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  • View Data Sheet

    Name :

    BD 1 Rat

    Description:

    Beta Defensin -1 Rat Recombinant

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

    Product # :

    CYT-062

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BD-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized BD-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.

    • Background

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

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

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

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

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

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

      What is the endotoxin level for BD1 Protein?
      The endotoxin level is minimal, BD1 Protein was purified using conventional chromatography techniques.

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

    Bd 1 Rat
  • View Data Sheet

    Description:

    Beta Defensin-3 Human Recombinant

    HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.

    Product # :

    CYT-461

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    Description

    Beta Defensin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 45 amino acids and having a molecular mass of 5161.2 Dalton. The BD-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HBD-3 was lyophilized without additives.

    Purity

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

    More Info

    • Introduction

      Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.

    • Synonyms

      HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.

    • Background

      Beta Defensin-3 Human Recombinant: Advancements in Antimicrobial Peptide Therapy

      Abstract:


      Beta Defensin-3 (hBD-3) human recombinant is a promising antimicrobial peptide with broad-spectrum activity against bacteria, viruses, and fungi. This research paper provides an overview of hBD-3, including its properties, mode of action, and potential applications. Additionally, novel methodologies for the production and optimization of hBD-3 human recombinant are discussed, highlighting its future implications in the field of infectious disease management.

      Introduction:


      The rise of drug-resistant pathogens necessitates exploring alternative therapeutic approaches, such as antimicrobial peptides. Beta Defensin-3 (hBD-3) human recombinant has emerged as a potent candidate due to its broad-spectrum antimicrobial activity. This paper aims to examine the unique features of hBD-3 and propose innovative methodologies for its production and optimization.

      Properties and Mode of Action:


      hBD-3 possesses a distinct structural composition consisting of 45 amino acids, including an N-terminal loop, three antiparallel β-strands, and a C-terminal α-helix. These structural elements contribute to its ability to disrupt microbial membranes and target selectivity. The mode of action involves electrostatic interactions with negatively charged microbial membranes, leading to membrane disruption and subsequent cell death. Furthermore, hBD-3 exhibits immunomodulatory functions by promoting chemotaxis, enhancing phagocytic activity, and modulating the release of pro-inflammatory cytokines.

      Production of hBD-3 Human Recombinant:


      Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored for the efficient production of hBD-3 human recombinant. Each system offers distinct advantages and challenges, requiring careful selection to achieve high yields and desired protein quality. Optimization strategies, including codon optimization, fusion protein tags, and appropriate growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-3 recombinant.

      Applications and Future Perspectives:


      hBD-3 human recombinant exhibits significant therapeutic potential against drug-resistant pathogens, making it a promising alternative to conventional antibiotics. It also demonstrates promise in wound healing and tissue regeneration by stimulating angiogenesis, extracellular matrix production, and keratinocyte migration. Moreover, the unique physicochemical properties of hBD-3 open avenues for its utilization in nanomedicine, enabling targeted therapy and improved drug delivery.

      Conclusion:


      hBD-3 human recombinant represents a potent antimicrobial peptide with broad-spectrum activity against diverse pathogens. The optimization of production methodologies and further exploration of its mechanisms of action will contribute to its clinical utility. With its potential applications in infectious disease management, wound healing, and nanomedicine, hBD-3 human recombinant holds promise as a versatile therapeutic agent.

      What is the molecular weight/Mw of BD3 Protein?
      BD3 Protein has a total Mw of 5.1kDa.

      What is the source or expression system of BD3 Protein?
      Escherichia Coli.

      What is the Purity of BD3 Protein?
      BD3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD3 Protein?
      The biological functionality of BD3 Protein will be determined in the future.

      What is the amino acid sequence of BD3 Protein?
      GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.

      What applications can BD3 Protein be used in?
      BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD3 Protein?
      The endotoxin level is minimal, BD3 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.

    Beta Defensin 3 Human
  • View Data Sheet

    Description:

    Human Clusterin

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    Product # :

    CYT-548

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    Source

    Plasma.

