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1000 results found for “HDGF”
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Name :
HBeAgDescription:
Hepatitis B Virus e-Antigen Recombinant
Product # :
HBV-272Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant hepatitis B virus “e” antigen is fused to a His Tag and having a molecular mass of approximately 18kDa.
Source
Escherichia Coli.
Formulation
20mM Tris-Hcl, 0.5M NaCl and 0.8M imidazole.
Purity
Protein is >95%
More Info
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Introduction
Hepatitis B virus is the main cause for human liver disease, chronic infection frequently causes liver cancer and cirrhosis. The HBV core gene codes 2 distinct protein products, a 21.5-kDa protein being assembled to form nucleocapsid particles designated HBcAg, which wraps the viral DNA as well as the viral polymerase and RNase H, and a precore protein, designated as HBeAg, which is directly to the endoplasmic reticulum, processed at N- and C-terminally and secreted as non-particulate e-anitgen (HBeAg). The pre-core protein contains an extra 29 N-terminal amino acids, serving as a signal peptide to direct the nascent polypeptide into secretory pathway. After the secretion, mature HBeAg is deleted at the residue 149 C-terminally and retains 10 precore residues N-terminally. HBcAg and HBeAg are distinctly recognized by antibodies but highly cross-reactive at the T-cell level.
The e antigen is found in the circulation, it is found during the active HBV infection, positive result indicates the risk for contagiousness, and is also used as indicator for the effectiveness of HBV treatment. Positive anti-HBeAg specifies an active stage of acute HBV infection that is in its final stages, the risk for contagiousness is dramatically reduced. -
Stability
HBeAg although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
s klclgwlwgm didpykefga svellsflps dffpsirdll dtasalyrea lespehcsph htalrqailc
wgelmnlatw vgsnledpas relvvsyvnv nmglkirqll wfhiscltfg retvleylvs fgvwirtpta
yrppnapils tlpettvv
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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.
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Name :
HTNV (1-200 a.a.)Description:
Hantavirus Recombinant (1-200 a.a.)
HTNV, Hantaan Virus, Hantanvirus.
Product # :
HTV-002Price :
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Description
The Hantavirus Recombinant (1-200 a.a.) protein is expressed in E. coli and is fused to a Six histidine tag at C-terminus and has a MW of 23.8kDa (pI 7.96).
Source
E.Coli
Formulation
HTNV is formulated in 1XPBS.
Purity
HTNV protein is >90% pure as determined by SDS PAGE.
More Info
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Synonyms
HTNV, Hantaan Virus, Hantanvirus.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Upon arrival, Store at -20°C. Please avoid multiple freeze/thaw cycles.
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Background
What is the source or expression system of Hantavirus- Nucleocapsid Protein?
Escherichia Coli.
What is the Purity of Hantavirus- Nucleocapsid Protein?
Hantavirus- Nucleocapsid Protein is >90% pure as determined by SDS-PAGE.
What is the molecular weight / Mw of Hantavirus- Nucleocapsid Protein?
Hantavirus- Nucleocapsid Protein having a total Mw of 23.8kDa.Is Hantavirus- Nucleocapsid conjugated to a Tag?
Hantavirus- Nucleocapsid is fused to 6xHis Tag at N-terminal.What is the Biological Activity of Hantavirus- Nucleocapsid Protein?
The biological functionality of Hantavirus- Nucleocapsid Protein will be determined in the future.
What is the endotoxin level for Hantavirus- Nucleocapsid Protein?
The endotoxin level is minimal, Hantavirus- Nucleocapsid Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of Hantavirus- Nucleocapsid Protein?
Hantavirus- Nucleocapsid Protein is composed from 1-200 amino acids.
What applications can Hantavirus- Nucleocapsid Protein be used in?
Hantavirus-Nucleocapsid Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the function of the hantavirus nucleocapsid (N) protein?
The hantavirus nucleocapsid (N) protein surrounds the viral RNA binding site and protects it during viral replication and assembly.
Why is hantavirus nucleocapsid protein commonly used in ELISA assays?
The hantavirus N protein is highly immunogenic, conserved and widely expressed and induces a strong antibody response in infected individuals.
Does hantavirus N protein bind RNA?
Hantavirus N protein contains RNA-binding domains that specifically interact with viral genomic
Is the hantavirus nucleocapsid protein suitable for antibody production?
