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Name :
RBP4 MouseDescription:
Retinol Binding Protein-4 Mouse Recombinant, BioActive
Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
Product # :
CYT-1158Price :
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Shipped with Ice Packs
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Description
RBP4 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 191 amino acids (19-201 a.a) and having a molecular mass of 22.4kDa. RBP4 is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The RBP4 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Retinol Binding Protein-4 or RBP4, is the retinol currier protein in the plasma. RBP4 takes part on the conversion of retinol to the stable and soluble retinol complex in the plasma. RBP4 carries retinol from the liver tissue where its store to peripheral tissues. RBP-retinol complex has interactions with transthyretin in the plasma, thus prevents its loss by filtration in the kidney.
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Synonyms
Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ERDCRVSSFR VKENFDKARF SGLWYAIAKK DPEGLFLQDN IIAEFSVDEK GHMSATAKGR VRLLSNWEVC ADMVGTFTDT EDPAKFKMKY WGVASFLQRG NDDHWIIDTD YDTFALQYSC RLQNLDGTCA DSYSFVFSRD PNGLSPETRR LVRQRQEELC LERQYRWIEH NGYCQSRPSR NSLLEHHHHH H.
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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Name :
Leptin Super Antagonist RatDescription:
Leptin Super Antagonist Rat Recombinant
Product # :
CYT-1240Price :
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Shipped at Room temp
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Description
Super Leptin Antagonist Rat Recombinant is a single polypeptide chain containing 146 amino acids. Super Rat Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super Rat leptin antagonist that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
ProSpec’s super Rat leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Rat leptin antagonist also inhibits various leptin effects in several in vitro bioassays.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super Rat leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Rat leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist 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.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-His.
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Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function and is encoded by the obese gene. Leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are expressed mainly in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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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Name :
Leptin SalamanderDescription:
Leptin Salamander Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
Product # :
CYT-704Price :
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Shipped at Room temp
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Description
Leptin Salamander Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of 16kDa. The Salamander Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Salamander Leptin was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
By inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity in that test is similar to that of mouse leptin.
More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized recombinant salamander leptin although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of recombinant salamander leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization recombinant salamander leptin can be stored at +4C for at least two weeks.
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Solubility
It is recommended to reconstitute the lyophilized Salamander Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the ten N-terminal amino acids was determined and was found to be Ala-Ile-Met-Val-Asp-Gln-Leu-Arg-Met-Asp.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.104 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AIF1 HumanDescription:
Allograft Inflammatory Factor 1 Human Recombinant
AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.
Product # :
CYT-697Price :
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Shipped with Ice Packs
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Description
AIF1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 18.9kDa. AIF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E. Coli.
Formulation
The AIF1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
2mM DTT, 200mM NaCl and 20% glycerol.Purity
Greater than 95% as determined by SDS PAGE.
sds-page
More Info
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Introduction
Human AIF1 protein shares 98% homology/identity with that of rat. AIF1 is expressed in macrophages and neutrophils. The expression of AIF1 transcripts is upregulated by IFN-g in rat macrophages. AIF1 is expressed selectively in human macrophage-like cell lines, and in a subset of CD68(+) macrophages in the interstitial and perivascular spaces of human heart allografts. In quiescent cultured human vascular smooth muscle cells synthesis of AIF1 is induced by IFN-g, IL1b, and conditioned medium of T-cells. Overexpression of AIF1 in human VSMCs results in enhanced growth of these cells. AIF1 is expressed during apoptosis rat mammary gland and ventral prostate tissues. Allograft Inflammatory Factor 1 is expressed by several tumor-associated activated macrophages and microglial cells in rat and human gliomas. There is an evident relationship of AIF1-expressing activated macrophages and microglial cells with tumor malignancy in humans.
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Synonyms
AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.
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Stability
Store AIF1 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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.
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Background
Allograft Inflammatory Factor 1 Human Recombinant: Uncovering its Role in Immune Responses and Therapeutic Prospects
1. Abstract
This paper explores the Allograft Inflammatory Factor 1 Human Recombinant (AIF-1), a cytoplasmic, IFN-gamma-inducible calcium-binding protein involved in inflammation and immunity. We review the structure, biological roles, and involvement of AIF-1 in disease pathology. The therapeutic potential of AIF-1 in immune-related disorders is also explored.