    Formulation

    Human native Clusterin was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.1M phosphate buffer, 0.15M NaCl pH 7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Clusterin 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 H2O to prepare a working stock solution of 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.

    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.

    Clusterin Human
  • View Data Sheet

    Description:

    P-selectin Human Recombinant

    P-selectin, Granule membrane protein 140, GMP-140, PADGEM, Leukocyte-endothelial cell adhesion molecule 3, LECAM3, CD62 antigen-like family member P, CD62P antigen, SELP, GMRP, GRMP, CD62, PSEL, CD62P, GMP140, FLJ45155.

    Product # :

    PRO-382

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    Description

    P-Selectin Human Recombinant is expressed in E. coli containing 566 amino acids 197-761 fused to an amino terminal hexahistidine tag.

    Source

    Escherichia Coli.

    Formulation

    P-Selectin is supplied in 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    More Info

    • Introduction

      P-Selectin also called Platelet Alpha-Granule Membrane Protein, CD62, and Granulocyte Membrane Protein GRMP belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Pselectin is expressed transiently on the surface of activated platelets and endothelial cells. P-Selectin is a 140 kDa protein which is stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Secreted P-selectin is thought to play a key role in the adhesion of platelets to monocytes and neutrophils during an inflammatory response. P-Selectin is a calcium-dependent receptor that binds to sialylated forms of Lewis blood group carbohydrate antigens on neutrophils and monocytes. Levels of P-Selectin may be elevated in a number of pathological conditions.

    • Synonyms

      P-selectin, Granule membrane protein 140, GMP-140, PADGEM, Leukocyte-endothelial cell adhesion molecule 3, LECAM3, CD62 antigen-like family member P, CD62P antigen, SELP, GMRP, GRMP, CD62, PSEL, CD62P, GMP140, FLJ45155.

    • Physical Appearance

      Sterile Filtered liquid formulation.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Applications

      P-Selectin can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    P Selectin Human
  • View Data Sheet

    Description:

    Actinin Alpha

    Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.

    Product # :

    PRO-518

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    Description

    Ultra pure Alpha Actinin having a Molecular mass of 95,000 Dalton.

    Source

    Chicken Gizzard.

    Formulation

    The protein was lyophilized from a 1mg/ml solution containing 10mM Tris acetate buffer pH 7.6, 0.1mM EDTA, 2mM DTT, and 20mM NaCl.

    Purity

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

    More Info

    • Introduction

      ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

    • Synonyms

      Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      Protein standard in 1D and 2D SDS gelelectrophoresis
      Immunoassays
      Immunization.

    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.

    Alpha Actinin
  • View Data Sheet

    Description:

    Intein Bacillus Circulans Recombinant

    Intein-CBD

    Product # :

    PRO-958

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    Description

    Intein Bacillus Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 533 amino acids (3-518) and having a molecular mass of 59.4 kDa.Intein is fused to a 16 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The Intein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Intein is a section of a protein which can remove itself and return the remaining segment with a peptide bond. In addition, Inteins hold an endonuclease domain which takes part in Intein proliferation. Actually, various genes have unrelated intein-coding segments inserted at altered positions and they were found in all three domains of life (eukaryotes, bacteria, and archaea) and in viruses.

    • Synonyms

      Intein-CBD

    • 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

      MKIEEGKLVI GSLEGCFAKG TNVLMADGSI ECIENIEVGN KVMGKDGRPR EVIKLPRGRE TMYSVVQKSQ HRAHKSDSSR EVPELLKFTC NATHELVVRT PRSVRRLSRT IKGVEYFEVI TFEMGQKKAP DGRIVELVKE VSKSYPISEG PERANELVES YRKASNKAYF EWTIEARDLS LLGSHVRKAT YQTYAPILYE NDHFFDYMQK SKFHLTIEGP KVLAYLLGLW IGDGLSDRAT FSVDSRDTSL MERVTEYAEK LNLCAEYKDR KEPQVAKTVN LYSKVVRGAS TNPGVSAWQV NTAYTAGQLV TYNGKTYKCL QPHTSLAGWE PSNVPALWQL QGGHGGIRNN LNTENPLWDA IVGLGFLKDG VKNIPSFLST DNIGTRETFL AGLIDSDGYV TDEHGIKATI KTIHTSVRDG LVSLARSLGL VVSVNAEPAK VDMNVTKHKI SYAIYMSGGD VLLNVLSKCA GSKKFRPAPA AAFARECRGF YFELQELKED DYYGITLSDD SDHQFLLGSQ VVVQNLEHHH HHH