Resulting from high immunogenicity, recombinant hantavirus N protein is highly used as an immunogen for generating both polyclonal and monoclonal antibodies.
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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.
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Name :
IGF1 N15 HumanDescription:
Insulin Like Growth Factor-1 N15 Labeled Human Recombinant
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Product # :
CYT-128Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
Description
IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N15 is stable isotope labeled. The IGF1 N15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IGF1 N15 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.sds-page
More Info
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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone 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' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
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Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF1 N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 N15 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 IGF1 N15 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
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 :
EGF RatDescription:
Epidermal Growth Factor Rat Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-669Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epidermal Growth Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6151 Dalton. The Rat EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Rat EGF was lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat EGF 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 Rat EGF in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
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Background
Pioneering Insights into Epidermal Growth Factor Rat Recombinant: Unraveling Signaling Dynamics and Therapeutic Implications
Abstract:
This research paper delves into the unexplored landscape of Epidermal Growth Factor Rat Recombinant (EGF-RR), delving into its intricate molecular attributes, signaling pathways, and potential therapeutic applications. By employing advanced methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the complex interplay between EGF-RR and cellular responses, offering a new perspective for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) holds a key role in cellular regulation. This paper navigates the intricacies of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and its potential therapeutic implications.
Protein Expression and Purification:
The paper delves into the meticulous engineering of EGF-RR, involving gene optimization for enhanced expression. Protein purification strategies, such as affinity chromatography, are employed to obtain highly purified EGF-RR for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Advanced receptor binding assays elucidate the interaction of EGF-RR with its cognate receptor. By quantifying binding affinities and kinetic rates, the study unveils the nuances of EGF-RR's engagement with its receptor, shedding light on potential structural determinants.
Cellular Signaling Pathways and Functional Responses:
Through in vitro cellular assays, the study unravels the intricate signaling pathways initiated by EGF-RR. Quantitative phosphoproteomic analyses expose the dynamic phosphorylation events triggered by EGF-RR, providing insights into its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Molecular Modeling:
Utilizing advanced bioinformatics tools, molecular dynamics simulations provide a deeper understanding of EGF-RR's interactions with its receptor and potential downstream effectors. Structural modeling unveils the conformational changes driving signaling cascades.
Therapeutic Prospects and Novel Avenues:
The molecular insights into EGF-RR's signaling dynamics open avenues for therapeutic exploration. Targeted interventions harnessing EGF-RR's potential in wound healing and tissue regeneration, as well as its role in modulating cancer microenvironments, emerge as promising prospects.
Challenges and Future Directions:
Despite progress, challenges such as deciphering context-dependent signaling responses remain. Future research should focus on unraveling the intricate cross-talk between different signaling pathways and exploring EGF-RR's role in specific disease contexts.
Conclusion:
In a convergence of advanced methodologies and visionary insights, Epidermal Growth Factor Rat Recombinant emerges as a captivating subject. Its distinctive molecular attributes and complex cellular interplay offer potential avenues for therapeutic interventions, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.1kDa.
What is the source or expression system of EGF RAT Protein?
Escherichia Coli.
What is the Purity of EGF RAT Protein?
EGF RAT Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF RAT Protein?
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.
What is the amino acid sequence of EGF RAT Protein?
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
What applications can EGF RAT Protein be used in?
EGF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT 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 :
Epigen Human, Sf9Description:
Epigen Human Recombinant, Sf9
Epithelial mitogen, EPG, Epithelial Mitogen Homolog (Mouse), Epithelial Mitogen Homolog, ALGV3072, PRO9904, Epigen, EPGN.
Product # :
CYT-1038Price :
Quantity :
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Shipped with Ice Packs
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- sds-page
Description
EPGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 97 amino acids (23-110a.a.) and having a molecular mass of 10.8kDa.EPGN is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
EPGN protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.
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Synonyms
Epithelial mitogen, EPG, Epithelial Mitogen Homolog (Mouse), Epithelial Mitogen Homolog, ALGV3072, PRO9904, Epigen, EPGN.
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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
ADPAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE KHHHHHH.
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Background
What is the molecular weight/Mw of EPIGEN Protein?
EPIGEN Protein has a total Mw of 10.8kDa.
What is the source or expression system of EPIGEN Protein?
Sf9, Insect cells.
What is the Purity of EPIGEN Protein?
EPIGEN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EPIGEN Protein?
The biological functionality of EPIGEN Protein will be determined in the future.
What is the amino acid sequence of EPIGEN Protein?
ADPAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE KHHHHHH.
What applications can EPIGEN Protein be used in?
EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPIGEN Protein?
The endotoxin level is minimal, EPIGEN 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 :
Periostin Human, HEKDescription:
Periostin Human Recombinant, HEK
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
Product # :
CYT-835Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Periostin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn22-Gln836) containing a total of 821 amino acids, having a calculated molecular mass of 91.8kDa and fused to a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
Periostin was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% trehalose.
Purity
Greater than 38.0% as determined by SDS-PAGE.
More Info
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Introduction
Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart. -
Synonyms
OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Periostin 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
NNHYDKILAH SRIRGRDQGP NVCALQQILG TKKKYFSTCK NWYKKSICGQ KTTVLYECCP GYMRMEGMKG CPAVLPIDHV YGTLGIVGAT TTQRYSDASK LREEIEGKGS FTYFAPSNEA WDNLDSDIRR GLESNVNVEL LNALHSHMIN KRMLTKDLKN GMIIPSMYNN LGLFINHYPN GVVTVNCARI IHGNQIATNG VVHVIDRVLT QIGTSIQDFI EAEDDLSSFR AAAITSDILE ALGRDGHFTL FAPTNEAFEK LPRGVLERIM GDKVASEALM KYHILNTLQC SESIMGGAVF ETLEGNTIEI GCDGDSITVN GIKMVNKKDI VTNNGVIHLI DQVLIPDSAK QVIELAGKQQ TTFTDLVAQL GLASALRPDG EYTLLAPVNN AFSDDTLSMD QRLLKLILQN HILKVKVGLN ELYNGQILET IGGKQLRVFV YRTAVCIENS CMEKGSKQGR NGAIHIFREI IKPAEKSLHE KLKQDKRFST FLSLLEAADL KELLTQPGDW TLFVPTNDAF KGMTSEEKEI LIRDKNALQN IILYHLTPGV FIGKGFEPGV TNILKTTQGS KIFLKEVNDT LLVNELKSKE SDIMTTNGVI HVVDKLLYPA DTPVGNDQLL EILNKLIKYI QIKFVRGSTF KEIPVTVYTT KIITKVVEPK IKVIEGSLQP IIKTEGPTLT KVKIEGEPEF RLIKEGETIT EVIHGEPIIK KYTKIIDGVP VEITEKETRE ERIITGPEIK YTRISTGGGE TEETLKKLLQ EEVTKVTKFI EGGDGHLFED EEIKRLLQGD TPVRKLQANK KVQGSRRRLR EGRSQHHHHH 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 :
CHGB HumanDescription:
Chromogranin B Human Recombinant
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
Product # :
PRO-824Price :
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Shipped with Ice Packs
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Description
CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.
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Synonyms
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
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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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.
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 :
GTF3C6 HumanDescription:
General Transcription Factor IIIC Polypeptide 6 Human Recombinant
bA397G5.3, C6orf51, TFIIIC35, General transcription factor 3C polypeptide 6, Transcription factor IIIC 35 kDa subunit, TFIIIC 35 kDa subunit, TFIIIC35, Transcription factor IIIC subunit 6, CDA020, NPD020.
Product # :
PRO-2127Price :
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Shipped with Ice Packs
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Description
GTF3C6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-213 a.a) and having a molecular mass of 26.4kDa.GTF3C6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GTF3C6 protein solution (0.5mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
In the absence of additional proteins - the general transcription factors (GTFs) RNA polymerases are unable to initiate RNA synthesis. GTFs accumulate in a complex on the DNA promoter and recruit the RNA polymerase. GTF3C family proteins are vital for RNA polymerase III to produce several small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin.
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Synonyms
bA397G5.3, C6orf51, TFIIIC35, General transcription factor 3C polypeptide 6, Transcription factor IIIC 35 kDa subunit, TFIIIC 35 kDa subunit, TFIIIC35, Transcription factor IIIC subunit 6, CDA020, NPD020.
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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 MGSMAAAADE RSPEDGEDEE EEEQLVLVEL SGIIDSDFLS KCENKCKVLG IDTERPILQV DSCVFAGEYE DTLGTCVIFE ENVEHADTEG NNKTVLKYKC HTMKKLSMTR TLLTEKKEGE ENIGGVEWLQ IKDNDFSYRP NMICNFLHEN EDEEVVASAP DKSLELEEEE IQMNDSSNLS CEQEKPMHLE IEDSGPLIDI PSETEGSVFM ETQMLP.
