Search: 1000 results found for "glucagon"

Description:

Growth Hormone Anatagonist Rat Recombinant

GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

CYT-1250

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Description

Rat Growth Hormone Anatagonist produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 22 kDa. GH Antagonist Rat is purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045M NaHCO3.

Purity

Greater than 98.0% as determined by:

(a) Analysis by RP-HPLC

(b) Analysis by Gel Filtration.

(c) Analysis by SDS-PAGE.

Biological Activity

Plays a role as antagonist using an in vitro bioassay in PDF-P1 3B9 cells stably transfected with rabbit GH receptors. It is capable of forming a 1:1 complex with the recombinant ovine growth hormone receptor extracellular domain and binds to this ECD with affinity similar the the wild type rGH.

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Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH Antagonist Rat although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 GH Antagonist Rat in 0.4% NaHCO3 or water adjusted to pH 9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Phe-Pro-Ala-Met.
Background
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with 4 other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which was evolved by a series of gene duplications. The 5 genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the 5 growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other 4 genes in the growth hormone locus.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman 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:

AOD-9604

Product # :

HOR-064

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Description

AOD-9604 is a synthetic single, non-glycosylated polypeptide chain containing 16 amino acids, having a molecular mass of 1815 Dalton and a Molecular formula of C78H123N23O23 S2.

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 AOD-9604 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AOD-9604 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 AOD-9604 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-Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-SerVal-Glu-Gly-Ser-Cys-Gly-Phe-OH (Disulfide bond).
Background
AOD-9604 is a synthetic analog of the C-terminal fragment (177–191) AOD-9604 stimulates lipolysis (fat breakdown) without the unwanted growth-promoting or insulin-antagonizing effects of full-length hGH. AOD-9604 is a potent lipolytic tool in animal models and researchers focus on its regenerative properties in joint health and its ability to modulate beta3 adrenergic receptors without the systemic risks of growth hormone.

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:

IGF-1 Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.

Product # :

CYT-216

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Description

IGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.6kDa.IGF-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated solution in PBS, pH 7.0.

Purity

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

Biological Activity

The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 105IU/mg.

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Introduction
The somatomedins, IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B.
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
Background
IGF stands for INS like growth factors, which are proteins that have a high similarity to INS. They are part of a complicated process that uses cells to communication with the physiologic environment around them. IGF’s complex system is often called the ‘axis’. This consists of:
● Two cell-surface receptors (IGF1R and IGF2R)
● Two ligands (IGF-1 and IGF-2)
● A family of six high-affinity IGF-binding proteins.
● Proteases.
The Effect IGF Has On The Body
Many unique tissue types express the IGF-1 receptor, and the effects can vary. It induces the survival of neurons, may catalyse skeletal muscle hypertrophy by inducing protein synthesis, and by blocking muscle atrophy. It works as a protector for cartilage cells, and may work to be an anabolic factor for the bones. When used in high concentrations, it can activate the INS receptor, and can even complement the effects that INS has on the body.
Diseases And IGF
Diseases and IGF are closely related, and a number of them can be affected. The INS IGF axis is thought to have an effect on aging, with an increased life span shown in fruit flies when used in studies.
It is also important to note the crucial role that IGF plays in cancer and diabetes - IGF- 1 has been shown to stimulate growth in both prostate and breast cancer cells. The degree of risk that IGF-1 poses is up for debate, and many scientists are not in agreement. IGF has also shown to have the ability to decrease blood glucose levels, although not quite as effective as INS.
How Was IGF Discovered?
Investigators began studying the effects of biological substances on cells and tissues outside the body when IGFs were discovered. The name is self explanatory in the fact that IGF performs INS actions in some tissues, but is less potent than INS at decreasing blood sugar. Its fundamental action is to stimulate growth, whether that be within the epidermal growth factor or the nerve growth factor.
What’s The Difference Between IGF-1 And IGF-2?
The two types of IGF are IGF-1 and IGF-2. Although the names are similar, the specific actions that they take are different - they bind and activate completely difference receptors. The major actor in them both is the effect that they have on cell growth. Most of the actions of the pituitary GH are mediated by IGFs, but predominantly IGF-1. GH works to stimulate many tissues within the body, especially the liver which then secretes IGF-1. This then causes hypertrophy, or in layman's terms, an increase in cell size, as well as hyperplasia which is an increase in the number of cells.
The IGF-1 concentration will increase during childhood and hit peak during puberty, but will then decrease afterwards, as does the hormone secretion itself. It has been proven that children and adults with a deficiency of the GH have low serum IGF-1 concentrations when put in comparison with others in the same age range. Patients who have conditions like acromegaly have been shown to have increased serum IGF-1 concentrations. The production of IGF-2 is less dependent on the secretion of GH than IGF-1, and is much less important for stimulating linear growth.
What is the molecular weight/Mw of IGF1 HUMAN Protein?
IGF1 HUMAN Protein has a total Mw of 7.6kDa.

