 amino acids fragment (117-269) and having a total molecular mass of 21.88 kDa fused with an amino-terminal hexahistidine tag. The IL-1b His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL-1b His tag protein solution is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-1b is a potent pro-inflammatory cytokine produced by a wide variety of cell types including monocytes and macrophages. It displays a broad range of biological activity including activation of B and T cells in response to inflammation and the activation of endothelial cells.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV

      QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME

      KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS

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

    Il 1 Beta Human His
  • View Data Sheet

    Name :

    IL 28A Mouse

    Description:

    Interleukin-28A Mouse Recombinant

    IFN-lambda-2, Interleukin-28A, IL-28A, Ifnl2, Il28a, EG330496.

    Product # :

    CYT-741

    Price :

    Quantity :

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    Shipped at Room temp

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    • description
    • source
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    • More Info

    Description

    Recombinant Mouse Interleukin-28A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a total molecular mass of 19.7kDa.The IL-28A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Mouse IL-28A is lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 and 5% trehalose.

    Purity

    Greater than 95% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by an anti-viral assay using human HepG2 cells infected with encephalomyocarditis(EMC) virus is less than 3 ng/ml, corresponding to a specific activity of > 3.3 × 105 IU/mg.

    More Info

    • Introduction

      IL-28A is distantly related to the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
      IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
      IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
      IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.

    • Synonyms

      IFN-lambda-2, Interleukin-28A, IL-28A, Ifnl2, Il28a, EG330496.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN-Lambda 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 2 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 IL-28A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DPVPRATRLP VEAKDCHIAQ FKSLSPKELQ AFKKAKDAIE KRLLEKDMRC SSHLISRAWD LKQLQVQERP KALQAEVALT LKVWENMTDS ALATILGQPL HTLSHIHSQL QTCTQLQATA EPKPPSRRLS RWLHRLQEAQ SKETPGCLED SVTSNLFRLL TRDLKCVASG DQCV.

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

    Il 28A Mouse
  • View Data Sheet

    Name :

    IL 29 Human

    Description:

    Interleukin-29 Human Recombinant

    Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.

    Product # :

    CYT-603

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    IL-29 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2 μm filtered solution containing no additives.

    Purity

    Greater than 90% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      IL-29 is distantly related to type I IFNs and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
      IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
      IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
      IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
      IFN-Lambda 1 antiviral and antiproliferative activity requires IFN-Lambda 2 receptor tyrosine residues.

    • Synonyms

      Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN-Lambda 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 1 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 IL-29 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GPVPTSKPTTT GKGCHIGRFK SLSPQELASF KKARDALEES LKLKNWSCSS PVFPGNWDLR LLQVRERPVA LEAELALTLK VLEAAAGPAL EDVLDQPLHTLHHILSQLQA CIQPQPTAGP RPRGRLHHWL HRLQEAPKKE SAGCLEASVT FNLFRLLTRD LKYVADGNLC LRTSTHPEST.

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

    Il 29 Human
  • View Data Sheet

    Name :

    AHA1 Antibody

    Description:

    Activator of HSP90 ATPase-1, Mouse Anti Human

    AHSA1, ACA1, p38, C14orf3, Activator of HSP90 ATPase-1.

    Product # :

    ANT-611

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      AHA1 is a cochaperone that stimulates hsp90 ATPase activity. AHSA1 binds the middle domain of Hsp90 (amino acid 272-627) and functions as an ATPase-activating protein that competes with p23 and other co-chaperones for Hsp90 binding.
      AHA1 affects a step in the endoplasmic reticulum to golgi trafficking.

    • Synonyms

      AHSA1, ACA1, p38, C14orf3, Activator of HSP90 ATPase-1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human AHA1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human AHA1 protein 19-337 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT3E9AT.

    • Applications

      AHA1 antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution for Western blot analysis is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      AHA1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Aha1 Antibody
  • View Data Sheet

    Name :

    GAPDH Antibody

    Description:

    Glyceraldehyde-3-Phosphate Dehydrogenase, Mouse Anti Human

    G3PD, GAPD, MGC88685, GAPDH, Glyceraldehyde-3-Phosphate Dehydrogenase.

