Search: 1000 results found for "Thyrostimulin"

Description:

Interleukin 10 Receptor Alpha Human Recombinant, BioActive

Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.

Product # :

CYT-1142

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Description

IL10RA Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 220 amino acids (22-235 aa) and having a molecular mass of 25.2kDa.IL10RA is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL10RA solution (0.2mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Determined by its ability to inhibit proliferation using MC/9 mouse mast cells. ED50 for this effect is ≤ 300 ng/ml with Human IL-10.

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Introduction
Interleukin 10 receptor, alpha subunit or CDW210A, is a part of the IL-10 receptor. This protein is encoded by the IL10RA gene in humans. IL10RA is a receptor for IL-10 (interleukin 10), it is part of the interferon receptors family. This protein is responsible for the inhibition of interferon receptors synthesis by taking part in the immunosuppressive signal of interleukin 10. Among its other roles are the insulin receptor substrate-2/PI 3-kinase/AKT pathway and phosphorylation of JAK1 and TYK2 kinases.
Synonyms
Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.
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
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH
Background
What is the molecular weight/Mw of IL10RA HUMAN, ACTIVE Protein?
IL10RA HUMAN, ACTIVE Protein has a total Mw of 25.2kDa.

What is the source or expression system of IL10RA HUMAN, ACTIVE Protein?
Sf9, Baculovirus cells.
What is the Purity of IL10RA HUMAN, ACTIVE Protein?
IL10RA HUMAN, ACTIVE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10RA HUMAN, ACTIVE Protein?
Determined by its ability to inhibit proliferation using MC/9 mouse mast cells. ED50 for this effect is ≤ 300 ng/ml with Human IL-10.

What is the amino acid sequence of IL10RA HUMAN, ACTIVE Protein?
HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH.

What applications can IL10RA HUMAN, ACTIVE Protein be used in?
IL10RA HUMAN, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10RA HUMAN, ACTIVE Protein?
The endotoxin level is minimal, IL10RA HUMAN, ACTIVE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10RA HUMAN, ACTIVE 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 IL10RA HUMAN, ACTIVE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Sjogren Syndrome/Scleroderma Autoantigen 1 Human Recombinant

Sjogren Syndrome/Scleroderma Autoantigen 1, Sjogren'S Syndrome/Scleroderma Autoantigen 1, Autoantigen P27, Centromeric Autoantigen (27kD), p27, Sjoegren Syndrome/Scleroderma Autoantigen 1.

Product # :

PRO-1743

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Description

SSSCA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-199aa) and having a molecular mass of 23.9kDa. SSSCA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SSSCA1 protein solution (0.5mg/ml) containing 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
Sjogren syndrome/scleroderma autoantigen 1, SSSCA1 is involved in mitosis. SSSCA1 is a centromere-associated protein which can induce anti-centromere antibodies. In addition SSSCA1 is recognized by a subset of anti-centromere antibodies from patients with sclerodermaand Sjogren's syndrome.
Synonyms
Sjogren Syndrome/Scleroderma Autoantigen 1, Sjogren'S Syndrome/Scleroderma Autoantigen 1, Autoantigen P27, Centromeric Autoantigen (27kD), p27, Sjoegren Syndrome/Scleroderma Autoantigen 1.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMALNGAE VDDFSWEPPT EAETKVLQAR RERQDRISRL MGDYLLRGYR MLGETCADCG TILLQDKQRK IYCVACQELD SDVDKDNPAL NAQAALSQAR EHQLASASEL PLGSRPAPQP PVPRPEHCEG AAAGLKAAQG PPAPAVPPNT DVMACTQTAL LQKLTWASAE LGSSTSLETS IQLCGLIRAC AEALRSLQQL QH

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.

Description:

Transcription Factor-A Recombinant Human

Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.

