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What is the molecular weight/Mw of G CSF Protein?
G CSF Protein has a total Mw of 18kDa.

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

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

What is the Biological Activity of G CSF Protein?
The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.07 ng/ml, corresponding to a Specific Activity of 1.27 x 108 IU/mg.

What is the amino acid sequence of G CSF Protein?
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL GHSLGIPWAP LSSCPSQALQ LAGCLSQLHS GLFLYQGLLQ ALEGISPELG PTLDTLQLDV ADFATTIWQQ MEELGMAPAL QPTQGAMPAF ASAFQRRAGG VLVASHLQSF LEVSYRVLRH LAQP.

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

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

Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function and is encoded by the obese gene. Leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are expressed mainly in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

What is the molecular weight/Mw of IL1A MOUSE, HIS Protein?
IL1A MOUSE, HIS Protein has a total Mw of 20.4kDa.

What is the source or expression system of IL1A MOUSE, HIS Protein?
Escherichia Coli.

What is the Purity of IL1A MOUSE, HIS Protein?
IL1A MOUSE, HIS Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A MOUSE, HIS Protein?
The biological functionality of IL1A MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1A MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQIS.

What applications can IL1A MOUSE, HIS Protein be used in?
IL1A MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A MOUSE, HIS Protein?
The endotoxin level is minimal, IL1A MOUSE, HIS Protein was purified using conventional chromatography techniques.

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.

What is the molecular weight/Mw of IL 4 RAT Protein?
IL 4 RAT Protein has a total Mw of 14kDa.

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

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

What is the Biological Activity of IL 4 RAT Protein?
The ED50 as determined in a cell proliferation assay using rat splenocytes is less than 2ng/ml corresponding to a specific activity of 500,000IU/mg.

What is the amino acid sequence of IL 4 RAT Protein?
HGCNDSPLR EIINTLNQVT EKGTPCTEMF VPDVLTATRN TTENELICRA SRVLRKFYFP RDVPPCLKNK SGVLGELRKL CRGVSGLNSL RSCTVNESTL TTLKDFLESL KSILRGKYLQ SCTSMS.

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

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

Who supplies recombinant IL 4 RAT 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 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

IFN-alpha forms are produced by monocytes/macrophages, lymphoblastoid cells, fibroblasts, and a number of different cell types following induction by viruses, nucleic acids, glucocorticoid hormones, and low-molecular weight substances (n-butyrate, 5-bromodeoxy uridine). At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end. Disulfide bonds are formed between cysteines at positions 1/98 and 29/138. The disulfide bond 29/138 is essential for biological activity while the 1/98 bond can be reduces without affecting biological activity. All IFN-alpha forms contain a potential glycosylation site but most subtypes are not glycosylated. In contrast to IFN-gamma IFN-alpha proteins are stable at pH2.

There are at least 23 different IFN-alpha genes. They have a length of 1-2 kb and are clustered on human chromosome 9p22. It is not known whether all these genes are expressed following stimulation of the cells. In some cell systems expression of some subtypes (IFN-alpha-1, IFN-alpha-2, IFN-alpha-4) is stronger than those of others. IFN-alpha genes do not contain intron sequences found in many other eukaryotic genes (see also: gene expression). Based upon the structures two types of IFN-alpha genes, designated class 1 and II, are distinguished. They encode proteins of 156-166 and172 amino acids, respectively. Deletions covering 9p22 are observed frequently in cells of lymphoblastoid leukemias. It is not known to date whether this is of significance with respect to IFN expression.

The gene encoding the IFN-alpha receptor maps to human chromosome 21q22.1. IFN-alpha and IFN-beta are thought to bind to the same IFN binding subunit which is expressed in 100-5000 copies in IFN-alpha sensitive and -resistant cells and is associated with other as yet unidentified proteins. The IFN-omega (Omega IFN) also binds to the IFN-alpha/IFN-beta receptor. Another receptor expressed on B-lymphocytes is identical with CD21. This receptor also binds Epstein-Barr virus through its gp350/220 coat protein.Signal transduction mechanisms elicited after binding of IFN-alpha to its receptors involves tyrosine phosphorylation (see also: PTK; protein tyrosine kinase) of various non-receptor tyrosine kinases belonging to the Janus kinases. Soluble forms of the IFN-alpha receptor, corresponding to truncated forms of the extracellular domain of the cell surface IFN-alpha receptor, have been found in human serum and in normal human urine.

All known subtypes of IFN-alpha show the same antiviral antiparasitic, antiproliferative activities in suitable bioassays although they may differ in relative activities. Human IFN-alpha is also a potent antiviral substance in murine, porcine, and bovine cell systems. Human IFN-alpha is less active in rodent cells. Site-directed mutagenesis techniques have been used to create some variants of certain subtypes (IFN-alpha-2) that display approximately 100-fold enhanced antiviral activities in mouse cells.

What is the molecular weight/Mw of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein has a total Mw of 19.4kDa.

What is the source or expression system of IFN A 2B HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2B HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

What is the amino acid sequence of IFN A 2B HUMAN Protein?
MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
What applications can IFN A 2B HUMAN Protein be used in?
IFN A 2B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN A 2B HUMAN Protein?
The endotoxin level is minimal, IFN A 2B HUMAN Protein was purified using conventional chromatography techniques.

The Troponin T1 Slow Skeletal Type (TNNT1) human recombinant protein has emerged as a focal point in biomedical research, offering a key to unraveling the complexities of muscle contraction and its implications in neuromuscular disorders. TNNT1 is a critical component of the troponin complex, which regulates striated muscle contraction by controlling the interaction between actin and myosin. The TNNT1 human recombinant, synthesized through advanced biotechnological techniques, provides a valuable tool to explore the intricate molecular characteristics and functional roles of this essential protein.