    Product # :

    ANT-005

    Price :

    Quantity :

    Shipping Method :

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    • formulation
    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    More Info

    • Introduction

      GAPDH is a catalytic enzyme normally known to play a role in glycolysis. GAPDH exists as a tetramer composed of 36-kDa subunits and has a range of intracellular functions. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Besides functioning as a glycolytic enzyme in cytoplasm, GAPDH has function in intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and DNA repair. GAPDH catalyzes a vital energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains.

    • Synonyms

      G3PD, GAPD, MGC88685, GAPDH, Glyceraldehyde-3-Phosphate Dehydrogenase.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human GAPDH mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GAPDH amino acids 1-335 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT8G4AT.

    • Applications

      GAPDH antibody has been tested by ELISA, Western blot and Immunofluorescence analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis and Immunofluorescence is 1:500 ~ 10,000.
      Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      GAPDH 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.

    Gapdh Antibody
  • View Data Sheet

    Name :

    Ornipressin

    Description:

    Ornipressin

    Product # :

    HOR-036

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    Description

    Ornipressin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1042.19 Dalton and a Molecular formula of C45H63N13O12 S2.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Orn-Gly-NH2.

    • Background

      Ornipressin, a naturally occurring non-mammalian vasopressin analogue, has been recognized for its role in vasoconstriction and antidiuresis, making it an invaluable agent in certain clinical settings (Holmes et al., 2003). This paper aims to comprehensively review ornipressin's biochemical properties, its clinical applications, and potential future directions for therapeutic use.

      Ornipressin is characterized by its strong vasopressin V1 receptor agonist activity, resulting in intense vasoconstriction. It also exhibits antidiuretic properties through the activation of V2 receptors in the renal collecting ducts, albeit to a lesser extent compared to vasopressin (Evans & Davidson, 1964).

      Clinical applications of ornipressin are mainly driven by its potent vasoconstrictor activity. It has shown promise in managing esophageal variceal bleeding, where its vasoconstrictive properties help achieve hemostasis (Bosch et al., 2004).

      Furthermore, it has been used as a rescue therapy in vasodilatory shock, where traditional vasoconstrictors may have limited effect (Morelli et al., 2005).
      As our understanding of ornipressin continues to expand, future research is directed toward fine-tuning its application in various clinical scenarios and exploring potential new therapeutic roles. Current research is investigating the possible neuroprotective role of ornipressin in conditions such as cerebral ischemia (Uchida et al., 2010).

      Ornipressin, with its robust vasoconstrictor and antidiuretic properties, plays a crucial role in managing certain clinical situations. As we continue to explore this intriguing compound, its therapeutic potential appears to be far-reaching, warranting continued research in this field

    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.

    Ornipressin
  • View Data Sheet

    Name :

    CFH Rat

    Description:

    Complement Factor H Rat

    Complement factor H, H factor 1, CFH, HF, HF1, HF2.

    Product # :

    PRO-2709

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    Description

    Rat Complement Factor H produced in Rat plasma having a total molecular mass of 155kDa.

    Source

    Rat Plasma.

    Formulation

    CFH protein solution contains phosphate Buffered Saline, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement factor H (CFH) is an important regulatory component of the alternative pathway of complement. CFH is prevents complement activation on host cells and tissues, mainly the kidney. CFH controls the formation and decay of the alternative pathway C3/C5 convertase and acts as a cofactor for factor I which proteolytically inactivates C3b when C3b is bound to factor H. The N-terminal 5 domains of CFH bind to C3b and inhibit binding of factor B thus reducing the formation of C3/C5 convertase. CFH also binds to preformed C3/C5 convertases and causes quick release of the catalytic subunit Bb. These activities are necessary for controlling the spontaneous activation of the alternative pathway amplification process in plasma. In addition, CFH controls the formation and decay of these enzymes when C3b is attached to the surface of particles.

    • Synonyms

      Complement factor H, H factor 1, CFH, HF, HF1, HF2.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFH Rat is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    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.

    Cfh Rat
  • View Data Sheet

    Name :

    Rubella Virus Capsid

    Description:

    Rubella Virus Capsid Recombinant

    Product # :

    RUB-294

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    Description

    The E.Coli derived recombinant Rubella Virus Capsid is a 35kDa protein which is fused to a His tag in N-terminus.

    Source

    Escherichia Coli.