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 :
MIF Human, ActiveDescription:
Macrophage Migration Inhibitory Factor Human Recombinant (Active)
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Product # :
CYT-596Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MIF human Recombinant was cloned into an E.coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chain containing 115 amino acids and having a molecular mass of 12.5 kDa.
Source
Escherichia Coli.
Formulation
MIF-Protein was lyophilized from 10mM sodium phosphate buffer pH-7.5.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Human PBMCs were cultured with 0 to 1000ng/ml Human MIF. Production of IL-8 was measured via ELISA after 24 hours. The ED50 which was found to be 88-132ng/ml.More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIF-protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF-protein 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 MIF-Protein in sterile 18MΩ-cm H2O at a concentration between 0.1mg-1mg per 1ml.
-
Amino Acid Sequence
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLM
AFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVY
INYYDMNAANVGWNNSTFA.
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 :
NT 3 HumanDescription:
Neurotrophin-3 Human Recombinant
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
Product # :
CYT-257Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 0.1% TFA.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.
More Info
-
Introduction
NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.
-
Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.
-
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 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). 2. Analysis by RP-HPLC, using a standard solution of NT-3 as a Reference Standard.
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 :
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
-
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.
-
Synonyms
Rho guanine nucleotide exchange factor 39, ARHGEF39, C9orf100, RP11-331F9.7.
-
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 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.
- View Data Sheet
Name :
PDRG1 HumanDescription:
p53 and DNA-Damage Regulated 1 Human Recombinant
p53 and DNA damage-regulated protein 1, PDRG1, C20orf126, PDRG.
Product # :
PRO-007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
PDRG1 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 153 amino acids (1-133 a.a.) and having a molecular mass of 17.6kDa. The PDRG1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PDRG1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
PDRG1 is a 133 amino acid protein that localizes to the cytoplasm and belongs to the prefoldin subunit beta family. PDRG1 is expressed primarily in normal testicular tissue, it is functionally induced by ultraviolet light and is thought to have a role in chaperone-mediated protein folding, possibly having a role in cellular degradation. PDRG1 is linked to Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome.
-
Synonyms
p53 and DNA damage-regulated protein 1, PDRG1, C20orf126, PDRG.
-
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 MLSPEAERVL RYLVEVEELA EEVLADKRQI VDLDTKRNQN REGLRALQKD LSLSEDVMVC FGNMFIKMPH PETKEMIEKD QDHLDKEIEK LRKQLKVKVN RLFEAQGKPE LKGFNLNPLN QDELKALKVI LKG.
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 :
TFF1 HumanDescription:
Trefoil Factor-1 Human Recombinant
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
Product # :
CYT-586Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
- formulation
- purity
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Description
TFF-1 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 60 amino acids which includes a 40 amino acid trefoil motif containing 3 conserved intramolecular disulfide bonds and having a total molecular mass of 13.2 kDa. TFF-1 Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Human TFF1 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 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 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.More Info
-
Introduction
The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are stable secretory proteins expressed in the gastrointestinal tract (gastric mucosa), and are involved in intestinal mucosal defense and repair. TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a gastric-specific tumor suppressor gene. TFF1 is a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 protects the mucosa from isults, stabilizes the mucus layer, & affects healing of the epithelium. TFF1 is commonly expressed in tumors. TFF1 is related with the cell membrane of MCF-7 cells. High levels of TFF1 and TFF2 are found in serum from inflammatory bowel disease.
-
Synonyms
TFF-1, TFF1, pS2, BCEI, HPS, HP1.A, pNR-2, D21S21, pS2 protein, Trefoil factor 1, Breast cancer estrogen-inducible protein.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TFF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF1 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 TFF1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
EAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFY
PNTIDVPPEEECEF.
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 :
FGF20 HumanDescription:
Fibroblast Growth Factor-20 Human Recombinant
Fibroblast Growth Factor 20, FGF-20, RHDA2, FGF20.
Product # :
CYT-875Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
FGF20 Human Recombinant (1-211) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids and having a molecular mass of 24kDa.The FGF-20 is fused to a 6 amino acid His tag [HHHHHH] at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in MOPS, (NH4)2SO4, DTT and EDTA.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 2.5ng/ml.More Info
-
Introduction
Fibroblast growth factor 20 (FGF20) belongs to the FGF gene family and member of FGF-9 subfamily (based upon its structure). Human FGF20 has several receptors which include FGF R1c, FGF R2c, FGF R3b, FGF R3c and FGF R4. FGF20 is expressed a various cells, including dopaminergic neurons, fibroblasts, keratinocytes and breast epithelium, and numerous sites in the fetus.