    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.

    Intein Bacillus Circulans
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    Description:

    Leptin Pufferfish Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-530

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    Description

    Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.

    More Info

    • Introduction

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

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE

      GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE

      QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 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).

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

    Leptin Pufferfish
  • View Data Sheet

    Description:

    Hepatitis B Surface Antigen, adw Recombinant

    Product # :

    HBS-872

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    Description

    HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.

    Source

    Pichia Pastoris.

    Formulation

    Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof 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 pale 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 Adw
  • View Data Sheet

    Description:

    Beta Defensin 118 Human Recombinant

    Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    Product # :

    CYT-714

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    • sds-page

    Description

    DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.

    • Synonyms

      Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    • 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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

    • Background

      Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications

      Abstract:


      Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.

      Production and Characterization:


      Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD118.

      Role in Innate Immunity:


      BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.

      Therapeutic Implications:


      Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.

      Conclusion:


      Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.

      What is the molecular weight/Mw of DEFB118 Protein?
      DEFB118 Protein has a total Mw of 13.8kDa.

      What is the source or expression system of DEFB118 Protein?
      Escherichia Coli.

      What is the Purity of DEFB118 Protein?
      DEFB118 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of DEFB118 Protein?
      The biological functionality of DEFB118 Protein will be determined in the future.

      What is the amino acid sequence of DEFB118 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

      What applications can DEFB118 Protein be used in?
      DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for DEFB118 Protein?
      The endotoxin level is minimal, DEFB118 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.

    Defb118 Human
  • View Data Sheet

    Description:

    Resistin Rat Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-1129

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    Description

    Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.

    Purity

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

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.

    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.

    Rat Resistin Protein
  • View Data Sheet

    Name :

    BD 4 Rat

    Description:

    BD 4 Rat

    Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.

    Product # :

    CYT-066

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    Description

    BD-4 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.4kDa.The BD-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BD-4 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.

    More Info

    • Introduction

      Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
      4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
      Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
      In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

    • Synonyms

      Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.

    • Background

      What is the molecular weight/Mw of BD4 Protein?
      BD4 Protein has a total Mw of 4.4kDa.

      What is the source or expression system of BD4 Protein?
      Escherichia Coli.

      What is the Purity of BD4 Protein?
      BD4 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD4 Protein?
      Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.

      What is the amino acid sequence of BD4 Protein?
      QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.

      What applications can BD4 Protein be used in?
      BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD4 Protein?
      The endotoxin level is minimal, BD4 Protein was purified using conventional chromatography techniques.

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

    Bd 4 Rat
  • View Data Sheet

    Name :

    Thymalin

    Description:

    Thymulin

    Product # :

    HOR-047

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    Description

    Thymulin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 858 Dalton and a Molecular formula of C33H54N12O15.

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

    • Amino Acid Sequence

      Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.

    • Background

      Thymulin, a nonapeptide hormone, is produced primarily by the thymus gland and has been recognized for its pivotal role in the immune system. It plays a significant role in the maturation and differentiation of T lymphocytes, which are crucial for immune function. Beyond its immune-related functions, research has increasingly unveiled the diverse physiological roles of thymulin. This study aims to comprehensively investigate thymulin, shedding light on its immunological functions and exploring its potential applications in various aspects of health and medicine.