What is the source or expression system of IGF1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IGF1 HUMAN Protein?
IGF1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 HUMAN Protein?
The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 105IU/mg.
What is the amino acid sequence of IGF1 HUMAN Protein?
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

What applications can IGF1 HUMAN Protein be used in?
IGF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 HUMAN Protein?
The endotoxin level is minimal, IGF1 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:

Myelin Oligodendrocyte Glycoprotein

Myelin Oligodendrocyte Glycoprotein, MOG.

Product # :

PRO-371

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Description

Myelin Oligodendrocyte Glycoprotein is a single, non-glycosylated polypeptide chain containing 21 amino acids and having a molecular mass of 2581 Dalton, the molecular formula: C118H177N35O29S.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 98.0% as determined by RP-HPLC.

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Introduction
MOG is a transmembrane protein expressed on the surface of oligodendrocyte cell and on the outermost surface of myelin sheaths. MOG comprises about 0.1% of total CNS myelin protein. The MOG gene is a member of the immunoglobulin gene superfamily and is found within the MHC. The MOG gene is found on chromosome 6p21.3-p22. Myelin Oligodendrocyte Glycoprotein is a glycoprotein thought to be significant in the process of myelinization of nerves in the central nervous system (CNS). MOG peptide (35-55) is highly encephalitogenic and can induce strong T and B cell responses. A single injection of this peptide produces a relapsing- remitting neurologic disease with extensive plaque-like demyelination. Because of the clinical, histophathologic, and immunologic similarities with multiple sclerosis (MS), the MOG induced demyelinating encephalomyelitis may serve as a model for investigating MS.
Synonyms
Myelin Oligodendrocyte Glycoprotein, MOG.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MOG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MOG 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 MOG in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Met-Glu-Val-Gly-Trp-Tyr-Arg-Ser-Pro-Phe-Ser-Arg-Val-Val-His-Leu-Tyr-Arg-Asn-Gly-Lys-OH.

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:

Maltose Binding Protein E.coli Recombinant, His Tag

Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

Product # :

PRO-2322

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Description

Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.

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:

Insulin Like Growth Factor-1, Mutant E3R Human Recombinant

Insulin-Like Growth Factor-1.

Product # :

CYT-1217

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Description

IGF1 E3R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (Gly49-Ala118) and having a molecular mass of 8.6kDa. IGF1 E3R Human is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The filtered (0.4µm) concentrated protein solution was lyophilized from 0.5mg/ml solution in 50 mM NaCl, 20 mM Tris and 5% (w/v) trehalose, pH 8.0.

Purity

Greater than 95% as determined by SDS-PAGE.