Product # :

PRO-095

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Description

TFAM produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (43-246.a.a) and having a molecular mass of 26.6kDa. TFAM is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TFAM protein solution (0.25mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
TFAM is a mitochondrial transcription factor which is a main activator of mitochondrial transcription and is also a participant in mitochondrial genome replication. TFAM is situated primarily in the nuclei of elongated spermatids and takes part in the regulation of gene expression of the haploid male genome. TFAM is linked to mitochondrial disorder in humans characterized by ocular myopathy, exercise intolerance and muscle wasting.
Synonyms
Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.
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 MSSVLASCPK KPVSSYLRFS KEQLPIFKAQ NPDAKTTELI RRIAQRWREL PDSKKKIYQD AYRAEWQVYK EEISRFKEQL TPSQIMSLEK EIMDKHLKRK AMTKKKELTL LGKPKRPRSA YNVYVAERFQ EAKGDSPQEK LKTVKENWKN LSDSEKELYI QHAKEDETRY HNEMKSWEEQ MIEVGRKDLL RRTIKKQRKY GAEEC

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.

Description:

Sclerostin Mouse Recombinant

SOST, Sclerostin, 5430411E23Rik.

Product # :

PRO-2670

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Description

SOST Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (24-211 a.a) containing 194 amino acids and having a molecular mass of 21.9 kDa.SOST is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

SOST protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is expressed mainly in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
Synonyms
SOST, Sclerostin, 5430411E23Rik.
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
QGWQAFRNDA TEVIPGLGEY PEPPPENNQT MNRAENGGRP PHHPYDAKDV SEYSCRELHY TRFLTDGPCR SAKPVTELVC SGQCGPARLL PNAIGRVKWW RPNGPDFRCI PDRYRAQRVQ LLCPGGAAPR SRKVRLVASC KCKRLTRFHN QSELKDFGPE TARPQKGRKP RPGARGAKAN QAELENAYHH 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.

Description:

Calmodulin Human

Calmodulin, CaM, CALM.

Product # :

PRO-2799

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Source

Human brain tissue.

Formulation

CALM was lyophilized with 2mM EDTA.

Purity

Greater than 95.0%.

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Synonyms
Calmodulin, CaM, CALM.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin 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 CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Applications
Blood samples from tissue donors were tested and found to be negative for syphilis, HBsAg, HIV-1 and HIV-2 antibodies and HCV.
Background
Calmodulin, a small, ubiquitous calcium-binding protein, stands as a linchpin in cellular signalling cascades. Its ability to modulate diverse cellular processes by transducing calcium signals has made it a focal point of scientific inquiry. With its role extending from muscle contraction to neurotransmitter release and gene expression, calmodulin orchestrates intricate physiological responses. This research delves into the multifaceted world of calmodulin, exploring its structural characteristics, calcium-binding properties, and its pivotal involvement in various biological pathways.
Structural Marvel of Calmodulin:
Calmodulin boasts a unique dumbbell-shaped structure, composed of four EF-hand motifs that enable it to bind calcium ions. When calcium binds to calmodulin, it undergoes a conformational change, allowing it to interact with a myriad of target proteins. This structural adaptability is fundamental to its ability to regulate a wide array of cellular activities.
Calcium Signalling and Transduction:
Intracellular calcium serves as a ubiquitous second messenger, and calmodulin is the key mediator of calcium signalling. When calcium levels rise, calmodulin binds calcium ions, triggering its activation. This activated form of calmodulin modulates the activity of various proteins, including enzymes, ion channels, and transcription factors. By doing so, calmodulin influences processes such as muscle contraction, neurotransmitter release, and cell proliferation.

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.

Description:

Prolactin Receptor Antagonist Human Recombinant

Mammotropin, Luteotropic hormone, Luteotropin, PRL.

Product # :

CYT-1254

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Description

Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.

Purity

Greater than 97.0% as determined by:

(a) Analysis by Gel Filtration.

(b) Analysis by SDS-PAGE.

Biological Activity

fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).

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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PRLR in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr
Background
Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

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.

Description:

SELANK

Product # :

HOR-035

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Description

SELANK Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 751.89 Dalton and a Molecular formula of C33H57N11O9.

Formulation

The protein was lyophilized with no additives.