      The primary objective of this research is to elucidate the mechanisms underlying thymulin's role in immune regulation. In vitro and in vivo experiments will be conducted to explore thymulin's interactions with immune cells, its impact on T cell development and function, and its potential modulation of immune responses. Understanding these mechanisms is fundamental for harnessing thymulin's immunomodulatory properties.

      The second objective is to assess the clinical relevance of thymulin in immune-related disorders. Clinical trials and studies involving individuals with autoimmune diseases, immunodeficiencies, and age-related immune decline will be conducted to evaluate the potential therapeutic applications of thymulin. These investigations may offer insights into the use of thymulin as an immunomodulatory agent in various clinical settings.

      The third objective is to explore the broader implications of thymulin in health and medicine. Research will investigate its potential roles in areas beyond immunology, such as neuroprotection, wound healing, and tissue regeneration. Understanding the multifaceted properties of thymulin may open new avenues for therapeutic interventions in various medical specialties.

      By delving into the diverse functions of thymulin, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may have implications for the development of innovative approaches in immunology and healthcare, ultimately benefiting patients affected by immune-related disorders and other medical conditions.

      What is the molecular weight/Mw of THYMALIN Protein?
      THYMALIN Protein has a total Mw of 0.85kDa.

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

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

      What is the amino acid sequence of THYMALIN Protein?
      Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.

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

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

    Thymulin
  • View Data Sheet

    Description:

    Nectin Cell Adhesion Molecule 1 Human Recombinant

    PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.

    Product # :

    PRO-2648

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    Description

    NECTIN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 334amino acids (31-355a.a) and having a molecular mass of 37.3kDa.NECTIN1 is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The NECTIN1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.

    • Synonyms

      PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.

    • 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

      ADPQVVQVND SMYGFIGTDV VLHCSFANPL PSVKITQVTW QKSTNGSKQN VAIYNPSMGV SVLAPYRERV EFLRPSFTDG TIRLSRLELE DEGVYICEFA TFPTGNRESQ LNLTVMAKPT NWIEGTQAVL RAKKGQDDKV LVATCTSANG KPPSVVSWET RLKGEAEYQE IRNPNGTVTV ISRYRLVPSR EAHQQSLACI VNYHMDRFKE SLTLNVQYEP EVTIEGFDGN WYLQRMDVKL
      TCKADANPPA TEYHWTTLNG SLPKGVEAQN RTLFFKGPIN YSLAGTYICE ATNPIGTRSG QVEVNITEFP YTPSPPEHGR RAGPVPTAHH HHHH

    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.

    Nectin1 Human
  • View Data Sheet

    Description:

    Noggin Human Recombinant

    SYM1, SYNS1, NOG.

    Product # :

    CYT-475

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    Description

    Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect  is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.

    More Info

    • Introduction

      The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
      EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
      RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
      TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC.

    • Background

      Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.

      Abstract:

      Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.

      Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.

      This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.

      Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      1. Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.

      Molecular Characteristics of Noggin :

      1. This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.

      Inhibition of BMP Signaling by Noggin:

      1. Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.

      Physiological Functions of Noggin:

      1. Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.

      Therapeutic Implications of Noggin:

      1. The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.

      Clinical Studies and Translational Research:

      1. This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.

    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.

    Noggin Human
  • View Data Sheet

    Description:

    Furin Human Recombinant

    Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    Product # :

    PRO-2199

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    Description

    FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.

    • Synonyms

      Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.

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    Furin Human
  • View Data Sheet

    Description:

    Bovine Vimentin

    Vimentin, Vim, FLJ36605.

    Product # :

    PRO-525

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    Description

    Bovine Vimentin protein produced in Bovine Lens, having a molecular weight of 57 kDa.

    Source

    Bovine Lens.

    Formulation

    The protein (1mg/ml) was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate pH 7.5, 6M urea, 2mM DTT, 1mM EDTA and 10mM methylammonium chloride.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.

    • Synonyms

      Vimentin, Vim, FLJ36605.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Reconstitution to filaments

      After vimentin is dissolved in 6M urea buffer (see above), 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 Sodium Phosphate, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco''s PBS).- Hatzfeld M. and Franke W.W. (1985). J. Cell Biol. 101, 1826-1841.- Hatzfeld M. et al. (1987). J. Mol. Biol. 197, 237-255.