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Synonyms
Insulin-Like Growth Factor-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
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. IGF1 E3R is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.
Background
Insulin-like Growth Factor 1 (IGF-1) is a critical peptide hormone that plays a central role in regulating growth and development. Genetic mutations in the IGF-1 gene can result in altered IGF-1 variants, leading to various physiological consequences. Understanding these IGF-1 mutants is of paramount importance as they offer insights into growth disorders, metabolic regulation, and potential therapeutic avenues. This research delves into the world of IGF-1 mutants, shedding light on their diverse functions and implications for human health.
The primary objective of this research is to elucidate the impact of IGF-1 mutations on growth regulation. In vitro and in vivo experiments will be conducted to investigate how these mutants interact with IGF-1 receptors, influence downstream signaling pathways, and modulate growth plate dynamics. Understanding these mechanisms is crucial for unraveling the complexities of growth disorders associated with IGF-1 mutations.
The second objective is to assess the clinical relevance of IGF-1 mutants in growth-related conditions. Clinical studies involving individuals with growth hormone deficiencies or growth disorders linked to IGF-1 mutations will be conducted to evaluate the effects of these mutants on stature and overall health. These investigations may provide valuable insights into potential therapeutic strategies for individuals affected by growth-related disorders.
The third objective is to explore the broader implications of IGF-1 mutants in metabolic regulation and age-related conditions. Research will investigate their roles in metabolic homeostasis, longevity, and susceptibility to age-related diseases. Understanding the multifaceted properties of IGF-1 mutants may open new avenues for therapeutic interventions in various health and aging-related conditions.
By delving into the diverse functions of IGF-1 mutants, this research aims to expand our understanding of their physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for growth disorders, metabolic conditions, and age-related diseases.
What is the molecular weight/Mw of IGF1 E3R HUMAN Protein?
IGF1 E3R HUMAN Protein has a total Mw of 8.6kDa.

What is the source or expression system of IGF1 E3R HUMAN Protein?
Escherichia Coli.

What is the Purity of IGF1 E3R HUMAN Protein?
IGF1 E3R HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 E3R HUMAN Protein?
The biological functionality of IGF1 E3R HUMAN Protein will be determined in the future.

What is the amino acid sequence of IGF1 E3R HUMAN Protein?
MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.

What applications can IGF1 E3R HUMAN Protein be used in?
IGF1 E3R HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 E3R HUMAN Protein?
The endotoxin level is minimal, IGF1 E3R 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:

IFN-Gamma Mouse Recombinant

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

Product # :

CYT-358

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Description

IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg

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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs.
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
Background
What is the molecular weight/Mw of IFNG MOUSE Protein?
IFNG MOUSE Protein has a total Mw of 15.6kDa.

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

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

What is the Biological Activity of IFNG MOUSE Protein?
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg

What is the amino acid sequence of IFNG MOUSE Protein?
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.

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

What is the endotoxin level for IFNG MOUSE Protein?
The endotoxin level is minimal, IFNG 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:

Regulator of G-Protein Signaling 16 Human Recombinant

A28-RGS14, A28-RGS14P, RGS-R, Regulator of G-protein signaling 16, RGS16, Retinally abundant regulator of G-protein signaling, Retinal-specific RGS, hRGS-r, RGSR.

Product # :

PRO-798

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Description

RGS16 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (1-202 a.a.) and having a molecular mass of 24.9 kDa. The RGS16 is fused to a 20 amino acid His Tag at N-terminal and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RGS16 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4), 0.1M NaCl and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
RGS16 is part of the ''regulator of G protein signaling'' family. RGS16 inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. RGS16 Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha. RGS16 regulates the kinetics of signaling in the phototransduction cascade.
Synonyms
A28-RGS14, A28-RGS14P, RGS-R, Regulator of G-protein signaling 16, RGS16, Retinally abundant regulator of G-protein signaling, Retinal-specific RGS, hRGS-r, RGSR.
Physical Appearance
Sterile Filtered clear 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 MCRTLAAFPT TCLERAKEFK TRLGIFLHKS ELGCDTGSTG KFEWGSKHSK ENRNFSEDVL GWRESFDLLL SSKNGVAAFH AFLKTEFSEE NLEFWLACEE FKKIRSATKL ASRAHQIFEE FICSEAPKEV NIDHETRELT RMNLQTATAT CFDAAQGKTR TLMEKDSYPR FLKSPAYRDL AAQASAASAT LSSCSLDEPS HT.