2. Introduction
AIF-1, also known as IBA1, plays an important role in immune responses. It is associated with various immune cells, particularly macrophages, and has been implicated in numerous inflammatory and immune-related diseases. Understanding the function of AIF-1 could aid the development of novel therapeutic strategies.
3. Structure and Signaling of AIF-1
AIF-1 is a small 17 kDa protein with an EF-hand calcium-binding motif. Although the precise mechanism by which AIF-1 exerts its functions is not entirely clear, it is known to regulate the activation, migration, and proliferation of macrophages, key cells involved in immune responses.
4. Biological Functions of AIF-1
AIF-1 has been shown to play key roles in macrophage activation and function, which are central to inflammation and immunity. It is also implicated in cell survival, proliferation, and differentiation.
5. AIF-1 in Disease Pathology
AIF-1 has been associated with a range of inflammatory and immune-related diseases, including rheumatoid arthritis, atherosclerosis, and multiple sclerosis. It is also implicated in several cancers, further underscoring its broad physiological and pathological relevance.
6. Therapeutic Potential of AIF-1
Given its pivotal role in immune responses, AIF-1 presents an intriguing target for therapeutic interventions in immune-related diseases. Modulating the activity of AIF-1 could potentially alleviate pathological inflammation and autoimmunity.
7. Conclusion and Future Perspectives
Our knowledge of AIF-1 and its functions has significantly improved in recent years, but much remains to be discovered. Further research into AIF-1's exact molecular mechanisms and roles in disease will undoubtedly contribute to the development of novel therapeutic strategies.
What is the molecular weight/Mw of AIF1 Protein?
AIF1 Protein has a total Mw of 18.9kDa.
What is the source or expression system of AIF1 Protein?
Escherichia Coli.
What is the Purity of AIF1 Protein?
AIF1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of AIF1 Protein?
The biological functionality of AIF1 Protein will be determined in the future.
What is the amino acid sequence of AIF1 Protein?
MGSSHHHHHH SSGLVPRGSH MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.
What applications can AIF1 Protein be used in?
AIF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for AIF1 Protein?
The endotoxin level is minimal, AIF1 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.
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Name :
Prolactin OvineDescription:
Prolactin Ovine Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-240Price :
Quantity :
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Shipped at Room temp
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Description
Prolactin Ovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 23 kDa. The Prolactin n is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Is fully biologically active as evidenced by inducing proliferation of Nb2 cells.More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prl 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.
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Solubility
It is recommended to reconstitute the lyophilized Prolactin in sterile 18MΩ-cm H2O or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Thr-Pro-Val-Cys-Pro.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.93 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC 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.
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Name :
Visfatin HumanDescription:
Visfatin Human Recombinant
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Product # :
CYT-318Price :
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Shipped at Room temp
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Description
Visfatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 466 amino acids. The total molecular mass is 52.6kDa (calculated). The Visfatin is purified by Flag-affinity chromatography.
Source
Escherichia Coli.
Formulation
Visfatin was lyophilized with no additives.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The activity is determined by its ability to induce IL-6, IL-1 beta and TNF alpha production from human PBMCs at 100ng/ml.More Info
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Introduction
Excess adiposity is the most important risk in the development of type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-a, and IL-6, that modulate sensitivity and appear to play an important role in the pathogenesis, diabetes, dyslipidemia, inflammation, and atherosclerosis. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
Visfatin exerts mimetic effects that are dose-dependent and quantitatively similar to stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its mimetic effects, visfatin was as effective in reducing hyperglycemia in deficient diabetic mice. Visfatin was also found to be bound to and activate receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin did not compete for binding to the receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes. -
Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Visfatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Visfatin 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.
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Solubility
Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with 20 mM HCl at a concentration of 0.1 mg/mL, which can be further diluted into other aqueous solutions. Wait several minutes for full reconstitution and solubility.