-
Synonyms
Fibroblast Growth Factor 20, FGF-20, RHDA2, FGF20.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FGF20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-20 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 FGF-20 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MHHHHHHAPL AEVGGFLGGL EGLGQQVGSH FLLPPAGERP PLLGERRSAA ERSARGGPGA AQLAHLHGIL RRRQLYCRTG FHLQILPDGS VQGTRQDHSL FGILEFISVA VGLVSIRGVD SGLYLGMNDK GELYGSEKLT SECIFREQFE ENWYNTYSSN IYKHGDTGRR YFVALNKDGT PRDGARSKRH QKFTHFLPRP VDPERVPELY KDLLMYT.
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Background
What is the molecular weight/Mw of FGF20 Protein?
FGF20 Protein has a total Mw of 24kDa.
What is the source or expression system of FGF20 Protein?
Escherichia Coli.
What is the Purity of FGF20 Protein?
FGF20 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF20 Protein?
The ED50, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 2.5ng/ml.
What is the amino acid sequence of FGF20 Protein?
MHHHHHHAPL AEVGGFLGGL EGLGQQVGSH FLLPPAGERP PLLGERRSAA ERSARGGPGA AQLAHLHGIL RRRQLYCRTG FHLQILPDGS VQGTRQDHSL FGILEFISVA VGLVSIRGVD SGLYLGMNDK GELYGSEKLT SECIFREQFE ENWYNTYSSN IYKHGDTGRR YFVALNKDGT PRDGARSKRH QKFTHFLPRP VDPERVPELY KDLLMYT.
What applications can FGF20 Protein be used in?
FGF20 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF20 Protein?
The endotoxin level is minimal, FGF20 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 :
CBX3 HumanDescription:
Chromobox Homolog 3 Human Recombinant
Chromobox homolog 3 (Drosophila HP1 gamma), Heterochromatin protein 1 homolog gamma, Modifier 2 protein, HP1 gamma homolog, HECH, HP1Hs-gamma.
Product # :
PRO-1057Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CBX3 Human Recombinant produced in E. coli is a single polypeptide chain containing 207 amino acids (1-183) and having a molecular mass of 23.4kDa.CBX3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CBX3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
CBX3 takes part in transcriptional silencing in heterochromatin-like complexes. CBX3 identifies and binds histone H3 tails methylated at 'Lys-9', thereby create an epigenetic repression. Additionally, CBX3 takes part in the formation of functional kinetochore by interacting with MIS12 complex proteins.
-
Synonyms
Chromobox homolog 3 (Drosophila HP1 gamma), Heterochromatin protein 1 homolog gamma, Modifier 2 protein, HP1 gamma homolog, HECH, HP1Hs-gamma.
-
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 MGSHMASNKT TLQKMGKKQN GKSKKVEEAE PEEFVVEKVL DRRVVNGKVE YFLKWKGFTD ADNTWEPEEN LDCPELIEAF LNSQKAGKEK DGTKRKSLSD SESDDSKSKK KRDAADKPRG FARGLDPERI IGATDSSGEL MFLMKWKDSD EADLVLAKEA NMKCPQIVIA FYEERLTWHS CPEDEAQ.
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 :
HDL HumanDescription:
High Density Lipoprotein Human
High Density Lipoprotein, HDL.
Product # :
PRO-559Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Human High Density Lipoprotein (HDL) produced in Human plasma.
Source
Human plasma.
Purity
Cholesterol level >200mg/l. <1% LDL.