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:

Insulin, Mouse Anti-Human

Product # :

ANT-100

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Description

These clones have been derived from hybridization of X63-Ag8-653 myeloma cells with spleen cells of Balb/c mice immunised with purified human insulin.

Formulation

The vial contains antibody in PBS, pH 7.4, containing 0.09% of sodium azide (NaN3) as preservative.

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Introduction
Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Physical Appearance
Sterile Filtered solution.
Stability
Store at + 4°C.
Clone
7F8.
Species Reactivity
These antibodies cross-react with human proinsulin, bovine insulin (30%) and porcine insulin. No cross-reaction with free C-peptide.
Specificity
Insulin, human.
Isotype
IgG1 kappa.
Type
Mouse Anti Human Monoclonal.
Purification Method
Purified by chromatography on 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:

Glycerol dehydrogenase E.coli Recombinant

ECK3937, JW5556, Glycerol dehydrogenase, GDH, GLDH, b3945.

Product # :

ENZ-827

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Description

GLDA E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-367 a.a) and having a molecular mass of 41.1kDa.GLDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GLDA protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Glycerol dehydrogenase (GldA) catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). The GldA protein allows microorganisms to use glycerol as a source of carbon under anaerobic conditions. Furthermore, in E.coli GldA has an imperative role by regulating the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. GldA possesses an extensive substrate specificity, due to its ability to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively.
Synonyms
ECK3937, JW5556, Glycerol dehydrogenase, GDH, GLDH, b3945.
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 MGSMDRIIQS PGKYIQGADV INRLGEYLKP LAERWLVVGD KFVLGFAQST VEKSFKDAGL VVEIAPFGGE CSQNEIDRLR GIAETAQCGA ILGIGGGKTL DTAKALAHFM GVPVAIAPTI ASTDAPCSAL SVIYTDEGEF DRYLLLPNNP NMVIVDTKIV AGAPARLLAA GIGDALATWF EARACSRSGA TTMAGGKCTQ AALALAELCY NTLLEEGEKA MLAAEQHVVT PALERVIEAN TYLSGVGFES GGLAAAHAVH NGLTAIPDAH HYYHGEKVAF GTLTQLVLEN APVEEIETVA ALSHAVGLPI TLAQLDIKED VPAKMRIVAE AACAEGETIH NMPGGATPDQ VYAALLVADQ YGQRFLQEWE.

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:

Glycerol kinase E. Coli Recombinant

Glycerol kinase, glycerol 3-phosphotransferase, Glycerokinase, GK.

Product # :

PKA-038

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Description

GlpK E. Coli Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 525 amino acids (1-502 a.a) and having a molecular mass of 58.6 kDa.GlpK is fused to a 23 amino acid His-tag at N-terminus& purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GlpK protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4),10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GlpK also known as glycerol kinase, is a member of the FGGY kinase family. GlpK catalyzes the transfer of a phosphate group from ATP to glycerol, thereby forming glycerol phosphate. Furthermore, this intermediate can then be converted to dihydroxyacetone phosphate (DHAP), which is utilized in either glycolysis or gluconeogenesis. The activity of GlpK is affected by numerous metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) triggers modifications in the quaternary structure of Glpk.
Synonyms
Glycerol kinase, glycerol 3-phosphotransferase, Glycerokinase, GK.
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 MGSMTEKKYI VALDQGTTSS RAVVMDHDAN IISVSQREFE QIYPKPGWVE HDPMEIWATQ SSTLVEVLAK ADISSDQIAA IGITNQRETT IVWEKETGKP IYNAIVWQCR RTAEICEHLK RDGLEDYIRS NTGLVIDPYF SGTKVKWILD HVEGSRERAR RGELLFGTVD TWLIWKMTQG RVHVTDYTNA SRTMLFNIHT LDWDDKMLEV LDIPREMLPE VRRSSEVYGQ TNIGGKGGTR IPISGIAGDQ QAALFGQLCV KEGMAKNTYG TGCFMLMNTG EKAVKSENGL LTTIACGPTG EVNYALEGAV FMAGASIQWL RDEMKLINDA YDSEYFATKV QNTNGVYVVP AFTGLGAPYW DPYARGAIFG LTRGVNANHI IRATLESIAY QTRDVLEAMQ ADSGIRLHAL RVDGGAVANN FLMQFQSDIL GTRVERPEVR EVTALGAAYL AGLAVGFWQN LDELQEKAVI EREFRPGIET TERNYRYAGW KKAVKRAMAW EEHDE.