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Amino Acid Sequence
MPPNTSKVYS YFECREKKTE NSKLRKVKYE ETVFYGLQYI LNKYLKGKVV TKEKIQEAKD VYKEHFQDDV FNEKGWNYIL EKYDGHLPIE IKAVPEGFVI PRGNVLFTVE NTDPECYWLT NWIETILVQS WYPITVATNS REQKKILAKY LLETSGNLDG LEYKLHDFGY RGVSSQETAG IGASAHLVNF KGTDTVAGLA LIKKYYGTKD PVPGYSVPAA EHSTITAWGK DHEKDAFEHI VTQFSSVPVS VVSDSYDIYN ACEKIWGEDL RHLIVSRSTQ APLIIRPDSG NPLDTVLKVL EILGKKFPVT ENSKGYKLLP PYLRVIQGDG VDINTLQEIV EGMKQKMWSI ENIAFGSGGG LLQKLTRDLL NCSFKCSYVV TNGLGINVFK DPVADPNKRS KKGRLSLHRT PAGNFVTLEE GKGDLEEYGQ DLLHTVFKNG KVTKSYSFDE IRKNAQLNIE LEAAHH.
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Background
About Visfatin Human
Visfatin is a cytokine expressed in visceral fat that was originally isolated as a secreted
element that synergized with stem cell factors and IL-7. One of its main functions is to
enhance the development of B cell precursors.The cytokine is also known as the “Pre-B Cell Colony-Enhancing Factor (PBEF).” It has been
identified in vertebrates, including mice and humans, and it’s being studied due to its link
to inflammatory conditions, beta cell function, and cardiovascular disease.
What’s the Function of Visfatin Human Recombinant?Visfatin human recombinant is produced in E. Coli. It’s a single, non-glycosylated,
polypeptide chain that contains 466 amino acids, it’s purified by FLAG-affinity
chromatography, and it contains a total molecular mass of 52.6 kDa.
What Are the Main Applications of Visfatin Human Recombinant?The cytokine is being researched because of its involvement in glucose homeostasis,
dysregulation in biosynthesis and signal transduction, and the pathogenesis of diabetes.
Visfatin human recombinant is tailored exclusively for laboratory research, ensuring
experts can get further answers regarding the cytokine’s involvement in different
processes, including pathogenesis, diabetes, inflammation, dyslipidemia, and
atherosclerosis.Findings can also help during the identification of high-risk people for cardiovascular
disease and diabetes.
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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Name :
SPINT2 Human, Sf9Description:
Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant, Sf9
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
Product # :
PRO-2219Price :
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Description
SPINT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 176 amino acids (28-197 a.a.) and having a molecular mass of 20kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SPINT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SPINT2 protein solution (0.2mg/ml) contains phosphate buffered saline (pH 7.4) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
SPINT2 is a transmembrane protein acts as an inhibitor of HGF activator. SPINT2 inhibits plasmin, plasma and tissue kallikrein, and factor XIa. SPINT2 has two extracellular Kunitz domains that inhibit few serine proteases. SPINT2 is assumed tumor suppressor, mutations in SPINT2 leads to a congenital sodium diarrhea.
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Synonyms
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
ADRERSIHDF CLVSKVVGRC RASMPRWWYN VTDGSCQLFV YGGCDGNSNN YLTKEECLKK CATVTENATG DLATSRNAAD SSVPSAPRRQ DSEDHSSDMF NYEEYCTANA VTGPCRASFP RWYFDVERNS CNNFIYGGCR GNKNSYRSEE ACMLRCFRQQ ENPPLPLGSK HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RANK MouseDescription:
RANK Mouse Recombinant
Tumor necrosis factor receptor superfamily member 11A, Osteoclast differentiation factor receptor, ODFR, Receptor activator of NF-KB, activator of NFKB, FEO, OFE, OSTS, PDB2, RANK, RANKLOH18CR1, CD265, CD265 antigen, OPTB7, TRANCER, LOH18CR1, receptor activator of nuclear factor-kappa B.