Purity

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

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SELANK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELANK 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 SELANK in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Thr-Lys-Pro-Arg-Pro-Gly-Pro-OH.
Background
Selank, also known as TP-7, is a synthetic peptide that has garnered significant attention in the scientific community due to its potential anxiolytic, neuroprotective, and nootropic effects. This heptapeptide, derived from the naturally occurring human tetrapeptide Tuftsin, has been shown to possess a wide range of biological activities, including enhancing memory, reducing anxiety, and potentially mitigating the effects of neurodegenerative diseases.
Selank's primary mechanism of action involves its interaction with the GABAergic system, the body's main inhibitory neurotransmitter system. By modulating the activity of GABA receptors, Selank can exert a calming effect on the brain, reducing anxiety and enhancing cognitive function. Studies by Semenova et al. (2014) have demonstrated that Selank can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.
In addition to its anxiolytic and nootropic effects, Selank has been shown to possess neuroprotective properties. Research by Ershov et al. (2016) found that Selank 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 anxiolytic, nootropic, and neuroprotective effects, Selank has been proposed as a potential therapeutic agent for a variety of conditions, including anxiety disorders, cognitive disorders, and neurodegenerative diseases. For instance, a study by Medvedev et al. (2017) found that Selank could improve symptoms in patients with generalized anxiety disorder, indicating its potential as a therapeutic agent in the treatment of anxiety disorders.
While research on Selank 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 Selank in humans. However, the existing body of research suggests that Selank could be a promising tool in the treatment of anxiety disorders, cognitive disorders, and neurodegenerative diseases.

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.

Description:

Leptin-A Tilapia Recombinant

Product # :

CYT-1109

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Description

Leptin-A Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 16,491 Dalton. The Leptin-A Tilapia is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.

Purity

Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.

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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin-A Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-A Tilapia 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 Leptin-A Tilapia 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.
Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.33 for 1 mg/ml Leptin-A Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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.

Description:

Interleukin-1 Receptor Antagonist Rat Recombinant, His Tag

Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.

Product # :

CYT-899

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Description

IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (27-178a.a.) and having a molecular mass of 19.8kDa.IL 1RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 1RA protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

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

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.
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 MGSHPAGKRP CKMQAFRIWD TNQKTFYLRN NQLIAGYLQG PNTKLEEKID MVPIDFRNVF LGIHGGKLCL SCVKSGDDTK LQLEEVNITD LNKNKEEDKR FTFIRSETGP TTSFESLACP GWFLCTTLEA DHPVSLTNTP KEPCTVTKFY FQEDQ.
Background
What is the molecular weight/Mw of IL1RA RAT, HIS Protein?
IL1RA RAT, HIS Protein has a total Mw of 19.8kDa.

What is the source or expression system of IL1RA RAT, HIS Protein?
Escherichia Coli.

What is the Purity of IL1RA RAT, HIS Protein?
IL1RA RAT, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1RA RAT, HIS Protein?
The biological functionality of IL1RA RAT, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1RA RAT, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHPAGKRP CKMQAFRIWD TNQKTFYLRN NQLIAGYLQG PNTKLEEKID MVPIDFRNVF LGIHGGKLCL SCVKSGDDTK LQLEEVNITD LNKNKEEDKR FTFIRSETGP TTSFESLACP GWFLCTTLEA DHPVSLTNTP KEPCTVTKFY FQEDQ.

What applications can IL1RA RAT, HIS Protein be used in?
IL1RA RAT, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1RA RAT, HIS Protein?
The endotoxin level is minimal, IL1RA RAT, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1RA RAT, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL1RA RAT, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Translocase of Inner Mitochondrial Membrane 8 Homolog A Human Recombinant

Mitochondrial import inner membrane translocase subunit Tim8 A, TIMM8A, Translocase of Inner Mitochondrial Membrane 8 Homolog A, DDP, DDP1, DFN1, MTS, TIM8, Deafness dystonia protein 1, X-linked deafness dystonia protein.