    Formulation

    25mM K2CO3 and PBS.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Rubella Virus Capsid although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Background

      The Rubella Capsid Protein is responsible for encapsidating the viral RNA genome, forming the nucleocapsid structure, which is crucial for viral assembly and replication. Studies using recombinant capsid protein have demonstrated its ability to self-assemble into virus-like particles (VLPs), which mimic the native structure of the virus and are valuable for studying viral assembly. The capsid protein is a major target of the host immune response during rubella infection. Recombinant Rubella Capsid Protein has been used to investigate the humoral and cellular immune responses it elicits. Understanding these immune responses is critical for improving vaccine design and developing diagnostic assays to detect rubella-specific antibodies.

    • Specificity

      Immunoassay.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    product_image.jpg
  • View Data Sheet

    Name :

    UBE2H Human

    Description:

    Ubiquitin-Conjugating Enzyme E2H Human Recombinant

    Ubiquitin-conjugating enzyme E2 H, UbcH2, Ubiquitin carrier protein H, Ubiquitin-conjugating enzyme E2-20K, Ubiquitin-protein ligase H, UBE2H, GID3, UBC8, UBCH.

    Product # :

    ENZ-603

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    Description

    UBE2H Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-183) and having a molecular mass of 23.1kDa.UBE2H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2H solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-conjugating enzyme E2 H (UBE2H) is a member of the ubiquitin-conjugating enzyme family. Protein modification with ubiquitin is a vital cellular apparatus for directing abnormal or short-lived proteins for degradation. Ubiquitination requires at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2H receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2H protein sequence is 100% identical to the mouse homolog and 98% identical to the frog and zebrafish homologs.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 H, UbcH2, Ubiquitin carrier protein H, Ubiquitin-conjugating enzyme E2-20K, Ubiquitin-protein ligase H, UBE2H, GID3, UBC8, UBCH.

    • 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 MGSMSSPSPG KRRMDTDVVK LIESKHEVTI LGGLNEFVVK FYGPQGTPYE GGVWKVRVDL PDKYPFKSPS IGFMNKIFHP NIDEASGTVC LDVINQTWTA LYDLTNIFES FLPQLLAYPN PIDPLNGDAA AMYLHRPEEY KQKIKEYIQK YATEEALKEQ EEGTGDSSSE SSMSDFSEDE AQDMEL.

    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.

    Ube2H Human
  • View Data Sheet

    Name :

    TARS Human

    Description:

    Threonyl-tRNA Synthetase Human Recombinant

    Threonine--tRNA ligase, cytoplasmic, Threonyl-tRNA synthetase, ThrRS, TARS.

    Product # :

    ENZ-571

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    Description

    TARS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 743 amino acids (1-723) and having a molecular mass of 85.6kDa.TARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TARS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 150mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Threonyl-tRNA synthetase, cytoplasmic (TARS) is a member of the class-II aminoacyl-tRNA synthetase family. The main role of TARS is in tRNA aminoacylation. The N-terminal domain of the TARS enzyme is responsible for the competition with the ribosome whereas the catalytic and the C-terminal domain are involved in binding the 2 anticodon arm-like structures in the operator.

    • Synonyms

      Threonine--tRNA ligase, cytoplasmic, Threonyl-tRNA synthetase, ThrRS, TARS.

    • 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 MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW PEYIYTRLEM YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE NGFYYDMYLE EGGVSSNDFS SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP
      GSCFFLPKGA YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE EEF.

    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.

    Tars Human
  • View Data Sheet

    Name :

    SCGB1A1 Human, His

    Description:

    Uteroglobin Human Recombinant, His Tag

    Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

    Product # :

    CYT-752

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    Description

    Uteroglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 9.2kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.

    • Synonyms

      Uteroglobin, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, Secretoglobin family 1A member 1, Urinary protein 1, UP-1, UP1, Urine protein 1, SCGB1A1, CCSP, UGB, CC16.

    • 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 deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SCGB1A1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASEICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN.

    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.

    Scgb1A1 Human His
  • View Data Sheet

    Name :

    ECHS1 Human

    Description:

    Enoyl CoA Hydratase, Short chain, 1, Mitochondrial Human Recombinant

    Enoyl-CoA hydratase 1, SCEH.