Product # :
CYT-1161Price :
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Shipping Method :
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Description
RANK Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 426 amino acids (31-214 aa) and having a molecular mass of 47.5kDa.RANK is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
RANK protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Tumor necrosis factor receptor superfamily member 11A or TNFRSF11A or RANK, is a protein, part of the tumor necrosis factor receptor (TNFR) group of proteins. RANK acts as the receptor of RANK-Ligand and regulates osteoclast activation & differentiation. RANK protein has been linked to activation of NF-kappa B & c-jun N-terminal kinase, enhancement of T cell growth, bone remodeling and repair, dendritic cell function, lymph node development, immune cell function, mammary gland development & thermal regulation.
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Synonyms
Tumor necrosis factor receptor superfamily member 11A, Osteoclast differentiation factor receptor, ODFR, Receptor activator of NF-KB, activator of NFKB, FEO, OFE, OSTS, PDB2, RANK, RANKLOH18CR1, CD265, CD265 antigen, OPTB7, TRANCER, LOH18CR1, receptor activator of nuclear factor-kappa B.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADLVTPPCTQ ERHYEHLGRC CSRCEPGKYL SSKCTPTSDS VCLPCGPDEY LDTWNEEDKC LLHKVCDAGK ALVAVDPGNH TAPRRCACTA GYHWNSDCEC CRRNTECAPG FGAQHPLQLN KDTVCTPCLL GFFSDVFSST DKCKPWTNCT LLGKLEAHQG TTESDVVCSS SMTLRRPPKE AQAYLPSLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI VEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PEDF Human, HEKDescription:
Pigment Epithelium-Derived Factor Human Recombinant, HEK
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
Product # :
CYT-553Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PEDF Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing a total of 410 amino acids, having a molecular mass of 45.6 kDa and fused to an 11 aa FLAG tag at C-Terminus.The Human PEDF is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
The filtered (0.4µm) concentrated (0.5mg/ml) protein solution was lyophilized with 20mM Tris & 20mM NaCl pH-7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
PEDF & VEGF genes contribute to the development of diabetic retinopathy.
PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
SerpinF1 is a new promising approach for the treatment of osteosarcoma.
Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
PEDF blocks angiogenic effects of leptin through its anti-oxidative properties. -
Synonyms
Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.
-
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.
-
Solubility
It is recomnded to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGPAAADYKDDDDK.
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.
- View Data Sheet
Name :
NFKBIA HumanDescription:
NF-kappa-B Inhibitor Alpha Human Recombinant
Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha, nuclear factor of kappa light chain gene enhancer in B-cells, IKBA, I-kappa-B-alpha, IkappaBalpha, ikB-alpha, NFKBI, MAD-3, Major histocompatibility complex enhancer-binding protein MAD3, NF-kappa-B inhibitor alpha.
Product # :
PRO-960Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NFKBIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-317) and having a molecular mass of 37.7 kDa.NFKBIA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NFKBIA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
NFKBIA belongs to the I-kappa-B family of proteins which is separated into four groups (IkB-a, IkB-b, IkB-g, IkB-e). NFKBIA inhibits the NFkB complex by binding and impounding it in the cytoplasm. When stimulated, NFKBIA is phosphorylated on serine residues targeting it for degradation by the ubiquitin pathway.
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Synonyms
Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha, nuclear factor of kappa light chain gene enhancer in B-cells, IKBA, I-kappa-B-alpha, IkappaBalpha, ikB-alpha, NFKBI, MAD-3, Major histocompatibility complex enhancer-binding protein MAD3, NF-kappa-B inhibitor alpha.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ EIRLEPQEVP RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD LAFLNFQNNL QQTPLHLAVI TNQPEIAEAL LGAGCDPELR DFRGNTPLHL ACEQGCLASV GVLTQSCTTP HLHSILKATN YNGHTCLHLA SIHGYLGIVE LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG ADVNRVTYQG YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE DELPYDDCVF GGQRLTL
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.
- View Data Sheet
Name :
TTC33 HumanDescription:
Tetratricopeptide Repeat Domain 33 Human Recombinant
Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.
