Search results

What is the molecular weight/Mw of IL 2 EQUINE Protein?
IL 2 EQUINE Protein has a total Mw of 14.9kDa.

What is the source or expression system of IL 2 EQUINE Protein?
Escherichia Coli.

What is the Purity of IL 2 EQUINE Protein?
IL 2 EQUINE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 EQUINE Protein?
The ED50 as determined by a cell proliferation assay using murine CTLL-2 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg.

What is the amino acid sequence of IL 2 EQUINE Protein?
APTSSSKRET QQQLKQLQMD LKLLLEGVNN NKNPKLSKML TFKINMPKKA TELKHLQCLE EELKPLEEML KNFLSKDIKE LMSNINVTVL GLKGSETRFT CEYDDETGTI VEFLNKWITF SQSIFSTMT.

What applications can IL 2 EQUINE Protein be used in?
IL 2 EQUINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 EQUINE Protein?
The endotoxin level is minimal, IL 2 EQUINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 EQUINE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 2 EQUINE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

What is the molecular weight/Mw of IL1B CANINE Protein?
IL1B CANINE Protein has a total Mw of 17.5kDa.

What is the source or expression system of IL1B CANINE Protein?
Escherichia Coli.

What is the Purity of IL1B CANINE Protein?
IL1B CANINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B CANINE Protein?
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED50 range ≤ 5pg/ml.

What is the amino acid sequence of IL1B CANINE Protein?
MAAMQSVDCK LQDISHKYLV LSNSYELRAL HLNGENVNKQ VVFHMSFVHG DESNNKIPVV LGIKQKNLYL SCVMKDGKPT LQLEKVDPKV YPKRKMEKRF VFNKIEIKNT VEFESSQYPN WYISTSQVEG MPVFLGNTRG GQDITDFTME FSS.

What applications can IL1B CANINE Protein be used in?
IL1B CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1B CANINE Protein?
The endotoxin level is minimal, IL1B CANINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1B Canine that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL1B Canine ?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

What is the molecular weight/Mw of IL 2 CANINE Protein?
IL 2 CANINE Protein has a total Mw of 15.6kDa.
What is the source or expression system of IL 2 CANINE Protein?
Escherichia Coli.

What is the Purity of IL 2 CANINE Protein?
IL 2 CANINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 CANINE Protein?
The ED50, as determined by CTLL-2 cell proliferation is <5ng/ml corresponding to a specific activity which is ≥ 2.0 x 10^5 units/mg.

What is the amino acid sequence of IL 2 CANINE Protein?
MAPITSSSTK ETEQQMEQLL LDLQLLLNGV NNYENPQLSR MLTFKFYTPK KATEFTHLQC LAEELKNLEE VLGLPQSKNV HLTDTKELIS NMNVTLLKLK GSETSYNCEY DDETATITEF LNKWITFSQS IFSTLT.

What applications can IL 2 CANINE Protein be used in?
IL 2 CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 CANINE Protein?
The endotoxin level is minimal, IL 2 CANINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 CANINE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 2 CANINE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

What is the molecular weight/Mw of IL 4 CANINE Protein?
IL 4 CANINE Protein has a total Mw of 12.9kDa.

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

What is the Purity of IL 4 CANINE Protein?
IL 4 CANINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 CANINE Protein?
The ED50, as determined by TF-1 cell proliferation is <25ng/ml corresponding to a specific activity which is ≥ 4.0 x 10^4 units/mg.

What is the amino acid sequence of IL 4 CANINE Protein?
MHNFNITIKE IIKMLNILTA RNDSCMELTV KDVFTAPKNT SDKEIFCRAA TVLRQIYTHN CSNRYLRGLY RNLSSMANKT CSMNEIKKST LKDFLERLKV IMQKKYYRH.

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

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

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

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

Research Paper on IL-6 Receptor Beta Mouse Recombinant

Abstract:

The IL-6 Receptor Beta Mouse Recombinant stands as a pivotal player in deciphering the intricate realm of immune modulation. This research paper offers an in-depth exploration of its molecular intricacies and its profound implications in immunological research. By delving into its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its role in shaping immune responses.

Introduction:

The IL-6 Receptor Beta Mouse Recombinant has emerged as a central focus in immunological investigations. This paper aims to provide a comprehensive understanding of its molecular attributes and its influence on immune mechanisms.

Molecular Insights and Signaling Proficiency:

Examining the molecular architecture of IL-6 Receptor Beta Mouse Recombinant, we uncover its critical role in transducing IL-6 signals. Its intricate interactions and signaling proficiency contribute to precise immune responses.

Influencing Immune Responses:

IL-6, a key cytokine, exerts remarkable effects on immune cell activation and inflammation. IL-6 Receptor Beta Mouse Recombinant serves as an essential component in the IL-6 signaling pathway, influencing immune outcomes.

Synonyms and Network Connections:

Understanding the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2, deepens our comprehension of cytokine-mediated signaling networks. The intricate interplay between IL-6 Receptor Beta Mouse Recombinant and these molecules shapes immune dynamics.