    Product # :

    ENZ-556

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    Description

    ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a.) and having a molecular mass of 30.6kDa.ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ECHS1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT,0.1M NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

    • Synonyms

      Enoyl-CoA hydratase 1, SCEH.

    • 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 MASGANFEYI IAEKRGKNNT VGLIQLNRPK ALNALCDGLI DELNQALKIF EEDPAVGAIV LTGGDKAFAA GADIKEMQNL SFQDCYSSKF LKHWDHLTQV KKPVIAAVNG YAFGGGCELA MMCDIIYAGE KAQFAQPEIL IGTIPGAGGT QRLTRAVGKS LAMEMVLTGD RISAQDAKQA GLVSKICPVE TLVEEAIQCA EKIASNSKIV VAMAKESVNA AFEMTLTEGS KLEKKLFYST FATDDRKEGM TAFVEKRKAN FKDQ.

    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.

    Echs1 Human
  • View Data Sheet

    Name :

    HBeAg

    Description:

    Hepatitis B Virus e-Antigen Recombinant

    Product # :

    HBV-272

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    Description

    Recombinant hepatitis B virus “e” antigen is fused to a His Tag and having a molecular mass of approximately 18kDa.

    Source

    Escherichia Coli.

    Formulation

    20mM Tris-Hcl, 0.5M NaCl and 0.8M imidazole.

    Purity

    Protein is >95%

    More Info

    • Introduction

      Hepatitis B virus is the main cause for human liver disease, chronic infection frequently causes liver cancer and cirrhosis. The HBV core gene codes 2 distinct protein products, a 21.5-kDa protein being assembled to form nucleocapsid particles designated HBcAg, which wraps the viral DNA as well as the viral polymerase and RNase H, and a precore protein, designated as HBeAg, which is directly to the endoplasmic reticulum, processed at N- and C-terminally and secreted as non-particulate e-anitgen (HBeAg). The pre-core protein contains an extra 29 N-terminal amino acids, serving as a signal peptide to direct the nascent polypeptide into secretory pathway. After the secretion, mature HBeAg is deleted at the residue 149 C-terminally and retains 10 precore residues N-terminally. HBcAg and HBeAg are distinctly recognized by antibodies but highly cross-reactive at the T-cell level.
      The e antigen is found in the circulation, it is found during the active HBV infection, positive result indicates the risk for contagiousness, and is also used as indicator for the effectiveness of HBV treatment. Positive anti-HBeAg specifies an active stage of acute HBV infection that is in its final stages, the risk for contagiousness is dramatically reduced.

    • Stability

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

    • Amino Acid Sequence

      s klclgwlwgm didpykefga svellsflps dffpsirdll dtasalyrea lespehcsph htalrqailc

      wgelmnlatw vgsnledpas relvvsyvnv nmglkirqll wfhiscltfg retvleylvs fgvwirtpta

      yrppnapils tlpettvv

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    Hbeag
  • View Data Sheet

    Name :

    T.pallidum TmpA partial

    Description:

    Treponema pallidum TmpA (partial) Recombinant

    Product # :

    TRP-245

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    Description

    The E.Coli derived 68kDa recombinant protein contains the Trp. Pallidum TmpA immunodominant regions, 23-41 amino acids and 288-325 amino acids.

    Source

    Escherichia Coli.

    Formulation

    10mM Tris-HCl pH8.0, 20mM DDT, 1mM EDTA and 8M urea.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Stability

      T.pallidum TmpA partial although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      This protein binds to murine anti-TmpA protein monoclonal antibodies and Treponema pallidum converted human serum polyclonal antibodies in ELISA and Western Elisa. Dot Blots and Lateral Flow immunochromatographic diagnostics test.

    • Specificity

      Immunoreactive with sera of Trp. Pallidum infected individuals.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    Tpallidum Tmpa Partial
  • View Data Sheet

    Name :

    HFE Human

    Description:

    Hemochromatosis Human Recombinant

    Hereditary hemochromatosis protein, HLA-H, HFE, HLAH, HH, HFE1, MVCD7, TFQTL2.