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:

Ganirelix

Product # :

HOR-276

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Description

Ganirelix acetate is a synthetic decapeptide with high antagonistic activity against naturally occurring gonadotropin-releasing hormone (GnRH). Ganirelix acetate is derived from native GnRH with substitutions of amino acids at positions 1, 2, 3, 6, 8, and 10 to form the following molecular formula of the peptide: N-acetyl-3-(2-napthyl)-D-alanyl-4-chloro-D-phenylalanyl-3-(3-pyridyl)-D-alanyl-L-seryl-L-tyrosyl-N 9 ,N 10 -diethyl- D-homoarginyl-L-leucyl-N 9 ,N 10 -diethyl-L-homoarginyl-L-prolyl-D-alanylamide acetate. The molecular weight for Ganirelix acetate is 1570.4 Dalton as an anhydrous free base.

Formulation

The Ganirelix hormone (0.5mg/ml) contains 0.1mg acetic acid and 23.5mg mannitol pH-5.

Purity

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

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Physical Appearance
Sterile Filtered colorless liquid formulation.
Stability
Ganirelix should be stored between 2°C- 8°C at all time. DO NOT FREEZE.
Background
What is the molecular weight/Mw of GANIRELIX PEPTIDE Protein?
GANIRELIX PEPTIDE Protein has a total Mw of 1.57kDa.

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

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

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

What is the endotoxin level for GANIRELIX PEPTIDE Protein?
The endotoxin level is minimal, GANIRELIX PEPTIDE 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:

S100 Calcium Binding Protein A11 Human Recombinant

Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.

Product # :

PRO-385

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Description

S100A11 Human Recombinant is expressed in E. coli having a molecular weight of 17kDa fused to an amino terminal hexahistidine tag.

Source

Escherichia Coli.

Formulation

S100A11 is supplied in PBS and 50% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.
2 bands on Western blot at 17 and 34 kDa, respectively representing monomeric and dimeric form.

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Introduction
S100A11 is a member of the S100 family of proteins which contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100A11 may function in motility, invasion and tubulin polymerisation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of S100A11 have been implicated in tumor metastasis.
Synonyms
Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.
Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Applications
S100A11 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.

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

Description:

TIMELESS Interacting Protein Human Recombinant

TIMELESS Interacting Protein, CSM3 Homolog.

Product # :

PRO-1710

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Description

TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.
Synonyms
TIMELESS Interacting Protein, CSM3 Homolog.
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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR

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:

Transketolase Human Recombinant

Transketolase, TK, TKT1, EC 2.2.1.1.

Product # :

ENZ-588

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Description

TKT Human Recombinant produced in E. coli is a single polypeptide chain containing 643 amino acids (1-623) and having a molecular mass of 70.0kDa.TKT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TKT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
TKT is a thiamine-dependent enzyme that takes part in the channeling of leftover sugar phosphates to glycolysis in the pentose phosphate pathway. Multiple alternatively spliced variants are known that encode the same protein.
Synonyms
Transketolase, TK, TKT1, EC 2.2.1.1.
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).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE LLKMFGIDRD AIAQAVRGLI TKA.