Product # :

PRO-1818

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Description

TIMM8A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-97) and having a molecular mass of 13.4 kDa.TIMM8A is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TIMM8A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Translocase of Inner Mitochondrial Membrane 8 Homolog A (TIMM8A) takes part in the import and insertion of hydrophobic membrane proteins from the cytoplasm into the mitochondrial. TIMM8A plays a role as a chaperone-like protein which protects the hydrophobic precursors from aggregation and leads them through the mitochondrial intermembrane space. TIMM8A is essential for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Defects in TIMM8A cause Jensen syndrome. TIMM8A and TIMM13, forms a 70 kDa heterohexamer.
Synonyms
Mitochondrial import inner membrane translocase subunit Tim8 A, TIMM8A, Translocase of Inner Mitochondrial Membrane 8 Homolog A, DDP, DDP1, DFN1, MTS, TIM8, Deafness dystonia protein 1, X-linked deafness dystonia protein.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDSSSSS SAAGLGAVDP QLQHFIEVET QKQRFQQLVH QMTELCWEKC MDKPGPKLDS RAEACFVNCV ERFIDTSQFI LNRLEQTQKS KPVFSESLSD.

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.

Description:

Mouse Anti Human Troponin I Type 1 Paired

DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.

Product # :

ANT-724

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Description

TNNI1 conjugation antibody and TNNI1 coating antibody are used to develop rapid test for TNNI1 rapid test.

Please note that when ordering for example: 100µg antibody we ship 50µg from each of the antibodies (100µg in total).

Formulation

* TNNI1 conjugation in 50mM Na-citrate, pH 6.0, 0.9% NaCl and 0.095 % NaN3.

* TNNI1 coating antibody in 50mM Na-citrate, pH 6.0 0.9% NaCl and 0.095 % NaN3.

Purity

Greater than 95%.

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Introduction
Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.
Synonyms
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
Physical Appearance
2 vials of sterile Filtered clear colorless solution.
Applications
Lateral flow immunoassay.
Type
Mouse Anti Human Monoclonal.
Purification Method
Purified monoclonal IgG by protein A chromatography.

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

Description:

Corticotropin Releasing Hormone (146-196 a.a.) Human Recombinant

CRF, Corticotropin-Releasing Factor.

Product # :

HOR-055

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Description

The CRHHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CRHHis-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 51 amino acid residues of the CRHHuman, 146-196 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
CRF, Corticotropin-Releasing Factor.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized CRH at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
CRH is a neuropeptide which regulates body's response to stress. CRH takes part in the hypothalamic-pituitary-adrenal axis which controls the production of cortisol and other glucocorticoids. CRH is synthesized in different tissues such as the brainstem, hypothalamus and peripheral organs. In Pregnancy, CRH regulates parturition and fetal development. CRH binds 2 types of receptors- CRH receptor 1 and CRH receptor 2, both are G-protein-coupled receptors (GPCRs). After binding CRHR1, CRH initiates a cascade of intracellular signalling which leads to the release of ACTH from the anterior pituitary. This release stimulates cortisol secretion from the adrenal glands, which is necessary for controlling the body's stress response and maintain energy balance and immune function.

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.

Description:

Tissue Inhibitor of Metalloprotease 2 Human Recombinant, His Tag

TIMP metallopeptidase inhibitor 2, metalloproteinase inhibitor 2, Tissue inhibitor of metalloproteinases 2, TIMP-2, CSC-21K.

Product # :

ENZ-646

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Description

TIMP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 232 amino acids (27-220) and having a molecular mass of 26.1 kDa.TIMP2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TIMP2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMP family members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.
Synonyms
TIMP metallopeptidase inhibitor 2, metalloproteinase inhibitor 2, Tissue inhibitor of metalloproteinases 2, TIMP-2, CSC-21K.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHM CS CSPVHPQQAF CNADVVIRAK AVSEKEVDSG NDIYGNPIKR IQYEIKQIKM FKGPEKDIEF IYTAPSSAVC GVSLDVGGKK EYLIAGKAEG DGKMHITLCD FIVPWDTLST TQKKSLNHRY QMGCECKITR CPMIPCYISS PDECLWMDWV TEKNINGHQA KFFACIKRSD GSCAWYRGAA PPKQEFLDIE DP

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.

Description:

Anti Human Follicle Stimulating Hormone Mouse

Product # :

ANT-788

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Description

Paired FSH monoclonal antibodies are composed of anti-FSH α and β subunits, the anti-FSH α is used for the coating and antibody to β subunit is used for colloid gold conjugation. Please note that when ordering for example: 100µg paired antibody, you receive 50µg from each antibody (100µg in total).