Understanding the molecular characteristics of TNNT1 is fundamental to comprehending its role in muscle physiology and pathology. TNNT1, a slow skeletal muscle isoform, possesses unique structural features that enable its binding to tropomyosin, a key regulator of muscle contraction. The interactions between TNNT1, tropomyosin, and other troponin subunits are central to the fine-tuned regulation of muscle contraction.

TNNT1 is primarily expressed in slow-twitch skeletal muscles, which are responsible for sustained, endurance-type activities. The functional significance of TNNT1 lies in its role in modulating muscle contraction kinetics, allowing for prolonged muscle activity without fatigue. Moreover, TNNT1 mutations have been associated with congenital myopathies and neuromuscular disorders, emphasizing its crucial role in muscle health.

The TNNT1 human recombinant has promising implications for both research and potential therapeutic applications. Researchers can utilize this recombinant protein to investigate the structural and functional properties of TNNT1, shedding light on its interactions with other muscle proteins and its role in muscle diseases. Additionally, TNNT1-based therapies may hold the key to addressing neuromuscular disorders, providing hope for improved treatments and patient outcomes.

This research aims to provide a comprehensive analysis of the TNNT1 human recombinant, focusing on its molecular characteristics, functional significance, and potential therapeutic implications. By delving into the intricate nature of TNNT1, we aim to contribute to a deeper understanding of muscle biology and pave the way for future research and therapeutic advancements in the realm of neuromuscular disorders.

Delta Sleep-Inducing Peptide (DSIP), also known as Sleep-Promoting Peptide, is a neuropeptide that has been the subject of extensive research due to its potential role in sleep regulation, stress response, and neuroprotection. This nonapeptide, first isolated from the cerebral venous blood of rabbits during sleep, has been shown to induce slow-wave sleep, modulate pain perception, and exhibit potential antioxidant and immunomodulatory properties.

DSIP's primary function is its interaction with the sleep regulatory system. By modulating the release of certain neurotransmitters, DSIP can influence sleep patterns, particularly promoting slow-wave sleep, the most restorative stage of sleep. Studies by Kovalzon et al. (2011) have demonstrated that DSIP can enhance sleep quality in rats, suggesting potential applications in sleep disorders and the promotion of healthy sleep patterns.

In addition to its sleep-inducing effects, DSIP has been shown to possess neuroprotective properties. Research by Zolotarev et al. (2014) found that DSIP could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.

Given its sleep-inducing and neuroprotective effects, DSIP has been proposed as a potential therapeutic agent for a variety of conditions, including sleep disorders, chronic pain, and neurodegenerative diseases. For instance, a study by Spong et al. (2016) found that DSIP could improve sleep quality in patients with chronic insomnia, indicating its potential as a therapeutic agent in the treatment of sleep disorders.

While research on DSIP is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of DSIP in humans. However, the existing body of research suggests that DSIP could be a promising tool in the treatment of sleep disorders, chronic pain, and neurodegenerative diseases.

Research Paper on Interleukin-6, Mouse Anti-Human

Abstract:

Unraveling Interleukin-6 (IL-6), a Mouse Anti-Human antibody! This research paper provides an extensive description of IL-6, a crucial cytokine with diverse roles in immune responses and inflammation. We explore its molecular properties, significance in various biological processes, and synonyms like DIF, TNFA, and TNFSF2. Join us as we uncover potential applications of IL-6 research using the Mouse Anti-Human antibody as a powerful tool.

Introduction:

Enter the realm of IL-6! This paper introduces IL-6, a multifunctional cytokine pivotal in immune regulation and inflammatory signaling. As researchers, we are driven to understand its complex interactions in health and disease to harness its therapeutic potential.

An Extensive Description of IL-6:

We present a comprehensive overview of IL-6, highlighting its structural characteristics and involvement in various cellular processes. From immune cell activation to tissue development, IL-6's pleiotropic effects make it a key player in maintaining homeostasis and cellular communication.

Significance in Immune Responses:

Marvel at IL-6's critical role in orchestrating immune responses! As a mediator between immune cells, IL-6 plays a vital role in coordinating the body's defense against infections and injuries. Its fine-tuned signaling ensures a balanced immune system.

Inflammatory Signaling Pathways:

Explore the intricate pathways through which IL-6 drives inflammation. As a major pro-inflammatory cytokine, IL-6 contributes to the initiation and propagation of inflammatory responses. Understanding these pathways aids in deciphering inflammation-related diseases.

Potential Therapeutic Implications:

Investigate the therapeutic potential of targeting IL-6 in various diseases. Dysregulation of IL-6 has been associated with autoimmune diseases and cancers. Exploring IL-6 as a therapeutic target opens avenues for novel treatments.

Interactions and Synonyms:

Learn about the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2. Understanding these synonyms helps establish the interconnectedness of cytokine signaling. Exploring IL-6's interactions with other molecules provides a holistic view of its role in cellular communication.

Mouse Anti-Human Antibody Applications:

Discover the versatile uses of Mouse Anti-Human antibodies in IL-6 research. From immunodetection to neutralization assays, these antibodies serve as indispensable tools for studying IL-6 biology. Their specificity ensures accurate detection of IL-6 in diverse experimental settings.

Conclusion:

As we conclude our exploration of IL-6 and its significance as a Mouse Anti-Human antibody target, we appreciate its vital role in immune responses and inflammation. The extensive description of IL-6 in this research paper lays the foundation for further advancements in medical research and therapeutic interventions. Understanding IL-6's complexities allows us to develop improved treatments and better health outcomes.

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

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

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

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

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

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

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

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

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