More Info
-
Introduction
HDL is a complex of lipids and proteins in approximately equal amounts that functions as a transporter of cholesterol in the blood. HDL is the smallest of the lipoprotein particles; it’s the densest because it contains the highest proportion of protein. The liver synthesizes these lipoproteins as complexes of apolipoproteins and phospholipid, which bear a resemblance to cholesterol-free flattened spherical lipoprotein particles. They pick up cholesterol; carry it internally, from cells by interaction with the ATP Binding Cassette Transporter A1. Lecithin-cholesterol acyltransferase (plasma enzyme) converts the free cholesterol into cholesteryl ester (a more hydrophobic form of cholesterol) which is then sequestered into the core of the lipoprotein particle ultimately making the newly synthesized HDL spherical. They increase in size as they pass through the bloodstream and integrate more cholesterol and phospholipid molecules from cells and other lipoproteins, for instance by the interaction with the ABCG1 transporter and the phospholipid transport protein. HDL transports their cholesterol generally to the liver or steroidogenic organs such as adrenals, ovary and testes by direct and indirect pathways. The release of HDL cholesterol to adrenals, ovaries and testes is important for the synthesis of steroid hormones. Since the triglycerides are not stable in HDL, they’re degraded by hepatic lipase in order that finally small HDL particles are left which resume the uptake of cholesterol from cells. The cholesterol supplied to the liver is excreted into the bile and consequently intestine either directly or indirectly after conversion into bile acids. High levels of HDL are associated with a decreased risk of atherosclerosis and coronary heart disease.
-
Synonyms
High Density Lipoprotein, HDL.
-
Physical Appearance
Yellow to orange liquid.
-
Stability
Human HDL although stable at 4°C for 1 week, should be stored below -15°C (short term i.e. < 3 months) and below -70°C for long term.
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Human Virus Test
Starting material donor tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, Hepatitis C antibodies, HIV1/HCV/HBV NAT 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.
- View Data Sheet
Name :
IGF1 RabbitDescription:
Insulin-Like Growth Factor 1 Rabbit Recombinant
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Product # :
CYT-427Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Insulin-Like Growth Factor-I Rabbit Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 7639 Dalton.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (0.5mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:(a) Gel-filtration chromatography under non denaturing conditions.(b) Analysis by SDS-PAGE.
Biological Activity
IGF-I is biologically active when compared to human IGF-1. The ED50, calculated by the dose -dependent proliferation of human MCF/7 cells is 5 to 25ng/ml in the cell culture mixture dependent on culture conditions. Its activity consists of 30-40 % compared to human IGF-1.More Info
-
Introduction
The IGFs comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone. Early studies showed that growth hormone 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, and somatomedin B. IGF-1 is a small protein secreted mostly but not exclusively by the liver and circulating in blood mostly as a complex with several IGF binding proteins. It has growth-regulating, insulin-like, and mitogenic functions and it is secreted in response to growth hormone stimulation.
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Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Insulin-Like Growth Factor-1 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 rbIGF-I in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MTAGPETLCG AELVDALQFV CGDRGFYFNK PTGYGSSSRR APQTGIVDEC CFRSCDLRRL EMYCAPLKP
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 :
M CSF Human, HisDescription:
Macrophage Colony Stimulating Factor Human Recombinant, His Tag
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
Product # :
CYT-695Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 179 amino acids (33-190 a.a.) and having a total molecular mass of 20.7 kDa.MCSF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MCSF protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT & 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
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Synonyms
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
-
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 MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ DVVTKPDCN.
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 :
GM-CSF K9Description:
Granulocyte Macrophage-Colony Stimulating Factor Canine Recombinant
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
Product # :
CYT-724Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GMCSF k9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14.2 kDa. GM-CSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GMCSF was lyophilized after extensive dialysis against 1xPBS pH 7.4.
Purity
Greater than 96.0% as determined by
1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.Biological Activity
The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF1 erythroleukemic cells is typically 1-4 ng/ml.More Info
-
Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APTRSPTLVT RPSQHVDAIQ EALSLLNNSN DVTAVMNKAV KVVSEVFDPE
GPTCLETRLQ LYKEGLQGSL TSLKNPLTMM ANHYKQHCPP TPESPCATQN
INFKSFKENL KDFLFNIPFD CWKPVKK. -
Background
What is the molecular weight/Mw of GM-CSF K9 Protein?
GM-CSF K9 Protein has a total Mw of 14.2kDa.
What is the source or expression system of GM-CSF K9 Protein?
Escherichia Coli.
What is the Purity of GM-CSF K9 Protein?
GM-CSF K9 Protein is >96% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF K9 Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF1 erythroleukemic cells is typically 1-4 ng/ml.
What is the amino acid sequence of GM-CSF K9 Protein?
APTRSPTLVT RPSQHVDAIQ EALSLLNNSN DVTAVMNKAV KVVSEVFDPE
GPTCLETRLQ LYKEGLQGSL TSLKNPLTMM ANHYKQHCPP TPESPCATQN
INFKSFKENL KDFLFNIPFD CWKPVKK.