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:

GDP Dissociation Inhibitor 1 Human Recombinant

Rab GDP dissociation inhibitor alpha, Rab GDI alpha, GDP Dissociation Inhibitor 1, GDI1, Guanosine diphosphate dissociation inhibitor 1, GDI-1, Oligophrenin-2, XAP-4, GDIL, OPHN2, RABGDIA, XAP4, MRX41, MRX48, 1A, RABGD1A.

Product # :

PRO-2023

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Description

GDI1 Human Recombinant produced in E. coli is a single polypeptide chain containing 470 amino acids (1-447) and having a molecular mass of 53 kDa.GDI1 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDI1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
GDP Dissociation Inhibitor 1 (GDI1) is expressed mainly in neural and sensory tissues. GDI1 regulates the GDP/GTP exchange reaction of nearly all Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. GDI1 is also promoting the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Mutations in GDI1 have been associated with X-linked nonspecific mental retardation.
Synonyms
Rab GDP dissociation inhibitor alpha, Rab GDI alpha, GDP Dissociation Inhibitor 1, GDI1, Guanosine diphosphate dissociation inhibitor 1, GDI-1, Oligophrenin-2, XAP-4, GDIL, OPHN2, RABGDIA, XAP4, MRX41, MRX48, 1A, RABGD1A.
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 MGSMDEEYDV IVLGTGLTEC ILSGIMSVNG KKVLHMDRNP YYGGESSSIT PLEELYKRFQ LLEGPPESMG RGRDWNVDLI PKFLMANGQL VKMLLYTEVT RYLDFKVVEG SFVYKGGKIY KVPSTETEAL ASNLMGMFEK RRFRKFLVFV ANFDENDPKT FEGVDPQTTS MRDVYRKFDL GQDVIDFTGH ALALYRTDDY LDQPCLETVN RIKLYSESLA RYGKSPYLYP LYGLGELPQG FARLSAIYGG TYMLNKPVDD IIMENGKVVG VKSEGEVARC KQLICDPSYI PDRVRKAGQV IRIICILSHP IKNTNDANSC QIIIPQNQVN RKSDIYVCMI SYAHNVAAQG KYIAIASTTV ETTDPEKEVE PALELLEPID QKFVAISDLY EPIDDGCESQ VFCSCSYDAT THFETTCNDI KDIYKRMAGT AFDFENMKRK QNDVFGEAEQ.

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:

Gastrokine 2 Human Recombinant

Gastrokine-2, Blottin, Down-regulated in gastric cancer, Trefoil factor interactions(z) 1, GKN2, BLOT, GDDR, TFIZ1, PRO813, BRICD1B, VLTI465.

Product # :

PRO-1588

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Description

Gastrokine 2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 21-184) containing 174 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 19.6kDa (calculated).

Source

Escherichia Coli.

Formulation

GKN2 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Gastrokine-2 (GKN2) is expressed in the gastric mucosa. GKN2 forms a heterodimer with TFF1- disulfide linked. GKN2 interacts with TFF2.
Synonyms
Gastrokine-2, Blottin, Down-regulated in gastric cancer, Trefoil factor interactions(z) 1, GKN2, BLOT, GDDR, TFIZ1, PRO813, BRICD1B, VLTI465.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely at 37°C. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. GKN2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASYEVFNIISPS NNGGNVQETV TIDNEKNTAI INIHAGSCSS TTIFDYKHGY IASRVLSRRA CFILKMDHQN IPPLNNLQWY IYEKQALDNM FSSKYTWVKY NPLESLIKDV DWFLLGSPIE KLCKHIPLYK GEVVENTHNV GAGGCAKAGL LGILGISICA DIHV.

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:

Procalcitonin Human Recombinant

Procalcitonin, PCT.