    Product # :

    PRO-1332

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    Description

    HFE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (23-306 a.a) and having a molecular mass of 35.7kDa.HFE is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hemochromatosis (HFE) is a member of the MHC class I family. The Hemochromatosis protein contains 1 Ig-like C1-type (immunoglobulin-like) domain. HFE is a membrane protein, which is similar to MHC class I-type proteins and associates with beta-2 microglobulin (beta2M). It is assumed that the HFE protein acts to regulate iron absorption by regulating the interaction of the transferrin receptor (TFR) with transferrin. HFE binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin.

    • Synonyms

      Hereditary hemochromatosis protein, HLA-H, HFE, HLAH, HH, HFE1, MVCD7, TFQTL2.

    • 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 MGSMRLLRSH SLHYLFMGAS EQDLGLSLFE ALGYVDDQLF VFYDHESRRV EPRTPWVSSR ISSQMWLQLS QSLKGWDHMF TVDFWTIMEN HNHSKESHTL QVILGCEMQE DNSTEGYWKY GYDGQDHLEF CPDTLDWRAA EPRAWPTKLE WERHKIRARQ NRAYLERDCP AQLQQLLELG RGVLDQQVPP LVKVTHHVTS SVTTLRCRAL NYYPQNITMK WLKDKQPMDA KEFEPKDVLP NGDGTYQGWI TLAVPPGEEQ RYTCQVEHPG LDQPLIVIWE PSPSGTLV.

    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.

    Hfe 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.

    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.

    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 :

    Betacellulin Bovine

    Description:

    Betacellulin Bovine Recombinant

    Product # :

    CYT-406

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    Description

    Betacellulin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9003 Dalton. Betacellulin Bovine Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Betacellulin Bovine Recombinant was lyophilized after extensive dialysis against 50mM acetic acid.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Betacellulin Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Bovine 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 BTC Bovine 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 Asp-Gly-Asn-Ser-Thr.

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 9kDa.

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

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

      What is the Biological Activity of BETACELLULIN Protein?
      The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

      What is the amino acid sequence of BETACELLULIN Protein?
      BETACELLULIN Protein is composed from 80 amino acids.

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

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

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.59 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 BTC 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.

    Betacellulin Bovine
  • View Data Sheet

    Name :

    HBsAg adr CHO

    Description:

    Hepatitis B Surface Antigen, adr CHO Recombinant

    Product # :

    HBS-875

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    Description

    Recombinant HBsAg adr produced in CHO cells, the molecular weight is approximately 23-27kDa.

    Source

    CHO.

    Formulation

    Sterile Filtered solution containing 20mM PB and 154mM NaCl.

    Purity

    Greater than 95.0% as determined by RP-HPLC.

    More Info

    • Introduction

      HBsAg is the surface antigen of the Hepatitis-B-Virus (HBV) S-gene. The capsid of a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      HBsAg Should be stored at 4°C, DO NOT FREEZE.

    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.

    Hbsag Adr Cho
  • View Data Sheet

    Name :

    GDF5 Mouse, His

    Description:

    Growth differentiation factor 5 Mouse Recombinant, His Tag

    Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.

    Product # :

    CYT-852

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    Description

    GDF5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (376-495 a.a) and having a molecular mass of 16kDa.GDF5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    GDF5-sds-page - Product image 1

    More Info

    • Introduction

      GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.

    • Synonyms

      Bmp-14, Bp, GDF-5, Bone morphogenetic protein 14, GDF5.

    • 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 MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.

    • Background

      What is the molecular weight/Mw of GDF5 MOUSE Protein?
      GDF5 MOUSE Protein has a total Mw of 16kDa.

      What is the source or expression system of GDF5 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of GDF5 MOUSE Protein?
      GDF5 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF5 MOUSE Protein?
      The biological functionality of GDF5 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of GDF5 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSAPLANRQ GKRPSKNLKA RCSRKALHVN FKDMGWDDWI IAPLEYEAFH CEGLCEFPLR SHLEPTNHAV IQTLMNSMDP ESTPPTCCVP TRLSPISILF IDSANNVVYK QYEDMVVESC GCR.

      What applications can GDF5 MOUSE Protein be used in?
      GDF5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF5 MOUSE Protein?
      The endotoxin level is minimal, GDF5 MOUSE 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.