What applications can GM-CSF K9 Protein be used in?
GM-CSF K9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF K9 Protein?
The endotoxin level is minimal, GM-CSF K9 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 :
ATF HumanDescription:
Apo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Human Apo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.
Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be <6 ppm.
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 :
TGFB3 Human, PlantDescription:
Transforming Growth Factor-Beta 3 Human Recombinant, Plant
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Product # :
CYT-588Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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- biological activity
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Description
TGFB3 Human Recombinant produced in plant is a disulfide-linked homodimeric, glycosylated, polypeptide chain containing 118 amino acids and having a molecular mass of 27.2kDa. The TGFB3 is fused to 6xHis tag at N-terminus and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The biological activity of TGFB3 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 ? 40ng/ml corresponding to a specific activity of 25,000 Units/mg.More Info
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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFB3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 Human 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 TGFB3 in sterile 5mM HCl & 50ug/ml BSA at a concentration of 0.05mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HHHHHALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKG
YYANFCSGPCPYLRSADTTHSTVLGLY
NTLNPEASASP
CCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS.
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 :
HEV ORF2 (403-461 a.a.)Description:
Hepatitis E Virus ORF2 (403-461 a.a.) Recombinant
Product # :
HEV-272Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- formulation
- purity
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Description
The e.coli derived HEV protein is fused with beta-galactosidase at the N-Terminus and contains the HEV immunodominant regions from ORF2 403-461 a.a.
Formulation
20mM Tris-HCl pH-8, 8M urea and 10mM B-ME.
Purity
HEV ORF2 Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
Hepatitis E virus (HEV), the major etiologic agent of enterically transmitted non-A, non-B hepatitis worldwide, is a spherical, non-enveloped, single stranded RNA virus that is approximately 32 to 34 nm in diameter. HEV belongs to a genus of HEV-like viruses (unassigned genus). HEV has a single-stranded polyadenylated RNA genome of approximately 8 kb. Based on its physicochemical properties it is presumed to be a calici-like virus.
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Stability
HEV ORF2 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HEV ORF2 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HEV with minimal specificity problems.
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Specificity
Immunoreactive with sera HEV-infected individuals.
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Purification Method
HEV ORF2 was 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.
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Name :
HTLV-1 gp21Description:
HTLV-1 gp21 Recombinant
Product # :
HIV-141Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- formulation
- purity
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Description
The E.Coli derived recombinant protein contains the gp21 immunodominant region, 1-152 amino acids, the MW is 17.9 kDa. Fused with a His tag at C-Terminus.
Formulation
1mg/ml solution in PBS
Purity
Protein is > 90% pure as determined by SDS-PAGE.
More Info
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Introduction
Human T-lymphotropic virus (HTLV) is a human, single-stranded RNA retrovirus that causes T-cell leukemia and T-cell lymphoma. The virus activates a subset of T-helper cellscalled Th1cells. The result is a proliferation of Th1 cells and overproduction of Th1 related cytokines (mainly IFN-gamma and TNF-alpha). Feedback mechanisms of these cytokines cause a suppression of the Th2 lymphocytes and a reduction of Th2 cytokine production (mainly IL-4, IL-5, IL-10 and IL-13). The end result is a reduction in the ability of the infected host to mount an adequate immune response to invading organisms that require a predominantly Th2 dependant response (these include parasitic infections and production of mucosal and humoral antibodies).
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Stability
HTLV-1 gp21 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Purification Method
HTLV-1 gp21 was 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.
- View Data Sheet
Name :
FGFR1OP Human (1-80)Description:
FGFR1 Oncogene Partner (1-80 a.a.) Human Recombinant
FGFR1 oncogene partner, FGFR1OP, FOP.
Product # :
PKA-138Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
The FGFR1O PHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FGFR1OP His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 80 amino acid residues of the FGFR1OP Human, 1-80 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
FGFR1 oncogene partner, FGFR1OP, FOP.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized FGFR1OP 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.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
L MAATAAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE SLRKFLNTKD GRLVASLVA
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Background
FGFR1 oncogene partner also known as FGFR1OP is a leucine-rich member of the FGFR1OP family. The ensuing chimeric protein contains the N-terminal leucine-rich region of the FGFR1OP protein fused to the catalytic domain of FGFR1. The FGFR1OP plays a main role in normal proliferation and differentiation of the erythroid lineage.
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.