Formulation

* FSH α (coating) antibody in 50mM NaCl, 10mM PBS, 0.1% NaN3, PH 8 (15.62mg/ml).
* FSH β (Labeling) antibody in 50mM NaCl, 10mM PBS, 0.1% NaN3, PH 8 (6mg/ml).

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Physical Appearance
2 vials of sterile Filtered clear colorless solution.
Stability
For periods up to 1month FSHPaired Antibody should be stored at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Applications
Lateral flow immunoassay.
Background
Follicle stimulating hormone (FSH) is synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproduction in women. FSH hormone stimulates the growth of immature Graafian follicles to maturation in the ovary. As the follicle grows it releases inhibin, which shuts off the FSH production. In men, FSH enhances the production of androgen-binding proteinby the Sertoli cells of the testes and is critical for spermatogenesis. In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, mainly affecting granulosa cells. Like LH, FSH release at the pituitary gland is controlled by pulses of gonadotropin-releasing hormone (GnRH). In turn, those pulses are subject to the estrogen feed-back from the gonads.
Type
Mouse antibody Monoclonal.
Purification Method
Purified by Ion Exchange (IEX) Chromatography.

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

Description:

BPC-157 Pentadecapeptide

Product # :

HOR-029

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Description

BPC-157 Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.

Formulation

The protein was lyophilized with no additives.

Purity

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

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BPC-157 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution bpc-157 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 BPC-157 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH
Background
BPC-157, short for Body Protection Compound-157, is a synthetic peptide that has garnered significant attention in the field of regenerative medicine and sports science. This peptide, derived from a portion of the human gastric juice protein known as BPC, exhibits remarkable healing and tissue regeneration properties. BPC-157 has shown promise in various preclinical and clinical studies, demonstrating its potential for the treatment of a wide range of injuries and disorders.
The research on BPC-157 encompasses investigations into its mechanisms of action, efficacy, safety, and potential therapeutic applications. Studies have elucidated the peptide's ability to enhance angiogenesis, promote collagen synthesis, modulate inflammatory responses, and protect against oxidative stress. These properties make BPC-157 an intriguing candidate for accelerating tissue healing, reducing inflammation, and improving overall recovery outcomes.
Preclinical studies have revealed the beneficial effects of BPC-157 in several injury models. For instance, BPC-157 has demonstrated its potential in accelerating tendon and ligament healing, mitigating muscle damage, and promoting bone regeneration. These findings suggest that BPC-157 could be a valuable therapeutic tool in orthopedic medicine and sports-related injuries.
Furthermore, BPC-157 has exhibited promising effects on gastrointestinal health. Studies have highlighted its ability to protect and heal the gut lining, reduce ulcer formation, and alleviate symptoms associated with inflammatory bowel disease. These observations open up avenues for BPC-157 as a potential treatment for gastrointestinal disorders.
In addition to its regenerative properties, BPC-157 has shown potential in neurological and psychiatric conditions. Research has indicated its neuroprotective effects, with implications for the treatment of traumatic brain injury, stroke, and neurodegenerative disorders. Preliminary studies also suggest BPC-157's potential as an antidepressant and anxiolytic agent.
Despite the promising findings, further research is needed to fully understand the mechanisms underlying BPC-157's actions and to assess its long-term safety and efficacy. Clinical trials are underway to explore its potential therapeutic applications in humans, including its use in tendon and ligament repair, inflammatory bowel disease, and neurodegenerative disorders.
This comprehensive review aims to summarize the current state of research on BPC-157, providing an overview of its mechanisms of action and therapeutic potential. By examining relevant studies and findings, we aim to shed light on the diverse applications of BPC-157 and its implications for regenerative medicine, sports science, and various disease

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.

Description:

Glial-Derived Neurotrophic Factor Human Recombinant

ATF1, ATF2, HFB1-GDNF, GDNF.

Product # :

CYT-305

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Description

Glial derived Neurotrophic Factor Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 x 135 amino acids and having a total molecular mass of approximately 30kDa. GDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDNF was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.