Product # :

HOR-304

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Description

Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids and having a molecular mass of 12.8 kDa.The Procalcitonin is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from 10mM sodium phosphate pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
Synonyms
Procalcitonin, PCT.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized procalcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution procalcitonin 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 procalcitonin sterile 18MΩ-cm H2O at 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN.

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:

Prostaglandin Reductase 2 Human Recombinant

Prostaglandin reductase 2, PRG-2, 15-oxoprostaglandin 13-reductase, Zinc-binding alcohol dehydrogenase domain-containing protein 1, PTGR2, ZADH1, PGR2.

Product # :

ENZ-601

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Description

PTGR2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (1-351) and having a molecular mass of 41.1kDa.PTGR2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PTGR2 solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 50mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Prostaglandin Reductase 2 (PTGR2) is a member of the medium-chain dehydrogenase/reductase superfamily. PTGR2 is an enzyme involved in the metabolism of prostaglandins. PTGR2 catalyzes an NADPH-dependent reduction of the conjugated alpha, beta-unsaturated double bond of 15-keto-PGE(2), which is a fundamental step in terminal inactivation of prostaglandins and suppression of PPARgamma-mediated adipocyte differentiation. PTGR2 may also be involved in controlling activation of the peroxisome proliferator-activated receptor.
Synonyms
Prostaglandin reductase 2, PRG-2, 15-oxoprostaglandin 13-reductase, Zinc-binding alcohol dehydrogenase domain-containing protein 1, PTGR2, ZADH1, PGR2.
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 MGSHMIVQRV VLNSRPGKNG NPVAENFRME EVYLPDNINE GQVQVRTLYL SVDPYMRCRM NEDTGTDYIT PWQLSQVVDG GGIGIIEESK HTNLTKGDFV TSFYWPWQTK VILDGNSLEK VDPQLVDGHL SYFLGAIGMP GLTSLIGIQE KGHITAGSNK
TMVVSGAAGA CGSVAGQIGH FLGCSRVVGI CGTHEKCILL TSELGFDAAI NYKKDNVAEQ LRESCPAGVD VYFDNVGGNI SDTVISQMNE NSHIILCGQI SQYNKDVPYP PPLSPAIEAI QKERNITRER FLVLNYKDKF EPGILQLSQW FKEGKLKIKE TVINGLENMG AAFQSMMTGG
NIGKQIVCIS EEISL.

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:

Wb123 Wuchereria Bancrofti Recombinant

Product # :

PRO-2820

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Description

The E.Coli derived Recombinant Wuchereria Bancrofti Wb123 is a 43kDa protein which is fused to a His tag in N-terminus.

Source

Escherichia Coli.

Formulation

25mM K2CO3 and PBS.

Purity

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

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Physical Appearance
Sterile Filtered clear solution.
Stability
Although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Background
One of the key antigens associated with Wuchereria bancrofti is Wb123, a protein that has emerged as a potential diagnostic marker for early infection and a target for vaccine development. Wb123 is a highly immunogenic protein that elicits a strong antibody response in individuals infected with Wuchereria bancrofti. Recombinant Wb123 is utilized in serological assays to detect specific IgG4 antibodies, which are indicative of active infection, particularly in the early stages before clinical symptoms manifest. Studies using rWb123 have demonstrated its high sensitivity and specificity, making it a valuable tool for diagnosing lymphatic filariasis and monitoring the effectiveness of mass drug administration (MDA) programs aimed at eliminating the disease.
Specificity
Immunoassay.
Purification Method
Purified by proprietary chromatographic technique.