    Gdf5 Mouse
  • View Data Sheet

    Name :

    IFNG Human, His

    Description:

    Interferon-Gamma Human Recombinant, His Tag

    Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

    Product # :

    CYT-478

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    • SDS-PAGE

    Description

    IFN-Gamma Human Recombinant produced in E.Coli is a single, glycosylated polypeptide chain containing 159 amino acids (24-161 a.a) without cysteine residues and having a molecular mass of 18.5kDa (confirmed by MALDI-TOF). IFN-Gamma is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interferon-g is supplied in phosphate-buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    SDS-PAGE

    IFNG  Human - Product image 1

    More Info

    • Introduction

      IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
      IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.

    • Synonyms

      Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.

    • Background

      What is the molecular weight/Mw of IFNG HUMAN, HIS Protein?
      IFNG HUMAN, HIS Protein has a total Mw of 18.5kDa.

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

      What is the Purity of IFNG HUMAN, HIS Protein?
      IFNG HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of IFNG HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.

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

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

    Interferon Gamma Human His
  • View Data Sheet

    Name :

    IL 3 Dog

    Description:

    Interleukin-3 Canine Recombinant

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

    Product # :

    CYT-722

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    Description

    Interleukin-3 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 14 kDa. The IL-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 1X PBS pH7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      RPFSTDLPKQ YFTMINEIME MLNKSPSPSE EPLDSNEKET LLEDTLLRPN LDVFLNASSK FHKNGLLIWN NLKEFLPLLP TPTPRGEPIS IMENNWGDFQ RKLKKYLEAL DNFLNFKNKP.

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

    Il 3 Dog
  • View Data Sheet

    Name :

    HB-EGF Mouse

    Description:

    HB-EGF Mouse Recombinant

    DTR, HEGFL, diphtheria toxin receptor, DTSF.

    Product # :

    CYT-068

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    Description

    HB-EGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids (63-148 a.a.) and having a molecular mass of 9.8 kDa.The HB-EGF is purified by proprietary chromatographic techniques

    Source

    Escherichia Coli.

    Formulation

    The protein was filtered (0.2µm) and lyophilized from a concentrated solution containing 10mM PB and 500mM NaCl, pH7.4.

    Purity

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

    Biological Activity

    The ED50 was determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.

    sds-page

    HB-EGF Mouse SDS-PAGE - Product image 1

    More Info

    • Introduction

      HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.

    • Synonyms

      DTR, HEGFL, diphtheria toxin receptor, DTSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL.

    • Background

      What is the molecular weight/Mw of HB-EGF Protein?
      HB-EGF Protein has a total Mw of 9.8kDa.

      What is the source or expression system of HB-EGF Protein?
      Escherichia Coli.

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

      What is the Biological Activity of HB-EGF Protein?
      The ED50 was determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.

      What is the amino acid sequence of HB-EGF Protein?
      DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL.

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

      What is the endotoxin level for HB-EGF Protein?
      The endotoxin level is minimal, HB-EGF 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.

    Hb Egf Mouse
  • View Data Sheet

    Name :

    BACE2 Mouse, HEK

    Description:

    Beta-Secretase 2 Mouse Recombinant, HEK

    BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

    Product # :

    ENZ-1188

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    Description

    BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa. BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    BACE2 (0.25mg/ml) is filtered in 10% (w/v) glycerol and Phosphate-Buffered Saline pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20 pmol/min/ug in which one unit will convert 1.0pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to Mca- Pro-Leu-OH per minute at pH 3.5 at 25C.

    More Info

    • Synonyms

      BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

    • Physical Appearance

      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

      AVPALAPAPF TLPLQVARAT NHRASAVPGL GTPELPRADG LALALEPVRA TANFLAMVDN LQGDSGRGYY LEMLIGTPPQ KVQILVDTGS SNFAVAGAPH SYIDTYFDSE SSSTYHSKGF DVTVKYTQGS WTGFVGEDLV TIPKGFNSSF LVNIATIFES ENFFLPGIKW NGILGLAYAA LAKPSSSLET FFDSLVAQAK IPDIFSMQMC GAGLPVAGSG TNGGSLVLGG IEPSLYKGDI

      WYTPIKEEWY YQIEILKLEI GGQNLNLDCR EYNADKAIVD SGTTLLRLPQ KVFDAVVEAV ARTSLIPEFS DGFWTGAQLA CWTNSETPWA YFPKISIYLR DENASRSFRI TILPQLYIQP MMGAGFNYEC YRFGISSSTN ALVIGATVME GFYVVFDRAQ RRVGFAVSPC AEIEGTTVSE ISGPFSTEDI ASNCVPAQAL NEP HHHHHH.