Product # :
PRO-1217Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TTC33 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-262) and having a molecular mass of 31.8 kDa.TTC33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TTC33 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Tetratricopeptide repeat protein 33 (TTC33) is comprised of 3 TPR repeats.
-
Synonyms
Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.
-
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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGS MASFGWK RKIGEKVSKV TSQQFEAEAA DEKDVVDNDE GNWLHAIKRR KEILLEGCAE KSKQLKDEGA SLAENKRYRE AIQKWDEALQ LTPNDATLYE MKSQVLMSLH EMFPAVHAAE MAVQQNPHSW ESWQTLGRAQ LGLGEIILAI RSFQVALHIY
PMNPEIWKED LSWARTLQEQ QKVAQRIKKS EAPAEVTHFS PKSIPDYDFE SDEIVAVCAA IAEKEKTVSA NKTMVIVSAS GAIETVTEKE DGATPPDGSV FIKAR
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.
- View Data Sheet
Name :
Erythropoietin Human, ActiveDescription:
Erythropoietin Receptor Human Recombinant, Active
EPO-R, EPOR, Erythropoietin Receptor.
Product # :
CYT-997Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EPOR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (25-250a.a.) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPOR is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPOR protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.More Info
-
Introduction
Erythropoietin receptor, also known as EPOR arbitrates erythropoietin-induced erythroblast proliferation as well as differentiation. During EPO binding, EPOR activates Jak2 tyrosine kinase which activates various intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. Furthermore, stimulated EPOR has a function in erythroid cell survival. Mutations in EPOR may possibly produce erythroleukemia and familial erythrocytosis. In addition, dysregulation of EPOR can affect on the growth of selected tumors.
-
Synonyms
EPO-R, EPOR, Erythropoietin Receptor.
-
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.
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Amino Acid Sequence
APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.
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Background
What is the molecular weight/Mw of ERYTHROPOIETIN Protein?
ERYTHROPOIETIN Protein has a total Mw of 25.6kDa.
What is the source or expression system of ERYTHROPOIETIN Protein?
Sf9, Baculovirus cells.
What is the Purity of ERYTHROPOIETIN Protein?
ERYTHROPOIETIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ERYTHROPOIETIN Protein?
Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.
What is the amino acid sequence of ERYTHROPOIETIN Protein?
APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.
What applications can ERYTHROPOIETIN Protein be used in?
ERYTHROPOIETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ERYTHROPOIETIN Protein?
The endotoxin level is minimal, ERYTHROPOIETIN 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.
- View Data Sheet
Name :
Epoetin Human, HisDescription:
Erythropoietin-alpha Human Recombinant, His Tag
800x600 Erythropoietin, EP, INN=Epoetin, EPO a, Erythropoietin-alpha, EPO. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}
Product # :
CYT-791Price :
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- sds-page
Description
800x600 EPO a Human Recombinant produced in Baculovirus is a single, glycosylated polypeptide chain containing 174 amino acids (28-193a.a.) and having a molecular mass of 19.5kDa.EPO a is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPO a protein solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The ED50 range is ≤0.5ng/ml and measured in a cell proliferation assay using TF-1 human erythroleukemic cells.
sds-page
More Info
-
Introduction
EPO a is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. EPO a is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO a also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
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Synonyms
Erythropoietin, EP, INN=Epoetin, EPO a, Erythropoietin-alpha, EPO.
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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.
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Amino Acid Sequence
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.
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Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 19.5kDa.
What is the source or expression system of EPOETIN Protein?
Sf9, Baculovirus cells.
What is the Purity of EPOETIN Protein?
EPOETIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EPOETIN Protein?
The ED50 range is ≤0.5ng/ml and measured in a cell proliferation assay using TF-1 human erythroleukemic cells.
What is the amino acid sequence of EPOETIN Protein?
APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALRAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDRLEHH HHHH.
What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN 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.
- View Data Sheet
Name :
TFRC HumanDescription:
Transferrin Receptor Human Recombinant
Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71.
Product # :
PRO-2180Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TFRC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 696 amino acids (89-760 a.a) and having a molecular mass of 77.7 kDa.TFRC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TFRC protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.