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

Description:

Thymulin

Product # :

HOR-047

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

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

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymulin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Thymulin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.
Background
Thymulin, a nonapeptide hormone, is produced primarily by the thymus gland and has been recognized for its pivotal role in the immune system. It plays a significant role in the maturation and differentiation of T lymphocytes, which are crucial for immune function. Beyond its immune-related functions, research has increasingly unveiled the diverse physiological roles of thymulin. This study aims to comprehensively investigate thymulin, shedding light on its immunological functions and exploring its potential applications in various aspects of health and medicine.
The primary objective of this research is to elucidate the mechanisms underlying thymulin's role in immune regulation. In vitro and in vivo experiments will be conducted to explore thymulin's interactions with immune cells, its impact on T cell development and function, and its potential modulation of immune responses. Understanding these mechanisms is fundamental for harnessing thymulin's immunomodulatory properties.
The second objective is to assess the clinical relevance of thymulin in immune-related disorders. Clinical trials and studies involving individuals with autoimmune diseases, immunodeficiencies, and age-related immune decline will be conducted to evaluate the potential therapeutic applications of thymulin. These investigations may offer insights into the use of thymulin as an immunomodulatory agent in various clinical settings.
The third objective is to explore the broader implications of thymulin in health and medicine. Research will investigate its potential roles in areas beyond immunology, such as neuroprotection, wound healing, and tissue regeneration. Understanding the multifaceted properties of thymulin may open new avenues for therapeutic interventions in various medical specialties.
By delving into the diverse functions of thymulin, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may have implications for the development of innovative approaches in immunology and healthcare, ultimately benefiting patients affected by immune-related disorders and other medical conditions.
What is the molecular weight/Mw of THYMALIN Protein?
THYMALIN Protein has a total Mw of 0.85kDa.

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

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

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

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

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

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

Description:

Neuregulin-1/Heregulin Alpha (EGF Domain) Human Recombinant

Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.

Product # :

CYT-736

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Shipped at Room temp

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Description

Recombinant Human Neuregulin-1/Heregulin Alpha (EGF Domain) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 65 amino acids and having a total molecular mass of 7.4kDa. NRG1-A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 6.0 and 150mM NaCl.

Purity

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

Biological Activity

The ED₅₀ was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 40 ng/ml, corresponding to a specific activity of > 2.5×10⁴ units/mg.

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Introduction
Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. These isoforms contain the heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). All these factors have the Ig and EGF-like domain, and are able to bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. NRG1 isoforms act to induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells.
Synonyms
Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NRG1-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-A should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized NRG1-A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCQPGF TGARCTENVP MKVQNQEKAE ELYQK.

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:

S100 Calcium Binding Protein A6 Human Recombinant

Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.

Product # :

PRO-148

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Shipped with Ice Packs

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Description

S100A6 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 110 amino acids (1-90 a.a.) and having a molecular mass of 12.3kDa. The S100A6 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The S100A6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 30% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A6 function in stimulation of prolactin secretion and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.
Synonyms
Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.
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 MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL DRNKDQEVNF QEYVTFLGAL ALIYNEALKG.

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:

S100 Calcium Binding Protein A8, His-Myc Tag Human Recombinant

S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.

Product # :

PRO-2329

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Shipping Method :

Shipped with Ice Packs

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Description

S100A8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids (1-93) and having a molecular mass of 14.5kDa. S100A8 is fused to a 24 aa His-tag at N-terminus and to a 10 aa Myc-tag at C-terminus.

Source

Escherichia Coli.

Formulation

The S100A8 solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
Synonyms
S100 Calcium Binding Protein A8, S100 Calcium-Binding Protein A8 (Calgranulin A), Migration Inhibitory Factor-Related Protein 8, Leukocyte L1 Complex Light Chain , Urinary Stone Protein Band A, Calprotectin L1L Subunit, Cystic Fibrosis Antigen, Calgranulin-A, MRP8, CAGA, CFAG, P8, S100 Calcium Binding Protein A8 (Calgranulin A), S100 Calcium-Binding Protein A8, Calgranulin A, 60B8AG, CP-10, MA38, MRP-8, CGLA, L1Ag, MIF, NIF.
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 MGSHMLTELE KALNSIIDVY HKYSLIKGNF HAVYRDDLKK LLETECPQYI RKKGADVWFK ELDINTDGAV NFQEFLILVI KMGVAAHKKS HEESHKEEQK LISEEDL.

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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