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    Vimentin Bovine
  • View Data Sheet

    Description:

    Deslorelin

    Product # :

    HOR-240

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    Description

    Deslorelin is a potent LHRH/GnRH agonist has a molecular formula of C64H83N17O12, pGlu-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-NHC2H5 having an Mw of 1284.4 Dalton.

    Formulation

    The Deslorelin peptide was lyophilized with no additives.

    Purity

    Greater than 99.0% as determined by RP-HPLC.

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    • Introduction

      Deslorelin is being studied in the treatment of cancer as a way to block sex hormones made by the ovaries or testicles. It belongs to the family of drugs called gonadotropin-releasing hormone analogs. It is used for the induction of ovulation in mares. Deslorelin binds to and activates pituitary gonadotropin releasing hormone (GnRH) receptors. Continuous, prolonged administration of goserelin in males results in pituitary GnRH receptor desensitization and inhibition of pituitary secretion of follicle stimulating hormone (FSH) and luteinizing hormone (LH), leading to a significant decline in testosterone production; in females, prolonged administration results in a decrease in estradiol production.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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    Deslorelin
  • View Data Sheet

    Description:

    Resistin Human Recombinant, HEK

    RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.

    Product # :

    CYT-1183

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    Description

    Resistin Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (19-108 a.a) containing 96 amino acids and having a molecular mass of 10.3 kDa.Resistin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    Resistin protein (1mg/ml) contains 20% glycerol and 20mM Sodium citrate (pH3.0).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis.Resistin blocks insulinstimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of lowdensity lipoprotein (LDL), increasing the risk of heart disease.

    • Synonyms

      RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.

    • 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

      KTLCSMEEAI NERIQEVAGS LIFRAISSIG LECQSVTSRG DLATCPRGFA VTGCTCGSAC GSWDVRAETT CHCQCAGMDW TGARCCRVQP HHHHHH

    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.

    Resistin Protein
  • View Data Sheet

    Description:

    Myozenin 1 Human Recombinant

    CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.

    Product # :

    PRO-1652

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    Description

    MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYOZ1 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.

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    • Introduction

      Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.

    • Synonyms

      CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.

    • 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 MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.

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    Myoz1 Human
  • View Data Sheet

    Description:

    Leptin Human Recombinant, PEG

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1108

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    Description

    Pegylated Leptin Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Leptin Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It’s in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo it has profound weight reducing effect, resulting mainly from reduced food intake.

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    • Introduction

      Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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 Pegylated leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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    Leptin Mutant
  • View Data Sheet

    Description:

    Ecotin E.Coli Recombinant

    E. coli serine protease inhibitor.

    Product # :

    ENZ-058

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

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

    • Synonyms

      E. coli serine protease inhibitor.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Ecotin Ecoli
  • View Data Sheet

    Description:

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

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

    Product # :

    CYT-431

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    Description

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

    Source

    Escherichia Coli.

    Formulation

    1mg/ml solution containing PBS pH-7.4.

    Purity

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

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    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Mif Human His N
  • View Data Sheet

    Description:

    Osteocrin Human Recombinant, HEK

    Osteocrin, Musclin, OSTN.

    Product # :

    PRO-2818

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    Description

    Osteocrin Human Recombinant is a single, glycosylated, polypeptide chain (28-133 a.a) containing a total of 112 amino acids and having a molecular mass of 12.5 kDa. Osteocrin is fused to a 6 a.a His-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 20 ng/ml measured by its binding ability in a functional ELISA with Human NPRC.

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    • Synonyms

      Osteocrin, Musclin, OSTN.

    • 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

      VDVTTTEAFD SGVIDVQSTP TVREEKSATD LTAKLLLLDE LVSLENDVIE TKKKRSFSGF GSPLDRLSAG SVDHKGKQRK VVDHPKRRFG IPMDRIGRNR LSNSRGHHHH HH.