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Synonyms
Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMCKGVEP KTECERLAGT ESPVREEPGE DFPAARRLYW DDLKRKLSEK LDSTDFTGTI KLLNENSYVP REAGSQKDEN LALYVENQFR EFKLSKVWRD QHFVKIQVKD SAQNSVIIVD KNGRLVYLVE NPGGYVAYSK AATVTGKLVH ANFGTKKDFE DLYTPVNGSI VIVRAGKITF AEKVANAESL NAIGVLIYMD QTKFPIVNAE LSFFGHAHLG TGDPYTPGFP SFNHTQFPPS RSSGLPNIPV QTISRAAAEK LFGNMEGDCP SDWKTDSTCR MVTSESKNVK LTVSNVLKEI KILNIFGVIK GFVEPDHYVV VGAQRDAWGP GAAKSGVGTA LLLKLAQMFS DMVLKDGFQP SRSIIFASWS AGDFGSVGAT EWLEGYLSSL HLKAFTYINL DKAVLGTSNF KVSASPLLYT LIEKTMQNVK HPVTGQFLYQ DSNWASKVEK LTLDNAAFPF LAYSGIPAVS FCFCEDTDYP YLGTTMDTYK ELIERIPELN KVARAAAEVA GQFVIKLTHD VELNLDYERY NSQLLSFVRD LNQYRADIKE MGLSLQWLYS ARGDFFRATS RLTTDFGNAE KTDRFVMKKL NDRVMRVEYH FLSPYVSPKE SPFRHVFWGS GSHTLPALLE NLKLRKQNNG AFNETLFRNQ LALATWTIQG AANALSGDVW DIDNEF.
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.
- View Data Sheet
Name :
Epoetin Human, HEKDescription:
Erythropoietin-alpha Human Recombinant, HEK
Erythropoietin-Alpha, EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Product # :
CYT-083Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
EPO-a Human Recombinant produced in HEK cells is a glycosylated monomer, having a total molecular weight of 36kDa.The EPO-alpha is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The EPO-alpha was lyophilized from 1mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) and is typically 0.5-2.5ng/ml, corresponding to a specific activity of 400,000-2,000,000 units/mg.More Info
-
Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
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Synonyms
Erythropoietin-Alpha, EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EPO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha 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.
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Solubility
It is recommended to reconstitute the lyophilized EPO-alpha in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 36kDa.
What is the source or expression system of EPOETIN Protein?
HEK.
What is the Purity of EPOETIN Protein?
EPOETIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EPOETIN Protein?
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) and is typically 0.5-2.5ng/ml, corresponding to a specific activity of 400,000-2,000,000 units/mg.
What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN 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.
- View Data Sheet
Name :
Prolactin Human, HisDescription:
Prolactin Human Recombinant, His Tag
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-493Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Prolactin-His Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids fragment (29-227) and having a molecular mass of 23 kDa with an amino-terminal hexahistidine tag. The Prolactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Prolactin His is supplied in 1x PBS and 50% glycerol.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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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.
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.
- View Data Sheet
Name :
GMFB AntibodyDescription:
Glia Maturation Factor Beta, Mouse Anti Human
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.
Product # :
ANT-680Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines. -
Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.
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Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human GMFB mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GMFB amino acids 1-142 purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and Kappa light chain.
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Clone
PAT44D8AT.
-
Applications
GMFB antibody has been tested by ELISA, Western blot and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
GMFB antibody was purified from mouse ascitic fluids by protein-A affinity 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.
- View Data Sheet
Name :
RBP2 HumanDescription:
Retinol Binding Protein-2 Human Recombinant
CRABP-II, CRBP2, CRBPII, RBPC2, Retinol-binding protein 2, Cellular retinol-binding protein II, RBP2.
Product # :
CYT-751Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (1-134 a.a.) and having a molecular mass of 18kDa. RBP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RBP2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Retinol Binding Protein-2 (RBP2) which is present in the small intestinal epithelium takes part in the uptake and intracellular metabolism of vitamin A. Vitamin A is a fat-soluble vitamin essential for growth, reproduction, differentiation of epithelial tissues, and vision. RBP2 moderates the supply of retinoic acid to the nuclei of endometrial cells throughout the menstrual cycle.