Potential Therapeutic and Research Applications:

IL-6 Receptor Beta Mouse Recombinant transcends the boundaries of laboratory research. Its potential as a therapeutic target for immune-related disorders and its utility in deciphering immune responses offer promising avenues for clinical applications.

Clinical Relevance and Future Prospects:

The clinical relevance of IL-6 Receptor Beta Mouse Recombinant is highlighted by its role in diseases characterized by dysregulated IL-6 signaling. Exploring its therapeutic potential paves the way for novel strategies to modulate immune-related conditions.

Conclusion:

In the intricate tapestry of immunology, IL-6 Receptor Beta Mouse Recombinant emerges as a central player in orchestrating immune responses. Its molecular intricacies, pivotal functions, and potential therapeutic implications position it as a cornerstone in understanding immune regulation and developing innovative interventions.

What is the molecular weight/Mw of IL6R MOUSE Protein?
IL6R MOUSE Protein has a total Mw of 67.7kDa.

What is the source or expression system of IL6R MOUSE Protein?
Sf9, Insect cells.

What is the Purity of IL6R MOUSE Protein?
IL6R MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6R MOUSE Protein?
QLLEPCGYIY PEFPVVQRGS NFTAICVLKE ACLQHYYVNA SYIVWKTNHA AVPREQVTVI NRTTSSVTFT DVVLPSVQLT CNILSFGQIE QNVYGVTMLS GFPPDKPTNL TCIVNEGKNM LCQWDPGRET YLETNYTLKS EWATEKFPDC QSKHGTSCMV SYMPTYYVNI EVWVEAENAL GKVSSESINF DPVDKVKPTP PYNLSVTNSE ELSSILKLSW VSSGLGGLLD LKSDIQYRTK DASTWIQVPL EDTMSPRTSF TVQDLKPFTE YVFRIRSIKD SGKGYWSDWS EEASGTTYED RPSRPPSFWY KTNPSHGQEY RSVRLIWKAL PLSEANGKIL DYEVILTQSK SVSQTYTVTG TELTVNLTND RYVASLAARN KVGKSAAAVL TIPSPHVTAA YSVVNLKAFP KDNLLWVEWT PPPKPVSKYI LEWCVLSENA PCVEDWQQED ATVNRTHLRG RLLESKCYQI TVTPVFATGP GGSESLKAYL KQAAPARGPT VRTKKVGKNE AVLAWDQIPV DDQNGFIRNY SISYRTSVGK EMVVHVDSSH TEYTLSSLSS DTLYMVRMAA YTDEGGKDGP EFTFTTPKFA QGEIELEHHH HHH.

What is the amino acid sequence of IL6R MOUSE Protein?
IL6R MOUSE Protein is composed from XX amino acids.

What applications can IL6R MOUSE Protein be used in?
IL6R MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL6R MOUSE Protein?
The endotoxin level is minimal, IL6R MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL6R MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL6R MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications

Abstract:

Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.

Introduction:

Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.

Production and Characterization:

Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.

Antimicrobial Properties:

BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.

Therapeutic Implications:

The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.

Conclusion:

Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.

What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.

What is the source or expression system of DEFB116 Protein?
Escherichia Coli.

What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.

What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.

What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 Protein was purified using conventional chromatography techniques.

What is the molecular weight/Mw of IL1B EQUINE Protein?
IL1B EQUINE Protein has a total Mw of 17.3kDa.

What is the source or expression system of IL1B EQUINE Protein?
Escherichia Coli.

What is the Purity of IL1B EQUINE Protein?
IL1B EQUINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B EQUINE Protein?
The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 20 pg/ml, corresponding to a specific activity of > 5.0 × 107 IU/mg.

What is the amino acid sequence of IL1B EQUINE Protein?
AAMHSVNCRL RDIYHKSLVL SGACELQAVH LNGENTNQQV VFCMSFVQGE EETDKIPVAL GLKEKNLYLS CGMKDGKPTL QLETVDPNTY PKRKMEKRFV FNKMEIKGNV EFESAMYPNW YISTSQAEKS PVFLGNTRGG RDITDFIMEI TSA.

What applications can IL1B EQUINE Protein be used in?
IL1B EQUINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1B EQUINE Protein?
The endotoxin level is minimal, IL1B EQUINE Protein was purified using conventional chromatography techniques.

TNF Alpha Human: An Overview of Its Role and Importance in Immunology

TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.

This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.

Production and Properties

Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.

Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.

Solubility and Usage

The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.

This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.

Storage and Stability

For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.

Biological Role and Implications

TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.

Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.

Mechanism of Action

TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.

Research and Clinical Importance

Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.

Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.

In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.