    • Background

      BACE2 protein, a member of the beta-secretase family, has gained attention as a key player in the pathogenesis of neurological disorders, particularly Alzheimer's disease. This research aims to explore the function and potential therapeutic implications of BACE2 protein in neurodegenerative conditions. Understanding the role of BACE2 protein can provide valuable insights into its significance as a therapeutic target for the development of novel treatment strategies.

      Function of BACE2 Protein:

      BACE2 is a transmembrane aspartic protease predominantly expressed in the central nervous system. It exhibits distinct cleavage activity on various protein substrates, including neuregulins, APP-like proteins, and TGF-β. Unlike its close homolog BACE1, BACE2 has been proposed to have non-amyloidogenic processing capabilities and has shown potential neuroprotective effects.

      Implications of BACE2 Protein in Alzheimer's Disease:

      Alzheimer's disease is characterized by the accumulation of amyloid-beta (Aβ) peptides in the brain, which are generated through the sequential cleavage of amyloid precursor protein (APP). BACE1 is primarily responsible for the cleavage of APP, leading to the production of toxic Aβ peptides. In contrast, BACE2 has been suggested to compete with BACE1, thereby reducing the levels of Aβ generation. This has led to speculation about the neuroprotective role of BACE2 and its potential as a therapeutic target for Alzheimer's disease.

      BACE2 Protein and Neuronal Survival:

      Emerging evidence suggests that BACE2 may play a role in promoting neuronal survival and function. Studies have shown that BACE2 deficiency leads to impaired synaptic plasticity, reduced dendritic branching, and altered neurotransmitter release. BACE2 has also been implicated in the regulation of axonal growth and guidance during development. These findings highlight the potential importance of BACE2 in maintaining neuronal integrity.

      Association of BACE2 Protein with Other Neurological Disorders:

      Apart from Alzheimer's disease, BACE2 has been implicated in other neurological conditions as well. Genetic studies have identified BACE2 gene variants associated with an increased risk of Parkinson's disease, suggesting its involvement in the pathogenesis of this disorder. Furthermore, BACE2 has been linked to the regulation of insulin signaling and glucose homeostasis, making it a potential target for diabetes-associated cognitive decline.

      Therapeutic Implications of BACE2 Protein:

      Given its potential neuroprotective effects and modulatory role in amyloid processing, BACE2 protein has emerged as a promising therapeutic target for neurodegenerative disorders. Strategies aimed at enhancing BACE2 activity or selectively activating BACE2-mediated non-amyloidogenic processing pathways hold promise for reducing amyloid pathology and preserving neuronal function. However, further research is needed to better understand the complex mechanisms underlying BACE2 function and to develop safe and effective therapeutic interventions.

      Conclusion:

      The investigation of BACE2 protein has provided valuable insights into its role in neurodegenerative diseases, particularly Alzheimer's disease. The potential neuroprotective effects and modulation of amyloid processing pathways by BACE2 make it an intriguing therapeutic target. Future studies should focus on unraveling the precise mechanisms by which BACE2 influences disease pathogenesis and developing strategies to harness its therapeutic potential. The exploration of BACE2 protein opens new avenues for the development of innovative treatment approaches for neurodegenerative disorders.

    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.

    Bace2 Mouse Hek
  • View Data Sheet

    Name :

    BLyS Human, Plant

    Description:

    BAFF (BLyS) Human Recombinant, Plant

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-054

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    • More Info

    Description

    BAFF human Recombinant produced in Nicotiana benthamiana plant is a single glycosilated polypeptide chain containing 151 amino acids fragment (134-285).BAFF (C830H1277N223O242S5) is fused to a 10-His-tag at the N-terminal having the total molecular mass of 18-20kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 20 mM PBS buffer pH 7 and 0.2 M NaCl.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
    *activity results may vary with PBMC donors.
    ED50 ? 50ng/ml

    More Info

    • Introduction

      BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity.A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 19kDa.

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

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

      What is the Biological Activity of BLYS Protein?
      The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.

      What is the amino acid sequence of BLYS Protein?
      HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL

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

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

    Baff Human Plant
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