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Synonyms
CRABP-II, CRBP2, CRBPII, RBPC2, Retinol-binding protein 2, Cellular retinol-binding protein II, RBP2.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTRDQN GTWEMESNEN FEGYMKALDI DFATRKIAVR LTQTKVIDQD GDNFKTKTTS TFRNYDVDFT VGVEFDEYTK SLDNRHVKAL VTWEGDVLVC VQKGEKENRG WKQWIEGDKL YLELTCGDQV CRQVFKKK.
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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Name :
RBP Human, NativeDescription:
Retinol Binding Protein Native Human
Product # :
CYT-1203Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Retinol Binding Protein Native produced in urine from the patients with renal tubular proteinuria having a molecular mass of approximately 21kD.
Source
Urine from the patients with renal tubular proteinuria.
Formulation
The protein was lyophilized (0.2 µm filtered) from 20mM NH4HCO3.
Purity
Greater than 96.0%.
More Info
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Introduction
Human Retinol Binding Protein, also known as RBP, is responsible for transporting and binding vitamin A. Human RBP has a binding site for 1 molecule of retinol and circulates in the plasma together with prealbumin as a protein complex. The prealbumin binding prevents greater glomerular losses of the human RBP. Only the retinol-free form of the RBP, which has no affinity for prealbumin, undergoes glomerular filtration unhindered as a result of its low Mw. Human RBP is re-absorbed by the tubular cells and catabolized there.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
RBP Human although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized RBP Human in phosphate buffer containing 0.15M NaCl.
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Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG and Syphilis.
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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Name :
TROVE2 HumanDescription:
TROVE Domain Family Member 2 Human Recombinant
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-329Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RO-60 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 60kDa. RO60 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 6M Urea, 500mM NaCl, 500mM imidazole and 10mM Tris pH-6.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
RO-60 although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent 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.
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Name :
ARHGEF39 HumanDescription:
Rho Guanine Nucleotide Exchange Factor 39 Human Recombinant
Rho guanine nucleotide exchange factor 39, ARHGEF39, C9orf100, RP11-331F9.7.
Product # :
PRO-2101Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARHGEF39 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-335 a.a) and having a molecular mass of 40.7kDa.ARHGEF39 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARHGEF39 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Rho Guanine Nucleotide Exchange Factor 39, also known as ARHGEF39, is a protein coding gene which owns one DH (DBL-homology) domain and one PH domain. ARHGEF39 encourages cell proliferation.
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Synonyms
Rho guanine nucleotide exchange factor 39, ARHGEF39, C9orf100, RP11-331F9.7.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMELSCPG SRCPVQEQRA RWERKRACTA RELLETERRY QEQLGLVATY FLGILKAKGT LRPPERQALF GSWELIYGAS QELLPYLEGG CWGQGLEGFC RHLELYNQFA ANSERSQTTL QEQLKKNKGF RRFVRLQEGR PEFGGLQLQD LLPLPLQRLQ QYENLVVALA ENTGPNSPDH QQLTRAARLI SETAQRVHTI GQKQKNDQHL RRVQALLSGR QAKGLTSGRW FLRQGWLLVV PPHGEPRPRM FFLFTDVLLM AKPRPPLHLL RSGTFACKAL YPMAQCHLSR VFGHSGGPCG GLLSLSFPHE KLLLMSTDQE ELSRWYHSLT WAISSQKN.
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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Name :
ETFB HumanDescription:
Electron-Transfer-Flavoprotein Beta Polypeptide Human Recombinant
Electron-transfer-flavoprotein beta polypeptide, MADD, beta-ETF.
Product # :
PRO-220Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ETFB 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 275 amino acids (1-255a.a.) and having a molecular mass of 30.0kDa. The ETFB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ETFB solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 40% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ETF is a heterodimer composed of alpha and beta subunit. ETFB protein is electron-transfer-flavoprotein, beta polypeptide that transports electrons between primary flavoprotein dehydrogenases involved in mitochondrial fatty acid and amino acid catabolism and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase.