Purity

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

Biological Activity

The ED₅₀ was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x10⁷ units/mg.

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Introduction
GDNF promotes the survival and differentiation of minergic neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of minergic neurons and increases their high-affinity uptake.
Synonyms
ATF1, ATF2, HFB1-GDNF, GDNF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF 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 Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
Background
What is the molecular weight/Mw of GDNF HUMAN Protein?
GDNF HUMAN Protein has a total Mw of 30kDa.

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

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

What is the Biological Activity of GDNF HUMAN Protein?
The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.

What is the amino acid sequence of GDNF HUMAN Protein?
SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
What applications can GDNF HUMAN Protein be used in?
GDNF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

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

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

Description:

Luteinizing Hormone Releasing Hormone Human

Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.

Product # :

HOR-261

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Description

Lutenizing Hormone Releasing Hormone Human Synthetic is a single, non-glycosylated, polypeptide chain containing 10 amino acids and having a molecular mass of 1182.2 Dalton. The molecular formula is C55H75N17O13.C2H4O2. The CAS Number is 71447-49-9.

Formulation

The LHRH was lyophilized from a concentrated (1 mg/ml) solution with no additives.

Purity

Greater than 98.0% as determined by RP-HPLC.

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Introduction
Gonadotropin-releasing hormone 1 (GNRH1), also known as Luteinising-hormone releasing hormone (LHRH), is a peptide hormone responsible for the release of FSH and LH from the anterior pituitary. GNRH1 is synthesized and released by the hypothalamus.
At the pituitary, GNRH1 stimulates the synthesis and secretion of the gonadotropins follicle-stimulating hormone (FSH) and luteinizing hormone (LH). These processes are controlled by the size and frequency of GNRH1 pulses, as well as by feedback from androgens and estrogens. Low requency GNRH1 pulses lead to FSH release, whereas high frequency GNRH1 pulses stimulate LH release.
There are differences in GNRH1 secretion between males and females. In males, GNRH1 is secreted in pulses at a constant frequency, but in females the frequency of the pulses varies during the menstrual cycle and there is a large surge of GNRH1 just before ovulation.
GNRH1 secretion is pulsatile in all vertebrates, and is necessary for correct reproductive function. Thus, a single hormone, GNRH1, controls a complex process of follicular growth, ovulation, and corpus luteum maintenance in the female, and spermatogenesis in the male.
Synonyms
Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized LHRH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LNRH 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 LHRH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. The LHRH is also soluble in a 1% glacial acetic acid.
Amino Acid Sequence
Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.

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.

Description:

Osteoclast Stimulating Factor-1 Human Recombinant

SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

Product # :

CYT-630

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Description

OSTF1 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 225 amino acids (1-217) and having a molecular mass of 25.1kDa. The OSTF1 is fused to an 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

OSTF1 protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH 8, 0.5mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.
Synonyms
SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MSKPPPKPVK PGEGGQVKVF RALYTFEPRT PDELYFEEGD IIYITDMSDT NWWKGTSKGR TGLIPSNYVA EQAESIDNPL HEAAKRGNLS WLRECLDNRV GVNGLDKAGS TALYWACHGG HKDIVEMLFT QPNIELNQQN KLGDTALHAA AWKGYADIVQ LFLAKGARTD LRNIEKKLAF DMATNAACAS LLKKKQGTDA VRTLSNAEDY LDDEDSDLEH HHHHH.

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

Description:

Cardiotrophin-1 Human Recombinant

CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.

Product # :

CYT-944

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Cardiotrophin-1 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids and having a molecular mass of 21.2kDa.The CTF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CTF-1 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

Purity

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

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×10⁶ IU/mg.