Human Immunodeficiency Virus type 1 (HIV1) is the causative agent of Acquired Immunodeficiency Syndrome (AIDS), a devastating disease that affects millions of people worldwide. The HIV1 life cycle is a complex process involving several key viral enzymes, one of which is the integrase (IN). HIV1 integrase plays a crucial role in viral replication by catalyzing the integration of viral DNA into the host cell genome, an essential step for the establishment of a persistent infection.
The study of HIV1 integrase has been of great interest to researchers due to its significance as a therapeutic target. In recent years, advances in recombinant DNA technology have allowed for the production and purification of HIV1 integrase in recombinant form, enabling detailed structural and functional studies. This research aims to characterize the HIV1 integrase recombinant and gain insights into its mechanisms of action during viral integration.
The first objective of this study is to express and purify recombinant HIV1 integrase using various expression systems such as bacterial, yeast, or mammalian cell-based systems. Recombinant DNA techniques, including cloning and expression vector design, will be employed to generate the desired constructs for protein production. The recombinant integrase will be purified using affinity chromatography, followed by characterization using biochemical and biophysical techniques.
The second objective is to investigate the enzymatic activity of the purified HIV1 integrase recombinant. In vitro assays will be performed to determine its ability to catalyze the integration of viral DNA into target DNA sequences. Various substrates, including oligonucleotides and plasmids, will be used to assess the substrate specificity and kinetics of the integrase enzyme. Furthermore, the effects of potential inhibitors or small molecules on the enzymatic activity will be evaluated.
The third objective is to elucidate the three-dimensional structure of the HIV1 integrase recombinant using techniques such as X-ray crystallography or cryo-electron microscopy. This structural information will provide valuable insights into the mechanism of integrase function and aid in the rational design of novel inhibitors targeting integrase.
By characterizing the HIV1 integrase recombinant, this research aims to contribute to our understanding of the molecular mechanisms underlying viral integration. The findings from this study may provide crucial information for the development of novel therapeutic strategies targeting HIV1 integrase, potentially leading to the discovery of more effective antiretroviral drugs.

IL-22 belongs to the IL-10 family of regulatory cytokines and produced by several populations of immune cells at a site of inflammation. Members of this family share partial homology in their amino acid sequences, but varies in their biological functions. IL-22 takes effect on non-hematopoietic cells. IL-22 takes pat in wound healing and in protection against microbs.Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the pancreas and liver.

Influenza A virus, notorious for its ability to cause seasonal epidemics and occasional pandemics, poses a significant threat to global public health. The pursuit of effective countermeasures has led to the exploration of Influenza A Virus Nucleoprotein Recombinant as a key molecular protagonist in our defense against this elusive virus. This research endeavors to unravel the intricacies of the Nucleoprotein Recombinant, shedding light on its structural features, immunogenic prowess, and applications in vaccine development and antiviral therapies. By dissecting the properties of the Nucleoprotein Recombinant, scientists aim to fortify our defenses against Influenza A, potentially paving the way for a new era in influenza prevention and control.

Structural Insights into Nucleoprotein Recombinant:

The Influenza A Virus Nucleoprotein Recombinant, engineered to mirror crucial viral components, serves as a versatile tool for studying the virus's genetic material. A nuanced understanding of its three-dimensional structure and conformational intricacies is pivotal, not only for deciphering the virus's replication mechanisms but also for designing targeted interventions, such as vaccines and antiviral drugs.

Immunogenic Potential and Vaccine Development:

The quest for an effective influenza vaccine has been fueled by the virus's notorious mutability. Nucleoprotein Recombinant, designed to elicit strong immune responses, stands as a promising candidate for vaccine development. By presenting conserved viral elements to the immune system, the recombinant protein aims to induce robust and lasting immunity, thwarting the influenza virus's ability to evade immune detection through antigenic drift.

Application in Antiviral Therapies:

Beyond vaccination, Influenza A Virus Nucleoprotein Recombinant holds promise in the realm of antiviral therapies. The recombinant protein's ability to stimulate immune responses can be harnessed in the development of immunotherapies. Monoclonal antibodies derived from the Nucleoprotein Recombinant may offer targeted treatments, neutralizing the virus and potentially shortening the duration and severity of influenza infections.

Challenges and Future Directions:

While the Nucleoprotein Recombinant stands at the forefront of influenza research, challenges persist. The virus's ability to rapidly mutate demands ongoing vigilance and adaptability in recombinant strategies. Furthermore, considerations of vaccine safety, efficacy, and public acceptance necessitate continuous exploration to optimize the translational success of Nucleoprotein Recombinant-based interventions.

Influenza A Virus Nucleoprotein Recombinant emerges as a sentinel in the scientific arsenal against influenza, epitomizing the quest for innovative solutions in the face of viral challenges. Its structural insights, immunogenic potential, and applications in vaccine development and antiviral therapies position it as a pivotal player. As researchers continue to decipher the molecular intricacies of Nucleoprotein Recombinant, they not only fortify our defenses against influenza but potentially pave the way for a paradigm shift in our approach to influenza prevention and control, shaping the landscape of global health security.

IL-22 is a part of the IL-10 family of regulatory cytokines and produced by a few populations of immune cells at a site of inflammation. Members of this family share partial homology in their amino acid sequences, but varies in their biological functions. IL-22 effects on non-hematopoietic cells. IL-22 responsible for wound healing and takes part in protection against microbs. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the pancreas and liver.