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Synonyms
Electron-transfer-flavoprotein beta polypeptide, MADD, beta-ETF.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAELRVLVAV KRVIDYAVKI RVKPDRTGVV TDGVKHSMNP FCEIAVEEAV RLKEKKLVKE VIAVSCGPAQ CQETIRTALA MGADRGIHVE VPPAEAERLG PLQVARVLAK LAEKEKVDLV LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA SQVTLEGDKL
KVEREIDGGL ETLRLKLPAV VTADLRLNEP RYATLPNIMK AKKKKIEVIK PGDLGVDLTS KLSVISVEDP PQRTAGVKVE TTEDLVAKLK EIGRI.
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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Name :
SMARCA4 HumanDescription:
SMARCA4 Human Recombinant
SWI/SNF Related, Matrix Associated, Actin Dependent Regulator Of Chromatin, Subfamily A, Member 4, Mitotic Growth And Transcription Activator, ATP-Dependent Helicase SMARCA4, BRG1, Global Transcription Activator Homologous Sequence Sucrose Nonfermenting-Like 4, BRG1-Associated Factor 190A, Protein Brahma Homolog 1, BRM/SWI2-Related Gene 1, Homeotic Gene Regulator, Brahma Protein-Like 1 Nuclear Protein GRB1, Protein BRG-1, SNF2-Like 4, SNF2-Beta, BAF190A, SNF2L4, MRD16, RTPS2, SWI/SNF-Related Matrix-Associated Actin-Dependent Regulator Of Chromatin Subfamily A Member 4, Transcription Activator BRG1, EC 3.6.4.-, EC 3.6.1, BAF190, SNF2LB, HSNF2b, SNF2B, SNF2, SWI2, Transcription activator BRG1.
Product # :
PRO-2071Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SMARCA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (362-549aa) and having a molecular mass of 25kDa. SMARCA4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SMARCA4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
SMARCA4 belongs to the SWI/SNF family of proteins and is similar to the brahma protein of Drosophila. Proteins in this family have helicase and ATPase activities and are considered to regulate transcription ofcertain genes by altering the chromatin structure around those genes. SMARCA4 is part of the large ATP-dependent chromatin remodeling complex SNF/SWI, which is essential for transcriptional activation of genesnormally repressed by chromatin. In addition, SMARCA4 is able to bind BRCA1, as well as regulating the expression ofthe tumorigenic protein CD44. Moreover, mutations in SMARCA4 cause rhabdoid tumor predisposition syndrome type 2.
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Synonyms
SWI/SNF Related, Matrix Associated, Actin Dependent Regulator Of Chromatin, Subfamily A, Member 4, Mitotic Growth And Transcription Activator, ATP-Dependent Helicase SMARCA4, BRG1, Global Transcription Activator Homologous Sequence Sucrose Nonfermenting-Like 4, BRG1-Associated Factor 190A, Protein Brahma Homolog 1, BRM/SWI2-Related Gene 1, Homeotic Gene Regulator, Brahma Protein-Like 1 Nuclear Protein GRB1, Protein BRG-1, SNF2-Like 4, SNF2-Beta, BAF190A, SNF2L4, MRD16, RTPS2, SWI/SNF-Related Matrix-Associated Actin-Dependent Regulator Of Chromatin Subfamily A Member 4, Transcription Activator BRG1, EC 3.6.4.-, EC 3.6.1, BAF190, SNF2LB, HSNF2b, SNF2B, SNF2, SWI2, Transcription activator BRG1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDPVEILQ EREYRLQARI AHRIQELENL PGSLAGDLRT KATIELKALR LLNFQRQLRQ EVVVCMRRDT ALETALNAKA YKRSKRQSLR EARITEKLEK QQKIEQERKR RQKHQEYLNS ILQHAKDFKE YHRSVTGKIQ KLTKAVATYH ANTEREQKKE NERIEKERMR RLMAEDEEGY RKLIDQKKDK R.
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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Name :
Leptin tA HumanDescription:
Leptin Antagonist Triple Mutant Human Recombinant
Product # :
CYT-352Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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.