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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.
Synonyms
CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF-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 CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.
Background
Title: Cardiotrophin-1 Human Recombinant: A Potential Therapeutic Target for Cardiovascular Diseases
Abstract:

Cardiotrophin-1 (CT-1) is a cytokine that plays a crucial role in cardiac development and homeostasis. This research paper provides a comprehensive analysis of human recombinant CT-1, focusing on its production, characterization, and potential therapeutic implications in cardiovascular diseases. The paper discusses the significance of CT-1 in cardiac cell survival, hypertrophy, and regeneration. Furthermore, it elucidates the ongoing research and clinical trials exploring the therapeutic potential of recombinant CT-1 in cardiovascular disorders. The information presented in this paper aims to enhance the understanding of human recombinant CT-1 and its utility as a research tool and a potential therapeutic agent for cardiovascular diseases.
Introduction:

Cardiotrophin-1 (CT-1) is a member of the interleukin-6 cytokine family, primarily produced by cardiac cells. It exerts its effects by binding to the CT-1 receptor complex, leading to the activation of various signaling pathways. Human recombinant CT-1, produced through genetic engineering techniques, provides researchers with a valuable tool to explore its biological functions and therapeutic potential.
Production and Characterization:

Recombinant CT-1 is typically produced using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CT-1.
Role in Cardiovascular Physiology:

CT-1 plays a critical role in cardiac cell survival, hypertrophy, and regeneration. It promotes cardiomyocyte growth and survival, contributing to the adaptation of the heart to stress and injury. CT-1 also exhibits angiogenic properties, stimulating the formation of new blood vessels in the heart. These functions make recombinant CT-1 an important tool for studying cardiac physiology and exploring potential therapeutic interventions.
Therapeutic Implications:

The dysregulation of CT-1 signaling has been implicated in various cardiovascular diseases, including heart failure, myocardial infarction, and cardiac hypertrophy. Recombinant CT-1 holds promise as a potential therapeutic agent for these conditions. Clinical trials are underway to evaluate the safety and efficacy of CT-1-based therapies, including recombinant CT-1 administration and gene therapy approaches.
Conclusion:

Human recombinant CT-1 is a valuable research tool and a potential therapeutic target for cardiovascular diseases. Its production, characterization, and applications in cardiac cell signaling contribute to our understanding of cardiovascular physiology and the development of novel treatments. Continued research and clinical trials exploring the therapeutic potential of recombinant CT-1 hold promise for improving outcomes in patients with cardiovascular disorders.
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.2kDa.

What is the source or expression system of CTF1 Protein?
Escherichia Coli.

What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CTF1 Protein?
The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 IU/mg.

What is the amino acid sequence of CTF1 Protein?
MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.

What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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.

Description:

Truncated BH3 Interacting Domain Death Agonist Mouse Recombinant

Truncated BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355, tBID.

Product # :

PRO-644

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Description

Truncated BID Mouse Recombinant also called BH3-interacting domain death agonist p15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 61-195 amino acids (135 a.a.) and having a molecular mass of 15.4 kDa.

Source

Escherichia Coli.

Formulation

The Mouse Truncated BID protein solution contains 10mM Tris-HCl pH-8, 1mM EDTA and 250mM NaCl.

Purity

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

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Introduction
Truncated BH3 interacting domain death agonist is a truncated form of the pro-apoptotic full-length BID. Truncated BH3 interacting domain death agonist is generated by Caspase-8 cleavage of BID. The truncated form of the protein translocates from the cytosol to mitochondria and transduces apoptotic signals.
BID is a pro-apoptotic Bcl-2 protein having only the BH3 domain. In reaction to apoptotic signaling, BID interacts with another Bcl-2 family of cell death regulators, called Bax, they form a heterodimer resulting to the insertion of Bax into the outer mitochondrial membrane. Bax induces the opening of the mitochondrial voltage-dependent anion channel which lead to the release of cytochrome c and other pro-apoptotic factors from the mitochondria resulting in activation of caspases. BID is a mediator of mitochondrial damage induced by caspase-8 (CASP8). CASP8 cleaves BID, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. The major proteolytic product p15 BID releasea cytochrome c. Isoform 1, Isoform 2 and Isoform 4 induce ice-like proteases and apoptosis while Isoform 3 does not induce apoptosis.
Synonyms
Truncated BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355, tBID.
Physical Appearance
Sterile Filtered colorless liquid formulation.
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.

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.

Description:

Follistatin Mouse Recombinant

Follistatin, FST, FS, Activin-binding protein, AL033346.