    • Background

      Research has demonstrated that osteocrin influences bone formation by enhancing the anabolic effects of osteoblasts, the cells responsible for new bone formation. In addition to its skeletal roles, osteocrin has been shown to regulate cardiovascular functions by modulating blood pressure and cardiac hypertrophy. Furthermore, emerging evidence suggests that osteocrin may play a role in the central nervous system, impacting cognitive function and neuroprotection.

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    Osteocrin Human
  • View Data Sheet

    Description:

    Beta Defensin-4 Human Recombinant

    HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.

    Product # :

    CYT-599

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    Description

    Beta Defensin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 50 amino acids and having a molecular mass of 6 kDa. The BD-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DEFB4 (1mg/ml) was lyophilized with 20mM sodium Phosphate buffer pH-7.4 and 130mM NaCl.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.

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    • Introduction

      Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
      4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
      Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
      In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

    • Synonyms

      HBD-4, DEFB-4, HBD4, DEFB104B, Beta-defensin 4, BD-4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.

    • Background

      Beta Defensin-4 Human Recombinant: Exploring the Potential of a Novel Antimicrobial Peptide

      Abstract:

      Beta Defensin-4 (hBD-4) human recombinant is a promising antimicrobial peptide with unique properties and potential therapeutic applications. This research paper provides an in-depth analysis of hBD-4, including its characteristics, mode of action, and potential uses. Furthermore, novel methodologies for the production and optimization of hBD-4 human recombinant are proposed, shedding light on its future implications in the field of infectious disease management.

      Introduction:

      In the face of increasing drug-resistant infections, alternative therapeutic strategies are crucial. Antimicrobial peptides, such as hBD-4, have gained attention due to their broad-spectrum activity against pathogens. This paper aims to explore the distinctive features of hBD-4 and propose innovative approaches for its production and optimization.

      Characteristics and Mode of Action:

      hBD-4 is a cationic peptide comprising 50 amino acids and is characterized by a unique structure that contributes to its antimicrobial properties. The mechanism of action involves the disruption of microbial membranes and subsequent cell death. Additionally, hBD-4 exhibits immunomodulatory effects, including the stimulation of chemotaxis and modulation of the inflammatory response.

      Production of hBD-4 Human Recombinant:

      Efficient production methodologies for hBD-4 human recombinant are essential for its therapeutic applications. Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents advantages and challenges, necessitating careful selection for high yields and protein quality. Optimization strategies, including codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-4 recombinant.

      Potential Applications:

      hBD-4 human recombinant demonstrates potential therapeutic applications in combating drug-resistant pathogens. Its broad-spectrum antimicrobial activity against bacteria, viruses, and fungi positions it as a promising candidate for infectious disease management. Moreover, hBD-4 shows promise in wound healing and tissue regeneration due to its ability to promote angiogenesis and stimulate cell migration. Exploring its potential in combination with drug delivery systems for targeted therapy is an exciting avenue for future research.

      Conclusion:

      hBD-4 human recombinant represents a novel antimicrobial peptide with diverse potential applications. Optimizing production methodologies and elucidating its mechanisms of action will further enhance its clinical utility. With its broad-spectrum antimicrobial activity and potential implications in wound healing and targeted therapy, hBD-4 human recombinant holds promise as an innovative therapeutic agent.

      What is the molecular weight/Mw of BD4 Protein?
      BD4 Protein has a total Mw of 6kDa.

      What is the source or expression system of BD4 Protein?
      Escherichia Coli.

      What is the Purity of BD4 Protein?
      BD4 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD4 Protein?
      Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-50 ng/ml, corresponding to a specific activity of 20,000-10,000,000 units/mg.

      What is the amino acid sequence of BD4 Protein?
      EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP.

      What applications can BD4 Protein be used in?
      BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD4 Protein?
      The endotoxin level is minimal, BD4 Protein was purified using conventional chromatography techniques.

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    Defb 4 Human