Product # :

CYT-124

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Shipped at Room temp

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Description

Follistatin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 289 amino acids and having a total molecular mass of 31.6kDa.The FST is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse Follistatin is lyophilized from 10mM Na2PO4 and 50mM NaCl, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.

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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
Synonyms
Follistatin, FST, FS, Activin-binding protein, AL033346.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.
Background
What is the molecular weight/Mw of FOLLISTATIN MOUSE Protein?
FOLLISTATIN MOUSE Protein has a total Mw of 31.6kDa.

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

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

What is the Biological Activity of FOLLISTATIN MOUSE Protein?
The ED50, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.

What is the amino acid sequence of FOLLISTATIN MOUSE Protein?
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.

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

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

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

Description:

Translocase Of Outer Mitochondrial Membrane 20 Human Recombinant

Mmitochondrial import receptor subunit TOM20 homolog, TOMM20, MAS20, MOM19, KIAA0016, Outer mitochondrial membrane receptor Tom20, Mitochondrial 20 kDa outer membrane protein.

Product # :

PRO-1471

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Shipped with Ice Packs

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Description

TOMM20 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (25-145) and having a molecular mass of 16.2 kDa. TOMM20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TOMM20 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 2mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Mmitochondrial import receptor subunit TOMM20 homolog (TOMM20) is a member of the Tom20 family. The Tom machinery consists of import receptors for the initial binding of cytosolically synthesized preproteins and a general import pore (GIP) for the membrane translocation of various preproteins into the mitochondria. TOMM20 acts as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore.
Synonyms
Mmitochondrial import receptor subunit TOM20 homolog, TOMM20, MAS20, MOM19, KIAA0016, Outer mitochondrial membrane receptor Tom20, Mitochondrial 20 kDa outer membrane protein.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDRKRRSD PNFKNRLRER RKKQKLAKER AGLSKLPDLK DAEAVQKFFL EEIQLGEELL AQGEYEKGVD HLTNAIAVCG QPQQLLQVLQ QTLPPPVFQM LLTKLPTISQ RIVSAQSLAE DDVE.

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.

Description:

Cardiac Troponin-C Human Recombinant

Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.

Product # :

PRO-959

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Shipped with Ice Packs

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Description

Cardiac Troponin-C Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 20.5 kDa.Cardiac Troponin-C is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The Cardiac Troponin-C 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.

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Introduction
Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.
Synonyms
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ NPTPEELQEM IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKSEEELSDL FRMFDKNADG YIDLDELKIM LQATGETITE DDIEELMKDG DKNNDGRIDY DEFLEFMKGV E

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.

Description:

Growth Hormone Releasing Peptide-2

GHRP-2, GHRP.

Product # :

HOR-271

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Shipped at Room temp

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Description

Growth Hormone Releasing Peptide-2 Synthetic is a single, non-glycosylated polypeptide chain containing 6 amino acids, having a molecular mass of 817.9 Dalton and a Molecular formula of C45H55N9O6.

Formulation

The GHRP-2 hormone was lyophilized with no additives.

Purity

Greater than 99.0% as determined by analysis by RP-HPLC.

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Introduction
GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH act directly on pituitary somatotrophs to stimulate GH release. GHRP-2, an investigational drug, is one of the most potent members of the GHRP family. It has been shown to be effective in adults via the oral and intranasal as well as the iv route of administration.
Synonyms
GHRP-2, GHRP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Growth Hormone Releasing Peptide-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP-2 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 GHRP-2 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-D-Ala-D-2-Nal-Ala-Trp-D-Phe-Lys-NH2.
Background
What is the molecular weight/Mw of GHRP2 Protein?
GHRP2 Protein has a total Mw of 0.817kDa.

What is the Purity of GHRP2 Protein?
GHRP2 Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of GHRP2 Protein?
The biological functionality of GHRP2 Protein will be determined in the future.

What is the amino acid sequence of GHRP2 Protein?
H-D-Ala-D-2-Nal-Ala-Trp-D-Phe-Lys-NH2.

What applications can GHRP2 Protein be used in?
GHRP2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GHRP2 Protein?
The endotoxin level is minimal, GHRP2 Protein was purified using conventional chromatography techniques.

Who supplies GHRP2 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 GHRP2?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

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